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Conserved domains on  [gi|530376195|ref|XP_005248086|]
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actin-binding LIM protein 2 isoform X38 [Homo sapiens]

Protein Classification

actin-binding LIM protein( domain architecture ID 10873311)

actin-binding LIM protein (abLIM) may act as a scaffold protein for signaling modules of the actin cytoskeleton

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AbLIM_anchor super family cl24685
Putative adherens-junction anchoring region of AbLIM; AbLIM_anchor is a domain lying between ...
281-476 7.09e-61

Putative adherens-junction anchoring region of AbLIM; AbLIM_anchor is a domain lying between the LIM actin-binding and the vilin-head domain of actin-binding LIM proteins. It is likely that this domain is involved in anchoring abLIMs to circumferential actin bundles in specific cell types.


The actual alignment was detected with superfamily member pfam16182:

Pssm-ID: 465046 [Multi-domain]  Cd Length: 319  Bit Score: 203.09  E-value: 7.09e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376195  281 TRTSSESIISVPASSTSGSPSRVIYAKLGGEILDYRDLAALPKSKAIYDIDRPDMISYSPYISHS---AGDRQSYGE--- 354
Cdd:pfam16182   1 TRTSSESIISPPGSSISGSPSRVIYAKLDNEILDYKDLAALPKVKAIYDIERPDLISYEPYVSYSsddRLERQSYGEsls 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376195  355 -------GDQDDRSYKQCRTSSPSSTGSVSLGR--YTPT-SRSPQHYSRP------------------------------ 394
Cdd:pfam16182  81 tlspsseDSYDSRELRQRRSSSPGSIGSPTYSRhgYTPTlSRSPQHFHRPgsesgrsspslsqpsdrkspptyvqapkhf 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376195  395 ------------------------------------AARRS---DGEDGSLDQDNRKQKSSW-------LMLKGDADTRT 428
Cdd:pfam16182 161 hvpdtgvkdniyrkppiykqhgtsasasqssediihSSRFPasgGEEEGWNRRLLQEEELSKiqsglgkLILKEEMEARS 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530376195  429 NSPDLDTQSLSHSSGTD------------------RDPLQRMAG-DSFHS------------QYKIYPYDSLIVTNRIR 476
Cdd:pfam16182 241 GSERRDPWSSPRSSPSGssgsdspysksaslpgygRNGLHRPQSaDFFQYgsdgdvswggmrEYKIYPYEMLAVTNRGR 319
LIM4_abLIM cd09330
The fourth LIM domain of actin binding LIM (abLIM) proteins; The fourth LIM domain of actin ...
217-272 1.52e-35

The fourth LIM domain of actin binding LIM (abLIM) proteins; The fourth LIM domain of actin binding LIM (abLIM) proteins: Three homologous members of the abLIM protein family have been identified; abLIM-1, abLIM-2 and abLIM-3. The N-terminal of abLIM consists of four tandem repeats of LIM domains and the C-terminal of acting binding LIM protein is a villin headpiece domain, which has strong actin binding activity. The abLIM-1, which is expressed in retina, brain, and muscle tissue, has been indicated to function as a tumor suppressor. AbLIM-2 and -3, mainly expressed in muscle and neuronal tissue, bind to F-actin strongly. They may serve as a scaffold for signaling modules of the actin cytoskeleton and thereby modulate transcription. It has shown that LIM domains of abLIMs interact with STARS (striated muscle activator of Rho signaling), which directly binds actin and stimulates serum-response factor (SRF)-dependent transcription. All LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


:

Pssm-ID: 188716  Cd Length: 56  Bit Score: 126.70  E-value: 1.52e-35
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 530376195 217 CDSCEKYITGRVLEAGEKHYHPSCALCVRCGQMFAEGEEMYLQGSSIWHPACRQAA 272
Cdd:cd09330    1 CEACDKFITGKVLEAGGKHYHPTCARCSRCGQMFGEGEEMYLQGSEIWHPDCRQAA 56
LIM2_abLIM cd09328
The second LIM domain on actin binding LIM (abLIM) proteins; The second LIM domain of actin ...
85-140 1.84e-32

The second LIM domain on actin binding LIM (abLIM) proteins; The second LIM domain of actin binding LIM (abLIM) proteins: Three homologous members of the abLIM protein family have been identified; abLIM-1, abLIM-2 and abLIM-3. The N-terminal of abLIM consists of four tandem repeats of LIM domains and the C-terminal of acting binding LIM protein is a villin headpiece domain, which has strong actin binding activity. The abLIM-1, which is expressed in retina, brain, and muscle tissue, has been indicated to function as a tumor suppressor. AbLIM-2 and -3, mainly expressed in muscle and neuronal tissue, bind to F-actin strongly. They may serve as a scaffold for signaling modules of the actin cytoskeleton and thereby modulate transcription. It has shown that LIM domains of abLIMs interact with STARS (striated muscle activator of Rho signaling), which directly binds actin and stimulates serum-response factor (SRF)-dependent transcription. All LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


:

Pssm-ID: 188714  Cd Length: 56  Bit Score: 118.22  E-value: 1.84e-32
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 530376195  85 GTRCFSCDQFIEGEVVSALGKTYHPDCFVCAVCRLPFPPGDRVTFNGKECMCQKCS 140
Cdd:cd09328    1 GTKCDSCQDFVEGEVVSALGKTYHPKCFVCSVCRQPFPPGDRVTFNGKECLCQKCS 56
LIM3_abLIM cd09329
The third LIM domain of actin binding LIM (abLIM) proteins; The third LIM domain of actin ...
158-209 9.12e-28

The third LIM domain of actin binding LIM (abLIM) proteins; The third LIM domain of actin binding LIM (abLIM) proteins: Three homologous members of the abLIM protein family have been identified; abLIM-1, abLIM-2 and abLIM-3. The N-terminal of abLIM consists of four tandem repeats of LIM domains and the C-terminal of acting binding LIM protein is a villin headpiece domain, which has strong actin binding activity. The abLIM-1, which is expressed in retina, brain, and muscle tissue, has been indicated to function as a tumor suppressor. AbLIM-2 and -3, mainly expressed in muscle and neuronal tissue, bind to F-actin strongly. They may serve as a scaffold for signaling modules of the actin cytoskeleton and thereby modulate transcription. It has shown that LIM domains of abLIMs interact with STARS (striated muscle activator of Rho signaling), which directly binds actin and stimulates serum-response factor (SRF)-dependent transcription. All LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


:

Pssm-ID: 188715 [Multi-domain]  Cd Length: 52  Bit Score: 105.09  E-value: 9.12e-28
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530376195 158 CGGCGTEIKNGQALVALDKHWHLGCFKCKSCGKLLNAEYISKDGLPYCEADY 209
Cdd:cd09329    1 CAGCGQEIKNGQALLALDKQWHVWCFKCKECGKVLTGEYMGKDGKPYCERDY 52
LIM1_abLIM cd09327
The first LIM domain of actin binding LIM (abLIM) proteins; The first LIM domain of actin ...
29-80 5.34e-27

The first LIM domain of actin binding LIM (abLIM) proteins; The first LIM domain of actin binding LIM (abLIM) proteins: Three homologous members of the abLIM protein family have been identified; abLIM-1, abLIM-2 and abLIM-3. The N-terminal of abLIM consists of four tandem repeats of LIM domains and the C-terminal of acting binding LIM protein is a villin headpiece domain, which has strong actin binding activity. The abLIM-1, which is expressed in retina, brain, and muscle tissue, has been indicated to function as a tumor suppressor. AbLIM-2 and -3, mainly expressed in muscle and neuronal tissue, bind to F-actin strongly. They may serve as a scaffold for signaling modules of the actin cytoskeleton and thereby modulate transcription. It has shown that LIM domains of abLIMs interact with STARS (striated muscle activator of Rho signaling), which directly binds actin and stimulates serum-response factor (SRF)-dependent transcription. All LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


:

Pssm-ID: 188713 [Multi-domain]  Cd Length: 52  Bit Score: 103.10  E-value: 5.34e-27
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530376195  29 CNTCGNVCKGEVLRVQDKYFHIKCFVCKACGCDLAEGGFFVRQGEYICTLDY 80
Cdd:cd09327    1 CYKCGKKCKGEVLRVQDKYFHIKCFTCKVCGCDLAQGGFFVKEGEYYCTDDY 52
VHP pfam02209
Villin headpiece domain;
491-526 5.84e-17

Villin headpiece domain;


:

Pssm-ID: 460493  Cd Length: 36  Bit Score: 74.34  E-value: 5.84e-17
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 530376195  491 HLSPEEFQEVFGMSIEEFDRLALWKRNDLKKKALLF 526
Cdd:pfam02209   1 YLSDEDFEEVFGMSREEFYKLPKWKQNNLKKKAGLF 36
 
Name Accession Description Interval E-value
AbLIM_anchor pfam16182
Putative adherens-junction anchoring region of AbLIM; AbLIM_anchor is a domain lying between ...
281-476 7.09e-61

Putative adherens-junction anchoring region of AbLIM; AbLIM_anchor is a domain lying between the LIM actin-binding and the vilin-head domain of actin-binding LIM proteins. It is likely that this domain is involved in anchoring abLIMs to circumferential actin bundles in specific cell types.


Pssm-ID: 465046 [Multi-domain]  Cd Length: 319  Bit Score: 203.09  E-value: 7.09e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376195  281 TRTSSESIISVPASSTSGSPSRVIYAKLGGEILDYRDLAALPKSKAIYDIDRPDMISYSPYISHS---AGDRQSYGE--- 354
Cdd:pfam16182   1 TRTSSESIISPPGSSISGSPSRVIYAKLDNEILDYKDLAALPKVKAIYDIERPDLISYEPYVSYSsddRLERQSYGEsls 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376195  355 -------GDQDDRSYKQCRTSSPSSTGSVSLGR--YTPT-SRSPQHYSRP------------------------------ 394
Cdd:pfam16182  81 tlspsseDSYDSRELRQRRSSSPGSIGSPTYSRhgYTPTlSRSPQHFHRPgsesgrsspslsqpsdrkspptyvqapkhf 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376195  395 ------------------------------------AARRS---DGEDGSLDQDNRKQKSSW-------LMLKGDADTRT 428
Cdd:pfam16182 161 hvpdtgvkdniyrkppiykqhgtsasasqssediihSSRFPasgGEEEGWNRRLLQEEELSKiqsglgkLILKEEMEARS 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530376195  429 NSPDLDTQSLSHSSGTD------------------RDPLQRMAG-DSFHS------------QYKIYPYDSLIVTNRIR 476
Cdd:pfam16182 241 GSERRDPWSSPRSSPSGssgsdspysksaslpgygRNGLHRPQSaDFFQYgsdgdvswggmrEYKIYPYEMLAVTNRGR 319
LIM4_abLIM cd09330
The fourth LIM domain of actin binding LIM (abLIM) proteins; The fourth LIM domain of actin ...
217-272 1.52e-35

The fourth LIM domain of actin binding LIM (abLIM) proteins; The fourth LIM domain of actin binding LIM (abLIM) proteins: Three homologous members of the abLIM protein family have been identified; abLIM-1, abLIM-2 and abLIM-3. The N-terminal of abLIM consists of four tandem repeats of LIM domains and the C-terminal of acting binding LIM protein is a villin headpiece domain, which has strong actin binding activity. The abLIM-1, which is expressed in retina, brain, and muscle tissue, has been indicated to function as a tumor suppressor. AbLIM-2 and -3, mainly expressed in muscle and neuronal tissue, bind to F-actin strongly. They may serve as a scaffold for signaling modules of the actin cytoskeleton and thereby modulate transcription. It has shown that LIM domains of abLIMs interact with STARS (striated muscle activator of Rho signaling), which directly binds actin and stimulates serum-response factor (SRF)-dependent transcription. All LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188716  Cd Length: 56  Bit Score: 126.70  E-value: 1.52e-35
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 530376195 217 CDSCEKYITGRVLEAGEKHYHPSCALCVRCGQMFAEGEEMYLQGSSIWHPACRQAA 272
Cdd:cd09330    1 CEACDKFITGKVLEAGGKHYHPTCARCSRCGQMFGEGEEMYLQGSEIWHPDCRQAA 56
LIM2_abLIM cd09328
The second LIM domain on actin binding LIM (abLIM) proteins; The second LIM domain of actin ...
85-140 1.84e-32

The second LIM domain on actin binding LIM (abLIM) proteins; The second LIM domain of actin binding LIM (abLIM) proteins: Three homologous members of the abLIM protein family have been identified; abLIM-1, abLIM-2 and abLIM-3. The N-terminal of abLIM consists of four tandem repeats of LIM domains and the C-terminal of acting binding LIM protein is a villin headpiece domain, which has strong actin binding activity. The abLIM-1, which is expressed in retina, brain, and muscle tissue, has been indicated to function as a tumor suppressor. AbLIM-2 and -3, mainly expressed in muscle and neuronal tissue, bind to F-actin strongly. They may serve as a scaffold for signaling modules of the actin cytoskeleton and thereby modulate transcription. It has shown that LIM domains of abLIMs interact with STARS (striated muscle activator of Rho signaling), which directly binds actin and stimulates serum-response factor (SRF)-dependent transcription. All LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188714  Cd Length: 56  Bit Score: 118.22  E-value: 1.84e-32
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 530376195  85 GTRCFSCDQFIEGEVVSALGKTYHPDCFVCAVCRLPFPPGDRVTFNGKECMCQKCS 140
Cdd:cd09328    1 GTKCDSCQDFVEGEVVSALGKTYHPKCFVCSVCRQPFPPGDRVTFNGKECLCQKCS 56
LIM3_abLIM cd09329
The third LIM domain of actin binding LIM (abLIM) proteins; The third LIM domain of actin ...
158-209 9.12e-28

The third LIM domain of actin binding LIM (abLIM) proteins; The third LIM domain of actin binding LIM (abLIM) proteins: Three homologous members of the abLIM protein family have been identified; abLIM-1, abLIM-2 and abLIM-3. The N-terminal of abLIM consists of four tandem repeats of LIM domains and the C-terminal of acting binding LIM protein is a villin headpiece domain, which has strong actin binding activity. The abLIM-1, which is expressed in retina, brain, and muscle tissue, has been indicated to function as a tumor suppressor. AbLIM-2 and -3, mainly expressed in muscle and neuronal tissue, bind to F-actin strongly. They may serve as a scaffold for signaling modules of the actin cytoskeleton and thereby modulate transcription. It has shown that LIM domains of abLIMs interact with STARS (striated muscle activator of Rho signaling), which directly binds actin and stimulates serum-response factor (SRF)-dependent transcription. All LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188715 [Multi-domain]  Cd Length: 52  Bit Score: 105.09  E-value: 9.12e-28
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530376195 158 CGGCGTEIKNGQALVALDKHWHLGCFKCKSCGKLLNAEYISKDGLPYCEADY 209
Cdd:cd09329    1 CAGCGQEIKNGQALLALDKQWHVWCFKCKECGKVLTGEYMGKDGKPYCERDY 52
LIM1_abLIM cd09327
The first LIM domain of actin binding LIM (abLIM) proteins; The first LIM domain of actin ...
29-80 5.34e-27

The first LIM domain of actin binding LIM (abLIM) proteins; The first LIM domain of actin binding LIM (abLIM) proteins: Three homologous members of the abLIM protein family have been identified; abLIM-1, abLIM-2 and abLIM-3. The N-terminal of abLIM consists of four tandem repeats of LIM domains and the C-terminal of acting binding LIM protein is a villin headpiece domain, which has strong actin binding activity. The abLIM-1, which is expressed in retina, brain, and muscle tissue, has been indicated to function as a tumor suppressor. AbLIM-2 and -3, mainly expressed in muscle and neuronal tissue, bind to F-actin strongly. They may serve as a scaffold for signaling modules of the actin cytoskeleton and thereby modulate transcription. It has shown that LIM domains of abLIMs interact with STARS (striated muscle activator of Rho signaling), which directly binds actin and stimulates serum-response factor (SRF)-dependent transcription. All LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188713 [Multi-domain]  Cd Length: 52  Bit Score: 103.10  E-value: 5.34e-27
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530376195  29 CNTCGNVCKGEVLRVQDKYFHIKCFVCKACGCDLAEGGFFVRQGEYICTLDY 80
Cdd:cd09327    1 CYKCGKKCKGEVLRVQDKYFHIKCFTCKVCGCDLAQGGFFVKEGEYYCTDDY 52
VHP pfam02209
Villin headpiece domain;
491-526 5.84e-17

Villin headpiece domain;


Pssm-ID: 460493  Cd Length: 36  Bit Score: 74.34  E-value: 5.84e-17
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 530376195  491 HLSPEEFQEVFGMSIEEFDRLALWKRNDLKKKALLF 526
Cdd:pfam02209   1 YLSDEDFEEVFGMSREEFYKLPKWKQNNLKKKAGLF 36
VHP smart00153
Villin headpiece domain;
491-526 4.80e-16

Villin headpiece domain;


Pssm-ID: 128458  Cd Length: 36  Bit Score: 71.58  E-value: 4.80e-16
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 530376195   491 HLSPEEFQEVFGMSIEEFDRLALWKRNDLKKKALLF 526
Cdd:smart00153   1 YLSDEDFEEVFGMTREEFYKLPLWKQNQLKKKKGLF 36
LIM pfam00412
LIM domain; This family represents two copies of the LIM structural domain.
158-213 2.44e-12

LIM domain; This family represents two copies of the LIM structural domain.


Pssm-ID: 395333 [Multi-domain]  Cd Length: 57  Bit Score: 61.58  E-value: 2.44e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 530376195  158 CGGCGTEIKNGQALVALDKHWHLGCFKCKSCGKLLNAEYI-SKDGLPYCEADYHAKF 213
Cdd:pfam00412   1 CAGCNRPIYDRELVRALGKVWHPECFRCAVCGKPLTTGDFyEKDGKLYCKHDYYKLF 57
LIM smart00132
Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM ...
157-208 3.35e-10

Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM domains bind protein partners via tyrosine-containing motifs. LIM domains are found in many key regulators of developmental pathways.


Pssm-ID: 214528 [Multi-domain]  Cd Length: 54  Bit Score: 55.47  E-value: 3.35e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 530376195   157 SCGGCGTEI-KNGQALVALDKHWHLGCFKCKSCGKLL-NAEYISKDGLPYCEAD 208
Cdd:smart00132   1 KCAGCGKPIyGTERVLRALGKVWHPECFKCATCGKPLsGDTFFEKDGKLYCKDC 54
LIM pfam00412
LIM domain; This family represents two copies of the LIM structural domain.
88-139 3.88e-09

LIM domain; This family represents two copies of the LIM structural domain.


Pssm-ID: 395333 [Multi-domain]  Cd Length: 57  Bit Score: 52.72  E-value: 3.88e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 530376195   88 CFSCDQFIEG-EVVSALGKTYHPDCFVCAVCRLPFPPGDRVTFNGKeCMCQKC 139
Cdd:pfam00412   1 CAGCNRPIYDrELVRALGKVWHPECFRCAVCGKPLTTGDFYEKDGK-LYCKHD 52
LIM pfam00412
LIM domain; This family represents two copies of the LIM structural domain.
29-84 2.17e-08

LIM domain; This family represents two copies of the LIM structural domain.


Pssm-ID: 395333 [Multi-domain]  Cd Length: 57  Bit Score: 50.41  E-value: 2.17e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 530376195   29 CNTCGN-VCKGEVLRVQDKYFHIKCFVCKACGCDLAEGGFFVRQGEYICTLDYQRLY 84
Cdd:pfam00412   1 CAGCNRpIYDRELVRALGKVWHPECFRCAVCGKPLTTGDFYEKDGKLYCKHDYYKLF 57
LIM smart00132
Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM ...
87-139 6.97e-07

Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM domains bind protein partners via tyrosine-containing motifs. LIM domains are found in many key regulators of developmental pathways.


Pssm-ID: 214528 [Multi-domain]  Cd Length: 54  Bit Score: 46.22  E-value: 6.97e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 530376195    87 RCFSCDQFIEG--EVVSALGKTYHPDCFVCAVCRLPFpPGDRVTFNGKECMCQKC 139
Cdd:smart00132   1 KCAGCGKPIYGteRVLRALGKVWHPECFKCATCGKPL-SGDTFFEKDGKLYCKDC 54
LIM smart00132
Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM ...
29-76 3.45e-06

Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM domains bind protein partners via tyrosine-containing motifs. LIM domains are found in many key regulators of developmental pathways.


Pssm-ID: 214528 [Multi-domain]  Cd Length: 54  Bit Score: 44.30  E-value: 3.45e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 530376195    29 CNTCGN--VCKGEVLRVQDKYFHIKCFVCKACGCDLAEGGFFVRQGEYIC 76
Cdd:smart00132   2 CAGCGKpiYGTERVLRALGKVWHPECFKCATCGKPLSGDTFFEKDGKLYC 51
LIM pfam00412
LIM domain; This family represents two copies of the LIM structural domain.
217-260 4.07e-03

LIM domain; This family represents two copies of the LIM structural domain.


Pssm-ID: 395333 [Multi-domain]  Cd Length: 57  Bit Score: 35.77  E-value: 4.07e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 530376195  217 CDSCEKYITGRVLE-AGEKHYHPSCALCVRCGQMFAEGEEMYLQG 260
Cdd:pfam00412   1 CAGCNRPIYDRELVrALGKVWHPECFRCAVCGKPLTTGDFYEKDG 45
LIM smart00132
Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM ...
216-248 8.69e-03

Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM domains bind protein partners via tyrosine-containing motifs. LIM domains are found in many key regulators of developmental pathways.


Pssm-ID: 214528 [Multi-domain]  Cd Length: 54  Bit Score: 34.67  E-value: 8.69e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 530376195   216 RCDSCEKYITG--RVLEAGEKHYHPSCALCVRCGQ 248
Cdd:smart00132   1 KCAGCGKPIYGteRVLRALGKVWHPECFKCATCGK 35
 
Name Accession Description Interval E-value
AbLIM_anchor pfam16182
Putative adherens-junction anchoring region of AbLIM; AbLIM_anchor is a domain lying between ...
281-476 7.09e-61

Putative adherens-junction anchoring region of AbLIM; AbLIM_anchor is a domain lying between the LIM actin-binding and the vilin-head domain of actin-binding LIM proteins. It is likely that this domain is involved in anchoring abLIMs to circumferential actin bundles in specific cell types.


Pssm-ID: 465046 [Multi-domain]  Cd Length: 319  Bit Score: 203.09  E-value: 7.09e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376195  281 TRTSSESIISVPASSTSGSPSRVIYAKLGGEILDYRDLAALPKSKAIYDIDRPDMISYSPYISHS---AGDRQSYGE--- 354
Cdd:pfam16182   1 TRTSSESIISPPGSSISGSPSRVIYAKLDNEILDYKDLAALPKVKAIYDIERPDLISYEPYVSYSsddRLERQSYGEsls 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376195  355 -------GDQDDRSYKQCRTSSPSSTGSVSLGR--YTPT-SRSPQHYSRP------------------------------ 394
Cdd:pfam16182  81 tlspsseDSYDSRELRQRRSSSPGSIGSPTYSRhgYTPTlSRSPQHFHRPgsesgrsspslsqpsdrkspptyvqapkhf 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376195  395 ------------------------------------AARRS---DGEDGSLDQDNRKQKSSW-------LMLKGDADTRT 428
Cdd:pfam16182 161 hvpdtgvkdniyrkppiykqhgtsasasqssediihSSRFPasgGEEEGWNRRLLQEEELSKiqsglgkLILKEEMEARS 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530376195  429 NSPDLDTQSLSHSSGTD------------------RDPLQRMAG-DSFHS------------QYKIYPYDSLIVTNRIR 476
Cdd:pfam16182 241 GSERRDPWSSPRSSPSGssgsdspysksaslpgygRNGLHRPQSaDFFQYgsdgdvswggmrEYKIYPYEMLAVTNRGR 319
LIM4_abLIM cd09330
The fourth LIM domain of actin binding LIM (abLIM) proteins; The fourth LIM domain of actin ...
217-272 1.52e-35

The fourth LIM domain of actin binding LIM (abLIM) proteins; The fourth LIM domain of actin binding LIM (abLIM) proteins: Three homologous members of the abLIM protein family have been identified; abLIM-1, abLIM-2 and abLIM-3. The N-terminal of abLIM consists of four tandem repeats of LIM domains and the C-terminal of acting binding LIM protein is a villin headpiece domain, which has strong actin binding activity. The abLIM-1, which is expressed in retina, brain, and muscle tissue, has been indicated to function as a tumor suppressor. AbLIM-2 and -3, mainly expressed in muscle and neuronal tissue, bind to F-actin strongly. They may serve as a scaffold for signaling modules of the actin cytoskeleton and thereby modulate transcription. It has shown that LIM domains of abLIMs interact with STARS (striated muscle activator of Rho signaling), which directly binds actin and stimulates serum-response factor (SRF)-dependent transcription. All LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188716  Cd Length: 56  Bit Score: 126.70  E-value: 1.52e-35
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 530376195 217 CDSCEKYITGRVLEAGEKHYHPSCALCVRCGQMFAEGEEMYLQGSSIWHPACRQAA 272
Cdd:cd09330    1 CEACDKFITGKVLEAGGKHYHPTCARCSRCGQMFGEGEEMYLQGSEIWHPDCRQAA 56
LIM2_abLIM cd09328
The second LIM domain on actin binding LIM (abLIM) proteins; The second LIM domain of actin ...
85-140 1.84e-32

The second LIM domain on actin binding LIM (abLIM) proteins; The second LIM domain of actin binding LIM (abLIM) proteins: Three homologous members of the abLIM protein family have been identified; abLIM-1, abLIM-2 and abLIM-3. The N-terminal of abLIM consists of four tandem repeats of LIM domains and the C-terminal of acting binding LIM protein is a villin headpiece domain, which has strong actin binding activity. The abLIM-1, which is expressed in retina, brain, and muscle tissue, has been indicated to function as a tumor suppressor. AbLIM-2 and -3, mainly expressed in muscle and neuronal tissue, bind to F-actin strongly. They may serve as a scaffold for signaling modules of the actin cytoskeleton and thereby modulate transcription. It has shown that LIM domains of abLIMs interact with STARS (striated muscle activator of Rho signaling), which directly binds actin and stimulates serum-response factor (SRF)-dependent transcription. All LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188714  Cd Length: 56  Bit Score: 118.22  E-value: 1.84e-32
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 530376195  85 GTRCFSCDQFIEGEVVSALGKTYHPDCFVCAVCRLPFPPGDRVTFNGKECMCQKCS 140
Cdd:cd09328    1 GTKCDSCQDFVEGEVVSALGKTYHPKCFVCSVCRQPFPPGDRVTFNGKECLCQKCS 56
LIM3_abLIM cd09329
The third LIM domain of actin binding LIM (abLIM) proteins; The third LIM domain of actin ...
158-209 9.12e-28

The third LIM domain of actin binding LIM (abLIM) proteins; The third LIM domain of actin binding LIM (abLIM) proteins: Three homologous members of the abLIM protein family have been identified; abLIM-1, abLIM-2 and abLIM-3. The N-terminal of abLIM consists of four tandem repeats of LIM domains and the C-terminal of acting binding LIM protein is a villin headpiece domain, which has strong actin binding activity. The abLIM-1, which is expressed in retina, brain, and muscle tissue, has been indicated to function as a tumor suppressor. AbLIM-2 and -3, mainly expressed in muscle and neuronal tissue, bind to F-actin strongly. They may serve as a scaffold for signaling modules of the actin cytoskeleton and thereby modulate transcription. It has shown that LIM domains of abLIMs interact with STARS (striated muscle activator of Rho signaling), which directly binds actin and stimulates serum-response factor (SRF)-dependent transcription. All LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188715 [Multi-domain]  Cd Length: 52  Bit Score: 105.09  E-value: 9.12e-28
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530376195 158 CGGCGTEIKNGQALVALDKHWHLGCFKCKSCGKLLNAEYISKDGLPYCEADY 209
Cdd:cd09329    1 CAGCGQEIKNGQALLALDKQWHVWCFKCKECGKVLTGEYMGKDGKPYCERDY 52
LIM1_abLIM cd09327
The first LIM domain of actin binding LIM (abLIM) proteins; The first LIM domain of actin ...
29-80 5.34e-27

The first LIM domain of actin binding LIM (abLIM) proteins; The first LIM domain of actin binding LIM (abLIM) proteins: Three homologous members of the abLIM protein family have been identified; abLIM-1, abLIM-2 and abLIM-3. The N-terminal of abLIM consists of four tandem repeats of LIM domains and the C-terminal of acting binding LIM protein is a villin headpiece domain, which has strong actin binding activity. The abLIM-1, which is expressed in retina, brain, and muscle tissue, has been indicated to function as a tumor suppressor. AbLIM-2 and -3, mainly expressed in muscle and neuronal tissue, bind to F-actin strongly. They may serve as a scaffold for signaling modules of the actin cytoskeleton and thereby modulate transcription. It has shown that LIM domains of abLIMs interact with STARS (striated muscle activator of Rho signaling), which directly binds actin and stimulates serum-response factor (SRF)-dependent transcription. All LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188713 [Multi-domain]  Cd Length: 52  Bit Score: 103.10  E-value: 5.34e-27
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530376195  29 CNTCGNVCKGEVLRVQDKYFHIKCFVCKACGCDLAEGGFFVRQGEYICTLDY 80
Cdd:cd09327    1 CYKCGKKCKGEVLRVQDKYFHIKCFTCKVCGCDLAQGGFFVKEGEYYCTDDY 52
VHP pfam02209
Villin headpiece domain;
491-526 5.84e-17

Villin headpiece domain;


Pssm-ID: 460493  Cd Length: 36  Bit Score: 74.34  E-value: 5.84e-17
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 530376195  491 HLSPEEFQEVFGMSIEEFDRLALWKRNDLKKKALLF 526
Cdd:pfam02209   1 YLSDEDFEEVFGMSREEFYKLPKWKQNNLKKKAGLF 36
VHP smart00153
Villin headpiece domain;
491-526 4.80e-16

Villin headpiece domain;


Pssm-ID: 128458  Cd Length: 36  Bit Score: 71.58  E-value: 4.80e-16
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 530376195   491 HLSPEEFQEVFGMSIEEFDRLALWKRNDLKKKALLF 526
Cdd:smart00153   1 YLSDEDFEEVFGMTREEFYKLPLWKQNQLKKKKGLF 36
LIM pfam00412
LIM domain; This family represents two copies of the LIM structural domain.
158-213 2.44e-12

LIM domain; This family represents two copies of the LIM structural domain.


Pssm-ID: 395333 [Multi-domain]  Cd Length: 57  Bit Score: 61.58  E-value: 2.44e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 530376195  158 CGGCGTEIKNGQALVALDKHWHLGCFKCKSCGKLLNAEYI-SKDGLPYCEADYHAKF 213
Cdd:pfam00412   1 CAGCNRPIYDRELVRALGKVWHPECFRCAVCGKPLTTGDFyEKDGKLYCKHDYYKLF 57
LIM cd08368
LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains ...
158-209 7.56e-12

LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains are identified in a diverse group of proteins with wide variety of biological functions, including gene expression regulation, cell fate determination, cytoskeleton organization, tumor formation and development. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes. They perform their functions through interactions with other protein partners. LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. The consensus sequence of LIM domain has been defined as C-x(2)-C-x(16,23)-H-x(2)-[CH]-x(2)-C-x(2)-C-x(16,21)-C-x(2,3)-[CHD] (where X denotes any amino acid).


Pssm-ID: 259829 [Multi-domain]  Cd Length: 53  Bit Score: 60.02  E-value: 7.56e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530376195 158 CGGCGTEIKNGQALVALDKHWHLGCFKCKSCGKLL-NAEYISKDGLPYCEADY 209
Cdd:cd08368    1 CAGCGKPIEGRELLRALGKKWHPECFKCAECGKPLgGDSFYEKDGKPYCEKCY 53
LIM smart00132
Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM ...
157-208 3.35e-10

Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM domains bind protein partners via tyrosine-containing motifs. LIM domains are found in many key regulators of developmental pathways.


Pssm-ID: 214528 [Multi-domain]  Cd Length: 54  Bit Score: 55.47  E-value: 3.35e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 530376195   157 SCGGCGTEI-KNGQALVALDKHWHLGCFKCKSCGKLL-NAEYISKDGLPYCEAD 208
Cdd:smart00132   1 KCAGCGKPIyGTERVLRALGKVWHPECFKCATCGKPLsGDTFFEKDGKLYCKDC 54
LIM1_LIMK1 cd09462
The first LIM domain of LIMK1 (LIM domain Kinase 1); The first LIM domain of LIMK1 (LIM domain ...
152-209 1.09e-09

The first LIM domain of LIMK1 (LIM domain Kinase 1); The first LIM domain of LIMK1 (LIM domain Kinase 1): LIMK1 belongs to the LIMK protein family, which comprises LIMK1 and LIMK2. LIMK contains two LIM domains, a PDZ domain, and a kinase domain. LIMK is involved in the regulation of actin polymerization and microtubule disassembly. LIMK influences architecture of the actin cytoskeleton by regulating the activity of the cofilin family proteins cofilin1, cofilin2, and destrin. The mechanism of the activation is to phosphorylates cofilin on serine 3 and inactivates its actin-severing activity, and altering the rate of actin depolymerization. LIMKs can function in both cytoplasm and nucleus. Both LIMK1 and LIMK2 can act in the nucleus to suppress Rac/Cdc42-dependent cyclin D1 expression. LIMK1 is expressed in all tissues and is localized to focal adhesions in the cell. LIMK1 can form homodimers upon binding of HSP90 and is activated by Rho effector Rho kinase and MAPKAPK2. LIMK1 is important for normal central nervous system development, and its deletion has been implicated in the development of the human genetic disorder Williams syndrome. Moreover, LIMK1 up-regulates the promoter activity of urokinase type plasminogen activator and induces its mRNA and protein expression in breast cancer cells. The LIM domains have been shown to play an important role in regulating kinase activity and likely also contribute to LIMK function by acting as sites of protein-to-protein interactions. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188846 [Multi-domain]  Cd Length: 74  Bit Score: 54.89  E-value: 1.09e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530376195 152 SQGLRSCGGCGTEIKNGQALVALDKHWHLGCFKCKSCGKLLNAEYISKDGLPYCEADY 209
Cdd:cd09462   16 GNVLPVCASCGQSIYDGQYLQALNSDWHADCFRCCECGASLSHWYYEKDGRLFCKKDY 73
LIM1_LIMK cd09364
The first LIM domain of LIMK (LIM domain Kinase ); The first LIM domain of LIMK (LIM domain ...
158-209 1.33e-09

The first LIM domain of LIMK (LIM domain Kinase ); The first LIM domain of LIMK (LIM domain Kinase ): LIMK protein family is comprised of two members LIMK1 and LIMK2. LIMK contains two LIM domains, a PDZ domain and a kinase domain. LIMK is involved in the regulation of actin polymerization and microtubule disassembly. LIMK influences architecture of the actin cytoskeleton by regulating the activity of the cofilin family proteins cofilin1, cofilin2, and destrin. The mechanism of the activation is to phosphorylates cofilin on serine 3 and inactivates its actin-severing activity, and altering the rate of actin depolymerisation. LIMKs can function in both cytoplasm and nucleus and are expressed in all tissues. Both LIMK1 and LIMK2 can act in the nucleus to suppress Rac/Cdc42-dependent cyclin D1 expression. However, LIMK1 and LIMk2 have different cellular locations. While LIMK1 localizes mainly at focal adhesions, LIMK2 is found in cytoplasmic punctae, suggesting that they may have different cellular functions. The LIM domains of LIMK have been shown to play an important role in regulating kinase activity and likely also contribute to LIMK function by acting as sites of protein-to-protein interactions. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188750 [Multi-domain]  Cd Length: 53  Bit Score: 54.03  E-value: 1.33e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530376195 158 CGGCGTEIKNGQALVALDKHWHLGCFKCKSCGKLLNAEYISKDGLPYCEADY 209
Cdd:cd09364    1 CAGCRGKILDSQYVQALNQDWHCDCFRCSVCSDSLSNWYFEKDGKLYCRKDY 52
LIM cd08368
LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains ...
88-139 1.97e-09

LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains are identified in a diverse group of proteins with wide variety of biological functions, including gene expression regulation, cell fate determination, cytoskeleton organization, tumor formation and development. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes. They perform their functions through interactions with other protein partners. LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. The consensus sequence of LIM domain has been defined as C-x(2)-C-x(16,23)-H-x(2)-[CH]-x(2)-C-x(2)-C-x(16,21)-C-x(2,3)-[CHD] (where X denotes any amino acid).


Pssm-ID: 259829 [Multi-domain]  Cd Length: 53  Bit Score: 53.48  E-value: 1.97e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530376195  88 CFSCDQFIEG-EVVSALGKTYHPDCFVCAVCRLPFPPGDRVTFNGKeCMCQKC 139
Cdd:cd08368    1 CAGCGKPIEGrELLRALGKKWHPECFKCAECGKPLGGDSFYEKDGK-PYCEKC 52
LIM cd08368
LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains ...
29-80 3.62e-09

LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains are identified in a diverse group of proteins with wide variety of biological functions, including gene expression regulation, cell fate determination, cytoskeleton organization, tumor formation and development. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes. They perform their functions through interactions with other protein partners. LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. The consensus sequence of LIM domain has been defined as C-x(2)-C-x(16,23)-H-x(2)-[CH]-x(2)-C-x(2)-C-x(16,21)-C-x(2,3)-[CHD] (where X denotes any amino acid).


Pssm-ID: 259829 [Multi-domain]  Cd Length: 53  Bit Score: 52.71  E-value: 3.62e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530376195  29 CNTCGNVCKG-EVLRVQDKYFHIKCFVCKACGCDLAEGGFFVRQGEYICTLDY 80
Cdd:cd08368    1 CAGCGKPIEGrELLRALGKKWHPECFKCAECGKPLGGDSFYEKDGKPYCEKCY 53
LIM pfam00412
LIM domain; This family represents two copies of the LIM structural domain.
88-139 3.88e-09

LIM domain; This family represents two copies of the LIM structural domain.


Pssm-ID: 395333 [Multi-domain]  Cd Length: 57  Bit Score: 52.72  E-value: 3.88e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 530376195   88 CFSCDQFIEG-EVVSALGKTYHPDCFVCAVCRLPFPPGDRVTFNGKeCMCQKC 139
Cdd:pfam00412   1 CAGCNRPIYDrELVRALGKVWHPECFRCAVCGKPLTTGDFYEKDGK-LYCKHD 52
LIM3_Paxillin_like cd09338
The third LIM domain of the paxillin like protein family; The third LIM domain of the paxillin ...
158-210 8.98e-09

The third LIM domain of the paxillin like protein family; The third LIM domain of the paxillin like protein family: This family consists of paxillin, leupaxin, Hic-5 (ARA55), and other related proteins. There are four LIM domains in the C-terminal of the proteins and leucine-rich LD-motifs in the N-terminal region. Members of this family are adaptor proteins to recruit key components of signal-transduction machinery to specific sub-cellular locations. Paxillin is found at the interface between the plasma membrane and the actin cytoskeleton. Paxillin serves as a platform for the recruitment of numerous regulatory and structural proteins that together control the dynamic changes in cell adhesion, cytoskeletal reorganization and gene expression that are necessary for cell migration and survival. Leupaxin is a cytoskeleton adaptor protein, which is preferentially expressed in hematopoietic cells. It associates with focal adhesion kinases PYK2 and pp125FAK and identified to be a component of the osteoclast pososomal signaling complex. Hic-5 controls cell proliferation, migration and senescence by functioning as coactivator for steroid receptors such as androgen receptor, glucocorticoid receptor and progesterone receptor. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188724 [Multi-domain]  Cd Length: 53  Bit Score: 51.57  E-value: 8.98e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530376195 158 CGGCGTEIKnGQALVALDKHWHLGCFKCKSCGK-LLNAEYISKDGLPYCEADYH 210
Cdd:cd09338    1 CGGCNKPIL-ENYISALNTQWHPECFVCRECHKpFINGSFFEHEGLPYCETHYH 53
LIM2_abLIM cd09328
The second LIM domain on actin binding LIM (abLIM) proteins; The second LIM domain of actin ...
214-263 9.50e-09

The second LIM domain on actin binding LIM (abLIM) proteins; The second LIM domain of actin binding LIM (abLIM) proteins: Three homologous members of the abLIM protein family have been identified; abLIM-1, abLIM-2 and abLIM-3. The N-terminal of abLIM consists of four tandem repeats of LIM domains and the C-terminal of acting binding LIM protein is a villin headpiece domain, which has strong actin binding activity. The abLIM-1, which is expressed in retina, brain, and muscle tissue, has been indicated to function as a tumor suppressor. AbLIM-2 and -3, mainly expressed in muscle and neuronal tissue, bind to F-actin strongly. They may serve as a scaffold for signaling modules of the actin cytoskeleton and thereby modulate transcription. It has shown that LIM domains of abLIMs interact with STARS (striated muscle activator of Rho signaling), which directly binds actin and stimulates serum-response factor (SRF)-dependent transcription. All LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188714  Cd Length: 56  Bit Score: 51.58  E-value: 9.50e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 530376195 214 GIRCDSCEKYITGRVLEAGEKHYHPSCALCVRCGQMFAEGEEMYLQGSSI 263
Cdd:cd09328    1 GTKCDSCQDFVEGEVVSALGKTYHPKCFVCSVCRQPFPPGDRVTFNGKEC 50
LIM pfam00412
LIM domain; This family represents two copies of the LIM structural domain.
29-84 2.17e-08

LIM domain; This family represents two copies of the LIM structural domain.


Pssm-ID: 395333 [Multi-domain]  Cd Length: 57  Bit Score: 50.41  E-value: 2.17e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 530376195   29 CNTCGN-VCKGEVLRVQDKYFHIKCFVCKACGCDLAEGGFFVRQGEYICTLDYQRLY 84
Cdd:pfam00412   1 CAGCNRpIYDRELVRALGKVWHPECFRCAVCGKPLTTGDFYEKDGKLYCKHDYYKLF 57
LIM3_Paxillin_like cd09338
The third LIM domain of the paxillin like protein family; The third LIM domain of the paxillin ...
88-125 2.34e-08

The third LIM domain of the paxillin like protein family; The third LIM domain of the paxillin like protein family: This family consists of paxillin, leupaxin, Hic-5 (ARA55), and other related proteins. There are four LIM domains in the C-terminal of the proteins and leucine-rich LD-motifs in the N-terminal region. Members of this family are adaptor proteins to recruit key components of signal-transduction machinery to specific sub-cellular locations. Paxillin is found at the interface between the plasma membrane and the actin cytoskeleton. Paxillin serves as a platform for the recruitment of numerous regulatory and structural proteins that together control the dynamic changes in cell adhesion, cytoskeletal reorganization and gene expression that are necessary for cell migration and survival. Leupaxin is a cytoskeleton adaptor protein, which is preferentially expressed in hematopoietic cells. It associates with focal adhesion kinases PYK2 and pp125FAK and identified to be a component of the osteoclast pososomal signaling complex. Hic-5 controls cell proliferation, migration and senescence by functioning as coactivator for steroid receptors such as androgen receptor, glucocorticoid receptor and progesterone receptor. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188724 [Multi-domain]  Cd Length: 53  Bit Score: 50.41  E-value: 2.34e-08
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 530376195  88 CFSCDQFIEGEVVSALGKTYHPDCFVCAVCRLPFPPGD 125
Cdd:cd09338    1 CGGCNKPILENYISALNTQWHPECFVCRECHKPFINGS 38
LIM_DA1 cd09396
The Lim domain of DA1; The Lim domain of DA1: DA1 contains one copy of LIM domain and a domain ...
158-204 2.53e-08

The Lim domain of DA1; The Lim domain of DA1: DA1 contains one copy of LIM domain and a domain of unknown function. DA1 is predicted as an ubiquitin receptor, which sets final seed and organ size by restricting the period of cell proliferation. The LIM domain is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188782 [Multi-domain]  Cd Length: 53  Bit Score: 50.33  E-value: 2.53e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 530376195 158 CGGCGTEIKNGQALVALDKHWHLGCFKCKSCGK-LLNAEYISKDGLPY 204
Cdd:cd09396    1 CAGCKSEIGHGRFLSALGAVWHPECFRCHACRKpIAEHEFSVSGNDPY 48
LIM1_LIMK2 cd09463
The first LIM domain of LIMK2 (LIM domain Kinase 2); The first LIM domain of LIMK2 (LIM domain ...
158-209 7.01e-08

The first LIM domain of LIMK2 (LIM domain Kinase 2); The first LIM domain of LIMK2 (LIM domain Kinase 2): LIMK2 is a member of the LIMK protein family, which comprises LIMK1 and LIMK2. LIMK contains two LIM domains, a PDZ domain, and a kinase domain. LIMK is involved in the regulation of actin polymerization and microtubule disassembly. LIMK influences architecture of the actin cytoskeleton by regulating the activity of the cofilin family proteins cofilin1, cofilin2, and destrin. The mechanism of the activation is to phosphorylates cofilin on serine 3 and inactivates its actin-severing activity, altering the rate of actin depolymerization. LIMK activity is activated by phosphorylation of a threonine residue within the activation loop of the kinase by p21-activated kinases 1 and 4 and by Rho kinase. LIMKs can function in both cytoplasm and nucleus. Both LIMK1 and LIMK2 can act in the nucleus to suppress Rac/Cdc42-dependent cyclin D1 expression. LIMK2 is expressed in all tissues. While LIMK1 localizes mainly at focal adhesions, LIMK2 is found in cytoplasmic punctae, suggesting that they may have different cellular functions. The activity of LIM kinase 2 to regulate cofilin phosphorylation is inhibited by the direct binding of Par-3. LIMK2 activation promotes cell cycle progression. The phenotype of Limk2 knockout mice shows a defect in spermatogenesis. The LIM domains have been shown to play an important role in regulating kinase activity and likely also contribute to LIMK function by acting as sites of protein-to-protein interactions. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188847 [Multi-domain]  Cd Length: 53  Bit Score: 49.10  E-value: 7.01e-08
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gi 530376195 158 CGGCGTEIKNGQALVALDKHWHLGCFKCKSCGKLLNAEYISKDGLPYCEADY 209
Cdd:cd09463    1 CTGCGGRIQDSFHYRVVQEAWHNSCFQCSVCQDLLTNWYYEKDGKLYCHKHY 52
LIM1_Paxillin_like cd09336
The first LIM domain of the paxillin like protein family; The first LIM domain of the paxillin ...
158-210 7.25e-08

The first LIM domain of the paxillin like protein family; The first LIM domain of the paxillin like protein family: This family consists of paxillin, leupaxin, Hic-5 (ARA55), and other related proteins. There are four LIM domains in the C-terminal of the proteins and leucine-rich LD-motifs in the N-terminal region. Members of this family are adaptor proteins to recruit key components of signal-transduction machinery to specific sub-cellular locations. Paxillin is found at the interface between the plasma membrane and the actin cytoskeleton. Paxillin serves as a platform for the recruitment of numerous regulatory and structural proteins that together control the dynamic changes in cell adhesion, cytoskeletal reorganization and gene expression that are necessary for cell migration and survival. Leupaxin is a cytoskeleton adaptor protein, which is preferentially expressed in hematopoietic cells. It associates with focal adhesion kinases PYK2 and pp125FAK and identified to be a component of the osteoclast pososomal signaling complex. Hic-5 controls cell proliferation, migration and senescence by functioning as coactivator for steroid receptors such as androgen receptor, glucocorticoid receptor and progesterone receptor. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 259830 [Multi-domain]  Cd Length: 53  Bit Score: 48.92  E-value: 7.25e-08
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gi 530376195 158 CGGCGTEIKnGQALVALDKHWHLGCFKCKSCGKLLNAE-YISKDGLPYCEADYH 210
Cdd:cd09336    1 CAACNKPIV-GQVVTALGKTWHPEHFVCVHCQTELGTSnFFERDGKPYCEKDYH 53
LIM_ALP cd09450
This family represents the LIM domain of ALP, actinin-associated LIM protein; This family ...
29-76 9.01e-08

This family represents the LIM domain of ALP, actinin-associated LIM protein; This family represents the LIM domain of ALP, actinin-associated LIM protein. ALP contains an N-terminal PDZ domain, a C-terminal LIM domain and an ALP-subfamily-specific 34-amino-acid motif termed ALP-like motif (AM), which contains a putative consensus protein kinase C (PKC) phosphorylation site and two alpha-helices. ALP proteins are found in heart and in skeletal muscle. ALP may act as a signaling molecule which is regulated by PKC-dependent signaling. ALP plays an essential role in the development of RV (right ventricle) chamber. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188834 [Multi-domain]  Cd Length: 53  Bit Score: 48.75  E-value: 9.01e-08
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                 ....*....|....*....|....*....|....*....|....*...
gi 530376195  29 CNTCGNVCKGEVLRVQDKYFHIKCFVCKACGCDLAEGGFFVRQGEYIC 76
Cdd:cd09450    1 CDKCGSGIVGTVVKARDKYRHPECFVCSDCNLNLKQKGYFFVEGQLYC 48
LIM1_Paxillin_like cd09336
The first LIM domain of the paxillin like protein family; The first LIM domain of the paxillin ...
88-118 1.05e-07

The first LIM domain of the paxillin like protein family; The first LIM domain of the paxillin like protein family: This family consists of paxillin, leupaxin, Hic-5 (ARA55), and other related proteins. There are four LIM domains in the C-terminal of the proteins and leucine-rich LD-motifs in the N-terminal region. Members of this family are adaptor proteins to recruit key components of signal-transduction machinery to specific sub-cellular locations. Paxillin is found at the interface between the plasma membrane and the actin cytoskeleton. Paxillin serves as a platform for the recruitment of numerous regulatory and structural proteins that together control the dynamic changes in cell adhesion, cytoskeletal reorganization and gene expression that are necessary for cell migration and survival. Leupaxin is a cytoskeleton adaptor protein, which is preferentially expressed in hematopoietic cells. It associates with focal adhesion kinases PYK2 and pp125FAK and identified to be a component of the osteoclast pososomal signaling complex. Hic-5 controls cell proliferation, migration and senescence by functioning as coactivator for steroid receptors such as androgen receptor, glucocorticoid receptor and progesterone receptor. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 259830 [Multi-domain]  Cd Length: 53  Bit Score: 48.54  E-value: 1.05e-07
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gi 530376195  88 CFSCDQFIEGEVVSALGKTYHPDCFVCAVCR 118
Cdd:cd09336    1 CAACNKPIVGQVVTALGKTWHPEHFVCVHCQ 31
LIM_LASP cd09447
The LIM domain of LIM and SH3 Protein (LASP); The LIM domain of LIM and SH3 Protein (LASP): ...
158-209 1.10e-07

The LIM domain of LIM and SH3 Protein (LASP); The LIM domain of LIM and SH3 Protein (LASP): LASP family contains two highly homologous members, LASP-1 and LASP-2. LASP contains a LIM motif at its amino terminus, a src homology 3 (SH3) domains at its C-terminal part, and a nebulin-like region in the middle. LASP-1 and -2 are highly conserved in their LIM, nebulin-like, and SH3 domains ,but differ significantly at their linker regions. Both proteins are ubiquitously expressed and involved in cytoskeletal architecture, especially in the organization of focal adhesions. LASP-1 and LASP-2, are important during early embryo- and fetogenesis and are highly expressed in the central nervous system of the adult. However, only LASP-1 seems to participate significantly in neuronal differentiation and plays an important functional role in migration and proliferation of certain cancer cells while the role of LASP-2 is more structural. The expression of LASP-1 in breast tumors is increased significantly. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188831  Cd Length: 53  Bit Score: 48.53  E-value: 1.10e-07
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gi 530376195 158 CGGCGTEIKNGQALVALDKHWHLGCFKCKSCGKLLNAE-YISKDGLPYCEADY 209
Cdd:cd09447    1 CARCGKTVYPTEKLNCLDKIWHKGCFKCEVCGMTLNMKnYKGYNKKPYCNAHY 53
LIM1_Lhx2_Lhx9 cd09369
The first LIM domain of Lhx2 and Lhx9 family; The first LIM domain of Lhx2 and Lhx9 family: ...
158-209 2.09e-07

The first LIM domain of Lhx2 and Lhx9 family; The first LIM domain of Lhx2 and Lhx9 family: Lhx2 and Lhx9 are highly homologous LHX regulatory proteins. They belong to the LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. Although Lhx2 and Lhx9 are highly homologous, they seems to play regulatory roles in different organs. In animals, Lhx2 plays important roles in eye, cerebral cortex, limb, the olfactory organs, and erythrocyte development. Lhx2 gene knockout mice exhibit impaired patterning of the cortical hem and the telencephalon of the developing brain, and a lack of development in olfactory structures. Lhx9 is expressed in several regions of the developing mouse brain , the spinal cord, the pancreas, in limb mesenchyme, and in the urogenital region. Lhx9 plays critical roles in gonad development. Homozygous mice lacking functional Lhx9 alleles exhibit numerous urogenital defects, such as gonadal agenesis, infertility, and undetectable levels of testosterone and estradiol coupled with high FSH levels. Lhx9 null mice are phenotypically female, even those that are genotypically male. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188755 [Multi-domain]  Cd Length: 54  Bit Score: 47.72  E-value: 2.09e-07
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gi 530376195 158 CGGCGTEIKNGQALVALDKHWHLGCFKCKSCGKLLNAEY--ISKDGLPYCEADY 209
Cdd:cd09369    1 CAGCGEKIQDRFYLLAVDRQWHASCLKCCECRLPLDSELscFSRDGNIYCKEDY 54
LIM1_Lrg1p_like cd09391
The first LIM domain of Lrg1p, a LIM and RhoGap domain containing protein; The first LIM ...
158-209 2.33e-07

The first LIM domain of Lrg1p, a LIM and RhoGap domain containing protein; The first LIM domain of Lrg1p, a LIM and RhoGap domain containing protein: The members of this family contain three tandem repeats of LIM domains and a Rho-type GTPase activating protein (RhoGap) domain. Lrg1p is a Rho1 GTPase-activating protein required for efficient cell fusion in yeast. Lrg1p-GAP domain strongly and specifically stimulates the GTPase activity of Rho1p, a regulator of beta (1-3)-glucan synthase in vitro. The LIM domain is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188777  Cd Length: 57  Bit Score: 47.68  E-value: 2.33e-07
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gi 530376195 158 CGGCGTEIkNGQALVALDKHWHLGCFKCKSCGKLLNAEYISKDG------LPYCEADY 209
Cdd:cd09391    1 CAKCGKPI-TGQFVRALGDVYHLDCFTCHDCGKPVASKFFPVDDpdtseqVPLCETDY 57
LIM4_PINCH cd09334
The fourth LIM domain of protein PINCH; The fourth LIM domain of protein PINCH: PINCH plays a ...
88-121 2.44e-07

The fourth LIM domain of protein PINCH; The fourth LIM domain of protein PINCH: PINCH plays a pivotal role in the assembly of focal adhesions (FAs), regulating diverse functions in cell adhesion, growth, and differentiation through LIM-mediated protein-protein interactions. PINCH comprises an array of five LIM domains that interact with integrin-linked kinase (ILK), Nck2 (also called Nckbeta or Grb4) and other interaction partners. These interactions are essential for triggering the FA assembly and for relaying diverse mechanical and biochemical signals between Cell-extracellular matrix and the actin cytoskeleton. The PINCH LIM4 domain recognizes the third SH3 domain of another adaptor protein, Nck2. This step is an important component of integrin signaling event. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assem bly of multimeric protein complexes.


Pssm-ID: 188720 [Multi-domain]  Cd Length: 54  Bit Score: 47.35  E-value: 2.44e-07
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gi 530376195  88 CFSCDQFIEGEVVSALGKTYHPDCFVCAVCRLPF 121
Cdd:cd09334    3 CGACRRPIEGRVVTALGKHWHVEHFVCAKCEKPF 36
LIM4_PINCH cd09334
The fourth LIM domain of protein PINCH; The fourth LIM domain of protein PINCH: PINCH plays a ...
158-209 4.75e-07

The fourth LIM domain of protein PINCH; The fourth LIM domain of protein PINCH: PINCH plays a pivotal role in the assembly of focal adhesions (FAs), regulating diverse functions in cell adhesion, growth, and differentiation through LIM-mediated protein-protein interactions. PINCH comprises an array of five LIM domains that interact with integrin-linked kinase (ILK), Nck2 (also called Nckbeta or Grb4) and other interaction partners. These interactions are essential for triggering the FA assembly and for relaying diverse mechanical and biochemical signals between Cell-extracellular matrix and the actin cytoskeleton. The PINCH LIM4 domain recognizes the third SH3 domain of another adaptor protein, Nck2. This step is an important component of integrin signaling event. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assem bly of multimeric protein complexes.


Pssm-ID: 188720 [Multi-domain]  Cd Length: 54  Bit Score: 46.58  E-value: 4.75e-07
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gi 530376195 158 CGGCGTEIkNGQALVALDKHWHLGCFKCKSCGK-LLNAEYISKDGLPYCEADY 209
Cdd:cd09334    3 CGACRRPI-EGRVVTALGKHWHVEHFVCAKCEKpFLGHRHYEKKGLAYCETHY 54
LIM1_LIMPETin cd09414
The first LIM domain of protein LIMPETin; The first LIM domain of protein LIMPETin: LIMPETin ...
158-209 5.25e-07

The first LIM domain of protein LIMPETin; The first LIM domain of protein LIMPETin: LIMPETin contains 6 LIM domains at the C-terminal and an N-terminal PET domain. Four of the six LIM domains are highly homologous to the four and half LIM domain protein family and two of them show sequence similarity to the LIM domains of the Testin family. Thus, LIMPETin may be the recombinant product of genes coding testin and FHL proteins. In Schistosoma mansoni, where LIMPETin was first identified, LIMPETin is down regulated in sexually mature adult Schistosoma females compared to sexually immature adult females and adult male. Its differential expression indicates that it is a transcription regulator. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188798 [Multi-domain]  Cd Length: 58  Bit Score: 46.62  E-value: 5.25e-07
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gi 530376195 158 CGGCGTEIKNGQALVALDKH-----WHLGCFKCKSCGKLL-NAEYISKDGLPYCEADY 209
Cdd:cd09414    1 CGGCSEPLKYGELAVTAPKFgesllWHPACFRCSTCEELLvDLTYCVHDDQIYCERHY 58
LIM smart00132
Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM ...
87-139 6.97e-07

Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM domains bind protein partners via tyrosine-containing motifs. LIM domains are found in many key regulators of developmental pathways.


Pssm-ID: 214528 [Multi-domain]  Cd Length: 54  Bit Score: 46.22  E-value: 6.97e-07
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                   ....*....|....*....|....*....|....*....|....*....|....*
gi 530376195    87 RCFSCDQFIEG--EVVSALGKTYHPDCFVCAVCRLPFpPGDRVTFNGKECMCQKC 139
Cdd:smart00132   1 KCAGCGKPIYGteRVLRALGKVWHPECFKCATCGKPL-SGDTFFEKDGKLYCKDC 54
LIM_TLP_like cd09401
The LIM domains of thymus LIM protein (TLP); The LIM domain of thymus LIM protein (TLP) like ...
158-205 7.22e-07

The LIM domains of thymus LIM protein (TLP); The LIM domain of thymus LIM protein (TLP) like proteins: This family includes the LIM domains of TLP and CRIP (Cysteine-Rich Intestinal Protein). TLP is the distant member of the CRP family of proteins. TLP has two isomers (TLP-A and TLP-B) and sharing approximately 30% with each of the three other CRPs. Like CRP1, CRP2 and CRP3/MLP, TLP has two LIM domains, connected by a flexible linker region. Unlike the CRPs, TLP lacks the nuclear targeting signal (K/R-K/R-Y-G-P-K) and is localized solely in the cytoplasm. TLP is specifically expressed in the thymus in a subset of cortical epithelial cells. TLP has a role in development of normal thymus and in controlling the development and differentiation of thymic epithelial cells. CRIP is a short LIM protein with only one LIM domain. CRIP gene is developmentally regulated and can be induced by glucocorticoid hormones during the first three postnatal weeks. The domain shows close sequence homology to LIM domain of thymus LIM protein. However, unlike the TLP proteins which have two LIM domains, the members of this family have only one LIM domain. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188785 [Multi-domain]  Cd Length: 53  Bit Score: 46.18  E-value: 7.22e-07
                         10        20        30        40
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gi 530376195 158 CGGCGTEIKNGQALVALDKHWHLGCFKCKSCGKLLNA-EYISKDGLPYC 205
Cdd:cd09401    1 CPKCGKPVYFAEKKTSLGRDWHKPCLRCEKCKKTLTPgQHSEHEGKPYC 49
LIM2_Paxillin_like cd09337
The second LIM domain of the paxillin like protein family; The second LIM domain of the ...
158-209 7.66e-07

The second LIM domain of the paxillin like protein family; The second LIM domain of the paxillin like protein family: This family consists of paxillin, leupaxin, Hic-5 (ARA55), and other related proteins. There are four LIM domains in the C-terminal of the proteins and leucine-rich LD-motifs in the N-terminal region. Members of this family are adaptor proteins to recruit key components of signal-transduction machinery to specific sub-cellular locations. Paxillin is found at the interface between the plasma membrane and the actin cytoskeleton. Paxillin serves as a platform for the recruitment of numerous regulatory and structural proteins that together control the dynamic changes in cell adhesion, cytoskeletal reorganization and gene expression that are necessary for cell migration and survival. Leupaxin is a cytoskeleton adaptor protein, which is preferentially expressed in hematopoietic cells. It associates with focal adhesion kinases PYK2 and pp125FAK and identified to be a component of the osteoclast pososomal signaling complex. Hic-5 controls cell proliferation, migration and senescence by functioning as coactivator for steroid receptors such as androgen receptor, glucocorticoid receptor and progesterone receptor. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188723 [Multi-domain]  Cd Length: 52  Bit Score: 45.84  E-value: 7.66e-07
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                 ....*....|....*....|....*....|....*....|....*....|...
gi 530376195 158 CGGCGTEIKnGQALVALDKHWHLGCFKCKSCGKLLNAE-YISKDGLPYCEADY 209
Cdd:cd09337    1 CAYCNGPIL-DKCVTALDKTWHPEHFFCAQCGKPFGDEgFHEKDGKPYCREDY 52
LIM1_Leupaxin cd09406
The first LIM domain of Leupaxin; The first LIM domain of Leupaxin: Leupaxin is a cytoskeleton ...
158-210 8.63e-07

The first LIM domain of Leupaxin; The first LIM domain of Leupaxin: Leupaxin is a cytoskeleton adaptor protein, which is preferentially expressed in hematopoietic cells. Leupaxin belongs to the paxillin focal adhesion protein family. Same as other members of the family, it has four leucine-rich LD-motifs in the N-terminus and four LIM domains in the C-terminus. It may function in cell type-specific signaling by associating with interaction partners PYK2, FAK, PEP and p95PKL. When expressed in human leukocytic cells, leupaxin significantly suppressed integrin-mediated cell adhesion to fibronectin and the tyrosine phosphorylation of paxillin. These findings indicate that leupaxin may negatively regulate the functions of paxillin during integrin signaling. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188790 [Multi-domain]  Cd Length: 55  Bit Score: 46.02  E-value: 8.63e-07
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                 ....*....|....*....|....*....|....*....|....*....|....
gi 530376195 158 CGGCGTEIKnGQALVALDKHWHLGCFKCKSCGKLLNAE-YISKDGLPYCEADYH 210
Cdd:cd09406    3 CASCQKPIA-GQVVTALGQTWHPEHFVCCQCGKELGSRpFFERNGQAYCEEDYH 55
LIM2_Paxillin_like cd09337
The second LIM domain of the paxillin like protein family; The second LIM domain of the ...
88-121 1.05e-06

The second LIM domain of the paxillin like protein family; The second LIM domain of the paxillin like protein family: This family consists of paxillin, leupaxin, Hic-5 (ARA55), and other related proteins. There are four LIM domains in the C-terminal of the proteins and leucine-rich LD-motifs in the N-terminal region. Members of this family are adaptor proteins to recruit key components of signal-transduction machinery to specific sub-cellular locations. Paxillin is found at the interface between the plasma membrane and the actin cytoskeleton. Paxillin serves as a platform for the recruitment of numerous regulatory and structural proteins that together control the dynamic changes in cell adhesion, cytoskeletal reorganization and gene expression that are necessary for cell migration and survival. Leupaxin is a cytoskeleton adaptor protein, which is preferentially expressed in hematopoietic cells. It associates with focal adhesion kinases PYK2 and pp125FAK and identified to be a component of the osteoclast pososomal signaling complex. Hic-5 controls cell proliferation, migration and senescence by functioning as coactivator for steroid receptors such as androgen receptor, glucocorticoid receptor and progesterone receptor. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188723 [Multi-domain]  Cd Length: 52  Bit Score: 45.46  E-value: 1.05e-06
                         10        20        30
                 ....*....|....*....|....*....|....
gi 530376195  88 CFSCDQFIEGEVVSALGKTYHPDCFVCAVCRLPF 121
Cdd:cd09337    1 CAYCNGPILDKCVTALDKTWHPEHFFCAQCGKPF 34
LIM2_ENH cd09457
The second LIM domain of the Enigma Homolog (ENH) family; The second LIM domain of the Enigma ...
158-209 1.27e-06

The second LIM domain of the Enigma Homolog (ENH) family; The second LIM domain of the Enigma Homolog (ENH) family: ENH was initially identified in rat brain. Same as enigma, it contains three LIM domains at the C-terminus and a PDZ domain at N-terminus. ENH is implicated in signal transduction processes involving protein kinases. It has also been shown that ENH interacts with protein kinase D1 (PKD1) via its LIM domains and forms a complex with PKD1 and the alpha1C subunit of cardiac L-type voltage-gated calcium channel in rat neonatal cardiomyocytes. The N-terminal PDZ domain interacts with alpha-actinin at the Z-line. ENH is expressed in multiple tissues, such as skeletal muscle, heart, bone, and brain. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188841 [Multi-domain]  Cd Length: 52  Bit Score: 45.40  E-value: 1.27e-06
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                 ....*....|....*....|....*....|....*....|....*....|...
gi 530376195 158 CGGCGTEIKnGQALVALDKHWHLGCFKCKSCGK-LLNAEYISKDGLPYCEADY 209
Cdd:cd09457    1 CGRCQRKIL-GEVINALKQTWHVSCFVCVACHNpIRNNVFHLEDGEPYCETDY 52
LIM1_Lhx2 cd09469
The first LIM domain of Lhx2; The first LIM domain of Lhx2: Lhx2 belongs to the LHX protein ...
158-209 1.35e-06

The first LIM domain of Lhx2; The first LIM domain of Lhx2: Lhx2 belongs to the LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. In animals, Lhx2 plays important roles in eye, cerebral cortex, limb, the olfactory organs, and erythrocyte development. Lhx2 gene knockout mice exhibit impaired patterning of the cortical hem and the telencephalon of the developing brain, and a lack of development in olfactory structures. The Lhx2 protein has been shown to bind to the mouse M71 olfactory receptor promoter. Similar to other LIM domains, this domain family is 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188853  Cd Length: 64  Bit Score: 45.77  E-value: 1.35e-06
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                 ....*....|....*....|....*....|....*....|....*....|....
gi 530376195 158 CGGCGTEIKNGQALVALDKHWHLGCFKCKSCGKLLNAEY--ISKDGLPYCEADY 209
Cdd:cd09469   11 CAGCGGKISDRYYLLAVDKQWHMRCLKCCECKLNLESELtcFSKDGSIYCKEDY 64
LIM1_LMO4 cd09386
The first LIM domain of LMO4 (LIM domain only protein 4); The first LIM domain of LMO4 (LIM ...
158-209 2.23e-06

The first LIM domain of LMO4 (LIM domain only protein 4); The first LIM domain of LMO4 (LIM domain only protein 4): LMO4 is a nuclear protein that plays important roles in transcriptional regulation and development. LMO4 is involved in various functions in tumorigenesis and cellular differentiation. LMO4 proteins regulate gene expression by interacting with a wide variety of transcription factors and cofactors to form large transcription complexes. It can interact with Smad proteins, and associate with the promoter of the PAI-1 (plasminogen activator inhibitor-1) gene in a TGFbeta (transforming growth factor beta)-dependent manner. LMO4 can also form a complex with transcription regulator CREB (cAMP response element-binding protein) and interact with CLIM1 and CLIM2. In breast tissue, LMO4 interacts with multiple proteins, including the cofactor CtIP [CtBP (C-terminal binding protein)-interacting protein], the breast and ovarian tumor suppressor BRCA1 (breast-cancer susceptibility gene 1) and the LIM-domain-binding protein LDB1. Functionally, LMO4 is shown to repress BRCA1-mediated transcription activation, thus invoking a potential role for LMO4 as a negative regulator of BRCA1 in sporadic breast cancer. LMO4 also forms complex to both ERa (oestrogen receptor alpha), MTA1 (metastasis tumor antigen 1), and HDACs (histone deacetylases), implying that LMO4 is also a component of the MTA1 corepressor complex. Over-expressed LMO4 represses ERa transactivation functions in an HDAC-dependent manner, and contributes to the process of breast cancer progression by allowing the development of Era-negative phenotypes. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188772 [Multi-domain]  Cd Length: 55  Bit Score: 44.72  E-value: 2.23e-06
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gi 530376195 158 CGGCGTEIKNGQALVALDKHWHLGCFKCKSCGKLL---NAEYISKDGLPYCEADY 209
Cdd:cd09386    1 CAGCGGKIVDRFLLHALDRYWHNGCLKCSCCQAQLgeiGSSCYTKGGMILCKNDY 55
LIM1_Lhx3_Lhx4 cd09368
The first LIM domain of Lhx3 and Lhx4 family; The first LIM domain of Lhx3-Lhx4 family: Lhx3 ...
158-209 2.68e-06

The first LIM domain of Lhx3 and Lhx4 family; The first LIM domain of Lhx3-Lhx4 family: Lhx3 and Lhx4 belong to the LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. The LHX3 and LHX4 LIM-homeodomain transcription factors play essential roles in pituitary gland and nervous system development. Although LHX3 and LHX4 share marked sequence homology, the genes have different expression patterns. They play overlapping, but distinct functions during the establishment of the specialized cells of the mammalian pituitary gland and the nervous system. Lhx3 proteins have been demonstrated the ability to directly bind to the promoters/enhancers of several pituitary hormone gene promoters to cause increased transcription. Lhx3a and Lhx3b, whose mRNAs have distinct temporal expression profiles during development, are two isoforms of Lhx3. LHX4 plays essential roles in pituitary gland and nervous system development. In mice, the lhx4 gene is expressed in the developing hindbrain, cerebral cortex, pituitary gland, and spinal cord. LHX4 shows significant sequence similarity to LHX3, particularly to isoforms Lhx3a. In gene regulation experiments, the LHX4 protein exhibits regulation roles towards pituitary genes, acting on their promoters/enhancers. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188754  Cd Length: 52  Bit Score: 44.33  E-value: 2.68e-06
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gi 530376195 158 CGGCGTEIKNGQALVALDKHWHLGCFKCKSCGKLLNAEYISKDGLPYCEADY 209
Cdd:cd09368    1 CGGCQEHILDRFILKVLDRTWHAKCLKCNDCGAQLTDKCFARNGHVYCKDDF 52
LIM1_Lhx4 cd09468
The first LIM domain of Lhx4; The first LIM domain of Lhx4. Lhx4 belongs to the LHX protein ...
158-209 2.79e-06

The first LIM domain of Lhx4; The first LIM domain of Lhx4. Lhx4 belongs to the LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. LHX4 plays essential roles in pituitary gland and nervous system development. In mice, the lhx4 gene is expressed in the developing hindbrain, cerebral cortex, pituitary gland, and spinal cord. LHX4 shows significant sequence similarity to LHX3, particularly to isoforms Lhx3a. In gene regulation experiments, the LHX4 protein exhibits regulation roles towards pituitary genes, acting on their promoters/enhancers. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188852  Cd Length: 52  Bit Score: 44.58  E-value: 2.79e-06
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gi 530376195 158 CGGCGTEIKNGQALVALDKHWHLGCFKCKSCGKLLNAEYISKDGLPYCEADY 209
Cdd:cd09468    1 CAGCNQHILDKFILKVLDRHWHSSCLKCADCQMQLAERCFSRAGNVYCKEDF 52
LIM1_Lhx9 cd09470
The first LIM domain of Lhx9; The first LIM domain of Lhx9: Lhx9 belongs to the LHX protein ...
158-209 2.85e-06

The first LIM domain of Lhx9; The first LIM domain of Lhx9: Lhx9 belongs to the LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. Lhx9 is highly homologous to Lhx2. It is expressed in several regions of the developing mouse brain, the spinal cord, the pancreas, in limb mesenchyme, and in the urogenital region. Lhx9 plays critical roles in gonad development. Homozygous mice lacking functional Lhx9 alleles exhibit numerous urogenital defects, such as gonadal agenesis, infertility, and undetectable levels of testosterone and estradiol coupled with high FSH levels. Lhx9 null mice have reduced levels of the Sf1 nuclear receptor that is required for gonadogenesis, and recent studies have shown that Lhx9 is able to activate the Sf1/FtzF1 gene. Lhx9 null mice are phenotypically female, even those that are genotypically male. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188854  Cd Length: 54  Bit Score: 44.66  E-value: 2.85e-06
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gi 530376195 158 CGGCGTEIKNGQALVALDKHWHLGCFKCKSCGKLLNAEY--ISKDGLPYCEADY 209
Cdd:cd09470    1 CAGCGGKISDRYYLLAVDKQWHLRCLKCCECKLALESELtcFAKDGSIYCKEDY 54
LIM_ALP_like cd09360
The LIM domain of ALP (actinin-associated LIM protein) family; This family represents the LIM ...
29-76 2.91e-06

The LIM domain of ALP (actinin-associated LIM protein) family; This family represents the LIM domain of ALP (actinin-associated LIM protein) family. Four proteins: ALP, CLP36, RIL, and Mystique have been classified into the ALP subfamily of LIM domain proteins. Each member of the subfamily contains an N-terminal PDZ domain and a C-terminal LIM domain. Functionally, these proteins bind to alpha-actinin through their PDZ domains and bind or other signaling molecules through their LIM domains. ALP proteins have been implicated in cardiac and skeletal muscle structure, function and disease, platelet, and epithelial cell motility. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188746 [Multi-domain]  Cd Length: 52  Bit Score: 44.29  E-value: 2.91e-06
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gi 530376195  29 CNTCGNVCKGEVLRVQDKYFHIKCFVCKACGCDLAEGGFFVRQGEYIC 76
Cdd:cd09360    1 CDKCGNGIVGVVVKARDKNRHPECFVCADCGLNLKNKGYFFIEDELYC 48
LIM2_Enigma_like cd09362
The second LIM domain of Enigma-like family; The second LIM domain of Enigma-like family: The ...
158-209 3.30e-06

The second LIM domain of Enigma-like family; The second LIM domain of Enigma-like family: The Enigma LIM domain family is comprised of three members: Enigma, ENH, and Cypher (mouse)/ZASP (human). These subfamily members contain a single PDZ domain at the N-terminus and three LIM domains at the C-terminus. Enigma was initially characterized in humans and is expressed in multiple tissues, such as skeletal muscle, heart, bone and brain. The third LIM domain specifically interacts with the insulin receptor and the second LIM domain interacts with the receptor tyrosine kinase Ret and the adaptor protein APS. Thus Enigma is implicated in signal transduction processes, such as mitogenic activity, insulin related actin organization, and glucose metabolism. The second member, ENH protein, was first identified in rat brain. It has been shown that ENH interacts with protein kinase D1 (PKD1) via its LIM domains and forms a complex with PKD1 and the alpha1C subunit of cardiac L-type voltage-gated calcium channel in rat neonatal cardiomyocytes. The N-terminal PDZ domain interacts with alpha-actinin at the Z-line. ZASP/Cypher is required for maintenance of Z-line structure during muscle contraction, but not required for Z-line assembly. In heart, Cypher/ZASP plays a structural role through its interaction with cytoskeletal Z-line proteins. In addition, there is increasing evidence that Cypher/ZASP also performs signaling functions. Studies reveal that Cypher/ZASP interacts with and directs PKC to the Z-line, where PKC phosphorylates downstream signaling targets. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188748 [Multi-domain]  Cd Length: 52  Bit Score: 44.39  E-value: 3.30e-06
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gi 530376195 158 CGGCGTEIKnGQALVALDKHWHLGCFKCKSCGK-LLNAEYISKDGLPYCEADY 209
Cdd:cd09362    1 CARCHKKIL-GEVMHALKQTWHVSCFVCAACKQpIGNSLFHMEDGEPYCEKDY 52
LIM2_Ajuba_like cd09355
The second LIM domain of Ajuba-like proteins; The second LIM domain of Ajuba-like proteins: ...
88-117 3.30e-06

The second LIM domain of Ajuba-like proteins; The second LIM domain of Ajuba-like proteins: Ajuba like LIM protein family includes three highly homologous proteins Ajuba, Limd1, and WTIP. Members of the family contain three tandem C-terminal LIM domains and a proline-rich N-terminal region. This family of proteins functions as scaffolds, participating in the assembly of numerous protein complexes. In the cytoplasm, Ajuba binds Grb2 to modulate serum-stimulated ERK activation. Ajuba also recruits the TNF receptor-associated factor 6 (TRAF6) to p62 and activates PKCKappa activity. Ajuba interacts with alpha-catenin and F-actin to contribute to the formation or stabilization of adheren junctions by linking adhesive receptors to the actin cytoskeleton. Although Ajuba is a cytoplasmic protein, it can shuttle into the nucleus. In nucleus, Ajuba functions as a corepressor for the zinc finger-protein Snail. It binds to the SNAG repression domain of Snail through its LIM region. Arginine methyltransferase-5 (Prmt5), a protein in the complex, is recruited to Snai l through an interaction with Ajuba. This ternary complex functions to repress E-cadherin, a Snail target gene. In addition, Ajuba contains functional nuclear-receptor interacting motifs and selectively interacts with retinoic acid receptors (RARs) and rexinoid receptor (RXRs) to negatively regulate retinoic acid signaling. Wtip, the Wt1-interacting protein, was originally identified as an interaction partner of the Wilms tumour protein 1 (WT1). Wtip is involved in kidney and neural crest development. Wtip interacts with the receptor tyrosine kinase Ror2 and inhibits canonical Wnt signaling. LIMD1 was reported to inhibit cell growth and metastases. The inhibition may be mediated through an interaction with the protein barrier-to-autointegration (BAF), a component of SWI/SNF chromatin-remodeling protein; or through the interaction with retinoblastoma protein (pRB), resulting in inhibition of E2F-mediated transcription, and expression of the majority of genes with E2F1- responsive elements. Recently, Limd1 was shown to interact with the p62/sequestosome protein and influence IL-1 and RANKL signaling by facilitating the assembly of a p62/TRAF6/a-PKC multi-protein complex. The Limd1-p62 interaction affects both NF-kappaB and AP-1 activity in epithelial cells and osteoclasts. Moreover, LIMD1 functions as tumor repressor to block lung tumor cell line in vitro and in vivo. Recent studies revealed that LIM proteins Wtip, LIMD1 and Ajuba interact with components of RNA induced silencing complexes (RISC) as well as eIF4E and the mRNA m7GTP cap-protein complex and are required for microRNA-mediated gene silencing. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188741 [Multi-domain]  Cd Length: 53  Bit Score: 44.26  E-value: 3.30e-06
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gi 530376195  88 CFSCDQFIEGEVVSALGKTYHPDCFVCAVC 117
Cdd:cd09355    1 CAVCGHLIMEMILQALGKSYHPGCFRCCVC 30
LIM_LASP_like cd09359
The LIM domain of LIM and SH3 Protein (LASP)-like proteins; The LIM domain of LIM and SH3 ...
158-209 3.43e-06

The LIM domain of LIM and SH3 Protein (LASP)-like proteins; The LIM domain of LIM and SH3 Protein (LASP) like proteins: This family contains two types of LIM containing proteins; LASP and N-RAP. LASP family contains two highly homologous members, LASP-1 and LASP-2. LASP contains a LIM motif at its amino terminus, a src homology 3 (SH3) domains at its C-terminal part, and a nebulin-like region in the middle. LASP-1 and -2 are highly conserved in their LIM, nebulin-like, and SH3 domains, but differ significantly at their linker regions. Both proteins are ubiquitously expressed and involved in cytoskeletal architecture, especially in the organization of focal adhesions. LASP-1 and LASP-2, are important during early embryo- and fetogenesis and are highly expressed in the central nervous system of the adult. However, only LASP-1 seems to participate significantly in neuronal differentiation and plays an important functional role in migration and proliferation of certain cancer cells while the role of LASP-2 is more structural. The expression of LASP-1 in breast tumors is increased significantly. N-RAP is a muscle-specific protein concentrated at myotendinous junctions in skeletal muscle and intercalated disks in cardiac muscle. LIM domain is found at the N-terminus of N-RAP and the C-terminal of N-RAP contains a region with multiple of nebulin repeats. N-RAP functions as a scaffolding protein that organizes alpha-actinin and actin into symmetrical I-Z-I structures in developing myofibrils. Nebulin repeat is known as actin binding domain. The N-RAP is hypothesized to form antiparallel dimerization via its LIM domain. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188745  Cd Length: 53  Bit Score: 44.18  E-value: 3.43e-06
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gi 530376195 158 CGGCGTEIKNGQALVALDKHWHLGCFKCKSCGKLLNAE-YISKDGLPYCEADY 209
Cdd:cd09359    1 CARCGKIVYPTEKVNCLDKTWHKACFHCEVCKMTLNMNnYKGYQKKPYCNAHY 53
LIM smart00132
Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM ...
29-76 3.45e-06

Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM domains bind protein partners via tyrosine-containing motifs. LIM domains are found in many key regulators of developmental pathways.


Pssm-ID: 214528 [Multi-domain]  Cd Length: 54  Bit Score: 44.30  E-value: 3.45e-06
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gi 530376195    29 CNTCGN--VCKGEVLRVQDKYFHIKCFVCKACGCDLAEGGFFVRQGEYIC 76
Cdd:smart00132   2 CAGCGKpiYGTERVLRALGKVWHPECFKCATCGKPLSGDTFFEKDGKLYC 51
LIM1_Paxillin cd09405
The first LIM domain of paxillin; The first LIM domain of paxillin: Paxillin is an adaptor ...
158-210 3.57e-06

The first LIM domain of paxillin; The first LIM domain of paxillin: Paxillin is an adaptor protein, which recruits key components of the signal-transduction machinery to specific sub-cellular locations to respond to environmental changes rapidly. The C-terminal region of paxillin contains four LIM domains which target paxillin to focal adhesions, presumably through a direct association with the cytoplasmic tail of beta-integrin. The N-terminal of paxillin is leucine-rich LD-motifs. Paxillin is found at the interface between the plasma membrane and the actin cytoskeleton. The binding partners of paxillin are diverse and include protein tyrosine kinases, such as Src and FAK, structural proteins, such as vinculin and actopaxin, and regulators of actin organization. Paxillin recruits these proteins to their function sites to control the dynamic changes in cell adhesion, cytoskeletal reorganization and gene expression. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight cons erved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188789 [Multi-domain]  Cd Length: 54  Bit Score: 44.23  E-value: 3.57e-06
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gi 530376195 158 CGGCGTEIKnGQALVALDKHWHLGCFKCKSCGKLLNAE-YISKDGLPYCEADYH 210
Cdd:cd09405    2 CGACKKPIA-GQVVTAMGKTWHPEHFVCTHCQEEIGSRnFFERDGQPYCEKDYH 54
LIM1_Lrg1p_like cd09391
The first LIM domain of Lrg1p, a LIM and RhoGap domain containing protein; The first LIM ...
88-117 3.71e-06

The first LIM domain of Lrg1p, a LIM and RhoGap domain containing protein; The first LIM domain of Lrg1p, a LIM and RhoGap domain containing protein: The members of this family contain three tandem repeats of LIM domains and a Rho-type GTPase activating protein (RhoGap) domain. Lrg1p is a Rho1 GTPase-activating protein required for efficient cell fusion in yeast. Lrg1p-GAP domain strongly and specifically stimulates the GTPase activity of Rho1p, a regulator of beta (1-3)-glucan synthase in vitro. The LIM domain is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188777  Cd Length: 57  Bit Score: 44.22  E-value: 3.71e-06
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gi 530376195  88 CFSCDQFIEGEVVSALGKTYHPDCFVCAVC 117
Cdd:cd09391    1 CAKCGKPITGQFVRALGDVYHLDCFTCHDC 30
LIM1_Enigma_like cd09361
The first LIM domain of Enigma-like family; The first LIM domain of Enigma-like family: The ...
88-118 4.14e-06

The first LIM domain of Enigma-like family; The first LIM domain of Enigma-like family: The Enigma LIM domain family is comprised of three members: Enigma, ENH, and Cypher (mouse)/ZASP (human). These subfamily members contain a single PDZ domain at the N-terminus and three LIM domains at the C-terminus. Enigma was initially characterized in humans and is expressed in multiple tissues, such as skeletal muscle, heart, bone, and brain. The third LIM domain specifically interacts with the insulin receptor and the second LIM domain interacts with the receptor tyrosine kinase Ret and the adaptor protein APS. Thus Enigma is implicated in signal transduction processes, such as mitogenic activity, insulin related actin organization, and glucose metabolism. The second member, ENH protein, was first identified in rat brain. It has been shown that ENH interacts with protein kinase D1 (PKD1) via its LIM domains and forms a complex with PKD1 and the alpha1C subunit of cardiac L-type voltage-gated calcium channel in rat neonatal cardiomyocytes. The N-terminal PDZ domain interacts with alpha-actinin at the Z-line. ZASP/Cypher is required for maintenance of Z-line structure during muscle contraction, but not required for Z-line assembly. In heart, Cypher/ZASP plays a structural role through its interaction with cytoskeletal Z-line proteins. In addition, there is increasing evidence that Cypher/ZASP also performs signaling functions. Studies reveal that Cypher/ZASP interacts with and directs PKC to the Z-line, where PKC phosphorylates downstream signaling targets. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188747 [Multi-domain]  Cd Length: 52  Bit Score: 43.89  E-value: 4.14e-06
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gi 530376195  88 CFSCDQFIEGEVVSALGKTYHPDCFVCAVCR 118
Cdd:cd09361    1 CAHCNQVIRGPFLVALGRSWHPEEFTCSHCH 31
LIM1_Lhx3a cd09466
The first LIM domain of Lhx3a; The first LIM domain of Lhx3a: Lhx3a is a member of LHX protein ...
158-209 5.63e-06

The first LIM domain of Lhx3a; The first LIM domain of Lhx3a: Lhx3a is a member of LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. Lhx3a is one of the two isoforms of Lhx3. The Lhx3 gene is expressed in the ventral spinal cord, the pons, the medulla oblongata, and the pineal gland of the developing nervous system during mouse embryogenesis, and transcripts are found in the emergent pituitary gland. Lhx3 functions in concert with other transcription factors to specify interneuron and motor neuron fates during development. Lhx3 proteins have been demonstrated to directly bind to the promoters of several pituitary hormone gene promoters. The Lhx3 gene encodes two isoforms, LHX3a and LHX3b that differ in their amino-terminal sequences, where Lhx3a has longer N-terminal. They show differential activation of pituitary hormone genes and distinct DNA binding properties. In human, Lhx3a trans-activated the alpha-glycoprotein subunit promoter and genes containing a high-affinity Lhx3 binding site more effectively than the hLhx3b isoform. In addition, hLhx3a induce transcription of the TSHbeta-subunit gene by acting on pituitary POU domain factor, Pit-1, while hLhx3b does not. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188850 [Multi-domain]  Cd Length: 56  Bit Score: 43.61  E-value: 5.63e-06
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gi 530376195 158 CGGCGTEIKNGQALVALDKHWHLGCFKCKSCGKLLNAEYISKDGLPYCEADY 209
Cdd:cd09466    4 CAGCDHPIFDRFILKVQDKPWHSKCLKCVDCQAQLTDKCFSRGGQVYCKEDF 55
LIM2_FBLP-1 cd09372
The second LIM domain of the filamin-binding LIM protein-1 (FBLP-1); The second LIM domain of ...
88-120 5.67e-06

The second LIM domain of the filamin-binding LIM protein-1 (FBLP-1); The second LIM domain of the filamin-binding LIM protein-1 (FBLP-1): Fblp-1 contains a proline-rich domain near its N terminus and two LIM domains at its C terminus. FBLP-1 mRNA was detected in a variety of tissues and cells including platelets and endothelial cells. FBLP-1 binds to Filamins. The association between filamin B and FBLP-1 may play an unknown role in cytoskeletal function, cell adhesion, and cell motility. As in other LIM domains, this domain family is 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188758 [Multi-domain]  Cd Length: 53  Bit Score: 43.57  E-value: 5.67e-06
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gi 530376195  88 CFSCDQFIEGEVVSALGKTYHPDCFVCAVCRLP 120
Cdd:cd09372    1 CAKCQGVITEHIIRALGKGYHPPCFTCVTCGRR 33
LIM2_TLP cd09477
The second LIM domain of thymus LIM protein (TLP); The second LIM domain of thymus LIM protein ...
158-205 5.88e-06

The second LIM domain of thymus LIM protein (TLP); The second LIM domain of thymus LIM protein (TLP): TLP is the distant member of the CRP family of proteins. TLP has two isomers (TLP-A and TLP-B) and sharing approximately 30% with each of the three other CRPs. Like CRP1, CRP2 and CRP3/MLP, TLP has two LIM domains, connected by a flexible linker region. Unlike the CRPs, TLP lacks the nuclear targeting signal (K/R-K/R-Y-G-P-K) and is localized solely in the cytoplasm. TLP is specifically expressed in the thymus in a subset of cortical epithelial cells. TLP has a role in development of normal thymus and in controlling the development and differentiation of thymic epithelial cells. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188861  Cd Length: 54  Bit Score: 43.46  E-value: 5.88e-06
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gi 530376195 158 CGGCGTEIKNGQALVALDKHWHLGCFKCKSCGKLLNA-EYISKDGLPYC 205
Cdd:cd09477    1 CPGCGKPVYFAEKVMSLGRNWHRPCLRCQRCKKTLTAgGHAEHDGSPYC 49
LIM1_abLIM cd09327
The first LIM domain of actin binding LIM (abLIM) proteins; The first LIM domain of actin ...
158-209 6.04e-06

The first LIM domain of actin binding LIM (abLIM) proteins; The first LIM domain of actin binding LIM (abLIM) proteins: Three homologous members of the abLIM protein family have been identified; abLIM-1, abLIM-2 and abLIM-3. The N-terminal of abLIM consists of four tandem repeats of LIM domains and the C-terminal of acting binding LIM protein is a villin headpiece domain, which has strong actin binding activity. The abLIM-1, which is expressed in retina, brain, and muscle tissue, has been indicated to function as a tumor suppressor. AbLIM-2 and -3, mainly expressed in muscle and neuronal tissue, bind to F-actin strongly. They may serve as a scaffold for signaling modules of the actin cytoskeleton and thereby modulate transcription. It has shown that LIM domains of abLIMs interact with STARS (striated muscle activator of Rho signaling), which directly binds actin and stimulates serum-response factor (SRF)-dependent transcription. All LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188713 [Multi-domain]  Cd Length: 52  Bit Score: 43.40  E-value: 6.04e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530376195 158 CGGCGTEIKnGQALVALDKHWHLGCFKCKSCGK-LLNAEYISKDGLPYCEADY 209
Cdd:cd09327    1 CYKCGKKCK-GEVLRVQDKYFHIKCFTCKVCGCdLAQGGFFVKEGEYYCTDDY 52
LIM1_Isl cd09366
The first LIM domain of Isl, a member of LHX protein family; The first LIM domain of Isl: Isl ...
158-209 6.88e-06

The first LIM domain of Isl, a member of LHX protein family; The first LIM domain of Isl: Isl is a member of LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Isl1 and Isl2 are the two conserved members of this family. Proteins in this group are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. Isl-1 is one of the LHX proteins isolated originally by virtue of its ability to bind DNA sequences from the 5'-flanking region of the rat insulin gene in pancreatic insulin-producing cells. Mice deficient in Isl-1 fail to form the dorsal exocrine pancreas and islet cells fail to differentiate. On the other hand, Isl-1 takes part in the pituitary development by activating the gonadotropin-releasing hormone receptor gene together with LHX3 and steroidogenic factor 1. Mouse Is l2 is expressed in the retinal ganglion cells and the developing spinal cord where it plays a role in motor neuron development. Same as Isl1, Isl2 may also be able to bind to the insulin gene enhancer to promote gene activation. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188752 [Multi-domain]  Cd Length: 55  Bit Score: 43.49  E-value: 6.88e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 530376195 158 CGGCGTEIKNGQAL-VALDKHWHLGCFKCKSCGKLL--NAEYISKDGLPYCEADY 209
Cdd:cd09366    1 CVGCGGKIHDQYILrVAPDLEWHAACLKCAECGQYLdeTCTCFVRDGKTYCKRDY 55
LIM5_PINCH cd09335
The fifth LIM domain of protein PINCH; The fifth LIM domain of protein PINCH: PINCH plays ...
88-139 6.89e-06

The fifth LIM domain of protein PINCH; The fifth LIM domain of protein PINCH: PINCH plays pivotal roles in the assembly of focal adhesions (FAs), regulating diverse functions in cell adhesion, growth, and differentiation through LIM-mediated protein-protein interactions. PINCH comprises an array of five LIM domains that interact with integrin-linked kinase (ILK), Nck2 (also called Nckbeta or Grb4) and other interaction partners. These interactions are essential for triggering the FA assembly and for relaying diverse mechanical and biochemical signals between Cell-extracellular matrix and the actin cytoskeleton. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188721 [Multi-domain]  Cd Length: 54  Bit Score: 43.49  E-value: 6.89e-06
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                 ....*....|....*....|....*....|....*....|....*....|...
gi 530376195  88 CFSCDQFIEGEVVSALGKTYHPDCFVCAVCRLPFPPGDR-VTFNGKEcMCQKC 139
Cdd:cd09335    1 CYHCNQVIEGDVVSALNKTWCVDHFSCSFCDTKLTLKSKfYEFDMKP-VCKKC 52
LIM_ALP_like cd09360
The LIM domain of ALP (actinin-associated LIM protein) family; This family represents the LIM ...
88-117 7.55e-06

The LIM domain of ALP (actinin-associated LIM protein) family; This family represents the LIM domain of ALP (actinin-associated LIM protein) family. Four proteins: ALP, CLP36, RIL, and Mystique have been classified into the ALP subfamily of LIM domain proteins. Each member of the subfamily contains an N-terminal PDZ domain and a C-terminal LIM domain. Functionally, these proteins bind to alpha-actinin through their PDZ domains and bind or other signaling molecules through their LIM domains. ALP proteins have been implicated in cardiac and skeletal muscle structure, function and disease, platelet, and epithelial cell motility. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188746 [Multi-domain]  Cd Length: 52  Bit Score: 43.13  E-value: 7.55e-06
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gi 530376195  88 CFSCDQFIEGEVVSALGKTYHPDCFVCAVC 117
Cdd:cd09360    1 CDKCGNGIVGVVVKARDKNRHPECFVCADC 30
LIM2_Zyxin cd09353
The second LIM domain of Zyxin; The second LIM domain of Zyxin: Zyxin exhibits three copies of ...
88-121 8.05e-06

The second LIM domain of Zyxin; The second LIM domain of Zyxin: Zyxin exhibits three copies of the LIM domain, an extensive proline-rich domain and a nuclear export signal. Localized at sites of cellsubstratum adhesion in fibroblasts, Zyxin interacts with alpha-actinin, members of the cysteine-rich protein (CRP) family, proteins that display Src homology 3 (SH3) domains and Ena/VASP family members. Zyxin and its partners have been implicated in the spatial control of actin filament assembly as well as in pathways important for cell differentiation. In addition to its functions at focal adhesion plaques, recent work has shown that zyxin moves from the sites of cell contacts to the nucleus, where it directly participates in the regulation of gene expression. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors o r scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188739 [Multi-domain]  Cd Length: 60  Bit Score: 43.38  E-value: 8.05e-06
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                 ....*....|....*....|....*....|....
gi 530376195  88 CFSCDQFIEGEVVSALGKTYHPDCFVCAVCRLPF 121
Cdd:cd09353    1 CAVCDQKITDRMLKATGKSYHPQCFTCVVCKCPL 34
LIM1_Testin_like cd09340
The first LIM domain of Testin-like family; The first LIM domain of Testin_like family: This ...
158-209 1.00e-05

The first LIM domain of Testin-like family; The first LIM domain of Testin_like family: This family includes testin, prickle, dyxin and LIMPETin. Structurally, testin and prickle proteins contain three LIM domains at C-terminal; LIMPETin has six LIM domains; and dyxin presents only two LIM domains. However, all members of the family contain a PET protein-protein interaction domain. Testin is a cytoskeleton associated focal adhesion protein that localizes along actin stress fibers, at cell-cell-contact areas, and at focal adhesion plaques. Testin interacts with a variety of cytoskeletal proteins, including zyxin, mena, VASP, talin, and actin and it is involved in cell motility and adhesion events. Prickles have been implicated in roles of regulating tissue polarity or planar cell polarity (PCP). Dyxin involves in lung and heart development by interaction with GATA6 and blocking GATA6 activated target genes. LIMPETin might be the recombinant product of genes coding testin and four and half LIM proteins and its function is not well understood. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188726  Cd Length: 58  Bit Score: 42.97  E-value: 1.00e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530376195 158 CGGCGTEIKNGQALV-----ALDKHWHLGCFKCKSCGKLL-NAEYISKDGLPYCEADY 209
Cdd:cd09340    1 CEKCKEPINPGEVAVfaeraGEDACWHPGCFVCETCNELLvDLIYFYHDGKIYCGRHY 58
LIM3_Paxillin cd09409
The third LIM domain of paxillin; The third LIM domain of paxillin: Paxillin is an adaptor ...
158-210 1.36e-05

The third LIM domain of paxillin; The third LIM domain of paxillin: Paxillin is an adaptor protein, which recruits key components of the signal-transduction machinery to specific sub-cellular locations to respond to environmental changes rapidly. The C-terminal region of paxillin contains four LIM domains which target paxillin to focal adhesions, presumably through a direct association with the cytoplasmic tail of beta-integrin. The N-terminal of paxillin is leucine-rich LD-motifs. Paxillin is found at the interface between the plasma membrane and the actin cytoskeleton. The binding partners of paxillin are diverse and include protein tyrosine kinases, such as Src and FAK, structural proteins, such as vinculin and actopaxin, and regulators of actin organization. Paxillin recruits these proteins to their function sites to control the dynamic changes in cell adhesion, cytoskeletal reorganization and gene expression. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188793 [Multi-domain]  Cd Length: 53  Bit Score: 42.52  E-value: 1.36e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530376195 158 CGGCGTEIKNgQALVALDKHWHLGCFKCKSC-GKLLNAEYISKDGLPYCEADYH 210
Cdd:cd09409    1 CGGCARAILE-NYISALNTLWHPECFVCRECfTPFVNGSFFEHDGQPYCEAHYH 53
LIM1_Leupaxin cd09406
The first LIM domain of Leupaxin; The first LIM domain of Leupaxin: Leupaxin is a cytoskeleton ...
88-118 1.40e-05

The first LIM domain of Leupaxin; The first LIM domain of Leupaxin: Leupaxin is a cytoskeleton adaptor protein, which is preferentially expressed in hematopoietic cells. Leupaxin belongs to the paxillin focal adhesion protein family. Same as other members of the family, it has four leucine-rich LD-motifs in the N-terminus and four LIM domains in the C-terminus. It may function in cell type-specific signaling by associating with interaction partners PYK2, FAK, PEP and p95PKL. When expressed in human leukocytic cells, leupaxin significantly suppressed integrin-mediated cell adhesion to fibronectin and the tyrosine phosphorylation of paxillin. These findings indicate that leupaxin may negatively regulate the functions of paxillin during integrin signaling. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188790 [Multi-domain]  Cd Length: 55  Bit Score: 42.55  E-value: 1.40e-05
                         10        20        30
                 ....*....|....*....|....*....|.
gi 530376195  88 CFSCDQFIEGEVVSALGKTYHPDCFVCAVCR 118
Cdd:cd09406    3 CASCQKPIAGQVVTALGQTWHPEHFVCCQCG 33
LIM2_Enigma_like cd09362
The second LIM domain of Enigma-like family; The second LIM domain of Enigma-like family: The ...
88-121 1.63e-05

The second LIM domain of Enigma-like family; The second LIM domain of Enigma-like family: The Enigma LIM domain family is comprised of three members: Enigma, ENH, and Cypher (mouse)/ZASP (human). These subfamily members contain a single PDZ domain at the N-terminus and three LIM domains at the C-terminus. Enigma was initially characterized in humans and is expressed in multiple tissues, such as skeletal muscle, heart, bone and brain. The third LIM domain specifically interacts with the insulin receptor and the second LIM domain interacts with the receptor tyrosine kinase Ret and the adaptor protein APS. Thus Enigma is implicated in signal transduction processes, such as mitogenic activity, insulin related actin organization, and glucose metabolism. The second member, ENH protein, was first identified in rat brain. It has been shown that ENH interacts with protein kinase D1 (PKD1) via its LIM domains and forms a complex with PKD1 and the alpha1C subunit of cardiac L-type voltage-gated calcium channel in rat neonatal cardiomyocytes. The N-terminal PDZ domain interacts with alpha-actinin at the Z-line. ZASP/Cypher is required for maintenance of Z-line structure during muscle contraction, but not required for Z-line assembly. In heart, Cypher/ZASP plays a structural role through its interaction with cytoskeletal Z-line proteins. In addition, there is increasing evidence that Cypher/ZASP also performs signaling functions. Studies reveal that Cypher/ZASP interacts with and directs PKC to the Z-line, where PKC phosphorylates downstream signaling targets. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188748 [Multi-domain]  Cd Length: 52  Bit Score: 42.46  E-value: 1.63e-05
                         10        20        30
                 ....*....|....*....|....*....|....
gi 530376195  88 CFSCDQFIEGEVVSALGKTYHPDCFVCAVCRLPF 121
Cdd:cd09362    1 CARCHKKILGEVMHALKQTWHVSCFVCAACKQPI 34
LIM2_Enigma cd09456
The second LIM domain of Enigma; The second LIM domain of Enigma: Enigma was initially ...
158-209 1.75e-05

The second LIM domain of Enigma; The second LIM domain of Enigma: Enigma was initially characterized in humans as a protein containing three LIM domains at the C-terminus and a PDZ domain at N-terminus. The third LIM domain specifically interacts with the insulin receptor and the second LIM domain interacts with the receptor tyrosine kinase Ret and the adaptor protein APS. Thus Enigma is implicated in signal transduction processes, such as mitogenic activity, insulin related actin organization, and glucose metabolism. Enigma is expressed in multiple tissues, such as skeletal muscle, heart, bone and brain. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188840 [Multi-domain]  Cd Length: 52  Bit Score: 42.29  E-value: 1.75e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530376195 158 CGGCGTEIkNGQALVALDKHWHLGCFKCKSCG-KLLNAEYISKDGLPYCEADY 209
Cdd:cd09456    1 CAKCKKKI-TGEIMHALKMTWHVHCFTCAACKtPIRNRAFYMEEGAPYCERDY 52
LIM2_Lrg1p_like cd09392
The second LIM domain of Lrg1p, a LIM and RhoGap domain containing protein; The second LIM ...
88-125 1.87e-05

The second LIM domain of Lrg1p, a LIM and RhoGap domain containing protein; The second LIM domain of Lrg1p, a LIM and RhoGap domain containing protein: The members of this family contain three tandem repeats of LIM domains and a Rho-type GTPase activating protein (RhoGap) domain. Lrg1p is a Rho1 GTPase-activating protein required for efficient cell fusion in yeast. Lrg1p-GAP domain strongly and specifically stimulates the GTPase activity of Rho1p, a regulator of beta (1-3)-glucan synthase in vitro. The LIM domain is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188778 [Multi-domain]  Cd Length: 53  Bit Score: 41.96  E-value: 1.87e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 530376195  88 CFSCDQFIEGEVVSALGKTYHPDCFVCAVCRLPFPPGD 125
Cdd:cd09392    1 CFKCGGALRGSYITALGRKYHVEHFTCSVCPTVFGPND 38
LIM2_CRP2 cd09840
The second LIM domain of Cysteine Rich Protein 2 (CRP2); The second LIM domain of Cysteine ...
158-209 1.88e-05

The second LIM domain of Cysteine Rich Protein 2 (CRP2); The second LIM domain of Cysteine Rich Protein 2 (CRP2): Cysteine-rich proteins (CRPs) are characterized by the presence of two LIM domains linked to short glycine-rich repeats (GRRs). The CRP family members include CRP1, CRP2, CRP3/MLP and TLPCRP1, CRP2 and CRP3 share a conserved nuclear targeting signal (K/R-K/R-Y-G-P-K), which supports the fact that these proteins function not only in the cytoplasm but also in the nucleus. CRPs control regulatory pathways during cellular differentiation, and involve in complex transcription circuits, and the organization as well as the arrangement of the myofibrillar/cytoskeletal network.CRP3 also called Muscle LIM Protein (MLP), which is a striated muscle-specific factor that enhances myogenic differentiation. The second LIM domain of CRP3/MLP interacts with cytoskeletal protein beta-spectrin. CRP3/MLP also interacts with the basic helix-loop-helix myogenic transcription factors MyoD, myogenin, and MRF4 thereby increasing their affinity for specific DNA regulatory elements. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188871 [Multi-domain]  Cd Length: 54  Bit Score: 42.40  E-value: 1.88e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530376195 158 CGGCGTEIKNGQALVALDKHWHLGCFKCKSCGKLLNAEYIS-KDGLPYCEADY 209
Cdd:cd09840    1 CSRCGDSVYAAEKIMGAGKPWHKNCFRCAKCGKSLESTTLTeKEGEIYCKGCY 53
LIM2_Enigma cd09456
The second LIM domain of Enigma; The second LIM domain of Enigma: Enigma was initially ...
88-120 3.07e-05

The second LIM domain of Enigma; The second LIM domain of Enigma: Enigma was initially characterized in humans as a protein containing three LIM domains at the C-terminus and a PDZ domain at N-terminus. The third LIM domain specifically interacts with the insulin receptor and the second LIM domain interacts with the receptor tyrosine kinase Ret and the adaptor protein APS. Thus Enigma is implicated in signal transduction processes, such as mitogenic activity, insulin related actin organization, and glucose metabolism. Enigma is expressed in multiple tissues, such as skeletal muscle, heart, bone and brain. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188840 [Multi-domain]  Cd Length: 52  Bit Score: 41.52  E-value: 3.07e-05
                         10        20        30
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gi 530376195  88 CFSCDQFIEGEVVSALGKTYHPDCFVCAVCRLP 120
Cdd:cd09456    1 CAKCKKKITGEIMHALKMTWHVHCFTCAACKTP 33
LIM cd08368
LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains ...
217-268 3.99e-05

LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains are identified in a diverse group of proteins with wide variety of biological functions, including gene expression regulation, cell fate determination, cytoskeleton organization, tumor formation and development. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes. They perform their functions through interactions with other protein partners. LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. The consensus sequence of LIM domain has been defined as C-x(2)-C-x(16,23)-H-x(2)-[CH]-x(2)-C-x(2)-C-x(16,21)-C-x(2,3)-[CHD] (where X denotes any amino acid).


Pssm-ID: 259829 [Multi-domain]  Cd Length: 53  Bit Score: 41.15  E-value: 3.99e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530376195 217 CDSCEKYITGR-VLEAGEKHYHPSCALCVRCGQMFaEGEEMYLQGSSIWHPAC 268
Cdd:cd08368    1 CAGCGKPIEGReLLRALGKKWHPECFKCAECGKPL-GGDSFYEKDGKPYCEKC 52
LIM1_Enigma_like cd09361
The first LIM domain of Enigma-like family; The first LIM domain of Enigma-like family: The ...
29-80 4.12e-05

The first LIM domain of Enigma-like family; The first LIM domain of Enigma-like family: The Enigma LIM domain family is comprised of three members: Enigma, ENH, and Cypher (mouse)/ZASP (human). These subfamily members contain a single PDZ domain at the N-terminus and three LIM domains at the C-terminus. Enigma was initially characterized in humans and is expressed in multiple tissues, such as skeletal muscle, heart, bone, and brain. The third LIM domain specifically interacts with the insulin receptor and the second LIM domain interacts with the receptor tyrosine kinase Ret and the adaptor protein APS. Thus Enigma is implicated in signal transduction processes, such as mitogenic activity, insulin related actin organization, and glucose metabolism. The second member, ENH protein, was first identified in rat brain. It has been shown that ENH interacts with protein kinase D1 (PKD1) via its LIM domains and forms a complex with PKD1 and the alpha1C subunit of cardiac L-type voltage-gated calcium channel in rat neonatal cardiomyocytes. The N-terminal PDZ domain interacts with alpha-actinin at the Z-line. ZASP/Cypher is required for maintenance of Z-line structure during muscle contraction, but not required for Z-line assembly. In heart, Cypher/ZASP plays a structural role through its interaction with cytoskeletal Z-line proteins. In addition, there is increasing evidence that Cypher/ZASP also performs signaling functions. Studies reveal that Cypher/ZASP interacts with and directs PKC to the Z-line, where PKC phosphorylates downstream signaling targets. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188747 [Multi-domain]  Cd Length: 52  Bit Score: 41.19  E-value: 4.12e-05
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gi 530376195  29 CNTCGNVCKGEVLRVQDKYFHIKCFVCKACGCDLAEGGFFVRQGEYICTLDY 80
Cdd:cd09361    1 CAHCNQVIRGPFLVALGRSWHPEEFTCSHCHCSLAEIGFVEEKGSLYCELCY 52
LIM_RIL cd09451
The LIM domain of RIL; The LIM domain of RIL: RIL contains an N-terminal PDZ domain, a LIM ...
29-76 4.21e-05

The LIM domain of RIL; The LIM domain of RIL: RIL contains an N-terminal PDZ domain, a LIM domain, and a short consensus C-terminal region. It is the smallest molecule in the ALP LIM domain containing protein family. RIL was identified in rat fibroblasts and in human lymphocytes. The LIM domain interacts with the AMPA glutamate receptor in dendritic spines. The consensus C-terminus interacts with PTP-BL, a submembranous protein tyrosine phosphatase and the PDZ domain is responsible to interact with alpha-actinin molecules. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188835  Cd Length: 53  Bit Score: 41.07  E-value: 4.21e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 530376195  29 CNTCGNVCKGEVLRVQDKYFHIKCFVCKACGCDLAEGGFFVRQGEYIC 76
Cdd:cd09451    1 CTRCGNGIVGTIVKARDKLYHPECFMCDDCGLNLKQRGYFFIDEQLYC 48
LIM4_Paxillin_like cd09339
The fourth LIM domain of the Paxillin-like protein family; The fourth LIM domain of the ...
88-139 4.49e-05

The fourth LIM domain of the Paxillin-like protein family; The fourth LIM domain of the Paxillin like protein family: This family consists of paxillin, leupaxin, Hic-5 (ARA55), and other related proteins. There are four LIM domains in the C-terminal of the proteins and leucine-rich LD-motifs in the N-terminal region. Members of this family are adaptor proteins to recruit key components of signal-transduction machinery to specific sub-cellular locations. Paxillin is found at the interface between the plasma membrane and the actin cytoskeleton. Paxillin serves as a platform for the recruitment of numerous regulatory and structural proteins that together control the dynamic changes in cell adhesion, cytoskeletal reorganization and gene expression that are necessary for cell migration and survival. Leupaxin is a cytoskeleton adaptor protein, which is preferentially expressed in hematopoietic cells. It associates with focal adhesion kinases PYK2 and pp125FAK and identified to be a component of the osteoclast pososomal signaling complex. Hic-5 controls cell proliferation, migration and senescence by functioning as coactivator for steroid receptors such as androgen receptor, glucocorticoid receptor and progesterone receptor. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188725 [Multi-domain]  Cd Length: 52  Bit Score: 41.17  E-value: 4.49e-05
                         10        20        30        40        50
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gi 530376195  88 CFSCDQFIEGEVVSALGKTYHPDCFVCAVCRLPFPPGdrvTF--NGKECMCQKC 139
Cdd:cd09339    1 CAGCGKPITGRCITAMGRKFHPEHFVCAFCLKQLSKG---TFkeQDDKPYCHPC 51
LIM2_Zyxin cd09353
The second LIM domain of Zyxin; The second LIM domain of Zyxin: Zyxin exhibits three copies of ...
29-87 4.58e-05

The second LIM domain of Zyxin; The second LIM domain of Zyxin: Zyxin exhibits three copies of the LIM domain, an extensive proline-rich domain and a nuclear export signal. Localized at sites of cellsubstratum adhesion in fibroblasts, Zyxin interacts with alpha-actinin, members of the cysteine-rich protein (CRP) family, proteins that display Src homology 3 (SH3) domains and Ena/VASP family members. Zyxin and its partners have been implicated in the spatial control of actin filament assembly as well as in pathways important for cell differentiation. In addition to its functions at focal adhesion plaques, recent work has shown that zyxin moves from the sites of cell contacts to the nucleus, where it directly participates in the regulation of gene expression. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors o r scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188739 [Multi-domain]  Cd Length: 60  Bit Score: 41.45  E-value: 4.58e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376195  29 CNTCGNVCKGEVLRVQDKYFHIKCFVCKACGCDLAEGGFFVRQGEYI-CTLDYQRLYGTR 87
Cdd:cd09353    1 CAVCDQKITDRMLKATGKSYHPQCFTCVVCKCPLEGESFIVDQANQPhCVNDYHRRYAPR 60
LIM1_Lhx3b cd09467
The first LIM domain of Lhx3b; The first LIM domain of Lhx3b. Lhx3b is a member of LHX protein ...
158-209 5.05e-05

The first LIM domain of Lhx3b; The first LIM domain of Lhx3b. Lhx3b is a member of LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. Lhx3b is one of the two isoforms of Lhx3. The Lhx3 gene is expressed in the ventral spinal cord, the pons, the medulla oblongata, and the pineal gland of the developing nervous system during mouse embryogenesis, and transcripts are found in the emergent pituitary gland. Lhx3 functions in concert with other transcription factors to specify interneuron and motor neuron fates during development. Lhx3 proteins have been demonstrated to directly bind to the promoters of several pituitary hormone gene promoters. The Lhx3 gene encodes two isoforms, LHX3a and LHX3b that differ in their amino-terminal sequences, where Lhx3a has longer N-terminal. They show differential activation of pituitary hormone genes and distinct DNA binding properties. In human, Lhx3a trans-activated the alpha-glycoprotein subunit promoter and genes containing a high-affinity Lhx3 binding site more effectively than the hLhx3b isoform. In addition, hLhx3a induce transcription of the TSHbeta-subunit gene by acting on pituitary POU domain factor, Pit-1, while hLhx3b does not. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188851 [Multi-domain]  Cd Length: 55  Bit Score: 41.07  E-value: 5.05e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530376195 158 CGGCGTEIKNGQALVALDKHWHLGCFKCKSCGKLLNAEYISKDGLPYCEADY 209
Cdd:cd09467    4 CAGCNQHIVDRFILKVLDRHWHSKCLKCSDCQTQLAEKCFSRGDSVYCKDDF 55
LIM3_Leupaxin cd09410
The third LIM domain of Leupaxin; The third LIM domain of Leupaxin: Leupaxin is a cytoskeleton ...
158-210 5.25e-05

The third LIM domain of Leupaxin; The third LIM domain of Leupaxin: Leupaxin is a cytoskeleton adaptor protein, which is preferentially expressed in hematopoietic cells. Leupaxin belongs to the paxillin focal adhesion protein family. Same as other members of the family, it has four leucine-rich LD-motifs in the N-terminus and four LIM domains in the C-terminus. It may function in cell type-specific signaling by associating with interaction partners PYK2, FAK, PEP and p95PKL. When expressed in human leukocytic cells, leupaxin significantly suppressed integrin-mediated cell adhesion to fibronectin and the tyrosine phosphorylation of paxillin. These findings indicate that leupaxin may negatively regulate the functions of paxillin during integrin signaling. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188794 [Multi-domain]  Cd Length: 53  Bit Score: 40.96  E-value: 5.25e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530376195 158 CGGCGTEIKNgQALVALDKHWHLGCFKCKSCGK-LLNAEYISKDGLPYCEADYH 210
Cdd:cd09410    1 CSGCGRPVKE-NYLSAANGVWHPECFVCSDCLKpFTDGSFFELDGRPLCELHYH 53
LIM2_Leupaxin cd09408
The second LIM domain of Leupaxin; The second LIM domain of Leupaxin: Leupaxin is a ...
158-209 5.34e-05

The second LIM domain of Leupaxin; The second LIM domain of Leupaxin: Leupaxin is a cytoskeleton adaptor protein, which is preferentially expressed in hematopoietic cells. Leupaxin belongs to the paxillin focal adhesion protein family. Same as other members of the family, it has four leucine-rich LD-motifs in the N-terminus and four LIM domains in the C-terminus. It may function in cell type-specific signaling by associating with interaction partners PYK2, FAK, PEP and p95PKL. When expressed in human leukocytic cells, leupaxin significantly suppressed integrin-mediated cell adhesion to fibronectin and the tyrosine phosphorylation of paxillin. These findings indicate that leupaxin may negatively regulate the functions of paxillin during integrin signaling. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188792 [Multi-domain]  Cd Length: 52  Bit Score: 40.96  E-value: 5.34e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530376195 158 CGGCGTEIKNgQALVALDKHWHLGCFKCKSCGKLLNAE-YISKDGLPYCEADY 209
Cdd:cd09408    1 CAYCAGPILQ-NVLTAMDQTWHPEHFFCSHCGELFGDEgFLERDGKPYCRRDF 52
LIM4_Leupaxin cd09412
The fourth LIM domain of Leupaxin; The fourth LIM domain of Leupaxin: Leupaxin is a ...
88-139 6.14e-05

The fourth LIM domain of Leupaxin; The fourth LIM domain of Leupaxin: Leupaxin is a cytoskeleton adaptor protein, which is preferentially expressed in hematopoietic cells. Leupaxin belongs to the paxillin focal adhesion protein family. Same as other members of the family, it has four leucine-rich LD-motifs in the N-terminus and four LIM domains in the C-terminus. It may function in cell type-specific signaling by associating with interaction partners PYK2, FAK, PEP and p95PKL. When expressed in human leukocytic cells, leupaxin significantly suppressed integrin-mediated cell adhesion to fibronectin and the tyrosine phosphorylation of paxillin. These findings indicate that leupaxin may negatively regulate the functions of paxillin during integrin signaling. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188796 [Multi-domain]  Cd Length: 52  Bit Score: 40.49  E-value: 6.14e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530376195  88 CFSCDQFIEGEVVSALGKTYHPDCFVCAVCRLPFPPGDRVTFNGKEcMCQKC 139
Cdd:cd09412    1 CGSCGLPITGRCISALGRKFHPEHFVCAFCLRPLTQGSFKEQSGKP-YCSTC 51
LIM1_Rga cd09394
The first LIM domain of Rga GTPase-Activating Proteins; The first LIM domain of Rga ...
158-195 1.01e-04

The first LIM domain of Rga GTPase-Activating Proteins; The first LIM domain of Rga GTPase-Activating Proteins: The members of this family contain two tandem repeats of LIM domains and a Rho-type GTPase activating protein (RhoGap) domain. Rga activates GTPases during polarized morphogenesis. In yeast, a known regulating target of Rga is CDC42p, a small GTPase. The LIM domain is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188780  Cd Length: 55  Bit Score: 40.04  E-value: 1.01e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 530376195 158 CGGCGTEIKNGQALVALDKHWHLGCFKCKSCGKLLNAE 195
Cdd:cd09394    1 CVGCKESITEGHAYELGGDRWHIHCFKCYKCDKKLSCD 38
LIM2_LMO4 cd09387
The second LIM domain of LMO4 (LIM domain only protein 4); The second LIM domain of LMO4 (LIM ...
88-132 1.11e-04

The second LIM domain of LMO4 (LIM domain only protein 4); The second LIM domain of LMO4 (LIM domain only protein 4): LMO4 is a nuclear protein that plays important roles in transcriptional regulation and development. LMO4 is involved in various functions in tumorigenesis and cellular differentiation. LMO4 proteins regulate gene expression by interacting with a wide variety of transcription factors and cofactors to form large transcription complexes. It can interact with Smad proteins, and associate with the promoter of the PAI-1 (plasminogen activator inhibitor-1) gene in a TGFbeta (transforming growth factor beta)-dependent manner. LMO4 can also form a complex with transcription regulator CREB (cAMP response element-binding protein) and interact with CLIM1 and CLIM2. In breast tissue, LMO4 interacts with multiple proteins, including the cofactor CtIP [CtBP (C-terminal binding protein)-interacting protein], the breast and ovarian tumor suppressor BRCA1 (breast-cancer susceptibility gene 1) and the LIM-domain-binding protein LDB1. Functionally, LMO4 is shown to repress BRCA1-mediated transcription activation, thus invoking a potential role for LMO4 as a negative regulator of BRCA1 in sporadic breast cancer. LMO4 also forms complex to both ERa (oestrogen receptor alpha), MTA1 (metastasis tumor antigen 1), and HDACs (histone deacetylases), implying that LMO4 is also a component of the MTA1 corepressor complex. Over-expressed LMO4 represses ERa transactivation functions in an HDAC-dependent manner, and contributes to the process of breast cancer progression by allowing the development of Era-negative phenotypes. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188773  Cd Length: 55  Bit Score: 40.16  E-value: 1.11e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 530376195  88 CFSCDQFIEGE--VVSALGKTYHPDCFVCAVCRLPFPPGDRVTF-NGK 132
Cdd:cd09387    1 CSACGQSIPASelVMRAQGNVYHLKCFTCSTCHNQLVPGDRFHYvNGS 48
LIM2_Testin_like cd09341
The second LIM domain of Testin-like family; The second LIM domain of Testin-like family: This ...
158-205 1.32e-04

The second LIM domain of Testin-like family; The second LIM domain of Testin-like family: This family includes testin, prickle, dyxin and LIMPETin. Structurally, testin and prickle proteins contain three LIM domains at C-terminal; LIMPETin has six LIM domains; and dyxin presents only two LIM domains. However, all members of the family contain a PET protein-protein interaction domain. Testin is a cytoskeleton associated focal adhesion protein that localizes along actin stress fibers, at cell-cell-contact areas, and at focal adhesion plaques. Testin interacts with a variety of cytoskeletal proteins, including zyxin, mena, VASP, talin, and actin and it is involved in cell motility and adhesion events. Prickles have been implicated in roles of regulating tissue polarity or planar cell polarity (PCP). Dyxin involves in lung and heart development by interaction with GATA6 and blocking GATA6 activated target genes. LIMPETin might be the recombinant product of genes coding testin and four and half LIM proteins and its function is not well understood. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188727  Cd Length: 56  Bit Score: 39.90  E-value: 1.32e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 530376195 158 CGGCGTEIKNGQALVALDKHWHLGCFKCKSCGKLLNAE-YISKDGLPYC 205
Cdd:cd09341    3 CAACDELIFSGEYTQAEGKNWHLKHFCCFQCDEPLGGQrYVLREGKPYC 51
LIM2_LIMK cd09365
The second LIM domain of LIMK (LIM domain Kinase ); The second LIM domain of LIMK (LIM domain ...
217-254 1.33e-04

The second LIM domain of LIMK (LIM domain Kinase ); The second LIM domain of LIMK (LIM domain Kinase ): LIMK protein family is comprised of two members LIMK1 and LIMK2. LIMK contains two LIM domains, a PDZ domain and a kinase domain. LIMK is involved in the regulation of actin polymerization and microtubule disassembly. LIMK influences architecture of the actin cytoskeleton by regulating the activity of the cofilin family proteins cofilin1, cofilin2, and destrin. The mechanism of the activation is to phosphorylates cofilin on serine 3 and inactivates its actin-severing activity, and altering the rate of actin depolymerization. LIMKs can function in both cytoplasm and nucleus and are expressed in all tissues. Both LIMK1 and LIMK2 can act in the nucleus to suppress Rac/Cdc42-dependent cyclin D1 expression. However, LIMK1 and LIMk2 have different cellular locations. While LIMK1 localizes mainly at focal adhesions, LIMK2 is found in cytoplasmic punctae, suggesting that they may have different cellular functions. The LIM domains of LIMK have been shown to play an important role in regulating kinase activity and likely also contribute to LIMK function by acting as sites of protein-to-protein interactions. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188751 [Multi-domain]  Cd Length: 54  Bit Score: 39.66  E-value: 1.33e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 530376195 217 CDSCEKYITGRVLEAGEKHYHPSCALCVRCGQMFAEGE 254
Cdd:cd09365    1 CHGCSQIITGPVMVAGDHKFHPECFSCSSCKAFIGDGD 38
LIM2_ENH cd09457
The second LIM domain of the Enigma Homolog (ENH) family; The second LIM domain of the Enigma ...
29-80 1.58e-04

The second LIM domain of the Enigma Homolog (ENH) family; The second LIM domain of the Enigma Homolog (ENH) family: ENH was initially identified in rat brain. Same as enigma, it contains three LIM domains at the C-terminus and a PDZ domain at N-terminus. ENH is implicated in signal transduction processes involving protein kinases. It has also been shown that ENH interacts with protein kinase D1 (PKD1) via its LIM domains and forms a complex with PKD1 and the alpha1C subunit of cardiac L-type voltage-gated calcium channel in rat neonatal cardiomyocytes. The N-terminal PDZ domain interacts with alpha-actinin at the Z-line. ENH is expressed in multiple tissues, such as skeletal muscle, heart, bone, and brain. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188841 [Multi-domain]  Cd Length: 52  Bit Score: 39.63  E-value: 1.58e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530376195  29 CNTCGNVCKGEVLRVQDKYFHIKCFVCKACGCDLAEGGFFVRQGEYICTLDY 80
Cdd:cd09457    1 CGRCQRKILGEVINALKQTWHVSCFVCVACHNPIRNNVFHLEDGEPYCETDY 52
LIM1_PINCH cd09331
The first LIM domain of protein PINCH; The first LIM domain of paxillin: Paxillin is an ...
88-124 1.71e-04

The first LIM domain of protein PINCH; The first LIM domain of paxillin: Paxillin is an adaptor protein, which recruits key components of the signal-transduction machinery to specific sub-cellular locations to respond to environmental changes rapidly. The C-terminal region of paxillin contains four LIM domains which target paxillin to focal adhesions, presumably through a direct association with the cytoplasmic tail of beta-integrin. The N-terminal of paxillin is leucine-rich LD-motifs. Paxillin is found at the interface between the plasma membrane and the actin cytoskeleton. The binding partners of paxillin are diverse and include protein tyrosine kinases, such as Src and FAK, structural proteins, such as vinculin and actopaxin, and regulators of actin organization. Paxillin recruits these proteins to their function sites to control the dynamic changes in cell adhesion, cytoskeletal reorganization and gene expression. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188717  Cd Length: 59  Bit Score: 39.62  E-value: 1.71e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 530376195  88 CFSC-DQFIEGE-VVSALGKTYHPDCFVCAVCRLPFPPG 124
Cdd:cd09331    1 CERCrEGFEPDEkIVNSNGELYHEQCFVCAQCFQPFPDG 39
LIM_CLP36 cd09448
This family represents the LIM domain of CLP36; This family represents the LIM domain of CLP36. ...
29-76 1.78e-04

This family represents the LIM domain of CLP36; This family represents the LIM domain of CLP36. CLP36 has also been named as CLIM1, Elfin, or PDLIM1. CLP36 contains a C-terminal LIM domain and an N-terminal PDZ domain. CLP36 is highly expressed in heart and is present in many other tissues including lung, liver, spleen, and blood. CLP36 has been implicated in many processes including hypoxia and regulation of actin stress fibers. CLP36 co-localizes with alpha-actinin-2 at the Z-lines in myocardium. In addition, CLP36 binds to alpha-actinin-1 and alpha-actinin-4, and associates with F-actin filaments and stress fibers. CLP36 might be involved in not only the function of sarcomeres in muscle cells, but also in actin stress fiber-mediated cellular processes, such as cell shape, migration, polarit, and cytokinesis in non-muscle cells. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188832  Cd Length: 52  Bit Score: 39.52  E-value: 1.78e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 530376195  29 CNTCGNVCKGEVLRVQDKYFHIKCFVCKACGCDLAEGGFFVRQGEYIC 76
Cdd:cd09448    1 CDKCGSGIVGVFVKIRDKPRHPECYVCTDCGTNLKQKGHFFVEDQIYC 48
LIM2_Enigma cd09456
The second LIM domain of Enigma; The second LIM domain of Enigma: Enigma was initially ...
29-80 2.01e-04

The second LIM domain of Enigma; The second LIM domain of Enigma: Enigma was initially characterized in humans as a protein containing three LIM domains at the C-terminus and a PDZ domain at N-terminus. The third LIM domain specifically interacts with the insulin receptor and the second LIM domain interacts with the receptor tyrosine kinase Ret and the adaptor protein APS. Thus Enigma is implicated in signal transduction processes, such as mitogenic activity, insulin related actin organization, and glucose metabolism. Enigma is expressed in multiple tissues, such as skeletal muscle, heart, bone and brain. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188840 [Multi-domain]  Cd Length: 52  Bit Score: 39.21  E-value: 2.01e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530376195  29 CNTCGNVCKGEVLRVQDKYFHIKCFVCKACGCDLAEGGFFVRQGEYICTLDY 80
Cdd:cd09456    1 CAKCKKKITGEIMHALKMTWHVHCFTCAACKTPIRNRAFYMEEGAPYCERDY 52
LIM_CRIP cd09478
The LIM domain of Cysteine-Rich Intestinal Protein (CRIP); The LIM domain of Cysteine-Rich ...
158-205 2.14e-04

The LIM domain of Cysteine-Rich Intestinal Protein (CRIP); The LIM domain of Cysteine-Rich Intestinal Protein (CRIP): CRIP is a short protein with only one LIM domain. CRIP gene is developmentally regulated and can be induced by glucocorticoid hormones during the first three postnatal weeks. The domain shows close sequence homology to LIM domain of thymus LIM protein. However, unlike the TLP proteins which have two LIM domains, the members of this family have only one LIM domain. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188862  Cd Length: 54  Bit Score: 39.09  E-value: 2.14e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 530376195 158 CGGCGTEIKNGQALVALDKHWHLGCFKCKSCGKLLNA-EYISKDGLPYC 205
Cdd:cd09478    1 CPKCDKEVYFAERVTSLGKDWHRPCLKCEKCGKTLTPgSHAEHDGKPYC 49
LIM2_LIMK2 cd09465
The second LIM domain of LIMK2 (LIM domain Kinase 2); The second LIM domain of LIMK2 (LIM ...
212-254 2.14e-04

The second LIM domain of LIMK2 (LIM domain Kinase 2); The second LIM domain of LIMK2 (LIM domain Kinase 2): LIMK2 is a member of the LIMK protein family, which comprises LIMK1 and LIMK2. LIMK contains two LIM domains, a PDZ domain, and a kinase domain. LIMK is involved in the regulation of actin polymerization and microtubule disassembly. LIMK influences architecture of the actin cytoskeleton by regulating the activity of the cofilin family proteins cofilin1, cofilin2, and destrin. The mechanism of the activation is to phosphorylates cofilin on serine 3 and inactivates its actin-severing activity, altering the rate of actin depolymerisation. LIMK activity is activated by phosphorylation of a threonine residue within the activation loop of the kinase by p21-activated kinases 1 and 4 and by Rho kinase. LIMKs can function in both cytoplasm and nucleus. Both LIMK1 and LIMK2 can act in the nucleus to suppress Rac/Cdc42-dependent cyclin D1 expression. LIMK2 is expressed in all tissues. While LIMK1 localizes mainly at focal adhesions, LIMK2 is found in cytoplasmic punctae, suggesting that they may have different cellular functions. The activity of LIM kinase 2 to regulate cofilin phosphorylation is inhibited by the direct binding of Par-3. LIMK2 activation promotes cell cycle progression. The phenotype of Limk2 knockout mice shows a defect in spermatogenesis. The LIM domains have been shown to play an important role in regulating kinase activity and likely also contribute to LIMK function by acting as sites of protein-to-protein interactions. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188849 [Multi-domain]  Cd Length: 59  Bit Score: 39.53  E-value: 2.14e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 530376195 212 KFGIRCDSCEKYITGRVLEAGEKHYHPSCALCVRCGQMFAEGE 254
Cdd:cd09465    1 KFGELCHGCSLLMTGPAMVAGEYKYHPECFACMSCKVIIEDGD 43
LIM2_LPP cd09354
The second LIM domain of lipoma preferred partner (LPP); The second LIM domain of lipoma ...
217-248 2.45e-04

The second LIM domain of lipoma preferred partner (LPP); The second LIM domain of lipoma preferred partner (LPP): LPP is a member of the zyxin LIM protein family and contains three LIM zinc-binding domains at the C-terminal and proline-rich region at the N-terminal. LPP initially identified as the most frequent translocation partner of HMGA2 (High Mobility Group A2) in a subgroup of benign tumors of adipose tissue (lipomas). It was also shown to be rearranged in a number of other soft tissues, as well as in a case of acute monoblastic leukemia. In addition to its involvement in tumors, LPP was inedited as a smooth muscle restricted LIM protein that plays an important role in SMC migration. LPP is localized at sites of cell adhesion, cell-cell contacts and transiently in the nucleus. In nucleus, it acts as a coactivator for the ETS domain transcription factor PEA3. In addition to PEA3, it interacts with alpha-actinin,vasodilator stimulated phosphoprotein (VASP),Palladin, and Scrib. The LIM domains are the main focal adhesion targeting elements and that the proline- rich region, which harbors binding sites for alpha-actinin and vasodilator- stimulated phosphoprotein (VASP), has a weak targeting capacity. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188740 [Multi-domain]  Cd Length: 60  Bit Score: 39.06  E-value: 2.45e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 530376195 217 CDSCEKYITGRVLEAGEKHYHPSCALCVRCGQ 248
Cdd:cd09354    1 CSVCSKPILDRILRATGKPYHPQCFTCVVCGK 32
LIM2_PINCH cd09332
The second LIM domain of protein PINCH; The second LIM domain of protein PINCH: PINCH plays a ...
29-76 2.46e-04

The second LIM domain of protein PINCH; The second LIM domain of protein PINCH: PINCH plays a pivotal role in the assembly of focal adhesions (FAs), regulating diverse functions in cell adhesion, growth, and differentiation through LIM-mediated protein-protein interactions. PINCH comprises an array of five LIM domains that interact with integrin-linked kinase (ILK), Nck2 (also called Nckbeta or Grb4) and other interaction partners. These interactions are essential for triggering the FA assembly and for relaying diverse mechanical and biochemical signals between Cell-extracellular matrix and the actin cytoskeleton. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188718 [Multi-domain]  Cd Length: 52  Bit Score: 38.86  E-value: 2.46e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 530376195  29 CNTCGNVCKGEVLRVQDKYFHIKCFVCKACGCDLAEGGFFVRQGEYIC 76
Cdd:cd09332    1 CGKCGEFVIGRVIKAMNNNWHPDCFRCEICNKELADIGFVKNAGRALC 48
LIM1_Paxillin_like cd09336
The first LIM domain of the paxillin like protein family; The first LIM domain of the paxillin ...
29-81 2.48e-04

The first LIM domain of the paxillin like protein family; The first LIM domain of the paxillin like protein family: This family consists of paxillin, leupaxin, Hic-5 (ARA55), and other related proteins. There are four LIM domains in the C-terminal of the proteins and leucine-rich LD-motifs in the N-terminal region. Members of this family are adaptor proteins to recruit key components of signal-transduction machinery to specific sub-cellular locations. Paxillin is found at the interface between the plasma membrane and the actin cytoskeleton. Paxillin serves as a platform for the recruitment of numerous regulatory and structural proteins that together control the dynamic changes in cell adhesion, cytoskeletal reorganization and gene expression that are necessary for cell migration and survival. Leupaxin is a cytoskeleton adaptor protein, which is preferentially expressed in hematopoietic cells. It associates with focal adhesion kinases PYK2 and pp125FAK and identified to be a component of the osteoclast pososomal signaling complex. Hic-5 controls cell proliferation, migration and senescence by functioning as coactivator for steroid receptors such as androgen receptor, glucocorticoid receptor and progesterone receptor. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 259830 [Multi-domain]  Cd Length: 53  Bit Score: 38.91  E-value: 2.48e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530376195  29 CNTCGNVCKGEVLRVQDKYFHIKCFVCKACGCDLAEGGFFVRQGEYICTLDYQ 81
Cdd:cd09336    1 CAACNKPIVGQVVTALGKTWHPEHFVCVHCQTELGTSNFFERDGKPYCEKDYH 53
LIM_DA1 cd09396
The Lim domain of DA1; The Lim domain of DA1: DA1 contains one copy of LIM domain and a domain ...
88-122 2.57e-04

The Lim domain of DA1; The Lim domain of DA1: DA1 contains one copy of LIM domain and a domain of unknown function. DA1 is predicted as an ubiquitin receptor, which sets final seed and organ size by restricting the period of cell proliferation. The LIM domain is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188782 [Multi-domain]  Cd Length: 53  Bit Score: 38.77  E-value: 2.57e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 530376195  88 CFSCDQFIE-GEVVSALGKTYHPDCFVCAVCRLPFP 122
Cdd:cd09396    1 CAGCKSEIGhGRFLSALGAVWHPECFRCHACRKPIA 36
LIM1_Zyxin cd09349
The first LIM domain of Zyxin; The first LIM domain of Zyxin: Zyxin exhibits three copies of ...
157-209 2.59e-04

The first LIM domain of Zyxin; The first LIM domain of Zyxin: Zyxin exhibits three copies of the LIM domain, an extensive proline-rich domain and a nuclear export signal. Localized at sites of cell substratum adhesion in fibroblasts, Zyxin interacts with alpha-actinin, members of the cysteine-rich protein (CRP) family, proteins that display Src homology 3 (SH3) domains and Ena/VASP family members. Zyxin and its partners have been implicated in the spatial control of actin filament assembly as well as in pathways important for cell differentiation. In addition to its functions at focal adhesion plaques, recent work has shown that zyxin moves from the sites of cell contacts to the nucleus, where it directly participates in the regulation of gene expression. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188735 [Multi-domain]  Cd Length: 87  Bit Score: 39.84  E-value: 2.59e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 530376195 157 SCGGCGTEIKNGQALV-ALDKHWHLGCFKCKSCGKLLNA-EYISKDGLPYCEADY 209
Cdd:cd09349   33 LCGICGQPLSRTQPAVrALGHLFHVTCFTCHQCEQQLQGqQFYSLEGKPYCEECY 87
LIM2_PINCH cd09332
The second LIM domain of protein PINCH; The second LIM domain of protein PINCH: PINCH plays a ...
88-120 2.69e-04

The second LIM domain of protein PINCH; The second LIM domain of protein PINCH: PINCH plays a pivotal role in the assembly of focal adhesions (FAs), regulating diverse functions in cell adhesion, growth, and differentiation through LIM-mediated protein-protein interactions. PINCH comprises an array of five LIM domains that interact with integrin-linked kinase (ILK), Nck2 (also called Nckbeta or Grb4) and other interaction partners. These interactions are essential for triggering the FA assembly and for relaying diverse mechanical and biochemical signals between Cell-extracellular matrix and the actin cytoskeleton. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188718 [Multi-domain]  Cd Length: 52  Bit Score: 38.86  E-value: 2.69e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 530376195  88 CFSCDQFIEGEVVSALGKTYHPDCFVCAVCRLP 120
Cdd:cd09332    1 CGKCGEFVIGRVIKAMNNNWHPDCFRCEICNKE 33
LIM2_CRP cd09403
The second LIM domain of Cysteine Rich Protein (CRP); The second LIM domain of Cysteine Rich ...
158-209 2.78e-04

The second LIM domain of Cysteine Rich Protein (CRP); The second LIM domain of Cysteine Rich Protein (CRP): Cysteine-rich proteins (CRPs) are characterized by the presence of two LIM domains linked to a short glycine-rich repeats (GRRs). The CRP family members include CRP1, CRP2, CRP3/MLP. CRP1, CRP2 and CRP3 share a conserved nuclear targeting signal (K/R-K/R-Y-G-P-K), which supports the fact that these proteins function not only in the cytoplasm but also in the nucleus. CRPs control regulatory pathways during cellular differentiation, and involve in complex transcription control, and the organization as well as the arrangement of the myofibrillar/cytoskeletal network. It is evident that CRP1, CRP2, and CRP3/MLP are involved in promoting protein assembly along the actin-based cytoskeleton. Although members of the CRP family share common binding partners, they are also capable of recognizing different and specific targets. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residu es, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188787  Cd Length: 54  Bit Score: 38.71  E-value: 2.78e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530376195 158 CGGCGTEIKNGQALVALDKHWHLGCFKCKSCGKLLNAEYIS-KDGLPYCEADY 209
Cdd:cd09403    1 CPRCGKSVYAAEKIIGAGKPWHKNCFRCAKCGKSLESTTLAdKDGEIYCKGCY 53
LIM1_LPP cd09351
The first LIM domain of lipoma preferred partner (LPP); The first LIM domain of lipoma ...
158-209 3.64e-04

The first LIM domain of lipoma preferred partner (LPP); The first LIM domain of lipoma preferred partner (LPP): LPP is a member of the zyxin LIM protein family and contains three LIM zinc-binding domains at the C-terminal and proline-rich region at the N-terminal. LPP initially identified as the most frequent translocation partner of HMGA2 (High Mobility Group A2) in a subgroup of benign tumors of adipose tissue (lipomas). It was also shown to be rearranged in a number of other soft tissues, as well as in a case of acute monoblastic leukemia. In addition to its involvement in tumors, LPP was inedited as a smooth muscle restricted LIM protein that plays an important role in SMC migration. LPP is localized at sites of cell adhesion, cell-cell contacts and transiently in the nucleus. In nucleus, it acts as a coactivator for the ETS domain transcription factor PEA3. In addition to PEA3, it interacts with alpha-actinin,vasodilator stimulated phosphoprotein (VASP),Palladin, and Scrib. The LIM domains are the main focal adhesion targeting elements and that the proline- rich region, which harbors binding sites for alpha-actinin and vasodilator- stimulated phosphoprotein (VASP), has a weak targeting capacity. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188737 [Multi-domain]  Cd Length: 54  Bit Score: 38.56  E-value: 3.64e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530376195 158 CGGCGTEIKN-GQALVALDKHWHLGCFKCKSCGKLLNAE-YISKDGLPYCEADY 209
Cdd:cd09351    1 CVKCGEKVLGeGSGCTAMDQVYHISCFTCHQCQINLQGKpFYALDGKPYCEEDY 54
LIM2_ENH cd09457
The second LIM domain of the Enigma Homolog (ENH) family; The second LIM domain of the Enigma ...
88-120 3.84e-04

The second LIM domain of the Enigma Homolog (ENH) family; The second LIM domain of the Enigma Homolog (ENH) family: ENH was initially identified in rat brain. Same as enigma, it contains three LIM domains at the C-terminus and a PDZ domain at N-terminus. ENH is implicated in signal transduction processes involving protein kinases. It has also been shown that ENH interacts with protein kinase D1 (PKD1) via its LIM domains and forms a complex with PKD1 and the alpha1C subunit of cardiac L-type voltage-gated calcium channel in rat neonatal cardiomyocytes. The N-terminal PDZ domain interacts with alpha-actinin at the Z-line. ENH is expressed in multiple tissues, such as skeletal muscle, heart, bone, and brain. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188841 [Multi-domain]  Cd Length: 52  Bit Score: 38.47  E-value: 3.84e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 530376195  88 CFSCDQFIEGEVVSALGKTYHPDCFVCAVCRLP 120
Cdd:cd09457    1 CGRCQRKILGEVINALKQTWHVSCFVCVACHNP 33
LIM2_Lhx1_Lhx5 cd09375
The second LIM domain of Lhx1 (also known as Lim1) and Lhx5; The second LIM domain of Lhx1 ...
40-80 3.96e-04

The second LIM domain of Lhx1 (also known as Lim1) and Lhx5; The second LIM domain of Lhx1 (also known as Lim1) and Lhx5. Lhx1 and Lhx5 are closely related members of LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. Lhx1 is required for regulating the vertebrate head organizer, the nervous system, and female reproductive tract development. During embryogenesis in the mouse, Lhx1 is expressed early in mesodermal tissue, then later during urogenital, kidney, liver, and nervous system development. In the adult, expression is restricted to the kidney and brain. A mouse embryos with Lhx1 gene knockout cannot grow normal anterior head structures, kidneys, and gonads, but with normally developed trunk and tail morphology. In the developing nervous system, Lhx1 is required to direct the trajectories of motor axons in the limb. Lhx1 null female mice lack the oviducts and uterus. Lhx5 protein may play complementary or overlapping roles with Lhx1. The expression of Lhx5 in the anterior portion of the mouse neural tube suggests a role in patterning of the forebrain. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188761  Cd Length: 56  Bit Score: 38.50  E-value: 3.96e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 530376195  40 VLRVQDKYFHIKCFVCKACGCDLAEGG--FFVRQGEYICTLDY 80
Cdd:cd09375   14 VRRARDKVFHLNCFTCMVCRKQLSTGEelYILDENKFICKEDY 56
LIM_Mical_like_2 cd09445
This domain belongs to the LIM domain family which are found on Mical (molecule interacting ...
158-205 4.52e-04

This domain belongs to the LIM domain family which are found on Mical (molecule interacting with CasL) like proteins; The LIM domain on proteins of unknown function: This domain belongs to the LIM domain family which are found on Mical (molecule interacting with CasL)-like proteins. Known members of the Mical-like family includes single LIM domain containing proteins, Mical (molecule interacting with CasL), pollen specific protein SF3, Eplin, xin actin-binding repeat-containing protein 2 (XIRP2), and Ltd-1. The members of this family function mainly at the cytoskeleton and focal adhesions. They interact with transcription factors or other signaling molecules to play roles in muscle development, neuronal differentiation, cell growth, and mobility. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188829 [Multi-domain]  Cd Length: 53  Bit Score: 38.21  E-value: 4.52e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 530376195 158 CGGCGTEIKNGQALVALDKHWHLGCFKCKSCGKLLNAE-YISKDGLPYC 205
Cdd:cd09445    1 CRSCGKPVYKMEEIIAEKHIYHKNCFRCKDCNKQLKVDnYQSHEGNLYC 49
LIM_N_RAP cd09446
The LIM domain of N-RAP; The LIM domain of N-RAP: N-RAP is a muscle-specific protein ...
158-207 5.11e-04

The LIM domain of N-RAP; The LIM domain of N-RAP: N-RAP is a muscle-specific protein concentrated at myotendinous junctions in skeletal muscle and intercalated disks in cardiac muscle. LIM domain is found at the N-terminus of N-RAP and the C-terminal of N-RAP contains a region with multiple of nebulin repeats. N-RAP functions as a scaffolding protein that organizes alpha-actinin and actin into symmetrical I-Z-I structures in developing myofibrils. Nebulin repeat is known as actin binding domain. The N-RAP is hypothesized to form antiparallel dimerization via its LIM domain. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188830  Cd Length: 53  Bit Score: 37.98  E-value: 5.11e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 530376195 158 CGGCGTEIKNGQALVALDKHWHLGCFKCKSCGKLLNA-EYISKDGLPYCEA 207
Cdd:cd09446    1 CARCGYGVYPAEKINCIDQTWHKACFHCEVCKMMLTVnNFVSHQKKPYCQA 51
LIM1_Paxillin cd09405
The first LIM domain of paxillin; The first LIM domain of paxillin: Paxillin is an adaptor ...
88-118 5.71e-04

The first LIM domain of paxillin; The first LIM domain of paxillin: Paxillin is an adaptor protein, which recruits key components of the signal-transduction machinery to specific sub-cellular locations to respond to environmental changes rapidly. The C-terminal region of paxillin contains four LIM domains which target paxillin to focal adhesions, presumably through a direct association with the cytoplasmic tail of beta-integrin. The N-terminal of paxillin is leucine-rich LD-motifs. Paxillin is found at the interface between the plasma membrane and the actin cytoskeleton. The binding partners of paxillin are diverse and include protein tyrosine kinases, such as Src and FAK, structural proteins, such as vinculin and actopaxin, and regulators of actin organization. Paxillin recruits these proteins to their function sites to control the dynamic changes in cell adhesion, cytoskeletal reorganization and gene expression. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight cons erved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188789 [Multi-domain]  Cd Length: 54  Bit Score: 38.07  E-value: 5.71e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 530376195  88 CFSCDQFIEGEVVSALGKTYHPDCFVCAVCR 118
Cdd:cd09405    2 CGACKKPIAGQVVTAMGKTWHPEHFVCTHCQ 32
LIM2_CRP3 cd09482
The second LIM domain of Cysteine Rich Protein 3 (CRP3/MLP); The second LIM domain of Cysteine ...
158-209 5.92e-04

The second LIM domain of Cysteine Rich Protein 3 (CRP3/MLP); The second LIM domain of Cysteine Rich Protein 3 (CRP3/MLP): Cysteine-rich proteins (CRPs) are characterized by the presence of two LIM domains linked to short glycine-rich repeats (GRRs). The CRP family members include CRP1, CRP2, CRP3/MLP and TLPCRP1, CRP2 and CRP3 share a conserved nuclear targeting signal (K/R-K/R-Y-G-P-K), which supports the fact that these proteins function not only in the cytoplasm but also in the nucleus. CRPs control regulatory pathways during cellular differentiation, and involve in complex transcription circuits, and the organization as well as the arrangement of the myofibrillar/cytoskeletal network.CRP3 also called Muscle LIM Protein (MLP), which is a striated muscle-specific factor that enhances myogenic differentiation. The second LIM domain of CRP3/MLP interacts with cytoskeletal protein beta-spectrin. CRP3/MLP also interacts with the basic helix-loop-helix myogenic transcription factors MyoD, myogenin, and MRF4 thereby increasing their affinity for specific DNA regulatory elements. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188866 [Multi-domain]  Cd Length: 54  Bit Score: 38.07  E-value: 5.92e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530376195 158 CGGCGTEIKNGQALVALDKHWHLGCFKCKSCGKLLNAEYIS-KDGLPYCEADY 209
Cdd:cd09482    1 CPRCGKSVYAAEKVMGGGKPWHKTCFRCAICGKSLESTTVTdKDGELYCKVCY 53
LIM1_ENH cd09453
The first LIM domain of the Enigma Homolog (ENH) family; The first LIM domain of the Enigma ...
88-118 6.03e-04

The first LIM domain of the Enigma Homolog (ENH) family; The first LIM domain of the Enigma Homolog (ENH) family: ENH was initially identified in rat brain. Same as enigma, it contains three LIM domains at the C-terminus and a PDZ domain at N-terminus. ENH is implicated in signal transduction processes involving protein kinases. It has also been shown that ENH interacts with protein kinase D1 (PKD1) via its LIM domains and forms a complex with PKD1 and the alpha1C subunit of cardiac L-type voltage-gated calcium channel in rat neonatal cardiomyocytes. The N-terminal PDZ domain interacts with alpha-actinin at the Z-line. ENH is expressed in multiple tissues, such as skeletal muscle, heart, bone, and brain. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188837 [Multi-domain]  Cd Length: 52  Bit Score: 38.07  E-value: 6.03e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 530376195  88 CFSCDQFIEGEVVSALGKTYHPDCFVCAVCR 118
Cdd:cd09453    1 CATCNQVIRGPFLVALGKSWHPEEFNCAHCK 31
LIM2_Lhx1_Lhx5 cd09375
The second LIM domain of Lhx1 (also known as Lim1) and Lhx5; The second LIM domain of Lhx1 ...
158-209 6.17e-04

The second LIM domain of Lhx1 (also known as Lim1) and Lhx5; The second LIM domain of Lhx1 (also known as Lim1) and Lhx5. Lhx1 and Lhx5 are closely related members of LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. Lhx1 is required for regulating the vertebrate head organizer, the nervous system, and female reproductive tract development. During embryogenesis in the mouse, Lhx1 is expressed early in mesodermal tissue, then later during urogenital, kidney, liver, and nervous system development. In the adult, expression is restricted to the kidney and brain. A mouse embryos with Lhx1 gene knockout cannot grow normal anterior head structures, kidneys, and gonads, but with normally developed trunk and tail morphology. In the developing nervous system, Lhx1 is required to direct the trajectories of motor axons in the limb. Lhx1 null female mice lack the oviducts and uterus. Lhx5 protein may play complementary or overlapping roles with Lhx1. The expression of Lhx5 in the anterior portion of the mouse neural tube suggests a role in patterning of the forebrain. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188761  Cd Length: 56  Bit Score: 38.11  E-value: 6.17e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 530376195 158 CGGCGTEI-KNGQALVALDKHWHLGCFKCKSCGKLLNAE---YISKDGLPYCEADY 209
Cdd:cd09375    1 CAGCDQGIsPNDLVRRARDKVFHLNCFTCMVCRKQLSTGeelYILDENKFICKEDY 56
LIM1_Leupaxin cd09406
The first LIM domain of Leupaxin; The first LIM domain of Leupaxin: Leupaxin is a cytoskeleton ...
29-80 6.37e-04

The first LIM domain of Leupaxin; The first LIM domain of Leupaxin: Leupaxin is a cytoskeleton adaptor protein, which is preferentially expressed in hematopoietic cells. Leupaxin belongs to the paxillin focal adhesion protein family. Same as other members of the family, it has four leucine-rich LD-motifs in the N-terminus and four LIM domains in the C-terminus. It may function in cell type-specific signaling by associating with interaction partners PYK2, FAK, PEP and p95PKL. When expressed in human leukocytic cells, leupaxin significantly suppressed integrin-mediated cell adhesion to fibronectin and the tyrosine phosphorylation of paxillin. These findings indicate that leupaxin may negatively regulate the functions of paxillin during integrin signaling. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188790 [Multi-domain]  Cd Length: 55  Bit Score: 37.93  E-value: 6.37e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530376195  29 CNTCGNVCKGEVLRVQDKYFHIKCFVCKACGCDLAEGGFFVRQGEYICTLDY 80
Cdd:cd09406    3 CASCQKPIAGQVVTALGQTWHPEHFVCCQCGKELGSRPFFERNGQAYCEEDY 54
LIM2_Zyxin cd09353
The second LIM domain of Zyxin; The second LIM domain of Zyxin: Zyxin exhibits three copies of ...
217-246 6.39e-04

The second LIM domain of Zyxin; The second LIM domain of Zyxin: Zyxin exhibits three copies of the LIM domain, an extensive proline-rich domain and a nuclear export signal. Localized at sites of cellsubstratum adhesion in fibroblasts, Zyxin interacts with alpha-actinin, members of the cysteine-rich protein (CRP) family, proteins that display Src homology 3 (SH3) domains and Ena/VASP family members. Zyxin and its partners have been implicated in the spatial control of actin filament assembly as well as in pathways important for cell differentiation. In addition to its functions at focal adhesion plaques, recent work has shown that zyxin moves from the sites of cell contacts to the nucleus, where it directly participates in the regulation of gene expression. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors o r scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188739 [Multi-domain]  Cd Length: 60  Bit Score: 37.99  E-value: 6.39e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 530376195 217 CDSCEKYITGRVLEAGEKHYHPSCALCVRC 246
Cdd:cd09353    1 CAVCDQKITDRMLKATGKSYHPQCFTCVVC 30
LIM_CRP_like cd09326
The LIM domains of Cysteine Rich Protein (CRP) family; The LIM domains of Cysteine Rich ...
158-209 6.89e-04

The LIM domains of Cysteine Rich Protein (CRP) family; The LIM domains of Cysteine Rich Protein (CRP) family: Cysteine-rich proteins (CRPs) are characterized by the presence of two LIM domains linked to a short glycine-rich repeats (GRRs). The known CRP family members include CRP1, CRP2, and CRP3/MLP. CRP1, CRP2 and CRP3 share a conserved nuclear targeting signal (K/R-K/R-Y-G-P-K), which supports the fact that these proteins function not only in the cytoplasm but also in the nucleus. CRPs control regulatory pathways during cellular differentiation, and involve in complex transcription control, and the organization as well as the arrangement of the myofibrillar/cytoskeletal network. CRP1, CRP2, and CRP3/MLP are involved in promoting protein assembly along the actin-based cytoskeleton. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188712  Cd Length: 53  Bit Score: 37.57  E-value: 6.89e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530376195 158 CGGCGTEIKNGQALVALDKHWHLGCFKCKSCGKLLNAEYIS-KDGLPYCEADY 209
Cdd:cd09326    1 CPRCGKSVYAAEEVIAAGKSWHKSCFTCAVCNKRLDSTTLAeHDGEIYCKSCY 53
LIM2_LIMK1 cd09464
The second LIM domain of LIMK1 (LIM domain Kinase 1); The second LIM domain of LIMK1 (LIM ...
217-258 7.02e-04

The second LIM domain of LIMK1 (LIM domain Kinase 1); The second LIM domain of LIMK1 (LIM domain Kinase 1): LIMK1 belongs to the LIMK protein family, which comprises LIMK1 and LIMK2. LIMK contains two LIM domains, a PDZ domain, and a kinase domain. LIMK is involved in the regulation of actin polymerization and microtubule disassembly. LIMK influences architecture of the actin cytoskeleton by regulating the activity of the cofilin family proteins cofilin1, cofilin2, and destrin. The mechanism of the activation is to phosphorylates cofilin on serine 3 and inactivates its actin-severing activity, and altering the rate of actin depolymerization. LIMKs can function in both cytoplasm and nucleus. Both LIMK1 and LIMK2 can act in the nucleus to suppress Rac/Cdc42-dependent cyclin D1 expression. LIMK1 is expressed in all tissues and is localized to focal adhesions in the cell. LIMK1 can form homodimers upon binding of HSP90 and is activated by Rho effector Rho kinase and MAPKAPK2. LIMK1 is important for normal central nervous system development, and its deletion has been implicated in the development of the human genetic disorder Williams syndrome. Moreover, LIMK1 up-regulates the promoter activity of urokinase type plasminogen activator and induces its mRNA and protein expression in breast cancer cells. The LIM domains have been shown to play an important role in regulating kinase activity and likely also contribute to LIMK function by acting as sites of protein-to-protein interactions. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188848  Cd Length: 55  Bit Score: 37.93  E-value: 7.02e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 530376195 217 CDSCEKYIT-GRVLEAGEKHYHPSCALCVRCGQMFAEGEEMYL 258
Cdd:cd09464    1 CHGCSETITtGLVMVAGEQKYHPECFSCLRCGAFIGDGDTYAL 43
LIM1_Enigma_like_1 cd09455
The first LIM domain of an Enigma subfamily with unknown function; The first LIM domain of an ...
88-120 7.92e-04

The first LIM domain of an Enigma subfamily with unknown function; The first LIM domain of an Enigma subfamily with unknown function: The Enigma LIM domain family is comprised of three characterized members: Enigma, ENH and Cypher (mouse)/ZASP (human). These subfamily members contain a single PDZ domain at the N-terminus and three LIM domains at the C-terminus. They serve as adaptor proteins, where the PDZ domain tethers the protein to the cytoskeleton and the LIM domains, recruit signaling proteins to implement corresponding functions. The members of the Enigma family have been implicated in regulating or organizing cytoskeletal structure, as well as involving multiple signaling pathways. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188839  Cd Length: 54  Bit Score: 37.44  E-value: 7.92e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 530376195  88 CFSCDQFIEGEVVSALGKTYHPDCFVCA--VCRLP 120
Cdd:cd09455    1 CESCNQQIRGPFITALGKIWCPDHFICAnaSCRRP 35
LIM1_Paxillin cd09405
The first LIM domain of paxillin; The first LIM domain of paxillin: Paxillin is an adaptor ...
28-81 7.98e-04

The first LIM domain of paxillin; The first LIM domain of paxillin: Paxillin is an adaptor protein, which recruits key components of the signal-transduction machinery to specific sub-cellular locations to respond to environmental changes rapidly. The C-terminal region of paxillin contains four LIM domains which target paxillin to focal adhesions, presumably through a direct association with the cytoplasmic tail of beta-integrin. The N-terminal of paxillin is leucine-rich LD-motifs. Paxillin is found at the interface between the plasma membrane and the actin cytoskeleton. The binding partners of paxillin are diverse and include protein tyrosine kinases, such as Src and FAK, structural proteins, such as vinculin and actopaxin, and regulators of actin organization. Paxillin recruits these proteins to their function sites to control the dynamic changes in cell adhesion, cytoskeletal reorganization and gene expression. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight cons erved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188789 [Multi-domain]  Cd Length: 54  Bit Score: 37.68  E-value: 7.98e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530376195  28 LCNTCGNVCKGEVLRVQDKYFHIKCFVCKACGCDLAEGGFFVRQGEYICTLDYQ 81
Cdd:cd09405    1 VCGACKKPIAGQVVTAMGKTWHPEHFVCTHCQEEIGSRNFFERDGQPYCEKDYH 54
LIM1_LMO1_LMO3 cd09388
The first LIM domain of LMO1 and LMO3 (LIM domain only protein 1 and 3); The first LIM domain ...
158-209 8.46e-04

The first LIM domain of LMO1 and LMO3 (LIM domain only protein 1 and 3); The first LIM domain of LMO1 and LMO3 (LIM domain only protein 1 and 3): LMO1 and LMO3 are highly homologous and belong to the LMO protein family. LMO1 and LMO3 are nuclear protein that plays important roles in transcriptional regulation and development. As LIM domains lack intrinsic DNA-binding activity, nuclear LMOs are involved in transcriptional regulation by forming complexes with other transcription factors or cofactors. For example, LMO1 interacts with the the bHLH domain of bHLH transcription factor, TAL1 (T-cell acute leukemia1)/SCL (stem cell leukemia) . LMO1 inhibits the expression of TAL1/SCL target genes. LMO3 facilitates p53 binding to its response elements, which suggests that LMO3 acts as a co-repressor of p53, suppressing p53-dependent transcriptional regulation. In addition, LMO3 interacts with neuronal transcription factor, HEN2, and acts as an oncogene in neuroblastoma. Another binding partner of LMO3 is calcium- and integrin-binding protein CIB, which binds via the second LIM domain (LIM2) of LMO3. One role of the CIB/LMO3 complex is to inhibit cell proliferation. Although LMO1 and LMO3 are highly homologous proteins, they play different roles in the regulation of the pituitary glycoprotein hormone alpha-subunit (alpha GSU) gene. Alpha GSU promoter activity was markedly repressed by LMO1 but activated by LMO3. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188774  Cd Length: 55  Bit Score: 37.53  E-value: 8.46e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 530376195 158 CGGCGTEIKNGQALVALDKHWHLGCFKCKSC----GKLLNAEYiSKDGLPYCEADY 209
Cdd:cd09388    1 CAGCNRKIKDRYLLKALDQYWHEDCLKCACCdcrlGEVGSTLY-TKANLILCRRDY 55
LIM4_Paxillin cd09411
The fourth LIM domain of Paxillin; The fourth LIM domain of Paxillin: Paxillin is an adaptor ...
88-139 8.47e-04

The fourth LIM domain of Paxillin; The fourth LIM domain of Paxillin: Paxillin is an adaptor protein, which recruits key components of the signal-transduction machinery to specific sub-cellular locations to respond to environmental changes rapidly. The C-terminal region of paxillin contains four LIM domains which target paxillin to focal adhesions, presumably through a direct association with the cytoplasmic tail of beta-integrin. The N-terminal of paxillin is leucine-rich LD-motifs. Paxillin is found at the interface between the plasma membrane and the actin cytoskeleton. The binding partners of paxillin are diverse and include protein tyrosine kinases, such as Src and FAK, structural proteins, such as vinculin and actopaxin, and regulators of actin organization. Paxillin recruits these proteins to their function sites to control the dynamic changes in cell adhesion, cytoskeletal reorganization and gene expression. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188795 [Multi-domain]  Cd Length: 52  Bit Score: 37.62  E-value: 8.47e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530376195  88 CFSCDQFIEGEVVSALGKTYHPDCFVCAVCRLPFPPGDRVTFNGKEcMCQKC 139
Cdd:cd09411    1 CSGCQKPITGRCITAMGKKFHPEHFVCAFCLKQLNKGTFKEQNDKP-YCHNC 51
LIM2_Lhx2_Lhx9 cd09377
The second LIM domain of Lhx2 and Lhx9 family; The second LIM domain of Lhx2 and Lhx9 family: ...
154-209 8.68e-04

The second LIM domain of Lhx2 and Lhx9 family; The second LIM domain of Lhx2 and Lhx9 family: Lhx2 and Lhx9 are highly homologous LHX regulatory proteins. They belong to the LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. Although Lhx2 and Lhx9 are highly homologous, they seems to play regulatory roles in different organs. In animals, Lhx2 plays important roles in eye, cerebral cortex, limb, the olfactory organs, and erythrocyte development. Lhx2 gene knockout mice exhibit impaired patterning of the cortical hem and the telencephalon of the developing brain, and a lack of development in olfactory structures. Lhx9 is expressed in several regions of the developing mouse brain, the spinal cord, the pancreas, in limb mesenchyme, and in the urogenital region. Lhx9 plays critical roles in gonad development. Homozygous mice lacking functional Lhx9 alleles exhibit numerous urogenital defects, such as gonadal agenesis, infertility, and undetectable levels of testosterone and estradiol coupled with high FSH levels. Lhx9 null mice are phenotypically female, even those that are genotypically male. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188763  Cd Length: 59  Bit Score: 37.64  E-value: 8.68e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376195 154 GLRSCGGCGTEIkNGQALV--ALDKHWHLGCFKCKSCGKLLNA--EYISKDGLPYCEADY 209
Cdd:cd09377    1 SVKRCARCHLGI-SASELVmrARDLVFHLNCFTCATCNKPLTKgdHFGMRDGLVYCRLHY 59
LIM3_Leupaxin cd09410
The third LIM domain of Leupaxin; The third LIM domain of Leupaxin: Leupaxin is a cytoskeleton ...
88-132 9.86e-04

The third LIM domain of Leupaxin; The third LIM domain of Leupaxin: Leupaxin is a cytoskeleton adaptor protein, which is preferentially expressed in hematopoietic cells. Leupaxin belongs to the paxillin focal adhesion protein family. Same as other members of the family, it has four leucine-rich LD-motifs in the N-terminus and four LIM domains in the C-terminus. It may function in cell type-specific signaling by associating with interaction partners PYK2, FAK, PEP and p95PKL. When expressed in human leukocytic cells, leupaxin significantly suppressed integrin-mediated cell adhesion to fibronectin and the tyrosine phosphorylation of paxillin. These findings indicate that leupaxin may negatively regulate the functions of paxillin during integrin signaling. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188794 [Multi-domain]  Cd Length: 53  Bit Score: 37.11  E-value: 9.86e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 530376195  88 CFSCDQFIEGEVVSALGKTYHPDCFVCAVCRLPFPPGDRVTFNGK 132
Cdd:cd09410    1 CSGCGRPVKENYLSAANGVWHPECFVCSDCLKPFTDGSFFELDGR 45
LIM1_TLP cd09476
The first LIM domain of thymus LIM protein (TLP); The first LIM domain of thymus LIM protein ...
158-205 1.00e-03

The first LIM domain of thymus LIM protein (TLP); The first LIM domain of thymus LIM protein (TLP): TLP is the distant member of the CRP family of proteins. TLP has two isomers (TLP-A and TLP-B) and sharing approximately 30% with each of the three other CRPs. Like CRP1, CRP2 and CRP3/MLP, TLP has two LIM domains, connected by a flexible linker region. Unlike the CRPs, TLP lacks the nuclear targeting signal (K/R-K/R-Y-G-P-K) and is localized solely in the cytoplasm. TLP is specifically expressed in the thymus in a subset of cortical epithelial cells. TLP has a role in development of normal thymus and in controlling the development and differentiation of thymic epithelial cells. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188860  Cd Length: 54  Bit Score: 37.25  E-value: 1.00e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 530376195 158 CGGCGTEIKNGQALVALDKHWHLGCFKCKSCGKLLNA-EYISKDGLPYC 205
Cdd:cd09476    1 CPRCDKTVYFAEKVSSLGKNWHRFCLKCERCSKILSPgGHAEHDGKPYC 49
LIM2_FBLP-1 cd09372
The second LIM domain of the filamin-binding LIM protein-1 (FBLP-1); The second LIM domain of ...
29-80 1.17e-03

The second LIM domain of the filamin-binding LIM protein-1 (FBLP-1); The second LIM domain of the filamin-binding LIM protein-1 (FBLP-1): Fblp-1 contains a proline-rich domain near its N terminus and two LIM domains at its C terminus. FBLP-1 mRNA was detected in a variety of tissues and cells including platelets and endothelial cells. FBLP-1 binds to Filamins. The association between filamin B and FBLP-1 may play an unknown role in cytoskeletal function, cell adhesion, and cell motility. As in other LIM domains, this domain family is 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188758 [Multi-domain]  Cd Length: 53  Bit Score: 37.02  E-value: 1.17e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530376195  29 CNTCGNVCKGEVLRVQDKYFHIKCFVCKACGCDLAEGGFFV-RQGEYICTLDY 80
Cdd:cd09372    1 CAKCQGVITEHIIRALGKGYHPPCFTCVTCGRRIGDESFAVdEQNEVYCLDDY 53
LIM3_Enigma_like_1 cd09461
The third LIM domain of an Enigma subfamily with unknown function; The third LIM domain of an ...
158-207 1.18e-03

The third LIM domain of an Enigma subfamily with unknown function; The third LIM domain of an Enigma subfamily with unknown function: The Enigma LIM domain family is comprised of three characterized members: Enigma, ENH, and Cypher (mouse)/ZASP (human). These subfamily members contain a single PDZ domain at the N-terminus and three LIM domains at the C-terminus. They serve as adaptor proteins, where the PDZ domain tethers the protein to the cytoskeleton and the LIM domains, recruit signaling proteins to implement corresponding functions. The members of the enigma family have been implicated in regulating or organizing cytoskeletal structure, as well as involving multiple signaling pathways. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188845  Cd Length: 54  Bit Score: 37.15  E-value: 1.18e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530376195 158 CGGCGTEIKNGQALV-ALDKHWHLGCFKCKSCGKLLNAE-YISKDGLPYCEA 207
Cdd:cd09461    1 CVSCGFPIEAGDRWVeALNNNYHSQCFNCTRCNVNLEGQsFYAKGGRPFCKL 52
LIM1_LMO2 cd09384
The first LIM domain of LMO2 (LIM domain only protein 2); The first LIM domain of LMO2 (LIM ...
158-209 1.18e-03

The first LIM domain of LMO2 (LIM domain only protein 2); The first LIM domain of LMO2 (LIM domain only protein 2): LMO2 is a nuclear protein that plays important roles in transcriptional regulation and development. The two tandem LIM domains of LMO2 support the assembly of a crucial cell-regulatory complex by interacting with both the TAL1-E47 and GATA1 transcription factors to form a DNA-binding complex that is capable of transcriptional activation. LMOs have also been shown to be involved in oncogenesis. LMO1 and LMO2 are activated in T-cell acute lymphoblastic leukemia by distinct chromosomal translocations. LMO2 was also shown to be involved in erythropoiesis and is required for the hematopoiesis in the adult animals. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188770  Cd Length: 56  Bit Score: 37.14  E-value: 1.18e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 530376195 158 CGGCGTEIKNGQALVALDKHWHLGCFKCKSCGKLL---NAEYISKDGLPYCEADY 209
Cdd:cd09384    1 CGGCQQNIGDRYFLKAIDQYWHEDCLSCDLCGCRLgevGRRLYYKLGRKLCRRDY 55
LIM1_TRIP6 cd09350
The first LIM domain of Thyroid receptor-interacting protein 6 (TRIP6); The first LIM domain ...
158-209 1.48e-03

The first LIM domain of Thyroid receptor-interacting protein 6 (TRIP6); The first LIM domain of Thyroid receptor-interacting protein 6 (TRIP6): TRIP6 is a member of the zyxin LIM protein family and contains three LIM zinc-binding domains at the C-terminal. TRIP6 protein localizes to focal adhesion sites and along actin stress fibers. Recruitment of this protein to the plasma membrane occurs in a lysophosphatidic acid (LPA)-dependent manner. TRIP6 recruits a number of molecules involved in actin assembly, cell motility, survival and transcriptional control. The function of TRIP6 in cell motility is regulated by Src-dependent phosphorylation at a Tyr residue. The phosphorylation activates the coupling to the Crk SH2 domain, which is required for the function of TRIP6 in promoting lysophosphatidic acid (LPA)-induced cell migration. TRIP6 can shuttle to the nucleus to serve as a coactivator of AP-1 and NF-kappaB transcriptional factors. Moreover, TRIP6 can form a ternary complex with the NHERF2 PDZ protein and LPA2 receptor to regulate LPA-induced activation of ERK and AKT, rendering cells resistant to chemotherapy. Recent evidence shows that TRIP6 antagonizes Fas-Induced apoptosis by enhancing the antiapoptotic effect of LPA in cells. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188736  Cd Length: 54  Bit Score: 37.00  E-value: 1.48e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530376195 158 CGGCGTE-IKNGQALVALDKHWHLGCFKCKSCG-KLLNAEYISKDGLPYCEADY 209
Cdd:cd09350    1 CGRCGENvVGEGTGCTAMDQVFHVDCFTCMTCNgKLRGQPFYAVEKKAYCEPCY 54
LIM2_LMO4 cd09387
The second LIM domain of LMO4 (LIM domain only protein 4); The second LIM domain of LMO4 (LIM ...
29-79 1.57e-03

The second LIM domain of LMO4 (LIM domain only protein 4); The second LIM domain of LMO4 (LIM domain only protein 4): LMO4 is a nuclear protein that plays important roles in transcriptional regulation and development. LMO4 is involved in various functions in tumorigenesis and cellular differentiation. LMO4 proteins regulate gene expression by interacting with a wide variety of transcription factors and cofactors to form large transcription complexes. It can interact with Smad proteins, and associate with the promoter of the PAI-1 (plasminogen activator inhibitor-1) gene in a TGFbeta (transforming growth factor beta)-dependent manner. LMO4 can also form a complex with transcription regulator CREB (cAMP response element-binding protein) and interact with CLIM1 and CLIM2. In breast tissue, LMO4 interacts with multiple proteins, including the cofactor CtIP [CtBP (C-terminal binding protein)-interacting protein], the breast and ovarian tumor suppressor BRCA1 (breast-cancer susceptibility gene 1) and the LIM-domain-binding protein LDB1. Functionally, LMO4 is shown to repress BRCA1-mediated transcription activation, thus invoking a potential role for LMO4 as a negative regulator of BRCA1 in sporadic breast cancer. LMO4 also forms complex to both ERa (oestrogen receptor alpha), MTA1 (metastasis tumor antigen 1), and HDACs (histone deacetylases), implying that LMO4 is also a component of the MTA1 corepressor complex. Over-expressed LMO4 represses ERa transactivation functions in an HDAC-dependent manner, and contributes to the process of breast cancer progression by allowing the development of Era-negative phenotypes. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188773  Cd Length: 55  Bit Score: 36.69  E-value: 1.57e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530376195  29 CNTCGNVCKGE--VLRVQDKYFHIKCFVCKACGCDLAEGG-FFVRQGEYICTLD 79
Cdd:cd09387    1 CSACGQSIPASelVMRAQGNVYHLKCFTCSTCHNQLVPGDrFHYVNGSLFCEHD 54
LIM_ALP_like cd09360
The LIM domain of ALP (actinin-associated LIM protein) family; This family represents the LIM ...
158-206 1.62e-03

The LIM domain of ALP (actinin-associated LIM protein) family; This family represents the LIM domain of ALP (actinin-associated LIM protein) family. Four proteins: ALP, CLP36, RIL, and Mystique have been classified into the ALP subfamily of LIM domain proteins. Each member of the subfamily contains an N-terminal PDZ domain and a C-terminal LIM domain. Functionally, these proteins bind to alpha-actinin through their PDZ domains and bind or other signaling molecules through their LIM domains. ALP proteins have been implicated in cardiac and skeletal muscle structure, function and disease, platelet, and epithelial cell motility. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188746 [Multi-domain]  Cd Length: 52  Bit Score: 36.58  E-value: 1.62e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 530376195 158 CGGCGTEIKnGQALVALDKHWHLGCFKCKSCG-KLLNAEYISKDGLPYCE 206
Cdd:cd09360    1 CDKCGNGIV-GVVVKARDKNRHPECFVCADCGlNLKNKGYFFIEDELYCE 49
LIM3_Zyxin_like cd09357
The third LIM domain of Zyxin-like family; The third LIM domain of Zyxin like family: This ...
158-195 1.75e-03

The third LIM domain of Zyxin-like family; The third LIM domain of Zyxin like family: This family includes Ajuba, Limd1, WTIP, Zyxin, LPP, and Trip6 LIM proteins. Members of Zyxin family contain three tandem C-terminal LIM domains, and a proline-rich N-terminal region. Zyxin proteins are detected primarily in focal adhesion plaques. They function as scaffolds, participating in the assembly of multiple interactions and signal transduction networks, which regulate cell adhesion, spreading, and motility. They can also shuffle into nucleus. In nucleus, zyxin proteins affect gene transcription by interaction with a variety of nuclear proteins, including several transcription factors, playing regulating roles in cell proliferation, differentiation and apoptosis. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188743  Cd Length: 63  Bit Score: 37.02  E-value: 1.75e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 530376195 158 CGGCGTEI--KNGQA----LVALDKHWHLGCFKCKSCGKLLNAE 195
Cdd:cd09357    1 CSVCGEPImpEPGQDetvrIVALDRSFHVNCYKCEDCGMLLSSE 44
LIM3_Paxillin cd09409
The third LIM domain of paxillin; The third LIM domain of paxillin: Paxillin is an adaptor ...
88-124 1.79e-03

The third LIM domain of paxillin; The third LIM domain of paxillin: Paxillin is an adaptor protein, which recruits key components of the signal-transduction machinery to specific sub-cellular locations to respond to environmental changes rapidly. The C-terminal region of paxillin contains four LIM domains which target paxillin to focal adhesions, presumably through a direct association with the cytoplasmic tail of beta-integrin. The N-terminal of paxillin is leucine-rich LD-motifs. Paxillin is found at the interface between the plasma membrane and the actin cytoskeleton. The binding partners of paxillin are diverse and include protein tyrosine kinases, such as Src and FAK, structural proteins, such as vinculin and actopaxin, and regulators of actin organization. Paxillin recruits these proteins to their function sites to control the dynamic changes in cell adhesion, cytoskeletal reorganization and gene expression. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188793 [Multi-domain]  Cd Length: 53  Bit Score: 36.74  E-value: 1.79e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 530376195  88 CFSCDQFIEGEVVSALGKTYHPDCFVCAVCRLPFPPG 124
Cdd:cd09409    1 CGGCARAILENYISALNTLWHPECFVCRECFTPFVNG 37
LIM1_Enigma cd09452
The first LIM domain of Enigma; The first LIM domain of Enigma: Enigma was initially ...
29-80 2.05e-03

The first LIM domain of Enigma; The first LIM domain of Enigma: Enigma was initially characterized in humans as a protein containing three LIM domains at the C-terminus and a PDZ domain at N-terminus. The third LIM domain specifically interacts with the insulin receptor and the second LIM domain interacts with the receptor tyrosine kinase Ret and the adaptor protein APS. Thus Enigma is implicated in signal transduction processes such as mitogenic activity, insulin related actin organization, and glucose metabolism. Enigma is expressed in multiple tissues, such as skeletal muscle, heart, bone and brain. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188836 [Multi-domain]  Cd Length: 52  Bit Score: 36.32  E-value: 2.05e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530376195  29 CNTCGNVCKGEVLRVQDKYFHIKCFVCKACGCDLAEGGFFVRQGEYICTLDY 80
Cdd:cd09452    1 CAQCNKIIRGRYLVALGRSYHPEEFTCSQCKKVLDEGGFFEEKGSIFCPKCY 52
LIM2_LPP cd09354
The second LIM domain of lipoma preferred partner (LPP); The second LIM domain of lipoma ...
88-117 2.05e-03

The second LIM domain of lipoma preferred partner (LPP); The second LIM domain of lipoma preferred partner (LPP): LPP is a member of the zyxin LIM protein family and contains three LIM zinc-binding domains at the C-terminal and proline-rich region at the N-terminal. LPP initially identified as the most frequent translocation partner of HMGA2 (High Mobility Group A2) in a subgroup of benign tumors of adipose tissue (lipomas). It was also shown to be rearranged in a number of other soft tissues, as well as in a case of acute monoblastic leukemia. In addition to its involvement in tumors, LPP was inedited as a smooth muscle restricted LIM protein that plays an important role in SMC migration. LPP is localized at sites of cell adhesion, cell-cell contacts and transiently in the nucleus. In nucleus, it acts as a coactivator for the ETS domain transcription factor PEA3. In addition to PEA3, it interacts with alpha-actinin,vasodilator stimulated phosphoprotein (VASP),Palladin, and Scrib. The LIM domains are the main focal adhesion targeting elements and that the proline- rich region, which harbors binding sites for alpha-actinin and vasodilator- stimulated phosphoprotein (VASP), has a weak targeting capacity. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188740 [Multi-domain]  Cd Length: 60  Bit Score: 36.75  E-value: 2.05e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 530376195  88 CFSCDQFIEGEVVSALGKTYHPDCFVCAVC 117
Cdd:cd09354    1 CSVCSKPILDRILRATGKPYHPQCFTCVVC 30
LIM2_TRIP6 cd09356
The second LIM domain of Thyroid receptor-interacting protein 6 (TRIP6); The second LIM domain ...
88-117 2.06e-03

The second LIM domain of Thyroid receptor-interacting protein 6 (TRIP6); The second LIM domain of Thyroid receptor-interacting protein 6 (TRIP6): TRIP6 is a member of the zyxin LIM protein family and contains three LIM zinc-binding domains at the C-terminal. TRIP6 protein localizes to focal adhesion sites and along actin stress fibers. Recruitment of this protein to the plasma membrane occurs in a lysophosphatidic acid (LPA)-dependent manner. TRIP6 recruits a number of molecules involved in actin assembly, cell motility, survival and transcriptional control. The function of TRIP6 in cell motility is regulated by Src-dependent phosphorylation at a Tyr residue. The phosphorylation activates the coupling to the Crk SH2 domain, which is required for the function of TRIP6 in promoting lysophosphatidic acid (LPA)-induced cell migration. TRIP6 can shuttle to the nucleus to serve as a coactivator of AP-1 and NF-kappaB transcriptional factors. Moreover, TRIP6 can form a ternary complex with the NHERF2 PDZ protein and LPA2 receptor to regulate LPA-induced activation of ERK and AKT, rendering cells resistant to chemotherapy. Recent evidence shows that TRIP6 antagonizes Fas-Induced apoptosis by enhancing the antiapoptotic effect of LPA in cells. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188742  Cd Length: 53  Bit Score: 36.38  E-value: 2.06e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 530376195  88 CFSCDQFIEGEVVSALGKTYHPDCFVCAVC 117
Cdd:cd09356    1 CSVCSKPIMERILRATGKAYHPHCFTCVVC 30
LIM2_Paxillin cd09407
The second LIM domain of paxillin; The second LIM domain of paxillin: Paxillin is an adaptor ...
88-123 2.17e-03

The second LIM domain of paxillin; The second LIM domain of paxillin: Paxillin is an adaptor protein, which recruits key components of the signal-transduction machinery to specific sub-cellular locations to respond to environmental changes rapidly. The C-terminal region of paxillin contains four LIM domains which target paxillin to focal adhesions, presumably through a direct association with the cytoplasmic tail of beta-integrin. The N-terminal of paxillin is leucine-rich LD-motifs. Paxillin is found at the interface between the plasma membrane and the actin cytoskeleton. The binding partners of paxillin are diverse and include protein tyrosine kinases, such as Src and FAK, structural proteins, such as vinculin and actopaxin, and regulators of actin organization. Paxillin recruits these proteins to their function sites to control the dynamic changes in cell adhesion, cytoskeletal reorganization and gene expression. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188791 [Multi-domain]  Cd Length: 52  Bit Score: 36.47  E-value: 2.17e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 530376195  88 CFSCDQFIEGEVVSALGKTYHPDCFVCAVCRLPFPP 123
Cdd:cd09407    1 CYYCNGPILDKVVTALDRTWHPEHFFCAQCGAFFGP 36
LIM2_LIMK2 cd09465
The second LIM domain of LIMK2 (LIM domain Kinase 2); The second LIM domain of LIMK2 (LIM ...
84-139 2.72e-03

The second LIM domain of LIMK2 (LIM domain Kinase 2); The second LIM domain of LIMK2 (LIM domain Kinase 2): LIMK2 is a member of the LIMK protein family, which comprises LIMK1 and LIMK2. LIMK contains two LIM domains, a PDZ domain, and a kinase domain. LIMK is involved in the regulation of actin polymerization and microtubule disassembly. LIMK influences architecture of the actin cytoskeleton by regulating the activity of the cofilin family proteins cofilin1, cofilin2, and destrin. The mechanism of the activation is to phosphorylates cofilin on serine 3 and inactivates its actin-severing activity, altering the rate of actin depolymerisation. LIMK activity is activated by phosphorylation of a threonine residue within the activation loop of the kinase by p21-activated kinases 1 and 4 and by Rho kinase. LIMKs can function in both cytoplasm and nucleus. Both LIMK1 and LIMK2 can act in the nucleus to suppress Rac/Cdc42-dependent cyclin D1 expression. LIMK2 is expressed in all tissues. While LIMK1 localizes mainly at focal adhesions, LIMK2 is found in cytoplasmic punctae, suggesting that they may have different cellular functions. The activity of LIM kinase 2 to regulate cofilin phosphorylation is inhibited by the direct binding of Par-3. LIMK2 activation promotes cell cycle progression. The phenotype of Limk2 knockout mice shows a defect in spermatogenesis. The LIM domains have been shown to play an important role in regulating kinase activity and likely also contribute to LIMK function by acting as sites of protein-to-protein interactions. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188849 [Multi-domain]  Cd Length: 59  Bit Score: 36.07  E-value: 2.72e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 530376195  84 YGTRCFSCDQFIEGEVVSALGKTYHPDCFVCAVCRLPFPPGDRVTFNGKECM-CQKC 139
Cdd:cd09465    2 FGELCHGCSLLMTGPAMVAGEYKYHPECFACMSCKVIIEDGDTYALVQHTTLyCGKC 58
LIM2_LIMPETin_like cd09417
The second LIM domain of protein LIMPETin and related proteins; The second LIM domain of ...
158-205 2.90e-03

The second LIM domain of protein LIMPETin and related proteins; The second LIM domain of protein LIMPETin: LIMPETin contains 6 LIM domains at the C-terminal and an N-terminal PET domain. Four of the six LIM domains are highly homologous to the four and half LIM domain protein family and two of them show sequence similarity to the LIM domains of the testin family. Thus, LIMPETin may be the recombinant product of genes coding testin and FHL proteins. In Schistosoma mansoni, where LIMPETin was first identified, LIMPETin is down regulated in sexually mature adult Schistosoma females compared to sexually immature adult females and adult male. Its differential expression indicates that it is a transcription regulator. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188801  Cd Length: 56  Bit Score: 35.97  E-value: 2.90e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 530376195 158 CGGCGTEIKNGQALVALDKHWHLGCFKCKSCGKLLNAE-YISKDGLPYC 205
Cdd:cd09417    3 SVQCDELIFSGEYTKAMNKDWHSGHFCCWQCDESLTGQrYVLRDEHPYC 51
LIM1_Lrg1p_like cd09391
The first LIM domain of Lrg1p, a LIM and RhoGap domain containing protein; The first LIM ...
29-59 3.18e-03

The first LIM domain of Lrg1p, a LIM and RhoGap domain containing protein; The first LIM domain of Lrg1p, a LIM and RhoGap domain containing protein: The members of this family contain three tandem repeats of LIM domains and a Rho-type GTPase activating protein (RhoGap) domain. Lrg1p is a Rho1 GTPase-activating protein required for efficient cell fusion in yeast. Lrg1p-GAP domain strongly and specifically stimulates the GTPase activity of Rho1p, a regulator of beta (1-3)-glucan synthase in vitro. The LIM domain is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188777  Cd Length: 57  Bit Score: 36.13  E-value: 3.18e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 530376195  29 CNTCGNVCKGEVLRVQDKYFHIKCFVCKACG 59
Cdd:cd09391    1 CAKCGKPITGQFVRALGDVYHLDCFTCHDCG 31
LIM1_LIMK cd09364
The first LIM domain of LIMK (LIM domain Kinase ); The first LIM domain of LIMK (LIM domain ...
88-117 3.48e-03

The first LIM domain of LIMK (LIM domain Kinase ); The first LIM domain of LIMK (LIM domain Kinase ): LIMK protein family is comprised of two members LIMK1 and LIMK2. LIMK contains two LIM domains, a PDZ domain and a kinase domain. LIMK is involved in the regulation of actin polymerization and microtubule disassembly. LIMK influences architecture of the actin cytoskeleton by regulating the activity of the cofilin family proteins cofilin1, cofilin2, and destrin. The mechanism of the activation is to phosphorylates cofilin on serine 3 and inactivates its actin-severing activity, and altering the rate of actin depolymerisation. LIMKs can function in both cytoplasm and nucleus and are expressed in all tissues. Both LIMK1 and LIMK2 can act in the nucleus to suppress Rac/Cdc42-dependent cyclin D1 expression. However, LIMK1 and LIMk2 have different cellular locations. While LIMK1 localizes mainly at focal adhesions, LIMK2 is found in cytoplasmic punctae, suggesting that they may have different cellular functions. The LIM domains of LIMK have been shown to play an important role in regulating kinase activity and likely also contribute to LIMK function by acting as sites of protein-to-protein interactions. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188750 [Multi-domain]  Cd Length: 53  Bit Score: 35.93  E-value: 3.48e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 530376195  88 CFSC-DQFIEGEVVSALGKTYHPDCFVCAVC 117
Cdd:cd09364    1 CAGCrGKILDSQYVQALNQDWHCDCFRCSVC 31
LIM1_Enigma cd09452
The first LIM domain of Enigma; The first LIM domain of Enigma: Enigma was initially ...
88-118 3.67e-03

The first LIM domain of Enigma; The first LIM domain of Enigma: Enigma was initially characterized in humans as a protein containing three LIM domains at the C-terminus and a PDZ domain at N-terminus. The third LIM domain specifically interacts with the insulin receptor and the second LIM domain interacts with the receptor tyrosine kinase Ret and the adaptor protein APS. Thus Enigma is implicated in signal transduction processes such as mitogenic activity, insulin related actin organization, and glucose metabolism. Enigma is expressed in multiple tissues, such as skeletal muscle, heart, bone and brain. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188836 [Multi-domain]  Cd Length: 52  Bit Score: 35.55  E-value: 3.67e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 530376195  88 CFSCDQFIEGEVVSALGKTYHPDCFVCAVCR 118
Cdd:cd09452    1 CAQCNKIIRGRYLVALGRSYHPEEFTCSQCK 31
LIM2_Enigma_like cd09362
The second LIM domain of Enigma-like family; The second LIM domain of Enigma-like family: The ...
29-80 3.85e-03

The second LIM domain of Enigma-like family; The second LIM domain of Enigma-like family: The Enigma LIM domain family is comprised of three members: Enigma, ENH, and Cypher (mouse)/ZASP (human). These subfamily members contain a single PDZ domain at the N-terminus and three LIM domains at the C-terminus. Enigma was initially characterized in humans and is expressed in multiple tissues, such as skeletal muscle, heart, bone and brain. The third LIM domain specifically interacts with the insulin receptor and the second LIM domain interacts with the receptor tyrosine kinase Ret and the adaptor protein APS. Thus Enigma is implicated in signal transduction processes, such as mitogenic activity, insulin related actin organization, and glucose metabolism. The second member, ENH protein, was first identified in rat brain. It has been shown that ENH interacts with protein kinase D1 (PKD1) via its LIM domains and forms a complex with PKD1 and the alpha1C subunit of cardiac L-type voltage-gated calcium channel in rat neonatal cardiomyocytes. The N-terminal PDZ domain interacts with alpha-actinin at the Z-line. ZASP/Cypher is required for maintenance of Z-line structure during muscle contraction, but not required for Z-line assembly. In heart, Cypher/ZASP plays a structural role through its interaction with cytoskeletal Z-line proteins. In addition, there is increasing evidence that Cypher/ZASP also performs signaling functions. Studies reveal that Cypher/ZASP interacts with and directs PKC to the Z-line, where PKC phosphorylates downstream signaling targets. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188748 [Multi-domain]  Cd Length: 52  Bit Score: 35.53  E-value: 3.85e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530376195  29 CNTCGNVCKGEVLRVQDKYFHIKCFVCKACGCDLAEGGFFVRQGEYICTLDY 80
Cdd:cd09362    1 CARCHKKILGEVMHALKQTWHVSCFVCAACKQPIGNSLFHMEDGEPYCEKDY 52
LIM3_abLIM cd09329
The third LIM domain of actin binding LIM (abLIM) proteins; The third LIM domain of actin ...
29-80 3.93e-03

The third LIM domain of actin binding LIM (abLIM) proteins; The third LIM domain of actin binding LIM (abLIM) proteins: Three homologous members of the abLIM protein family have been identified; abLIM-1, abLIM-2 and abLIM-3. The N-terminal of abLIM consists of four tandem repeats of LIM domains and the C-terminal of acting binding LIM protein is a villin headpiece domain, which has strong actin binding activity. The abLIM-1, which is expressed in retina, brain, and muscle tissue, has been indicated to function as a tumor suppressor. AbLIM-2 and -3, mainly expressed in muscle and neuronal tissue, bind to F-actin strongly. They may serve as a scaffold for signaling modules of the actin cytoskeleton and thereby modulate transcription. It has shown that LIM domains of abLIMs interact with STARS (striated muscle activator of Rho signaling), which directly binds actin and stimulates serum-response factor (SRF)-dependent transcription. All LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188715 [Multi-domain]  Cd Length: 52  Bit Score: 35.37  E-value: 3.93e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530376195  29 CNTCGNVCK-GEVLRVQDKYFHIKCFVCKACGCDLAeGGFFVRQGEYICTLDY 80
Cdd:cd09329    1 CAGCGQEIKnGQALLALDKQWHVWCFKCKECGKVLT-GEYMGKDGKPYCERDY 52
LIM pfam00412
LIM domain; This family represents two copies of the LIM structural domain.
217-260 4.07e-03

LIM domain; This family represents two copies of the LIM structural domain.


Pssm-ID: 395333 [Multi-domain]  Cd Length: 57  Bit Score: 35.77  E-value: 4.07e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 530376195  217 CDSCEKYITGRVLE-AGEKHYHPSCALCVRCGQMFAEGEEMYLQG 260
Cdd:pfam00412   1 CAGCNRPIYDRELVrALGKVWHPECFRCAVCGKPLTTGDFYEKDG 45
LIM3_Paxillin_like cd09338
The third LIM domain of the paxillin like protein family; The third LIM domain of the paxillin ...
29-80 4.23e-03

The third LIM domain of the paxillin like protein family; The third LIM domain of the paxillin like protein family: This family consists of paxillin, leupaxin, Hic-5 (ARA55), and other related proteins. There are four LIM domains in the C-terminal of the proteins and leucine-rich LD-motifs in the N-terminal region. Members of this family are adaptor proteins to recruit key components of signal-transduction machinery to specific sub-cellular locations. Paxillin is found at the interface between the plasma membrane and the actin cytoskeleton. Paxillin serves as a platform for the recruitment of numerous regulatory and structural proteins that together control the dynamic changes in cell adhesion, cytoskeletal reorganization and gene expression that are necessary for cell migration and survival. Leupaxin is a cytoskeleton adaptor protein, which is preferentially expressed in hematopoietic cells. It associates with focal adhesion kinases PYK2 and pp125FAK and identified to be a component of the osteoclast pososomal signaling complex. Hic-5 controls cell proliferation, migration and senescence by functioning as coactivator for steroid receptors such as androgen receptor, glucocorticoid receptor and progesterone receptor. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188724 [Multi-domain]  Cd Length: 53  Bit Score: 35.39  E-value: 4.23e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530376195  29 CNTCGNVCKGEVLRVQDKYFHIKCFVCKACGCDLAEGGFFVRQGEYICTLDY 80
Cdd:cd09338    1 CGGCNKPILENYISALNTQWHPECFVCRECHKPFINGSFFEHEGLPYCETHY 52
LIM2_Prickle cd09418
The second LIM domain of Prickle; The second LIM domain of Prickle: Prickle contains three ...
158-205 4.48e-03

The second LIM domain of Prickle; The second LIM domain of Prickle: Prickle contains three C-terminal LIM domains and a N-terminal PET domain. Prickles have been implicated in roles of regulating tissue polarity or planar cell polarity (PCP). PCP establishment requires the conserved Frizzled/Dishevelled PCP pathway. Prickle interacts with Dishevelled, thereby modulating Frizzled/Dishevelled activity and PCP signaling. Two forms of prickles have been identified; namely prickle 1 and prickle 2. Prickle 1 and prickle 2 are differentially expressed. While prickle 1 is expressed in fetal heart and hematological malignancies, prickle 2 is found in fetal brain, adult cartilage, pancreatic islet, and some types of timorous cells. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188802  Cd Length: 56  Bit Score: 35.48  E-value: 4.48e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 530376195 158 CGGCGTEIKNGQALVALDKHWHLGCFKCKSCGKLLNAE-YISKDGLPYC 205
Cdd:cd09418    3 CSACDEIIFADECTEAEGRHWHMKHFCCFECECQLGGQrYIMREGRPYC 51
LIM3_Enigma_like cd09363
The third LIM domain of Enigma-like family; The third LIM domain of Enigma-like family: The ...
88-117 4.92e-03

The third LIM domain of Enigma-like family; The third LIM domain of Enigma-like family: The Enigma LIM domain family is comprised of three members: Enigma, ENH, and Cypher (mouse)/ZASP (human). These subfamily members contain a single PDZ domain at the N-terminus and three LIM domains at the C-terminus. Enigma was initially characterized in humans and is expressed in multiple tissues, such as skeletal muscle, heart, bone, and brain. The third LIM domain specifically interacts with the insulin receptor and the second LIM domain interacts with the receptor tyrosine kinase Ret and the adaptor protein APS. Thus Enigma is implicated in signal transduction processes, such as mitogenic activity, insulin related actin organization, and glucose metabolism. The second member, ENH protein, was first identified in rat brain. It has been shown that ENH interacts with protein kinase D1 (PKD1) via its LIM domains and forms a complex with PKD1 and the alpha1C subunit of cardiac L-type voltage-gated calcium channel in rat neonatal cardiomyocytes. The N-terminal PDZ domain interacts with alpha-actinin at the Z-line. ZASP/Cypher is required for maintenance of Z-line structure during muscle contraction, but not required for Z-line assembly. In heart, Cypher/ZASP plays a structural role through its interaction with cytoskeletal Z-line proteins. In addition, there is increasing evidence that Cypher/ZASP also performs signaling functions. Studies reveal that Cypher/ZASP interacts with and directs PKC to the Z-line, where PKC phosphorylates downstream signaling targets. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188749 [Multi-domain]  Cd Length: 54  Bit Score: 35.49  E-value: 4.92e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 530376195  88 CFSCDQFIEG--EVVSALGKTYHPDCFVCAVC 117
Cdd:cd09363    1 CHGCDFPIEAgdRFLEALGHTWHDTCFVCAVC 32
LIM1_Lmx1b cd09371
The first LIM domain of Lmx1b; The first LIM domain of Lmx1b: Lmx1b belongs to the LHX protein ...
158-209 5.41e-03

The first LIM domain of Lmx1b; The first LIM domain of Lmx1b: Lmx1b belongs to the LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. In mouse, Lmx1b functions in the developing limbs and eyes, the kidneys, the brain, and in cranial mesenchyme. The disruption of Lmx1b gene results kidney and limb defects. In the brain, Lmx1b is important for generation of mesencephalic dopamine neurons and the differentiation of serotonergic neurons. In the mouse eye, Lmx1b regulates anterior segment (cornea, iris, ciliary body, trabecular meshwork, and lens) development. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188757 [Multi-domain]  Cd Length: 53  Bit Score: 35.05  E-value: 5.41e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530376195 158 CGGCGTEIKNGQALVALDKHWHLGCFKCKSCGKLLNAEYISKDGLPYCEADY 209
Cdd:cd09371    1 CAGCQRPISDRYLLRVNERSWHEECLQCSVCQQPLTTSCYFRDRKLYCKQDY 52
LIM2_FBLP-1 cd09372
The second LIM domain of the filamin-binding LIM protein-1 (FBLP-1); The second LIM domain of ...
217-261 5.45e-03

The second LIM domain of the filamin-binding LIM protein-1 (FBLP-1); The second LIM domain of the filamin-binding LIM protein-1 (FBLP-1): Fblp-1 contains a proline-rich domain near its N terminus and two LIM domains at its C terminus. FBLP-1 mRNA was detected in a variety of tissues and cells including platelets and endothelial cells. FBLP-1 binds to Filamins. The association between filamin B and FBLP-1 may play an unknown role in cytoskeletal function, cell adhesion, and cell motility. As in other LIM domains, this domain family is 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188758 [Multi-domain]  Cd Length: 53  Bit Score: 35.09  E-value: 5.45e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 530376195 217 CDSCEKYITGRVLEAGEKHYHPSCALCVRCGQmfAEGEEMYLQGS 261
Cdd:cd09372    1 CAKCQGVITEHIIRALGKGYHPPCFTCVTCGR--RIGDESFAVDE 43
LIM_ALP cd09450
This family represents the LIM domain of ALP, actinin-associated LIM protein; This family ...
88-119 5.83e-03

This family represents the LIM domain of ALP, actinin-associated LIM protein; This family represents the LIM domain of ALP, actinin-associated LIM protein. ALP contains an N-terminal PDZ domain, a C-terminal LIM domain and an ALP-subfamily-specific 34-amino-acid motif termed ALP-like motif (AM), which contains a putative consensus protein kinase C (PKC) phosphorylation site and two alpha-helices. ALP proteins are found in heart and in skeletal muscle. ALP may act as a signaling molecule which is regulated by PKC-dependent signaling. ALP plays an essential role in the development of RV (right ventricle) chamber. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188834 [Multi-domain]  Cd Length: 53  Bit Score: 35.27  E-value: 5.83e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 530376195  88 CFSCDQFIEGEVVSALGKTYHPDCFVCAVCRL 119
Cdd:cd09450    1 CDKCGSGIVGTVVKARDKYRHPECFVCSDCNL 32
LIM1_LMO2 cd09384
The first LIM domain of LMO2 (LIM domain only protein 2); The first LIM domain of LMO2 (LIM ...
41-80 6.20e-03

The first LIM domain of LMO2 (LIM domain only protein 2); The first LIM domain of LMO2 (LIM domain only protein 2): LMO2 is a nuclear protein that plays important roles in transcriptional regulation and development. The two tandem LIM domains of LMO2 support the assembly of a crucial cell-regulatory complex by interacting with both the TAL1-E47 and GATA1 transcription factors to form a DNA-binding complex that is capable of transcriptional activation. LMOs have also been shown to be involved in oncogenesis. LMO1 and LMO2 are activated in T-cell acute lymphoblastic leukemia by distinct chromosomal translocations. LMO2 was also shown to be involved in erythropoiesis and is required for the hematopoiesis in the adult animals. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188770  Cd Length: 56  Bit Score: 35.21  E-value: 6.20e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 530376195  41 LRVQDKYFHIKCFVCKACGCDLAEGG--FFVRQGEYICTLDY 80
Cdd:cd09384   14 LKAIDQYWHEDCLSCDLCGCRLGEVGrrLYYKLGRKLCRRDY 55
LIM_ALP_like cd09360
The LIM domain of ALP (actinin-associated LIM protein) family; This family represents the LIM ...
217-247 6.21e-03

The LIM domain of ALP (actinin-associated LIM protein) family; This family represents the LIM domain of ALP (actinin-associated LIM protein) family. Four proteins: ALP, CLP36, RIL, and Mystique have been classified into the ALP subfamily of LIM domain proteins. Each member of the subfamily contains an N-terminal PDZ domain and a C-terminal LIM domain. Functionally, these proteins bind to alpha-actinin through their PDZ domains and bind or other signaling molecules through their LIM domains. ALP proteins have been implicated in cardiac and skeletal muscle structure, function and disease, platelet, and epithelial cell motility. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188746 [Multi-domain]  Cd Length: 52  Bit Score: 35.04  E-value: 6.21e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 530376195 217 CDSCEKYITGRVLEAGEKHYHPSCALCVRCG 247
Cdd:cd09360    1 CDKCGNGIVGVVVKARDKNRHPECFVCADCG 31
LIM3_Zyxin cd09435
The third LIM domain of Zyxin; The third LIM domain of Zyxin: Zyxin exhibits three copies of ...
171-195 6.44e-03

The third LIM domain of Zyxin; The third LIM domain of Zyxin: Zyxin exhibits three copies of the LIM domain, an extensive proline-rich domain and a nuclear export signal. Localized at sites of cellsubstratum adhesion in fibroblasts, Zyxin interacts with alpha-actinin, members of the cysteine-rich protein (CRP) family, proteins that display Src homology 3 (SH3) domains and Ena/VASP family members. Zyxin and its partners have been implicated in the spatial control of actin filament assembly as well as in pathways important for cell differentiation. In addition to its functions at focal adhesion plaques, recent work has shown that zyxin moves from the sites of cell contacts to the nucleus, where it directly participates in the regulation of gene expression. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188819  Cd Length: 67  Bit Score: 35.62  E-value: 6.44e-03
                         10        20
                 ....*....|....*....|....*
gi 530376195 171 LVALDKHWHLGCFKCKSCGKLLNAE 195
Cdd:cd09435   20 VVALEKNFHMKCYKCEDCGRPLSIE 44
LIM2_Paxillin cd09407
The second LIM domain of paxillin; The second LIM domain of paxillin: Paxillin is an adaptor ...
169-209 6.49e-03

The second LIM domain of paxillin; The second LIM domain of paxillin: Paxillin is an adaptor protein, which recruits key components of the signal-transduction machinery to specific sub-cellular locations to respond to environmental changes rapidly. The C-terminal region of paxillin contains four LIM domains which target paxillin to focal adhesions, presumably through a direct association with the cytoplasmic tail of beta-integrin. The N-terminal of paxillin is leucine-rich LD-motifs. Paxillin is found at the interface between the plasma membrane and the actin cytoskeleton. The binding partners of paxillin are diverse and include protein tyrosine kinases, such as Src and FAK, structural proteins, such as vinculin and actopaxin, and regulators of actin organization. Paxillin recruits these proteins to their function sites to control the dynamic changes in cell adhesion, cytoskeletal reorganization and gene expression. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188791 [Multi-domain]  Cd Length: 52  Bit Score: 34.93  E-value: 6.49e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 530376195 169 QALVALDKHWHLGCFKCKSCGKLLNAE-YISKDGLPYCEADY 209
Cdd:cd09407   11 KVVTALDRTWHPEHFFCAQCGAFFGPEgFHEKDGKAYCRKDY 52
LIM2_Paxillin_like cd09337
The second LIM domain of the paxillin like protein family; The second LIM domain of the ...
29-80 6.71e-03

The second LIM domain of the paxillin like protein family; The second LIM domain of the paxillin like protein family: This family consists of paxillin, leupaxin, Hic-5 (ARA55), and other related proteins. There are four LIM domains in the C-terminal of the proteins and leucine-rich LD-motifs in the N-terminal region. Members of this family are adaptor proteins to recruit key components of signal-transduction machinery to specific sub-cellular locations. Paxillin is found at the interface between the plasma membrane and the actin cytoskeleton. Paxillin serves as a platform for the recruitment of numerous regulatory and structural proteins that together control the dynamic changes in cell adhesion, cytoskeletal reorganization and gene expression that are necessary for cell migration and survival. Leupaxin is a cytoskeleton adaptor protein, which is preferentially expressed in hematopoietic cells. It associates with focal adhesion kinases PYK2 and pp125FAK and identified to be a component of the osteoclast pososomal signaling complex. Hic-5 controls cell proliferation, migration and senescence by functioning as coactivator for steroid receptors such as androgen receptor, glucocorticoid receptor and progesterone receptor. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188723 [Multi-domain]  Cd Length: 52  Bit Score: 35.06  E-value: 6.71e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530376195  29 CNTCGNVCKGEVLRVQDKYFHIKCFVCKACGCDLAEGGFFVRQGEYICTLDY 80
Cdd:cd09337    1 CAYCNGPILDKCVTALDKTWHPEHFFCAQCGKPFGDEGFHEKDGKPYCREDY 52
LIM2_Testin_like cd09341
The second LIM domain of Testin-like family; The second LIM domain of Testin-like family: This ...
87-139 7.03e-03

The second LIM domain of Testin-like family; The second LIM domain of Testin-like family: This family includes testin, prickle, dyxin and LIMPETin. Structurally, testin and prickle proteins contain three LIM domains at C-terminal; LIMPETin has six LIM domains; and dyxin presents only two LIM domains. However, all members of the family contain a PET protein-protein interaction domain. Testin is a cytoskeleton associated focal adhesion protein that localizes along actin stress fibers, at cell-cell-contact areas, and at focal adhesion plaques. Testin interacts with a variety of cytoskeletal proteins, including zyxin, mena, VASP, talin, and actin and it is involved in cell motility and adhesion events. Prickles have been implicated in roles of regulating tissue polarity or planar cell polarity (PCP). Dyxin involves in lung and heart development by interaction with GATA6 and blocking GATA6 activated target genes. LIMPETin might be the recombinant product of genes coding testin and four and half LIM proteins and its function is not well understood. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188727  Cd Length: 56  Bit Score: 34.89  E-value: 7.03e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530376195  87 RCFSCDQFI-EGEVVSALGKTYHPDCFVCAVCRLPFPPGDRVTFNGKECmCQKC 139
Cdd:cd09341    2 RCAACDELIfSGEYTQAEGKNWHLKHFCCFQCDEPLGGQRYVLREGKPY-CLDC 54
LIM1_Ajuba_like cd09352
The first LIM domain of Ajuba-like proteins; The first LIM domain of Ajuba-like proteins: ...
158-209 7.77e-03

The first LIM domain of Ajuba-like proteins; The first LIM domain of Ajuba-like proteins: Ajuba like LIM protein family includes three highly homologous proteins Ajuba, Limd1, and WTIP. Members of the family contain three tandem C-terminal LIM domains and a proline-rich N-terminal region. This family of proteins functions as scaffolds, participating in the assembly of numerous protein complexes. In the cytoplasm, Ajuba binds Grb2 to modulate serum-stimulated ERK activation. Ajuba also recruits the TNF receptor-associated factor 6 (TRAF6) to p62 and activates PKCKappa activity. Ajuba interacts with alpha-catenin and F-actin to contribute to the formation or stabilization of adheren junctions by linking adhesive receptors to the actin cytoskeleton. Although Ajuba is a cytoplasmic protein, it can shuttle into the nucleus. In nucleus, Ajuba functions as a corepressor for the zinc finger-protein Snail. It binds to the SNAG repression domain of Snail through its LIM region. Arginine methyltransferase-5 (Prmt5), a protein in the complex, is recruited to Snai l through an interaction with Ajuba. This ternary complex functions to repress E-cadherin, a Snail target gene. In addition, Ajuba contains functional nuclear-receptor interacting motifs and selectively interacts with retinoic acid receptors (RARs) and rexinoid receptor (RXRs) to negatively regulate retinoic acid signaling. Wtip, the Wt1-interacting protein, was originally identified as an interaction partner of the Wilms tumour protein 1 (WT1). Wtip is involved in kidney and neural crest development. Wtip interacts with the receptor tyrosine kinase Ror2 and inhibits canonical Wnt signaling. LIMD1 was reported to inhibit cell growth and metastases. The inhibition may be mediated through an interaction with the protein barrier-to-autointegration (BAF), a component of SWI/SNF chromatin-remodeling protein; or through the interaction with retinoblastoma protein (pRB), resulting in inhibition of E2F-mediated transcription, and expression of the majority of genes with E2F1- responsive elements. Recently, Limd1 was shown to interact with the p62/sequestosome protein and influence IL-1 and RANKL signaling by facilitating the assembly of a p62/TRAF6/a-PKC multi-protein complex. The Limd1-p62 interaction affects both NF-kappaB and AP-1 activity in epithelial cells and osteoclasts. Moreover, LIMD1 functions as tumor repressor to block lung tumor cell line in vitro and in vivo. Recent studies revealed that LIM proteins Wtip, LIMD1 and Ajuba interact with components of RNA induced silencing complexes (RISC) as well as eIF4E and the mRNA m7GTP cap-protein complex and are required for microRNA-mediated gene silencing. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188738  Cd Length: 54  Bit Score: 34.72  E-value: 7.77e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530376195 158 CGGCGTEIKN-GQALVALDKHWHLGCFKCKSCG-KLLNAEYISKDGLPYCEADY 209
Cdd:cd09352    1 CVKCGKGVYGaSQACQAMGNLYHTNCFTCCSCGrTLRGKAFYNVNGKVYCEEDY 54
LIM2_Lrg1p_like cd09392
The second LIM domain of Lrg1p, a LIM and RhoGap domain containing protein; The second LIM ...
158-209 8.22e-03

The second LIM domain of Lrg1p, a LIM and RhoGap domain containing protein; The second LIM domain of Lrg1p, a LIM and RhoGap domain containing protein: The members of this family contain three tandem repeats of LIM domains and a Rho-type GTPase activating protein (RhoGap) domain. Lrg1p is a Rho1 GTPase-activating protein required for efficient cell fusion in yeast. Lrg1p-GAP domain strongly and specifically stimulates the GTPase activity of Rho1p, a regulator of beta (1-3)-glucan synthase in vitro. The LIM domain is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188778 [Multi-domain]  Cd Length: 53  Bit Score: 34.64  E-value: 8.22e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530376195 158 CGGCGTEIKnGQALVALDKHWHLGCFKCKSCGKLLNAE--YISKDGLPYCEADY 209
Cdd:cd09392    1 CFKCGGALR-GSYITALGRKYHVEHFTCSVCPTVFGPNdsYYEHEGKIYCHYHY 53
LIM_like_1 cd09400
LIM domain in proteins of unknown function; LIM domain in proteins of unknown function: LIM ...
28-76 8.62e-03

LIM domain in proteins of unknown function; LIM domain in proteins of unknown function: LIM domains are identified in a diverse group of proteins with wide variety of biological functions, including gene expression regulation, cell fate determination, cytoskeleton organization, tumor formation, and development. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes. They perform their functions through interactions with other protein partners. The LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. The consensus sequence of LIM domain has been defined as C-x(2)-C-x(16,23)-H-x(2)-[CH]-x(2)-C-x(2)-C-x(16,21)-C-x(2,3)-[CHD] (where X denotes any amino acid).


Pssm-ID: 188784  Cd Length: 61  Bit Score: 34.71  E-value: 8.62e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 530376195  28 LCNTCGN-VCKGEVLRVQDKYFHIKCFVCKACGCDLAEGGFFVRQ-GEYIC 76
Cdd:cd09400    4 PCASCGLpVFLAERLLIEGKVYHRTCFKCARCGVQLTPGSFYETEyGSYCC 54
LIM smart00132
Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM ...
216-248 8.69e-03

Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM domains bind protein partners via tyrosine-containing motifs. LIM domains are found in many key regulators of developmental pathways.


Pssm-ID: 214528 [Multi-domain]  Cd Length: 54  Bit Score: 34.67  E-value: 8.69e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 530376195   216 RCDSCEKYITG--RVLEAGEKHYHPSCALCVRCGQ 248
Cdd:smart00132   1 KCAGCGKPIYGteRVLRALGKVWHPECFKCATCGK 35
LIM2_LIMK cd09365
The second LIM domain of LIMK (LIM domain Kinase ); The second LIM domain of LIMK (LIM domain ...
88-118 9.07e-03

The second LIM domain of LIMK (LIM domain Kinase ); The second LIM domain of LIMK (LIM domain Kinase ): LIMK protein family is comprised of two members LIMK1 and LIMK2. LIMK contains two LIM domains, a PDZ domain and a kinase domain. LIMK is involved in the regulation of actin polymerization and microtubule disassembly. LIMK influences architecture of the actin cytoskeleton by regulating the activity of the cofilin family proteins cofilin1, cofilin2, and destrin. The mechanism of the activation is to phosphorylates cofilin on serine 3 and inactivates its actin-severing activity, and altering the rate of actin depolymerization. LIMKs can function in both cytoplasm and nucleus and are expressed in all tissues. Both LIMK1 and LIMK2 can act in the nucleus to suppress Rac/Cdc42-dependent cyclin D1 expression. However, LIMK1 and LIMk2 have different cellular locations. While LIMK1 localizes mainly at focal adhesions, LIMK2 is found in cytoplasmic punctae, suggesting that they may have different cellular functions. The LIM domains of LIMK have been shown to play an important role in regulating kinase activity and likely also contribute to LIMK function by acting as sites of protein-to-protein interactions. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188751 [Multi-domain]  Cd Length: 54  Bit Score: 34.65  E-value: 9.07e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 530376195  88 CFSCDQFIEGEVVSALGKTYHPDCFVCAVCR 118
Cdd:cd09365    1 CHGCSQIITGPVMVAGDHKFHPECFSCSSCK 31
LIM1_AWH cd09373
The first LIM domain of Arrowhead (AWH); The first LIM domain of Arrowhead (AWH): Arrowhead ...
158-209 9.64e-03

The first LIM domain of Arrowhead (AWH); The first LIM domain of Arrowhead (AWH): Arrowhead belongs to the LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. During embryogenesis of Drosophila, Arrowhead is expressed in each abdominal segment and in the labial segment. Late in embryonic development, expression of arrowhead is refined to the abdominal histoblasts and salivary gland imaginal ring cells themselves. The Arrowhead gene required for establishment of a subset of imaginal tissues: the abdominal histoblasts and the salivary gland imaginal rings. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188759 [Multi-domain]  Cd Length: 54  Bit Score: 34.66  E-value: 9.64e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530376195 158 CGGCGTEIKNGQALVALDKHWHLGCFKCKSCGKLLNAEY--ISKDGLPYCEADY 209
Cdd:cd09373    1 CTGCGEPITDRFLLKVSGRSWHVSCLRCCVCQTPLERQPscFTRDRQIYCKADY 54
LIM_ALP cd09450
This family represents the LIM domain of ALP, actinin-associated LIM protein; This family ...
217-254 9.65e-03

This family represents the LIM domain of ALP, actinin-associated LIM protein; This family represents the LIM domain of ALP, actinin-associated LIM protein. ALP contains an N-terminal PDZ domain, a C-terminal LIM domain and an ALP-subfamily-specific 34-amino-acid motif termed ALP-like motif (AM), which contains a putative consensus protein kinase C (PKC) phosphorylation site and two alpha-helices. ALP proteins are found in heart and in skeletal muscle. ALP may act as a signaling molecule which is regulated by PKC-dependent signaling. ALP plays an essential role in the development of RV (right ventricle) chamber. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188834 [Multi-domain]  Cd Length: 53  Bit Score: 34.49  E-value: 9.65e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 530376195 217 CDSCEKYITGRVLEAGEKHYHPSCALCVRC-------GQMFAEGE 254
Cdd:cd09450    1 CDKCGSGIVGTVVKARDKYRHPECFVCSDCnlnlkqkGYFFVEGQ 45
LIM_RIL cd09451
The LIM domain of RIL; The LIM domain of RIL: RIL contains an N-terminal PDZ domain, a LIM ...
88-119 9.67e-03

The LIM domain of RIL; The LIM domain of RIL: RIL contains an N-terminal PDZ domain, a LIM domain, and a short consensus C-terminal region. It is the smallest molecule in the ALP LIM domain containing protein family. RIL was identified in rat fibroblasts and in human lymphocytes. The LIM domain interacts with the AMPA glutamate receptor in dendritic spines. The consensus C-terminus interacts with PTP-BL, a submembranous protein tyrosine phosphatase and the PDZ domain is responsible to interact with alpha-actinin molecules. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188835  Cd Length: 53  Bit Score: 34.52  E-value: 9.67e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 530376195  88 CFSCDQFIEGEVVSALGKTYHPDCFVCAVCRL 119
Cdd:cd09451    1 CTRCGNGIVGTIVKARDKLYHPECFMCDDCGL 32
LIM1_Testin_like cd09340
The first LIM domain of Testin-like family; The first LIM domain of Testin_like family: This ...
88-118 9.95e-03

The first LIM domain of Testin-like family; The first LIM domain of Testin_like family: This family includes testin, prickle, dyxin and LIMPETin. Structurally, testin and prickle proteins contain three LIM domains at C-terminal; LIMPETin has six LIM domains; and dyxin presents only two LIM domains. However, all members of the family contain a PET protein-protein interaction domain. Testin is a cytoskeleton associated focal adhesion protein that localizes along actin stress fibers, at cell-cell-contact areas, and at focal adhesion plaques. Testin interacts with a variety of cytoskeletal proteins, including zyxin, mena, VASP, talin, and actin and it is involved in cell motility and adhesion events. Prickles have been implicated in roles of regulating tissue polarity or planar cell polarity (PCP). Dyxin involves in lung and heart development by interaction with GATA6 and blocking GATA6 activated target genes. LIMPETin might be the recombinant product of genes coding testin and four and half LIM proteins and its function is not well understood. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188726  Cd Length: 58  Bit Score: 34.50  E-value: 9.95e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 530376195  88 CFSCDQFI-EGEVV-----SALGKTYHPDCFVCAVCR 118
Cdd:cd09340    1 CEKCKEPInPGEVAvfaerAGEDACWHPGCFVCETCN 37
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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