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Conserved domains on  [gi|341898957|gb|EGT54892|]
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Protein Classification

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List of domain hits

Name Accession Description Interval E-value
Peptidase_S28 pfam05577
Serine carboxypeptidase S28; These serine proteases include several eukaryotic enzymes such as ...
61-501 0e+00

Serine carboxypeptidase S28; These serine proteases include several eukaryotic enzymes such as lysosomal Pro-X carboxypeptidase, dipeptidyl-peptidase II, and thymus-specific serine peptidase.


:

Pssm-ID: 310284  Cd Length: 434  Bit Score: 610.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341898957   61 QKLDHFDPYNTKTWNQKYFYNPIYSRNNSIIFLMIGGEGPENGKWAAYPQvqYLQWAKEFGADVFDLEHRFFGDSWPIPD 140
Cdd:pfam05577   1 QKLDHFDPSNNRTFQQRYFYNDQHYRNGGPIFLMIGGEGPESASWVRNGH--WLDLAKEFGALVFSLEHRFYGQSRPIGD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341898957  141 METSSLRYLTTQQALADLAFFIESMNQQY-GFKNPRWVTFGGSYPGSLSAWFRQKYPQLTVGSVASSAPVNLKLDFYEYA 219
Cdd:pfam05577  79 LSTENLRYLSSLQALADLASFIKAMNQKFnGLSSSKWITFGGSYSGSLAAWFRKKYPHLVVGAVASSAPLLAKVDFKEYN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341898957  220 MVVQDDLQLTDANCAPAVRDAFTQIQQLSLTVDGRNKLNNYFNLQPPFDaNTTKLDINNFFGNLFNTFQGMTQYTYDGQS 299
Cdd:pfam05577 159 MVVETSLRQTGGECADAIEQGFAEVEQLLLTKEGRQALSSELQLCPPLD-QTTDLDQLNFFSNIYSNFQGVVQYTYDGQG 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341898957  300 NSTHTDKTVKKMCEIMTNTTEPDKVKRVENLFLWFNQMEPAGPDLSVMPNSYWDVikqVGSGDLKVLGEdGAAARGWMWL 379
Cdd:pfam05577 238 NSTLNGYTIPDMCKIMLNATTTDLILRVEVLIQLFNYLNQKSGNNSTADISYQLA---NADYGDSSYGS-YADDRQWTWQ 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341898957  380 CCNEIGFLQTTNQGNNVFGTGVPLNLFIDMCTDMFGDSMKIKNIMAGNKKSQNYYGGADFYNATNVVLPNGSLDPWHALG 459
Cdd:pfam05577 314 TCTEFGFYQTTDSGNQPFGSPFPVTLYIDMCMDVFGASYNSTKISLRVLATNYYYGGADNPNATNVVFVNGDLDPWHALG 393
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 341898957  460 tYNKKEAQSQLPYLINGTAHCGDMYASYDGEPQSLLAARAFI 501
Cdd:pfam05577 394 -LGDSTDSSVVPYLIPGAAHCADMYPARPSDSPELKAARALI 434
RING-HC_RNFT1_like cd16532
RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein ...
764-802 1.96e-20

RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein RNFT1, RNFT2, and similar proteins; Both RNFT1 and RNFT2 are multi-pass membrane proteins containing a C3HC4-type RING-HC finger. Their biological roles remain unclear.


:

Pssm-ID: 319446 [Multi-domain]  Cd Length: 40  Bit Score: 84.64  E-value: 1.96e-20
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 341898957 764 CTVCHEDFSHPIKLECNHIFCKSCIETWLDQKSTCPMCR 802
Cdd:cd16532    2 CPICQDEFKDPIKLRCKHIFCEDCVSEWFDRERTCPLCR 40
HRD1 super family cl34953
HRD ubiquitin ligase complex, ER membrane component [Posttranslational modification, protein ...
726-808 1.51e-06

HRD ubiquitin ligase complex, ER membrane component [Posttranslational modification, protein turnover, chaperones];


The actual alignment was detected with superfamily member COG5243:

Pssm-ID: 227568 [Multi-domain]  Cd Length: 491  Bit Score: 51.51  E-value: 1.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341898957 726 KVGEIYRYSLFVKKSVKCLITdssvgTSVKILECDDNQCTVCHEDFSH-------------PIKLECNHIFCKSCIETWL 792
Cdd:COG5243  257 RIREHARFRRATKDLNAMYPT-----ATEEQLTNSDRTCTICMDEMFHpdheplprgldmtPKRLPCGHILHLHCLKNWL 331
                         90
                 ....*....|....*.
gi 341898957 793 DQKSTCPMCRAEVTKD 808
Cdd:COG5243  332 ERQQTCPICRRPVIFD 347
 
Name Accession Description Interval E-value
Peptidase_S28 pfam05577
Serine carboxypeptidase S28; These serine proteases include several eukaryotic enzymes such as ...
61-501 0e+00

Serine carboxypeptidase S28; These serine proteases include several eukaryotic enzymes such as lysosomal Pro-X carboxypeptidase, dipeptidyl-peptidase II, and thymus-specific serine peptidase.


Pssm-ID: 310284  Cd Length: 434  Bit Score: 610.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341898957   61 QKLDHFDPYNTKTWNQKYFYNPIYSRNNSIIFLMIGGEGPENGKWAAYPQvqYLQWAKEFGADVFDLEHRFFGDSWPIPD 140
Cdd:pfam05577   1 QKLDHFDPSNNRTFQQRYFYNDQHYRNGGPIFLMIGGEGPESASWVRNGH--WLDLAKEFGALVFSLEHRFYGQSRPIGD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341898957  141 METSSLRYLTTQQALADLAFFIESMNQQY-GFKNPRWVTFGGSYPGSLSAWFRQKYPQLTVGSVASSAPVNLKLDFYEYA 219
Cdd:pfam05577  79 LSTENLRYLSSLQALADLASFIKAMNQKFnGLSSSKWITFGGSYSGSLAAWFRKKYPHLVVGAVASSAPLLAKVDFKEYN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341898957  220 MVVQDDLQLTDANCAPAVRDAFTQIQQLSLTVDGRNKLNNYFNLQPPFDaNTTKLDINNFFGNLFNTFQGMTQYTYDGQS 299
Cdd:pfam05577 159 MVVETSLRQTGGECADAIEQGFAEVEQLLLTKEGRQALSSELQLCPPLD-QTTDLDQLNFFSNIYSNFQGVVQYTYDGQG 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341898957  300 NSTHTDKTVKKMCEIMTNTTEPDKVKRVENLFLWFNQMEPAGPDLSVMPNSYWDVikqVGSGDLKVLGEdGAAARGWMWL 379
Cdd:pfam05577 238 NSTLNGYTIPDMCKIMLNATTTDLILRVEVLIQLFNYLNQKSGNNSTADISYQLA---NADYGDSSYGS-YADDRQWTWQ 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341898957  380 CCNEIGFLQTTNQGNNVFGTGVPLNLFIDMCTDMFGDSMKIKNIMAGNKKSQNYYGGADFYNATNVVLPNGSLDPWHALG 459
Cdd:pfam05577 314 TCTEFGFYQTTDSGNQPFGSPFPVTLYIDMCMDVFGASYNSTKISLRVLATNYYYGGADNPNATNVVFVNGDLDPWHALG 393
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 341898957  460 tYNKKEAQSQLPYLINGTAHCGDMYASYDGEPQSLLAARAFI 501
Cdd:pfam05577 394 -LGDSTDSSVVPYLIPGAAHCADMYPARPSDSPELKAARALI 434
RING-HC_RNFT1_like cd16532
RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein ...
764-802 1.96e-20

RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein RNFT1, RNFT2, and similar proteins; Both RNFT1 and RNFT2 are multi-pass membrane proteins containing a C3HC4-type RING-HC finger. Their biological roles remain unclear.


Pssm-ID: 319446 [Multi-domain]  Cd Length: 40  Bit Score: 84.64  E-value: 1.96e-20
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 341898957 764 CTVCHEDFSHPIKLECNHIFCKSCIETWLDQKSTCPMCR 802
Cdd:cd16532    2 CPICQDEFKDPIKLRCKHIFCEDCVSEWFDRERTCPLCR 40
zf-RING_2 pfam13639
Ring finger domain;
762-802 1.91e-14

Ring finger domain;


Pssm-ID: 338865 [Multi-domain]  Cd Length: 44  Bit Score: 67.80  E-value: 1.91e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 341898957  762 NQCTVCHEDFS---HPIKLECNHIFCKSCIETWLDQKSTCPMCR 802
Cdd:pfam13639   1 DECPICLEEFEegdKVVILPCGHHFHRECLDKWLRSSNTCPLCR 44
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
764-801 1.01e-11

Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and is likely to be a general function of this domain; Various RING fingers exhibit binding activity towards E2 ubiquitin-conjugating enzymes (Ubc' s)


Pssm-ID: 214546 [Multi-domain]  Cd Length: 40  Bit Score: 59.83  E-value: 1.01e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 341898957   764 CTVCHEDFSH-PIKLECNHIFCKSCIETWLDQKS-TCPMC 801
Cdd:smart00184   1 CPICLEEYLKdPVILPCGHTFCRSCIRKWLESGNnTCPIC 40
rad18 TIGR00599
DNA repair protein rad18; All proteins in this family for which functions are known are ...
745-804 3.05e-09

DNA repair protein rad18; All proteins in this family for which functions are known are involved in nucleotide excision repair.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273165 [Multi-domain]  Cd Length: 397  Bit Score: 59.63  E-value: 3.05e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 341898957  745 ITDSS--VGTSVKILECDDN--QCTVCHEDFSHPIKLECNHIFCKSCIETWLDQKSTCPMCRAE 804
Cdd:TIGR00599   6 ITDSSdwLTTPIPSLYPLDTslRCHICKDFFDVPVLTSCSHTFCSLCIRRCLSNQPKCPLCRAE 69
RAD18 COG5432
RING-finger-containing E3 ubiquitin ligase [Signal transduction mechanisms];
745-804 6.94e-08

RING-finger-containing E3 ubiquitin ligase [Signal transduction mechanisms];


Pssm-ID: 227719 [Multi-domain]  Cd Length: 391  Bit Score: 55.48  E-value: 6.94e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 341898957 745 ITDSSVGTSVKI-----LECDDnQCTVCHEDFSHPIKLECNHIFCKSCIETWLDQKSTCPMCRAE 804
Cdd:COG5432    5 ATDPSDWNQTKIpslkgLDSML-RCRICDCRISIPCETTCGHTFCSLCIRRHLGTQPFCPVCRED 68
PHA02929 PHA02929
N1R/p28-like protein; Provisional
761-807 1.19e-07

N1R/p28-like protein; Provisional


Pssm-ID: 222944  Cd Length: 238  Bit Score: 53.24  E-value: 1.19e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 341898957 761 DNQCTVCHED-FSHPIK-------LECNHIFCKSCIETWLDQKSTCPMCRAE---VTK 807
Cdd:PHA02929 174 DKECAICMEKvYDKEIKnmyfgilSNCNHVFCIECIDIWKKEKNTCPVCRTPfisVIK 231
HRD1 COG5243
HRD ubiquitin ligase complex, ER membrane component [Posttranslational modification, protein ...
726-808 1.51e-06

HRD ubiquitin ligase complex, ER membrane component [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227568 [Multi-domain]  Cd Length: 491  Bit Score: 51.51  E-value: 1.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341898957 726 KVGEIYRYSLFVKKSVKCLITdssvgTSVKILECDDNQCTVCHEDFSH-------------PIKLECNHIFCKSCIETWL 792
Cdd:COG5243  257 RIREHARFRRATKDLNAMYPT-----ATEEQLTNSDRTCTICMDEMFHpdheplprgldmtPKRLPCGHILHLHCLKNWL 331
                         90
                 ....*....|....*.
gi 341898957 793 DQKSTCPMCRAEVTKD 808
Cdd:COG5243  332 ERQQTCPICRRPVIFD 347
 
Name Accession Description Interval E-value
Peptidase_S28 pfam05577
Serine carboxypeptidase S28; These serine proteases include several eukaryotic enzymes such as ...
61-501 0e+00

Serine carboxypeptidase S28; These serine proteases include several eukaryotic enzymes such as lysosomal Pro-X carboxypeptidase, dipeptidyl-peptidase II, and thymus-specific serine peptidase.


Pssm-ID: 310284  Cd Length: 434  Bit Score: 610.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341898957   61 QKLDHFDPYNTKTWNQKYFYNPIYSRNNSIIFLMIGGEGPENGKWAAYPQvqYLQWAKEFGADVFDLEHRFFGDSWPIPD 140
Cdd:pfam05577   1 QKLDHFDPSNNRTFQQRYFYNDQHYRNGGPIFLMIGGEGPESASWVRNGH--WLDLAKEFGALVFSLEHRFYGQSRPIGD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341898957  141 METSSLRYLTTQQALADLAFFIESMNQQY-GFKNPRWVTFGGSYPGSLSAWFRQKYPQLTVGSVASSAPVNLKLDFYEYA 219
Cdd:pfam05577  79 LSTENLRYLSSLQALADLASFIKAMNQKFnGLSSSKWITFGGSYSGSLAAWFRKKYPHLVVGAVASSAPLLAKVDFKEYN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341898957  220 MVVQDDLQLTDANCAPAVRDAFTQIQQLSLTVDGRNKLNNYFNLQPPFDaNTTKLDINNFFGNLFNTFQGMTQYTYDGQS 299
Cdd:pfam05577 159 MVVETSLRQTGGECADAIEQGFAEVEQLLLTKEGRQALSSELQLCPPLD-QTTDLDQLNFFSNIYSNFQGVVQYTYDGQG 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341898957  300 NSTHTDKTVKKMCEIMTNTTEPDKVKRVENLFLWFNQMEPAGPDLSVMPNSYWDVikqVGSGDLKVLGEdGAAARGWMWL 379
Cdd:pfam05577 238 NSTLNGYTIPDMCKIMLNATTTDLILRVEVLIQLFNYLNQKSGNNSTADISYQLA---NADYGDSSYGS-YADDRQWTWQ 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341898957  380 CCNEIGFLQTTNQGNNVFGTGVPLNLFIDMCTDMFGDSMKIKNIMAGNKKSQNYYGGADFYNATNVVLPNGSLDPWHALG 459
Cdd:pfam05577 314 TCTEFGFYQTTDSGNQPFGSPFPVTLYIDMCMDVFGASYNSTKISLRVLATNYYYGGADNPNATNVVFVNGDLDPWHALG 393
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 341898957  460 tYNKKEAQSQLPYLINGTAHCGDMYASYDGEPQSLLAARAFI 501
Cdd:pfam05577 394 -LGDSTDSSVVPYLIPGAAHCADMYPARPSDSPELKAARALI 434
RING-HC_RNFT1_like cd16532
RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein ...
764-802 1.96e-20

RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein RNFT1, RNFT2, and similar proteins; Both RNFT1 and RNFT2 are multi-pass membrane proteins containing a C3HC4-type RING-HC finger. Their biological roles remain unclear.


Pssm-ID: 319446 [Multi-domain]  Cd Length: 40  Bit Score: 84.64  E-value: 1.96e-20
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 341898957 764 CTVCHEDFSHPIKLECNHIFCKSCIETWLDQKSTCPMCR 802
Cdd:cd16532    2 CPICQDEFKDPIKLRCKHIFCEDCVSEWFDRERTCPLCR 40
zf-RING_2 pfam13639
Ring finger domain;
762-802 1.91e-14

Ring finger domain;


Pssm-ID: 338865 [Multi-domain]  Cd Length: 44  Bit Score: 67.80  E-value: 1.91e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 341898957  762 NQCTVCHEDFS---HPIKLECNHIFCKSCIETWLDQKSTCPMCR 802
Cdd:pfam13639   1 DECPICLEEFEegdKVVILPCGHHFHRECLDKWLRSSNTCPLCR 44
RING-H2_TTC3 cd16481
RING finger, H2 subclass, found in Tetratricopeptide repeat protein 3 (TTC3) and similar ...
764-802 6.60e-14

RING finger, H2 subclass, found in Tetratricopeptide repeat protein 3 (TTC3) and similar proteins; TTC3, also known as protein DCRR1, or TPR repeat protein D, or TPR repeat protein 3, or RING finger protein 105 (RNF105), is an E3 ubiquitin-protein ligase encoded by a gene within the Down syndrome (DS) critical region on chromosome 21. It affects differentiation and Golgi compactness in neurons through specific actin-regulating pathways. It inhibits the neuronal-like differentiation of pheocromocytoma cells by activating RhoA and by binding to Citron proteins. TTC3 is an Akt-specific E3 ligase that binds to phosphorylated Akt and facilitates its ubiquitination and degradation within the nucleus. TTC3 contains four N-terminal TPR motifs, a potential coiled-coil region and a Citron binding region in the central part, and a C-terminal C3H2C2-type RING-H2 finger.TTC3, also known as protein DCRR1, TPR repeat protein D, TPR repeat protein 3, or RING finger protein 105 (RNF105), is an E3 ubiquitin-protein ligase encoded by a gene within the Down syndrome (DS) critical region on chromosome 21. It also affects differentiation and Golgi compactness in neurons through specific actin-regulating pathways. It inhibits the neuronal-like differentiation of pheocromocytoma cells by activating RhoA and by binding to Citron proteins. TTC3 is an Akt-specific E3 ligase that binds to phosphorylated Akt and facilitates its ubiquitination and degradation within the nucleus. TTC3 contains four N-terminal TPR motifs, a potential coiled-coil region and a Citron binding region in the central part, and a C-terminal C3H2C2-type RING-H2 finger.


Pssm-ID: 319395 [Multi-domain]  Cd Length: 42  Bit Score: 66.22  E-value: 6.60e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 341898957 764 CTVCHEDFSHP--IKLECNHIFCKSCIETWLDQKSTCPMCR 802
Cdd:cd16481    2 CSICHEELKPGtvRKLDCGHRFHKGCIRQWLKEQSTCPTCR 42
RING-H2_PA-TM-RING cd16454
RING finger, H2 subclass, found in the PA-TM-RING ubiquitin ligase family; The PA-TM-RING ...
763-802 1.70e-12

RING finger, H2 subclass, found in the PA-TM-RING ubiquitin ligase family; The PA-TM-RING family represents a group of transmembrane-type E3 ubiquitin ligases, which has been characterized by an N-terminal transient signal peptide, a PA (protease-associated) domain, a TM (transmembrane) domain, as well as a C-terminal C3H2C3-type RING-H2 finger domain. It includes RNF13, RNF167, ZNRF4 (zinc and RING finger 4), GRAIL (gene related to anergy in lymphocytes)/RNF128, RNF130, RNF133, RNF148, RNF149 and RNF150 (which are more closely related), as well as RNF43 and ZNRF3 which have substantially longer C-terminal tail extensions compared with the others. PA-TM-RING proteins are expressed at low levels in all mammalian tissues and species, but they are not present in yeast. They play a common regulatory role in intracellular trafficking/sorting, suggesting that abrogation of their function may result in dysregulation of cellular signaling events in cancer.


Pssm-ID: 319368 [Multi-domain]  Cd Length: 43  Bit Score: 61.93  E-value: 1.70e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 341898957 763 QCTVCHEDFSHP---IKLECNHIFCKSCIETWLDQKSTCPMCR 802
Cdd:cd16454    1 TCAICLEEFEDGeevRVLPCNHLFHSNCIDPWLEQHATCPLCR 43
RING-H2_synoviolin cd16479
RING finger, H2 subclass, found in synoviolin and similar proteins; Synoviolin, also known as ...
761-802 2.26e-12

RING finger, H2 subclass, found in synoviolin and similar proteins; Synoviolin, also known as synovial apoptosis inhibitor 1 (Syvn1), Hrd1, or Der3, is an endoplasmic reticulum (ER)-anchoring E3 ubiquitin ligase that functions as a suppressor of ER stress-induced apoptosis and plays a role in homeostasis maintenance. It also targets tumor suppressor gene p53 for proteasomal degradation, suggesting the crosstalk between ER associated degradation (ERAD) and p53 mediated apoptotic pathway under ER stress. Moreover, Synoviolin controls body weight and mitochondrial biogenesis through negative regulation of the thermogenic coactivator peroxisome proliferator-activated receptor coactivator (PGC)-1beta. It upregulates amyloid beta production by targeting a negative regulator of gamma-secretase, Retention in endoplasmic reticulum 1 (Rer1), for degradation. It is also involved in the degradation of endogenous immature nicastrin, and affects amyloid beta-protein generation. Moreover, Synoviolin is highly expressed in rheumatoid synovial cells and may be involved in the pathogenesis of rheumatoid arthritis (RA). It functions as an anti-apoptotic factor that is responsible for the outgrowth of synovial cells during the development of RA. It promotes inositol-requiring enzyme 1 (IRE1) ubiquitination and degradation in synovial fibroblasts with collagen-induced arthritis. Furthermore, the upregulation of Synoviolin may represent a protective response against neurodegeneration in Parkinson"s disease (PD). In addition, Synoviolin is involved in liver fibrogenesis. Synoviolin contains a C3H2C2-type RING-H2 finger.


Pssm-ID: 319393 [Multi-domain]  Cd Length: 43  Bit Score: 61.93  E-value: 2.26e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 341898957 761 DNQCTVCHED-FSHPIKLECNHIFCKSCIETWLDQKSTCPMCR 802
Cdd:cd16479    1 DDTCIICREEmVSGAKKLPCGHIFHLSCLRSWLQRQQTCPTCR 43
RING-HC_RNFT1 cd16741
RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein 1 ...
764-802 3.94e-12

RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein 1 (RNFT1); RNFT1, also known as protein PTD016, is a multi-pass membrane protein containing a C3HC4-type RING-HC finger. Its biological role remains unclear.


Pssm-ID: 319655 [Multi-domain]  Cd Length: 40  Bit Score: 61.10  E-value: 3.94e-12
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 341898957 764 CTVCHEDFSHPIKLECNHIFCKSCIETWLDQKSTCPMCR 802
Cdd:cd16741    2 CPICQAEFQKPILLICQHIFCEECISLWFNREKTCPLCR 40
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
764-801 1.01e-11

Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and is likely to be a general function of this domain; Various RING fingers exhibit binding activity towards E2 ubiquitin-conjugating enzymes (Ubc' s)


Pssm-ID: 214546 [Multi-domain]  Cd Length: 40  Bit Score: 59.83  E-value: 1.01e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 341898957   764 CTVCHEDFSH-PIKLECNHIFCKSCIETWLDQKS-TCPMC 801
Cdd:smart00184   1 CPICLEEYLKdPVILPCGHTFCRSCIRKWLESGNnTCPIC 40
RING-H2_RNF126_like cd16667
RING finger, H2 subclass, found in RING finger proteins RNF126, RNF115, and similar proteins; ...
763-802 1.29e-11

RING finger, H2 subclass, found in RING finger proteins RNF126, RNF115, and similar proteins; The family includes RING finger proteins RNF126, RNF115, and similar proteins. RNF126 is a Bag6-dependent E3 ubiquitin ligase that is involved in the mislocalized protein (MLP) pathway of quality control. It regulates the retrograde sorting of the cation-independent mannose 6-phosphate receptor (CI-MPR). RNF126 promotes cancer cell proliferation by targeting the tumor suppressor p21 for ubiquitin-mediated degradation, and could be a novel therapeutic target in breast and prostate cancers. It is also able to ubiquitylate cytidine deaminase (AID), a poorly soluble protein that is essential for antibody diversification. RNF115, also known as Rab7-interacting ring finger protein (Rabring 7), or zinc finger protein 364 (ZNF364), or breast cancer-associated gene 2 (BCA2), is an E3 ubiquitin-protein ligase that is an endogenous inhibitor of adenosine monophosphate-activated protein kinase (AMPK) activation and its inhibition increases the efficacy of metformin in breast cancer cells. It also functions as a co-factor in the restriction imposed by tetherin on HIV-1, and targets HIV-1 Gag for lysosomal degradation, impairing virus assembly and release, in a tetherin-independent manner. Moreover, RNF115 is a Rab7-binding protein that stimulates c-Myc degradation through mono-ubiquitination of MM-1. It also plays crucial roles as a Rab7 target protein in vesicle traffic to late endosome/lysosome and lysosome biogenesis. RNF115 and RNF126 associate with the epidermal growth factor receptor (EGFR) and promote ubiquitylation of EGFR, suggesting they play a role in the ubiquitin-dependent sorting and downregulation of membrane receptors. Both of them contain an N-terminal BCA2 Zinc-finger domain (BZF), the AKT-phosphorylation sites, and the C-terminal C3H2C3-type RING-H2 finger.


Pssm-ID: 319581 [Multi-domain]  Cd Length: 43  Bit Score: 59.64  E-value: 1.29e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 341898957 763 QCTVCHEDFS---HPIKLECNHIFCKSCIETWLDQKSTCPMCR 802
Cdd:cd16667    1 ECAVCKEDFKvgeKVRQLPCNHVFHPDCIVPWLEQHNTCPVCR 43
RING-HC cd16449
HC subclass of RING (RING-HC) finger and its variants; RING finger is a specialized type of ...
764-801 2.12e-11

HC subclass of RING (RING-HC) finger and its variants; RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized into two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers. Some have a different Cys/His pattern. Some lack a single Cys or His residue at typical Zn ligand positions, especially, the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can chelate Zn in a RING finger as well. This family corresponds to HC subclass of RING (RING-HC) finger proteins that are characterized by containing C3HC4-type canonical RING-HC fingers or noncanonical RING-HC finger variants, including C4C4-, C3HC3D-, C2H2C4-, and C3HC5-type modified RING-HC fingers. The canonical RING-HC finger has been defined as C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-C-X2-C-X(4-48)-C-X2-C. It binds two Zn ions in a unique "cross-brace" arrangement, which distinguishes it from tandem zinc fingers and other similar motifs. RING-HC finger can be found in a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle, and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serve as scaffolds for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enables efficient transfer of ubiquitin from E2 to the substrates.


Pssm-ID: 319363 [Multi-domain]  Cd Length: 39  Bit Score: 59.02  E-value: 2.12e-11
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 341898957 764 CTVCHEDFSHPIKLECNHIFCKSCIETWL-DQKSTCPMC 801
Cdd:cd16449    1 CPICLELLKDPVLLPCGHTFCRSCLRRLLkEGKKKCPIC 39
RING-H2_EL5_like cd16461
RING finger, H2 subclass, found in rice E3 ubiquitin-protein ligase EL5 and similar proteins; ...
763-802 2.45e-11

RING finger, H2 subclass, found in rice E3 ubiquitin-protein ligase EL5 and similar proteins; EL5, also known as protein ELICITOR 5, is an E3 ubiquitin-protein ligase containing an N-terminal transmembrane domain and a C3H2C3-type RING-H2 finger that is a binding site for ubiquitin-conjugating enzyme (E2). It can be rapidly induced by N-acetylchitooligosaccharide elicitor. EL5 catalyzes polyubiquitination via the Lys48 residue of ubiquitin, and thus plays a crucial role as a membrane-anchored E3 in the maintenance of cell viability after the initiation of root primordial formation in rice. It also acts as an anti-cell death enzyme that might be responsible for mediating the degradation of cytotoxic proteins produced in root cells after the actions of phytohormones. Moreover, EL5 interacts with UBC5b, a rice ubiquitin carrier protein, through its RING-H2 finger. EL5 is an unstable protein, and its degradation is regulated by the C3H2C3-type RING-H2 finger in a proteasome-independent manner.


Pssm-ID: 319375 [Multi-domain]  Cd Length: 43  Bit Score: 58.86  E-value: 2.45e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 341898957 763 QCTVCHEDF--SHPIKL-ECNHIFCKSCIETWLDQKSTCPMCR 802
Cdd:cd16461    1 ECPICLEDFedGELVRLlKCGHVFHKECIDLWLRSHSTCPLCR 43
RING-HC_RNFT2 cd16742
RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein 2 ...
764-802 2.90e-11

RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein 2(RNFT2); RNFT2, also known as transmembrane protein 118 (TMEM118), is a multi-pass membrane protein containing a C3HC4-type RING-HC finger. Its biological role remains unclear.


Pssm-ID: 319656 [Multi-domain]  Cd Length: 41  Bit Score: 58.68  E-value: 2.90e-11
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 341898957 764 CTVCHEDFSHPIKLECNHIFCKSCIETWLDQKSTCPMCR 802
Cdd:cd16742    3 CAICQAEFREPLILICQHVFCEECLCLWFDRERTCPLCR 41
RING-HC_RNF219 cd16562
RING finger, HC subclass, found in RING finger protein 219 (RNF219) and similar proteins; ...
762-802 3.63e-11

RING finger, HC subclass, found in RING finger protein 219 (RNF219) and similar proteins; RNF219 may function as a modulator of late-onset Alzheimer"s disease (LOAD) associated amyloid beta A4 precursor protein (APP) endocytosis and metabolism. It genetically interacts with apolipoprotein E epsilon4 allele (APOE4). Thus a genetic variant within RNF219 was found to affect amyloid deposition in human brain and LOAD age-of-onset. Moreover, common genetic variants at the RNF219 locus had been associated with alternations in lipid metabolism, cognitive performance and central nervous system ventricle volume. RNF219 contains a C3HC4-type RING-HC finger.


Pssm-ID: 319476 [Multi-domain]  Cd Length: 42  Bit Score: 58.16  E-value: 3.63e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 341898957 762 NQCTVCHEDFSHPIKLECNHIFCKSCIETWLDQKSTCPMCR 802
Cdd:cd16562    2 ISCHICLGKVKQPVICPNNHVFCSSCMDLWLKRNNQCPACR 42
RING-HC_RNF8 cd16535
RING finger, HC subclass, found in RING finger protein 8 (RNF8) and similar proteins; RNF8 is ...
763-802 4.75e-11

RING finger, HC subclass, found in RING finger protein 8 (RNF8) and similar proteins; RNF8 is a telomere-associated E3 ubiquitin-protein ligase that plays an important role in DNA double-strand break (DSB) repair via histone ubiquitination. It is localized in the nucleus and interacts with class III E2s (UBE2E2, UbcH6, and UBE2E3), but not with other E2s (UbcH5, UbcH7, UbcH10, hCdc34, and hBendless). It recruits UBC13 for lysine 63-based self polyubiquitylation. Its deficiency causes neuronal pathology and cognitive decline, and its loss results in neuron degeneration. RNF8, together with RNF168, catalyzes a series of ubiquitylation events on substrates such as H2A and H2AX, with the H2AK13/15 ubiquitylation being particularly important for recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of DSBs. Specially, RNF8 mediates the ubiquitination of gammaH2AX, and recruits 53BP1 and BRCA1 to DNA damage sites which promotes DNA damage response (DDR) and inhibits chromosomal instability. Moreover, RNF8 interacts with retinoid X receptor alpha (RXR alpha) and enhances its transcription-stimulating activity. It also regulates the rate of exit from mitosis and cytokinesis. RNF8 contains an N-terminal forkhead-associated (FHA) domain and a C-terminal C3HC4-type RING-HC finger.


Pssm-ID: 319449 [Multi-domain]  Cd Length: 42  Bit Score: 57.82  E-value: 4.75e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 341898957 763 QCTVCHEDFSHPIKLECNHIFCKSCIETWLDQKSTCPMCR 802
Cdd:cd16535    3 QCSICSELFIEAVTLNCSHSFCSYCITEWMKRKKECPICR 42
RING-HC_LNX3_like cd16512
RING finger, HC subclass, found in ligand of Numb protein LNX3, LNX4, and similar proteins; ...
763-802 6.65e-11

RING finger, HC subclass, found in ligand of Numb protein LNX3, LNX4, and similar proteins; The ligand of Numb protein X (LNX) family, also known as PDZ and RING (PDZRN) family, includes LNX1-5, which can interact with Numb, a key regulator of neurogenesis and neuronal differentiation. LNX5 (also known as PDZK4, or PDZRN4L) shows high sequence homology to LNX3 and LNX4, but it lacks the RING domain. LNX1-4 proteins function as E3 ubiquitin ligases and have a unique domain architecture consisting of an N-terminal RING-HC finger for E3 ubiquitin ligase activity and either two or four PDZ domains necessary for the substrate-binding. This family corresponds to LNX3/LNX4-like proteins, which contains a typical C3HC4-type RING-HC finger and two PDZ domains.


Pssm-ID: 319426 [Multi-domain]  Cd Length: 41  Bit Score: 57.52  E-value: 6.65e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 341898957 763 QCTVCHEDFSHPIKLECNHIFCKSCIETWLDQKSTCPM-CR 802
Cdd:cd16512    1 KCSICLEVLEDPLTTPCGHVFCSGCILPWLVQNGSCPVkCR 41
RING-HC_PEX10 cd16527
RING finger, HC subclass, found in peroxin-10 (PEX10) and similar proteins; PEX10, also known ...
763-802 8.23e-11

RING finger, HC subclass, found in peroxin-10 (PEX10) and similar proteins; PEX10, also known as peroxisome biogenesis factor 10, peroxisomal biogenesis factor 10, peroxisome assembly protein 10, or RING finger protein 69 (RNF69), is an integral peroxisomal membrane protein with two transmembrane regions and a C3HC4-type RING-HC finger within its cytoplasmically exposed C-terminus. It plays an essential role in peroxisome assembly, import of target substrates, and recycling or degradation of protein complexes and amino acids. It is an essential component of the spinal locomotor circuit, and thus its mutations may be involved in peroxisomal biogenesis disorders (PBD). Mutations in human PEX10 also result in autosomal recessive ataxia. Moreover, PEX10 functions as an E3-ubiquitin ligase with an E2, UBCH5C. It mono- or poly-ubiquitinates PEX5, a key player in peroxisomal matrix protein import, in a UBC4-dependent manner, to control PEX5 receptor recycling or degradation. It also links the E2 ubiquitin conjugating enzyme PEX4 to the protein import machinery of the peroxisome.


Pssm-ID: 319441 [Multi-domain]  Cd Length: 40  Bit Score: 57.23  E-value: 8.23e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 341898957 763 QCTVCHEDFSHPIKLECNHIFCKSCIETWLDQKSTCPMCR 802
Cdd:cd16527    1 KCSLCLESRRHPTATPCGHLFCWSCITEWCNEKPECPLCR 40
RING-HC_RNF151 cd16547
RING finger, HC subclass, found in RING finger protein 151 (RNF151) and similar proteins; ...
764-802 1.38e-10

RING finger, HC subclass, found in RING finger protein 151 (RNF151) and similar proteins; RNF151 is a testis-specific RING finger protein that interacts with dysbindin, a synaptic and microtubular protein that binds brain snapin, a SNARE-binding protein that mediated intracellular membrane fusion in both neuronal and non-neuronal cells. Thus, it may be involved in acrosome formation of spermatids through interacting with multiple proteins participating in membrane biogenesis and microtubule organization. RNF151 contains a C3HC4-type RING finger domain, a putative nuclear localization signal (NLS), and a TNF receptor associated factor (TRAF)-type zinc finger domain.


Pssm-ID: 319461 [Multi-domain]  Cd Length: 39  Bit Score: 56.75  E-value: 1.38e-10
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 341898957 764 CTVCHEDFSHPIKLECNHIFCKSCIETWLDQKSTCPMCR 802
Cdd:cd16547    1 CSICHGVLKCPYMLPCSHIFCKKCILQWLKRQETCPCCR 39
RING-HC_TRIM40-C-V cd16583
RING finger, HC subclass, found in tripartite motif-containing protein 40 (TRIM40) and similar ...
764-803 1.76e-10

RING finger, HC subclass, found in tripartite motif-containing protein 40 (TRIM40) and similar proteins; TRIM40, also known as probable E3 NEDD8-protein ligase or RING finger protein 35 (RNF35), is highly expressed in the gastrointestinal tract including the stomach, small intestine, and large intestine. It enhances neddylation of inhibitor of nuclear factor kappaB kinase subunit gamma (IKKgamma), inhibits the activity of nuclear factor-kappaB (NF-kappaB)-mediated transcription, and thus prevents inflammation-associated carcinogenesis in the gastrointestinal tract. TRIM40 belongs to the C-V subclass of TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region , as well as an uncharacterized region positioned C-terminal to the RBCC domain.


Pssm-ID: 319497 [Multi-domain]  Cd Length: 46  Bit Score: 56.44  E-value: 1.76e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 341898957 764 CTVCHEDFSHPIKLECNHIFCKSCIETWLDQKS-----TCPMCRA 803
Cdd:cd16583    2 CPICLDPLKEPVSTTCGHVFCRGCIAQHLEKASvsgvlCCPVCRK 46
RING-H2_RNF24_like cd16469
RING finger, H2 subclass, found in RING finger proteins RNF24, RNF122, and similar proteins; ...
764-805 5.62e-10

RING finger, H2 subclass, found in RING finger proteins RNF24, RNF122, and similar proteins; The family includes RNF24, RNF122, and similar proteins. RNF24 is an intrinsic membrane protein localized in the Golgi apparatus. It specifically interacts with the ankyrin-repeats domains (ARDs) of TRPC1, ?3, ?4, ?5, ?6, and ?7, and affects TRPC intracellular trafficking without affecting their activity. RNF122 is a RING finger protein associated with HEK 293T cell viability. It is localized to the endoplasmic reticulum (ER) and the Golgi apparatus, and overexpressed in anaplastic thyroid cancer cells. RNF122 functions as an E3 ubiquitin ligase that can ubiquitinate itself and undergoes degradation through its RING finger in a proteasome-dependent manner. Both RNF24 and RNF122 contain an N-terminal transmembrane domain and a C-terminal C3H2C3-type RING-H2 finger.


Pssm-ID: 319383 [Multi-domain]  Cd Length: 47  Bit Score: 55.15  E-value: 5.62e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 341898957 764 CTVCHEDFSHPIKL---ECNHIFCKSCIETWLDQKSTCPMCRAEV 805
Cdd:cd16469    3 CAVCLEDFKKKEELgvcPCGHAFHRKCLLKWLEVRNVCPMCNSPV 47
RING-H2_AMFR cd16455
RING finger, H2 subclass, found in autocrine motility factor receptor (AMFR) and similar ...
762-802 7.45e-10

RING finger, H2 subclass, found in autocrine motility factor receptor (AMFR) and similar proteins; AMFR, also known as AMF receptor, or RING finger protein 45, or ER-protein gp78, is an internalizing cell surface glycoprotein localized in both plasma membrane caveolae and the endoplasmic reticulum (ER). It is involved in the regulation of cellular adhesion, proliferation, motility and apoptosis, as well as in the process of learning and memory. AMFR also functions as a RING finger-dependent ubiquitin protein ligase (E3) implicated in degradation from the ER. AMFR contains an N-terminal RING-H2 finger and a C-terminal ubiquitin-associated (UBA)-like CUE domain.


Pssm-ID: 319369 [Multi-domain]  Cd Length: 44  Bit Score: 54.68  E-value: 7.45e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 341898957 762 NQCTVCHEDFSHPIKLECNHIFCKSCIETWLDQKSTCPMCR 802
Cdd:cd16455    1 DDCAICWESMQTARKLPCGHLFHNSCLRSWLEQDTSCPTCR 41
RING-H2_RNF126 cd16801
RING finger, H2 subclass, found in RING finger protein 126 (RNF126) and similar proteins; ...
763-802 9.68e-10

RING finger, H2 subclass, found in RING finger protein 126 (RNF126) and similar proteins; RNF126 is a Bag6-dependent E3 ubiquitin ligase that is involved in the mislocalized protein (MLP) pathway of quality control. It regulates the retrograde sorting of the cation-independent mannose 6-phosphate receptor (CI-MPR). Moreover, RNF126 promotes cancer cell proliferation by targeting the tumor suppressor p21 for ubiquitin-mediated degradation, and could be a novel therapeutic target in breast and prostate cancers. It is also able to ubiquitylate cytidine deaminase (AID), a poorly soluble protein that is essential for antibody diversification. In addition, RNF126 and the related protein, RNF115 associate with the epidermal growth factor receptor (EGFR) and promote ubiquitylation of EGFR, suggesting they play a role in the ubiquitin-dependent sorting and downregulation of membrane receptors. RNF126 contains an N-terminal BCA2 Zinc-finger domain (BZF), the AKT-phosphorylation sites, and the C-terminal C3H2C3-type RING-H2 finger.


Pssm-ID: 319715 [Multi-domain]  Cd Length: 44  Bit Score: 54.57  E-value: 9.68e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 341898957 763 QCTVCHEDFS---HPIKLECNHIFCKSCIETWLDQKSTCPMCR 802
Cdd:cd16801    1 ECPVCKEDYAvgeNVRQLPCNHLFHNDCIVPWLEQHDTCPVCR 43
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
760-806 1.10e-09

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 339001 [Multi-domain]  Cd Length: 48  Bit Score: 54.31  E-value: 1.10e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 341898957  760 DDNQCTVCHEDFSHPIKLECNH-IFCKSCIETWLDQKSTCPMCRAEVT 806
Cdd:pfam13920   1 EDRLCVICLDRPRNVVLLPCGHlCLCEECAERLRKKKKKCPICRQPIE 48
zf-rbx1 pfam12678
RING-H2 zinc finger domain; There are 8 cysteine/ histidine residues which are proposed to be ...
757-802 1.28e-09

RING-H2 zinc finger domain; There are 8 cysteine/ histidine residues which are proposed to be the conserved residues involved in zinc binding. The protein, of which this domain is the conserved region, participates in diverse functions relevant to chromosome metabolism and cell cycle control.


Pssm-ID: 315369 [Multi-domain]  Cd Length: 55  Bit Score: 54.24  E-value: 1.28e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 341898957  757 LECDDNQCTVChedfshPIKL-ECNHIFCKSCIETWLDQKSTCPMCR 802
Cdd:pfam12678  15 PECQAPGDDEC------PVVWgECGHAFHLHCISRWLKTNNTCPLCR 55
RING-H2_GRAIL cd16668
RING finger, H2 subclass, found in the GRAIL transmembrane proteins family; The GRAIL ...
763-807 1.37e-09

RING finger, H2 subclass, found in the GRAIL transmembrane proteins family; The GRAIL transmembrane proteins family includes RING finger proteins RNF128 (also known as GRAIL), RNF130, RNF133, RNF148, RNF149, and RNF150, which belong to a larger PA-TM-RING ubiquitin ligase family that has been characterized by an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C-terminal C3H2C3-type RING-H2 finger domain followed by a putative PEST sequence. RNF128 is a type 1 transmembrane E3 ubiquitin-protein ligase that is a critical regulator of adaptive immunity and development. RNF130, also known as Goliath homolog (H-Goliath), is a paralog of RNF128. It is a transmembrane E3 ubiquitin-protein ligase expressed in leukocytes. It has a self-ubiquitination property, and controls the development of T cell clonal anergy by ubiquitination. RNF133 is a testis-specific endoplasmic reticulum-associated E3 ubiquitin ligase that may play a role in sperm maturation through an ER-associated degradation (ERAD) pathway. RNF148 is a testis-specific E3 ubiquitin ligase that is abundantly expressed in testes and slightly expressed in pancreas. Its expression regulated by histone deacetylases. RNF149, also known as DNA polymerase-transactivated protein 2, is an E3 ubiquitin-protein ligase that induces the ubiquitination of wild-type v-Raf murine sarcoma viral oncogene homolog B1 (BRAF) and promotes its proteasome-dependent degradation. RNF150 is a RING finger protein that its polymorphisms may be associated with chronic obstructive pulmonary disease (COPD) risk in the Chinese population. The family also includes Drosophila melanogaster protein goliath (d-goliath), also known as protein g1, which is one of the funding members of the family. It was originally identified as a transcription factor involved in the embryo mesoderm formation.


Pssm-ID: 319582 [Multi-domain]  Cd Length: 48  Bit Score: 53.89  E-value: 1.37e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 341898957 763 QCTVCHEDF--SHPIK-LECNHIFCKSCIETWLDQKSTCPMCRAEVTK 807
Cdd:cd16668    1 QCAVCIEPYkpGDVVRiLPCKHIFHKSCVDPWLLEHRTCPMCKLDILK 48
RING-H2 cd16448
H2 subclass of RING (RING-H2) finger and its variants; RING finger is a specialized type of ...
764-802 1.65e-09

H2 subclass of RING (RING-H2) finger and its variants; RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized as two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers. Some have different Cys/His pattern. Some lack a single Cys or His residues at typical Zn ligand positions. Especially, the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can indeed chelate Zn in a RING finger as well. This family corresponds to H2 subclass of RING (RING-H2) finger proteins that are characterized by containing C3H2C3-type canonical RING-H2 fingers or noncanonical RING-H2 finger variants, including C4HC3- (RING-CH alias RINGv), C3H3C2-, C3H2C2D-, C3DHC3-, and C4HC2H-type modified RING-H2 fingers. The canonical RING-H2 finger has been defined as C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-H-X2-C-X(4-48)-C-X2-C, X is any amino acid and the number of X residues varies in different fingers. It binds two Zn ions in a unique "cross-brace" arrangement, which distinguishes it from tandem zinc fingers and other similar motifs. RING-H2 finger can be found in a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serves as a scaffold for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enables efficient transfer of ubiquitin from E2 to the substrates.


Pssm-ID: 319362 [Multi-domain]  Cd Length: 44  Bit Score: 53.61  E-value: 1.65e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 341898957 764 CTVCHEDF----SHPIKLECNHIFCKSCIETWL-DQKSTCPMCR 802
Cdd:cd16448    1 CAICLEEFeegdCPVRLLPCGHVFHKSCIDKWLeSGNRTCPLCR 44
RING-HC_RNF141 cd16545
RING finger, HC subclass, found in RING finger protein 141 (RNF141) and similar proteins; ...
763-802 2.46e-09

RING finger, HC subclass, found in RING finger protein 141 (RNF141) and similar proteins; RNF141, also known as zinc finger protein 230 (ZNF230), is a RING finger protein present primarily in the nuclei of spermatogonia, the acrosome, and the tail of spermatozoa. It may have a broad function during early development of vertebrates. It plays an important role in spermatogenesis, including spermatogenic cell proliferation and sperm maturation, as well as motility and fertilization. It also exhibits DNA binding activity. RNF141 corresponding ZNF230 gene mutation may be associated with azoospermia. RNF141 contains a C3HC4-type RING finger domain that may function as an activator module in transcription.


Pssm-ID: 319459 [Multi-domain]  Cd Length: 39  Bit Score: 53.18  E-value: 2.46e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 341898957 763 QCTVCHEDFSHPIkLECNHIFCKSCIETWLDQKSTCPMCR 802
Cdd:cd16545    1 ECCICMDRKPDTI-LPCAHSFCQKCIDKWSVRHRTCPICR 39
rad18 TIGR00599
DNA repair protein rad18; All proteins in this family for which functions are known are ...
745-804 3.05e-09

DNA repair protein rad18; All proteins in this family for which functions are known are involved in nucleotide excision repair.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273165 [Multi-domain]  Cd Length: 397  Bit Score: 59.63  E-value: 3.05e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 341898957  745 ITDSS--VGTSVKILECDDN--QCTVCHEDFSHPIKLECNHIFCKSCIETWLDQKSTCPMCRAE 804
Cdd:TIGR00599   6 ITDSSdwLTTPIPSLYPLDTslRCHICKDFFDVPVLTSCSHTFCSLCIRRCLSNQPKCPLCRAE 69
RING-HC_RNF146 cd16546
RING finger, HC subclass, found in RING finger protein 146 (RNF146) and similar proteins; ...
763-802 3.81e-09

RING finger, HC subclass, found in RING finger protein 146 (RNF146) and similar proteins; RNF146, also known as dactylidin, or iduna, is a cytoplasmic E3 ubiquitin-protein ligase that is responsible for PARylation-dependent ubiquitination (PARdU). It displays neuroprotective property due to its inhibition of Parthanatos, a PAR dependent cell death, via binding with Poly(ADP-ribose) (PAR). It also modulates PAR polymerase-1 (PARP-1)-mediated oxidative cell injury in cardiac myocytes. Moreover, RNF146 mediates tankyrase-dependent degradation of axin, thereby positively regulates Wnt signaling. It also facilitates DNA repair and protects against cell death induced by DNA damaging agents or gamma-irradiation through translocating to the nucleus after cellular injury and promoting the ubiquitination and degradation of various nuclear proteins involved in DNA damage repair. Furthermore, RNF146 is implicated in neurodegenerative disease and cancer development. It regulates the development and progression of non-small cell lung cancer (NSCLC) by enhancing cell growth, invasion, and survival. RNF146 contains an N-terminal C3HC4-type RING-HC finger followed by a WWE domain with a poly(ADP-ribose) (PAR) binding motif at the tail.


Pssm-ID: 319460 [Multi-domain]  Cd Length: 40  Bit Score: 52.39  E-value: 3.81e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 341898957 763 QCTVCHEDFSHPIKLECNHIFCKSCIETWLDQKSTCPMCR 802
Cdd:cd16546    1 ECAICLQTCVHPVRLPCGHIFCYLCVKGVAWQSKRCALCR 40
RING2-HC_LONFs cd16514
RING finger 2, HC subclass, found in the LON peptidase N-terminal domain and RING finger ...
761-802 5.85e-09

RING finger 2, HC subclass, found in the LON peptidase N-terminal domain and RING finger proteins family; The LON peptidase N-terminal domain and RING finger proteins family includes LONRF1 (also known as RING finger protein 191 or RNF191), LONRF2 (also known as RING finger protein 192 or RNF192, or neuroblastoma apoptosis-related protease), LONRF3 (also known as RING finger protein 127 or RNF127), which are characterized by containing two C3HC4-type RING-HC fingers, four tetratricopeptide (TPR) repeats, and one N-terminal domain of the ATP-dependent protease La (LON) domain at the C-terminus. Their biological function remain unclear. This family corresponds to the second RING-HC finger.


Pssm-ID: 319428 [Multi-domain]  Cd Length: 42  Bit Score: 51.94  E-value: 5.85e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 341898957 761 DNQCTVCHEDFSHPIKLECNHIFCKSCIETWLDQKSTCPMCR 802
Cdd:cd16514    1 DFECSLCMRLLYEPVTTPCGHTFCKKCLERCLDHSPKCPLCK 42
zf-RING_UBOX pfam13445
RING-type zinc-finger; This zinc-finger is a typical RING-type of plant ubiquitin ligases.
764-799 6.09e-09

RING-type zinc-finger; This zinc-finger is a typical RING-type of plant ubiquitin ligases.


Pssm-ID: 338747 [Multi-domain]  Cd Length: 38  Bit Score: 52.00  E-value: 6.09e-09
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 341898957  764 CTVCHEDFSHPiKLECNHIFCKSCIETWLDQKS---TCP 799
Cdd:pfam13445   1 CPICLELFTDP-VLPCGHTFCRECLEEMSLLKGgrfKCP 38
zf-C3HC4_2 pfam13923
Zinc finger, C3HC4 type (RING finger);
763-801 8.13e-09

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 316445 [Multi-domain]  Cd Length: 40  Bit Score: 51.65  E-value: 8.13e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 341898957  763 QCTVCHEDFSHPIKL-ECNHIFCKSCIETWLDQKSTCPMC 801
Cdd:pfam13923   1 MCPICLDMLKDPSTTtPCGHVFCQKCILRALRSGNECPLC 40
RING-H2_RNF115 cd16800
RING finger, H2 subclass, found in RING finger protein 115 (RNF115) and similar proteins; ...
763-802 8.35e-09

RING finger, H2 subclass, found in RING finger protein 115 (RNF115) and similar proteins; RNF115, also known as Rab7-interacting ring finger protein (Rabring 7), or zinc finger protein 364 (ZNF364), or breast cancer-associated gene 2 (BCA2), is an E3 ubiquitin-protein ligase that is an endogenous inhibitor of adenosine monophosphate-activated protein kinase (AMPK) activation and its inhibition increases the efficacy of metformin in breast cancer cells. It also functions as a co-factor in the restriction imposed by tetherin on HIV-1, and targets HIV-1 Gag for lysosomal degradation, impairing virus assembly and release, in a tetherin-independent manner. Moreover, RNF115 is a Rab7-binding protein that stimulates c-Myc degradation through mono-ubiquitination of MM-1. It also plays crucial roles as a Rab7 target protein in vesicle traffic to late endosome/lysosome and lysosome biogenesis. Furthermore, RNF115 and the related protein, RNF126 associate with the epidermal growth factor receptor (EGFR) and promote ubiquitylation of EGFR, suggesting they play a role in the ubiquitin-dependent sorting and downregulation of membrane receptors. RNF115 contains an N-terminal BCA2 Zinc-finger domain (BZF), the AKT-phosphorylation sites, and the C-terminal C3H2C3-type RING-H2 finger.


Pssm-ID: 319714 [Multi-domain]  Cd Length: 47  Bit Score: 51.91  E-value: 8.35e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 341898957 763 QCTVCHEDFS--HPIK-LECNHIFCKSCIETWLDQKSTCPMCR 802
Cdd:cd16800    2 ECPVCKEDYTveEQVRqLPCNHFFHSDCIVPWLELHDTCPVCR 44
RING-HC_TRIM21_C-IV cd16596
RING finger, HC subclass, found in tripartite motif-containing protein TRIM21 and similar ...
764-802 8.65e-09

RING finger, HC subclass, found in tripartite motif-containing protein TRIM21 and similar proteins; TRIM21, also known as 52 kDa Ro protein, 52 kDa ribonucleoprotein autoantigen Ro/SS-A, Ro(SS-A), RING finger protein 81 (RNF81), or Sjoegren syndrome type A antigen (SS-A), is a ubiquitously expressed E3 ubiquitin-protein ligase and a high affinity antibody receptor uniquely expressed in the cytosol of mammalian cells. As a cytosolic Fc receptor, TRIM21 binds the Fc of virus-associated antibodies and targets the complex in the cytosol for proteasomal degradation in a process known as antibody-dependent intracellular neutralization (ADIN), and provides an intracellular immune response to protect host defense against pathogen infection. It shows remarkably broad isotype specificity as it does not only bind IgG, but also IgM and IgA. Moreover, TRIM21 promotes the cytosolic DNA sensor cGAS and the cytosolic RNA sensor RIG-I sensing of viral genomes during infection by antibody-opsonized virus. It stimulates inflammatory signaling and activates innate transcription factors, such as nuclear factor-kappaB (NF-kappaB). TRIM21 also plays an essential role in p62-regulated redox homeostasis, suggesting a viable target for treating pathological conditions resulting from oxidative damage. Furthermore, TRIM21 may have implications for various autoimmune diseases associated uncontrolled antiviral signaling through the regulation of Nmi-IFI35 complex-mediated inhibition of innate antiviral response. TRIM21 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 319510 [Multi-domain]  Cd Length: 44  Bit Score: 51.81  E-value: 8.65e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 341898957 764 CTVCHEDFSHPIKLECNHIFCKSCI-ETWLDQKSTCPMCR 802
Cdd:cd16596    5 CSICLDPFVEPMSIECGHSFCQECIsEVGKYGGSVCPVCR 44
zf-C3HC4 pfam00097
Zinc finger, C3HC4 type (RING finger); The C3HC4 type zinc-finger (RING finger) is a ...
764-801 1.11e-08

Zinc finger, C3HC4 type (RING finger); The C3HC4 type zinc-finger (RING finger) is a cysteine-rich domain of 40 to 60 residues that coordinates two zinc ions, and has the consensus sequence: C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-C-X2-C-X(4-48)-C-X2-C where X is any amino acid. Many proteins containing a RING finger play a key role in the ubiquitination pathway.


Pssm-ID: 333836 [Multi-domain]  Cd Length: 40  Bit Score: 51.21  E-value: 1.11e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 341898957  764 CTVCHEDFSHPIK-LECNHIFCKSCIETWL-DQKSTCPMC 801
Cdd:pfam00097   1 CPICLEEPKDPVTiLPCGHLFCSKCILSWLeSGNVTCPLC 40
RING-HC_MID_C-I cd16575
RING finger, HC subclass, found in midline-1 (MID1), midline-2 (MID2) and similar proteins; ...
764-802 1.35e-08

RING finger, HC subclass, found in midline-1 (MID1), midline-2 (MID2) and similar proteins; MID1, also known as midin, midline 1 RING finger protein, putative transcription factor XPRF, RING finger protein 59 (RNF59), or tripartite motif-containing protein 18 (TRIM18), is a microtubule-associated E3 ubiquitin-protein ligase implicated in epithelial-mesenchymal differentiation, cell migration and adhesion, and programmed cell death along specific regions of the ventral midline during embryogenesis. MID2, also known as midin-2, midline defect 2, RING finger protein 60 (RNF60), or tripartite motif-containing protein 1 (TRIM1), is highly related to MID1. It associates with the microtubule network and may at least partially compensate for the loss of MID1. Both MID1 and MID2 interacts with Alpha 4, which is a regulatory subunit of PP2-type phosphatases, such as PP2A, and an integral component of the rapamycin-sensitive signaling pathway. They also play a central role in the regulation of granule exocytosis and the functional redundancy exists between MID1 and MID2 in cytotoxic lymphocytes (CTL). Both MID1 and MID2 belong to the C-I subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 319489 [Multi-domain]  Cd Length: 52  Bit Score: 51.38  E-value: 1.35e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 341898957 764 CTVCHEDFSHPIKLECNHIFCKSCIETWL------------DQKSTCPMCR 802
Cdd:cd16575    1 CPICLELFEDPILLPCSHNLCKSCAERLVvshcgsgesgetRESFRCPTCR 51
RING-H2_RNF181 cd16669
RING finger, H2 subclass, found in RING finger protein 181 (RNF181) and similar proteins; ...
763-804 1.67e-08

RING finger, H2 subclass, found in RING finger protein 181 (RNF181) and similar proteins; RNF181, also known as HSPC238, is a platelet E3 ubiquitin-protein ligase containing a C3H2C3-type RING-H2 finger. It interacts with the KVGFFKR motif of platelet integrin alpha(IIb)beta3, suggesting a role for RNF181-mediated ubiquitination in integrin and platelet signaling. It also suppresses the tumorigenesis of hepatocellular carcinoma (HCC) through the inhibition of extracellular signal-regulated kinase/mitogen-activated protein kinase (ERK/MAPK) signaling in the liver.


Pssm-ID: 319583 [Multi-domain]  Cd Length: 46  Bit Score: 50.83  E-value: 1.67e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 341898957 763 QCTVCHEDFSHP---IKLECNHIFCKSCIETWLDQKSTCPMCRAE 804
Cdd:cd16669    1 KCPVCLLEFEEGeevKEMPCKHSFHSGCILPWLKKTNSCPLCRHE 45
RING-HC_HLTF cd16509
RING finger, HC subclass, found in helicase-like transcription factor (HLTF) and similar ...
764-802 1.70e-08

RING finger, HC subclass, found in helicase-like transcription factor (HLTF) and similar proteins; HLTF, also known as DNA-binding protein/plasminogen activator inhibitor 1 regulator, or HIP116, or RING finger protein 80, or SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 3, or sucrose nonfermenting protein 2-like 3, is a yeast RAD5 homolog found in mammals. It has both E3 ubiquitin ligase and DNA helicase activities, and plays a pivotal role in the template-switching pathway of DNA damage tolerance. It is involved in Lys-63-linked poly-ubiquitination of proliferating cell nuclear antigen (PCNA) at Lys-164 and in the regulation of DNA damage tolerance. It shows double-stranded DNA translocase activity with 3'-5' polarity, thereby facilitating regression of the replication fork. HLTF contains an N-terminal HIRAN (HIP116 and RAD5 N-terminal) domain, a SWI/SNF helicase domain that is divided into N- and C-terminal parts by an insertion of a C3HC4-type RING-HC finger involved in the poly-ubiquitination of PCNA.


Pssm-ID: 319423 [Multi-domain]  Cd Length: 43  Bit Score: 50.76  E-value: 1.70e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 341898957 764 CTVCHEDFSHPIKLECNHIFCKSCIETWLD--QKSTCPMCR 802
Cdd:cd16509    3 CPICLDSLKDPVITPCAHVFCRGCIEQVIQrePNAKCPLCR 43
RING-HC_RNF168 cd16550
RING finger, HC subclass, found in RING finger protein 168 (RNF168) and similar proteins; ...
764-802 2.40e-08

RING finger, HC subclass, found in RING finger protein 168 (RNF168) and similar proteins; RNF168 is an E3 ubiquitin-protein ligase that promotes noncanonical K27 ubiquitination to signal DNA damage. It, together with RNF8, functions as a DNA damage response (DDR) factor that promotes a series of ubiquitylation events on substrates, such as H2A and H2AX with H2AK13/15 ubiquitylation, facilitates recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of double-strand breaks (DSBs), and inhibits homologous recombination (HR) in cells deficient in the tumor suppressor BRCA1. RNF168 also promotes H2A neddylation, which antagonizes ubiquitylation of H2A and regulates DNA damage repair. Moreover, RNF168 forms a functional complex with RAD6A or RAD6B during the DNA damage response. RNF168 contains an N-terminal C3HC4-type RING-HC finger that catalyzes H2A-K15ub and interacts with H2A, and two MIU (motif interacting with ubiquitin) domains responsible for the interaction with K63 linked poly-ubiquitin.


Pssm-ID: 319464 [Multi-domain]  Cd Length: 42  Bit Score: 50.37  E-value: 2.40e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 341898957 764 CTVCHEDFSHPIKLECNHIFCKSCIETWLDQKS-TCPMCR 802
Cdd:cd16550    1 CPICLEILVEPVTLPCKHELCLPCFQQTVEKANlCCPLCR 40
RING-H2_DZIP3 cd16460
RING finger, H2 subclass, found in DAZ (deleted in azoospermia)-interacting protein 3 (DZIP3) ...
764-802 3.07e-08

RING finger, H2 subclass, found in DAZ (deleted in azoospermia)-interacting protein 3 (DZIP3) and similar proteins; DZIP3, also known as RNA-binding ubiquitin ligase of 138 kDa (RUL138) or 2A-HUB protein, is an RNA-binding E3 ubiquitin-protein ligase that interacts with coactivator-associated arginine methyltransferase 1 (CARM1) and acts as a transcriptional coactivator of estrogen receptor (ER) alpha. It is also a histone H2A ubiquitin ligase that catalyzes monoubiquitination of H2A at lysine 119, functioning as a combinatoric component of the repression machinery required for repressing a specific chemokine gene expression program, critically modulating migratory responses to Toll-like receptors (TLR) activation. DZIP3 contains a C3H2C3-type RING-H2 finger at the C-terminus.


Pssm-ID: 319374 [Multi-domain]  Cd Length: 43  Bit Score: 50.02  E-value: 3.07e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 341898957 764 CTVCHEDFS--HPIKLECNHIFCKSCIETWLDQKSTCPMCR 802
Cdd:cd16460    3 CVICHENLSpeNLSVLPCAHKFHSQCIRPWLMQQRTCPTCR 43
RING-HC_AtRMA_like cd16745
RING finger, HC subclass, found in Arabidopsis thaliana RING membrane-anchor proteins (AtRMAs) ...
764-803 3.46e-08

RING finger, HC subclass, found in Arabidopsis thaliana RING membrane-anchor proteins (AtRMAs) and similar proteins; AtRMAs, including AtRma1, AtRma2, and AtRma3, are endoplasmic reticulum (ER)-localized Arabidopsis homologs of human outer membrane of the ER-anchor E3 ubiquitin-protein ligase, RING finger protein 5 (RNF5). AtRMAs possess E3 ubiquitin ligase activity, and may play a role in the growth and development of Arabidopsis. The AtRMA1 and AtRMA3 genes are predominantly expressed in major tissues, such as cotyledons, leaves, shoot-root junction, roots, and anthers, while AtRMA2 expression is restricted to the root tips and leaf hydathodes. AtRma1 probably functions with the Ubc4/5 subfamily of E2. AtRma2 is likely involved in the cellular regulation of ABP1 expression levels through interacting with auxin binding protein 1 (ABP1). AtRMA proteins contain an N-terminal C3HC4-type RING-HC finger and a trans-membrane-anchoring domain in their extreme C-terminal region.


Pssm-ID: 319659 [Multi-domain]  Cd Length: 45  Bit Score: 50.00  E-value: 3.46e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 341898957 764 CTVCHEDFSHPIKLECNHIFCKSCIETWLDQKS---TCPMCRA 803
Cdd:cd16745    3 CNICLDLASDPVVTLCGHLFCWPCLYRWLQRHSenrECPVCKA 45
RING-HC_COP1 cd16504
RING finger, HC subclass, found in constitutive photomorphogenesis protein 1 (COP1) and ...
760-802 3.58e-08

RING finger, HC subclass, found in constitutive photomorphogenesis protein 1 (COP1) and similar proteins; COP1, also known as RING finger and WD repeat domain protein 2 (RFWD2) or RING finger protein 200 (RNF200), was defined as a central regulator of photomorphogenic development in plants, which targets key transcription factors for proteasome-dependent degradation. It is localized predominantly in the nucleus, but may also be present in the cytosol. Mammalian COP1 functions as an E3 ubiquitin-protein ligase that interacts with Jun transcription factors and modulates their transcriptional activity. It also interacts with and negatively regulates the tumor-suppressor protein p53. Moreover, COP1 associates with COP9 signalosome subunit 6 (CSN6), and is involved in 14-3-3 delta ubiquitin-mediated degradation. The CSN6-COP1 link enhances ubiquitin-mediated degradation of p27(Kip1), a critical CDK inhibitor involved in cell cycle regulation, to promote cancer cell growth. Furthermore, COP1 functions as the negative regulator of ETV1 and influences prognosis in triple-negative breast cancer. COP1 contains an N-terminal extension, a C3HC4-type RING-HC finger, a coiled coil domain, and seven WD40 repeats. In human COP1, a classic leucine-rich NES, and a novel bipartite NLS is bridged by the RING-HC finger.


Pssm-ID: 319418 [Multi-domain]  Cd Length: 46  Bit Score: 49.95  E-value: 3.58e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 341898957 760 DDNQCTVCHEDFSHPIKLECNHIFCKSCIETWLDQKSTCPMCR 802
Cdd:cd16504    1 NDFICPICFDIIEEAYMTKCGHSFCYKCIRTSLEQSNRCPKCN 43
RING-HC_TRIM65_C-IV cd16609
RING finger, HC subclass, found in tripartite motif-containing protein TRIM65 and similar ...
763-802 3.62e-08

RING finger, HC subclass, found in tripartite motif-containing protein TRIM65 and similar proteins; TRIM65 is an E3 ubiquitin-protein ligase that interacts with the innate immune receptor MDA5 enhancing its ability to stimulate interferon-beta signaling. It functions as a potential oncogenic protein that negatively regulates p53 through ubiquitination, providing insight into development of novel approaches targeting TRIM65 for non-small cell lung carcinoma (NSCLC) treatment, and also overcoming chemotherapy resistance. Moreover, TRIM65 negatively regulates microRNA-driven suppression of mRNA translation by targeting TNRC6 proteins for ubiquitination and degradation. TRIM65 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 319523 [Multi-domain]  Cd Length: 47  Bit Score: 50.18  E-value: 3.62e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 341898957 763 QCTVCHEDFSHPIKLECNHIFCKSCIETWLDQKS------TCPMCR 802
Cdd:cd16609    2 TCSICLELFTDPVTLPCGHNFCGECIRDHWDKCElikkgySCPQCR 47
RING-H2_RNF130 cd16803
RING finger, H2 subclass, found in RING finger protein 130 (RNF130) and similar proteins; ...
762-807 4.34e-08

RING finger, H2 subclass, found in RING finger protein 130 (RNF130) and similar proteins; RNF130, also known as Goliath homolog (H-Goliath), is a paralog of RNF128, also known as gene related to anergy in lymphocytes protein (GRAIL). It is a transmembrane E3 ubiquitin-protein ligase expressed in leukocytes. It has a self-ubiquitination property, and controls the development of T cell clonal anergy by ubiquitination. RNF130 contains an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C-terminal C3H2C3-type RING-H2 finger domain followed by a putative PEST sequence.


Pssm-ID: 319717 [Multi-domain]  Cd Length: 49  Bit Score: 49.97  E-value: 4.34e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 341898957 762 NQCTVCHEDFSHP--IK-LECNHIFCKSCIETWLDQKSTCPMCRAEVTK 807
Cdd:cd16803    1 DHCAVCIEGYKQNdvVRiLPCKHVFHKSCVDPWLNEHCTCPMCKLNILK 49
RING-HC_TRIM4_C-IV_like cd16590
RING finger, HC subclass, found in tripartite motif-containing proteins, TRIM4, TRIM75, ...
764-802 4.82e-08

RING finger, HC subclass, found in tripartite motif-containing proteins, TRIM4, TRIM75, tripartite motif family-like protein 1 (TRIML1) and similar proteins; TRIM4 and TRIM75, two closely related tripartite motif-containing proteins, belong to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a SPRY/B30.2 domain positioned C-terminal to the RBCC domain. TRIM4, also known as RING finger protein 87 (RNF87), is a cytoplasmic E3 ubiquitin-protein ligase that it had recently evolved and is present only in higher mammals. It transiently interacts with mitochondria, induces mitochondrial aggregation and sensitizes the cells to hydrogen peroxide (H2O2) induced death. Its interaction with peroxiredoxin 1 (PRX1) is critical for the regulation of H2O2 induced cell death. Moreover, TRIM4 functions as a positive regulator of RIG-I-mediated type I interferon induction. It regulates the K63-linked ubiquitination of RIG-1 and assembly of antiviral signaling complex at mitochondria. TRIM75 mainly localizes within spindles, suggesting it may function in spindle organization and thereby affect meiosis. The family also includes TRIML1 that is identical to TRIM11 and TRIM17 except for the absence of B-box domain. TRIML1, also known as RING finger protein 209 (RNF209), is a probable E3 ubiquitin-protein ligase expressed in embryo before implantation. It plays an important role in blastocyst development. By interacting with USP5 (also known as isoT), TRIML1 may exerts its influence on debranching ubiquitin from multi-chains on the stability and activity of protein substrates in the preimplantation embryo.


Pssm-ID: 319504 [Multi-domain]  Cd Length: 45  Bit Score: 49.40  E-value: 4.82e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 341898957 764 CTVCHEDFSHPIKLECNHIFCKSCI-ETWLDQKS--TCPMCR 802
Cdd:cd16590    4 CSICLDYFKDPVTIECGHNFCRGCIlQSWENLNTpfSCPECR 45
RING-H2_RNF128_like cd16802
RING finger, H2 subclass, found in RING finger protein 128 (RNF128) and similar proteins; This ...
762-807 4.96e-08

RING finger, H2 subclass, found in RING finger protein 128 (RNF128) and similar proteins; This subfamily includes RING finger proteins RNF128, RNF133, RNF148, and similar proteins, which belong to a larger PA-TM-RING ubiquitin ligase family that has been characterized by containing an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C-terminal C3H2C3-type RING-H2 finger domain followed by a putative PEST sequence. RNF128, also known as gene related to anergy in lymphocytes protein (GRAIL), is a type 1 transmembrane E3 ubiquitin-protein ligase that is a critical regulator of adaptive immunity and development. It inhibits cytokine gene transcription is expressed in anergic CD4+ T cells, and has been implicated in primary T cell activation, survival, and differentiation, as well as in T cell anergy and oral tolerance. It induces T cell anergy through the ubiquitination activity of its cytosolic RING finger. It regulates expression of the costimulatory molecule CD40L on CD4 T cells, and ubiquitinates the costimulatory molecule CD40 ligand (CD40L) during the induction of T cell anergy. Moreover, RNF128 interacts with the luminal/extracellular portion of both CD151 and the related tetraspanin CD81 via its PA domain, which promoted ubiquitination of cytosolic lysine residues. It also down-modulates the expression of CD83 (previously described as a cell surface marker for mature dendritic cells) on CD4 T cells. Furthermore, Rho guanine dissociation inhibitor (RhoGDI) has been identified as a potential substrate of RNF128, suggesting a role for Rho effector molecules in T cell anergy. In addition, RNF128 plays a role in environmental stress responses. It promotes environmental salinity tolerance in euryhaline tilapia. RNF133 is a testis-specific endoplasmic reticulum-associated E3 ubiquitin ligase that is mainly present in the cytoplasm of elongated spermatids. It may play a role in sperm maturation through an ER-associated degradation (ERAD) pathway. RNF148 is a testis-specific E3 ubiquitin ligase that is abundantly expressed in testes and slightly expressed in pancreas. Its expression regulated by histone deacetylases.


Pssm-ID: 319716 [Multi-domain]  Cd Length: 49  Bit Score: 49.82  E-value: 4.96e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 341898957 762 NQCTVCHEDF--SHPIK-LECNHIFCKSCIETWLDQKSTCPMCRAEVTK 807
Cdd:cd16802    1 DSCAVCIEPYkpNDVVRiLTCNHFFHKSCIDPWLLEHRTCPMCKCDILK 49
RING-HC_TRIM50_like_C-IV cd16605
RING finger, HC subclass, found in tripartite motif-containing protein TRIM50, TRIM73, TRIM74 ...
763-802 5.02e-08

RING finger, HC subclass, found in tripartite motif-containing protein TRIM50, TRIM73, TRIM74 and similar proteins; TRIM50 is a stomach-specific E3 ubiquitin-protein ligase, encoded by the Williams-Beuren syndrome (WBS) TRIM50 gene, which regulates vesicular trafficking for acid secretion in gastric parietal cells. It colocalizes, interacts with, and increases the level of p62/SQSTM1, a multifunctional adaptor protein implicated in various cellular processes including the autophagy clearance of polyubiquitinated protein aggregates. It also promotes the formation and clearance of aggresome-associated polyubiquitinated proteins through the interaction with the histone deacetylase 6 (HDAC6), a tubulin specific deacetylase that regulates microtubule-dependent aggresome formation. TRIM50 can be acetylated by PCAF and p300. TRIM50 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. The family also includes two paralogs of TRIM50, tripartite motif-containing protein 73 (TRIM73), also known as tripartite motif-containing protein 50B (TRIM50B), and tripartite motif-containing protein 74 (TRIM74), also known as tripartite motif-containing protein 50C (TRIM50C), both of which are WBS-related genes encoding proteins and may also act as E3 ligases. In contrast with TRIM50, TRIM73 and TRIM74 belong to the C-V subclass of TRIM family of proteins that are defined by an N-terminal RBCC domains only.


Pssm-ID: 319519 [Multi-domain]  Cd Length: 45  Bit Score: 49.44  E-value: 5.02e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 341898957 763 QCTVCHEDFSHPIKLECNHIFCKSCIETW---LDQKSTCPMCR 802
Cdd:cd16605    2 LCPICLEVFKEPLMLQCGHSYCKSCLVSLsceLDGQLLCPVCR 44
RAD18 COG5432
RING-finger-containing E3 ubiquitin ligase [Signal transduction mechanisms];
745-804 6.94e-08

RING-finger-containing E3 ubiquitin ligase [Signal transduction mechanisms];


Pssm-ID: 227719 [Multi-domain]  Cd Length: 391  Bit Score: 55.48  E-value: 6.94e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 341898957 745 ITDSSVGTSVKI-----LECDDnQCTVCHEDFSHPIKLECNHIFCKSCIETWLDQKSTCPMCRAE 804
Cdd:COG5432    5 ATDPSDWNQTKIpslkgLDSML-RCRICDCRISIPCETTCGHTFCSLCIRRHLGTQPFCPVCRED 68
RING-HC_RAD18 cd16529
RING finger, HC subclass, found in postreplication repair protein RAD18 and similar proteins; ...
763-802 8.94e-08

RING finger, HC subclass, found in postreplication repair protein RAD18 and similar proteins; RAD18, also known as HR18 or RING finger protein 73 (RNF73), is an E3 ubiquitin-protein ligase involved in post replication repair of UV-damaged DNA via its recruitment to stalled replication forks. It associates to the E2 ubiquitin conjugating enzyme UBE2B to form the UBE2B-RAD18 ubiquitin ligase complex involved in mono-ubiquitination of DNA-associated PCNA on K164. It also interacts with another E2 ubiquitin conjugating enzyme RAD6 to form a complex that monoubiquitinates proliferating cell nuclear antigen at stalled replication forks in DNA translesion synthesis. Moreover, Rad18 is a key factor in double-strand break DNA damage response (DDR) pathways via its association with K63-linked polyubiquitylated chromatin proteins. It can function as a mediator for DNA damage response signals to activate the G2/M checkpoint in order to maintain genome integrity and cell survival after ionizing radiation (IR) exposure. RAD18 contains a C3HC4-type RING-HC finger, a ubiquitin-binding zinc finger domain (UBZ), a SAP (SAF-A/B, Acinus and PIAS) domain, and a RAD6-binding domain (R6BD).


Pssm-ID: 319443 [Multi-domain]  Cd Length: 42  Bit Score: 48.80  E-value: 8.94e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 341898957 763 QCTVCHEDFSH-PIKLECNHIFCKSCIETWLDQKSTCPMCR 802
Cdd:cd16529    2 RCPICFDYFDTaPMITPCSHNFCSLCIRRHLSYKTQCPTCR 42
RING-HC_RNF208 cd16559
RING finger, HC subclass, found in RING finger protein 208 (RNF208) and similar proteins; ...
764-804 1.03e-07

RING finger, HC subclass, found in RING finger protein 208 (RNF208) and similar proteins; RNF208 is an E3 ubiquitin-protein ligase whose activity can be modulated by S-nitrosylation. It contains a C3HC4-type RING-HC finger.


Pssm-ID: 319473 [Multi-domain]  Cd Length: 50  Bit Score: 48.63  E-value: 1.03e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 341898957 764 CTVCHEDFSHPIKLECNHIFCKSCIETWLDQKS-----TCPMCRAE 804
Cdd:cd16559    4 CPLCGETYNRPRILSCLHSFCEPCLQKLYESCPkykfiSCPTCKRE 49
RING-HC_RNF213 cd16561
RING finger, HC subclass, found in RING finger protein 213 (RNF213) and similar proteins; ...
764-802 1.07e-07

RING finger, HC subclass, found in RING finger protein 213 (RNF213) and similar proteins; RNF213, also known as ALK lymphoma oligomerization partner on chromosome 17 or Moyamoya steno-occlusive disease-associated AAA+ and RING finger protein (mysterin), is an intracellular soluble protein that functions as an E3 ubiquitin-protein ligase and AAA+ ATPase, which possibly contributes to vascular development through mechanical processes in the cell. It plays a unique role in endothelial cells for proper gene expression in response to inflammatory signals from the environment. Mutations in RNF213 may associate with Moyamoya disease (MMD), an idiopathic cerebrovascular occlusive disorder prevalent in East Asia. It also acts as a nuclear marker for acanthomorph phylogeny. RNF213 contains two tandem enzymatically active AAA+ ATPase modules and a C3HC4-type RING-HC finger. It can forms huge ring-shaped oligomeric complex.


Pssm-ID: 319475 [Multi-domain]  Cd Length: 41  Bit Score: 48.63  E-value: 1.07e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 341898957 764 CTVCHEDFSHPIKLECNHIFCKSCIETWLDQ--KSTCPMCR 802
Cdd:cd16561    1 CSICLEDPKDPVSLPCDHIHCLTCLRQWFRPvgQMHCPTCR 41
RING-HC_TRIM11_like_C-IV cd16594
RING finger, HC subclass, found in tripartite motif-containing proteins, TRIM11 and TRIM27, ...
764-802 1.07e-07

RING finger, HC subclass, found in tripartite motif-containing proteins, TRIM11 and TRIM27, and similar proteins; TRIM11 and TRIM27, two closely related tripartite motif-containing proteins, belong to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a SPRY/B30.2 domain positioned C-terminal to the RBCC domain. TRIM11, also known as protein BIA1, or RING finger protein 92 (RNF92), is an E3 ubiquitin-protein ligase involved in the development of the central nervous system. It is overexpressed in high-grade gliomas and promotes proliferation, invasion, migration and glial tumor growth. TRIM11 acts as a potential therapeutic target for congenital central hypoventilation syndrome (CCHS) through mediating the degradation of congenital central hypoventilation syndrome-associated polyalanine-expanded Phox2b. Trim11 modulates the function of neurogenic transcription factor Pax6 through ubiquitin-proteosome system, and thus plays an essential role for the Pax6-dependent neurogenesis. It also binds to and destabilizes a key component of the activator-mediated cofactor complex (ARC105), humanin, a neuroprotective peptide against Alzheimer"s disease-relevant insults, through the ubiquitin-proteasome system, and further regulates ARC105 function in transforming growth factor beta (TGFbeta) signaling. Moreover, TRIM11 negatively regulates retinoic acid-inducible gene-I (RIG-I)-mediated interferon-beta (IFNbeta) production and antiviral activity by targeting TANK-binding kinase-1 (TBK1). It may contribute to the endogenous restriction of retroviruses in cells. It enhances N-tropic murine leukemia virus (N-MLV) entry by interfering with Ref1 restriction. It also suppresses the early steps of human immunodeficiency virus HIV-1 transduction, resulting in decreased reverse transcripts. TRIM27, also known as RING finger protein 76 (RNF76), RET finger protein (RFP), or zinc finger protein RFP, is a nuclear E3 ubiquitin-protein ligase that is highly expressed in testis and in various tumor cell lines. Expression of TRIM27 is associated with prognosis of colon and endometrial cancers. TRIM27 was first identified as a fusion partner of the RET receptor tyrosine kinase. It functions as a transcriptional repressor and associates with several proteins involved in transcriptional activity, such as enhancer of polycomb 1 (Epc1), a member of the Polycomb group proteins, and Mi-2beta, a main component of the nucleosome remodeling and deacetylase (NuRD) complex, and the cell cycle regulator retinoblastoma protein (RB1). It also interacts with HDAC1, leading to downregulation of thioredoxin binding protein 2 (TBP-2), which inhibits the function of thioredoxin. Moreover, TRIM27 mediates Pax7-induced ubiquitination of MyoD in skeletal muscle atrophy. In addition, it inhibits muscle differentiation by modulating serum response factor (SRF) and Epc1. Furthermore, TRIM27 promote a non-canonical polyubiquitinations of PTEN, a lipid phosphatase that catalyzes PtdIns(3,4,5)P3 (PIP3) to PtdIns(4,5)P2 (PIP2). It is an IKKepsilon-interacting protein that regulates IkappaB kinase (IKK) function and negatively regulates signaling involved in the antiviral response and inflammation. In addition, TRIM27 forms a protein complex with MBD4 or MBD2 or MBD3, and thus plays an important role in the enhancement of transcriptional repression through MBD proteins in tumorigenesis, spermatogenesis, and embryogenesis. It is also a component of an estrogen receptor 1 (ESR1) regulatory complex, and is involved in estrogen receptor-mediated transcription in MCF-7 cells. Meanwhile, TRIM27 interacts with the hinge region of chromosome 3 protein (SMC3), a component of the multimeric cohesin complex that holds sister chromatids together and prevents their premature separation during mitosis.


Pssm-ID: 319508 [Multi-domain]  Cd Length: 45  Bit Score: 48.62  E-value: 1.07e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 341898957 764 CTVCHEDFSHPIKLECNHIFCKSCI-ETWLDQK--STCPMCR 802
Cdd:cd16594    4 CPVCLEYFTDPVILDCGHNFCRACIlRCWETRAtpVSCPQCR 45
RING-HC_TRIM35_C-IV cd16599
RING finger, HC subclass, found in tripartite motif-containing protein 35 (TRIM35) and similar ...
764-802 1.17e-07

RING finger, HC subclass, found in tripartite motif-containing protein 35 (TRIM35) and similar proteins; TRIM35, also known as hemopoietic lineage switch protein 5 (HLS5), is a putative hepatocellular carcinoma (HCC) suppressor that inhibits phosphorylation of pyruvate kinase isoform M2 (PKM2), which is involved in aerobic glycolysis of cancer cells and further suppresses the Warburg effect and tumorigenicity in HCC. It also negatively regulates Toll-like receptor 7 (TLR7)- and TLR9-mediated type I interferon production by suppressing the stability of interferon regulatory factor 7 (IRF7). Moreover, TRIM35 regulates erythroid differentiation by modulating globin transcription factor 1 (GATA-1) activity. TRIM35 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 319513 [Multi-domain]  Cd Length: 44  Bit Score: 48.39  E-value: 1.17e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 341898957 764 CTVCHEDFSHPIKLECNHIFCKSCI-ETWLDQKSTCPMCR 802
Cdd:cd16599    4 CPICYDPFREAVTLRCGHNFCKGCVsRSWEVRSHTCPVCK 43
PHA02929 PHA02929
N1R/p28-like protein; Provisional
761-807 1.19e-07

N1R/p28-like protein; Provisional


Pssm-ID: 222944  Cd Length: 238  Bit Score: 53.24  E-value: 1.19e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 341898957 761 DNQCTVCHED-FSHPIK-------LECNHIFCKSCIETWLDQKSTCPMCRAE---VTK 807
Cdd:PHA02929 174 DKECAICMEKvYDKEIKnmyfgilSNCNHVFCIECIDIWKKEKNTCPVCRTPfisVIK 231
RING-HC_DTX3L cd16712
RING finger, HC subclass, found in protein Deltex-3-like (DTX3L) and similar proteins; DTX3L, ...
764-801 1.23e-07

RING finger, HC subclass, found in protein Deltex-3-like (DTX3L) and similar proteins; DTX3L, also known as B-lymphoma- and BAL-associated protein (BBAP) or Rhysin-2 (Rhysin2), is a RING-domain E3 ubiquitin-protein ligase that regulates endosomal sorting of the G protein-coupled receptor CXCR4 from endosomes to lysosomes. It also regulates subcellular localization of its partner protein, B aggressive lymphoma (BAL), by a dynamic nucleocytoplasmic trafficking mechanism. DTX3L has a unique N-terminus, but lacks the highly basic N-terminal motif and the central proline-rich motif present in other Deltex (DTX) family members, such as DTX1, DTX2, and DTX4. Moreover, its C-terminal region is highly homologous to DTX3. It includes a C3HC4-type RING-HC finger, and a previously unidentified C-terminal domain. DTX3L can associate with DTX1 through its unique N-terminus and further enhance self-ubiquitination.


Pssm-ID: 319626 [Multi-domain]  Cd Length: 41  Bit Score: 48.22  E-value: 1.23e-07
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 341898957 764 CTVCHEDFSHPIKLE-CNHIFCKSCIETWLDQKSTCPMC 801
Cdd:cd16712    2 CPICMDKVSDPKVLPkCKHVFCAACIDEAFKHKPVCPVC 40
RING-H2_RNF149 cd16804
RING finger, H2 subclass, found in RING finger protein 149 (RNF149) and similar proteins; ...
764-807 1.35e-07

RING finger, H2 subclass, found in RING finger protein 149 (RNF149) and similar proteins; RNF149, also known as DNA polymerase-transactivated protein 2, is an E3 ubiquitin-protein ligase that interacts with wild-type v-Raf murine sarcoma viral oncogene homolog B1 (BRAF), a RING domain-containing E3 ubiquitin ligase involved in control of gene transcription, translation, cytoskeletal organization, cell adhesion, and epithelial development. RNF149 induces the ubiquitination of wild-type BRAF and promotes its proteasome-dependent degradation. Mutated RNF149 has been found in some human breast, ovarian, and colorectal cancers. RNF149 contains an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C-terminal C3H2C3-type RING-H2 finger domain followed by a putative PEST sequence.


Pssm-ID: 319718 [Multi-domain]  Cd Length: 48  Bit Score: 48.35  E-value: 1.35e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 341898957 764 CTVCHEDFSHP--IK-LECNHIFCKSCIETWLDQKSTCPMCRAEVTK 807
Cdd:cd16804    2 CAVCIENYKPKdvVRiLPCKHIFHRICIDPWLLEHRTCPMCKLDVIK 48
RING-HC_LNX3 cd16718
RING finger, HC subclass, found in ligand of numb protein X 3 (LNX3); LNX3, also known as PDZ ...
763-802 1.97e-07

RING finger, HC subclass, found in ligand of numb protein X 3 (LNX3); LNX3, also known as PDZ domain-containing RING finger protein 3 (PDZRN3), or Semaphorin cytoplasmic domain-associated protein 3 (SEMACAP3), is an E3 ubiquitin-protein ligase that was first identified as a Semaphorin-binding partner. It is also responsible for the ubiquitination and degradation of Numb, a component of the Notch signaling pathway that functions in the specification of cell fates during development and is known to control cell numbers during neurogenesis in vertebrates. LNX3 acts as a negative regulator of osteoblast differentiation by inhibiting Wnt-beta-catenin signaling. LNX3 also plays an important role in neuromuscular junction formation. It interacts with and ubiquitinates the muscle specific tyrosine kinase (MuSK), thus promoting its endocytosis and negatively regulating the cell surface expression of this key regulator of postsynaptic assembly. LNX3 contains an N-terminal typical C3HC4-type RING-HC finger, two PDZ domains, and a C-terminal LNX3 homology (LNX3H) domain.


Pssm-ID: 319632 [Multi-domain]  Cd Length: 42  Bit Score: 47.67  E-value: 1.97e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 341898957 763 QCTVCHEDFSHPIKLECNHIFCKSCIETWLDQKSTCPM-CR 802
Cdd:cd16718    1 KCNLCNKVLEDPLTTPCGHVFCAGCVLPWVVQQGSCPVkCQ 41
RING-HC_TRIM7_C-IV cd16592
RING finger, HC subclass, found in tripartite motif-containing protein 7 (TRIM7) and similar ...
763-802 1.99e-07

RING finger, HC subclass, found in tripartite motif-containing protein 7 (TRIM7) and similar proteins; TRIM7, also known as glycogenin-interacting protein (GNIP) or RING finger protein 90 (RNF90), is an E3 ubiquitin-protein ligase that mediates c-Jun/AP-1 activation by Ras signalling. Its phosphorylation and activation by MSK1 in response to direct activation by the Ras-Raf-MEK-ERK pathway can stimulate TRIM7 E3 ubiquitin ligase activity in mediating Lys63-linked ubiquitination of the AP-1 coactivator RACO-1, leading to RACO-1 protein stabilization. Moreover, TRIM7 binds and activates glycogenin, the self-glucosylating initiator of glycogen biosynthesis. TRIM7 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 319506 [Multi-domain]  Cd Length: 45  Bit Score: 47.86  E-value: 1.99e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 341898957 763 QCTVCHEDFSHPIKLECNHIFCKSCI-ETWLDQKST--CPMCR 802
Cdd:cd16592    3 SCSICLDLFRDPVSIPCGHNFCRACIrRCWELQGSTfsCPQCR 45
RING_Ubox cd00162
The superfamily of RING finger (Really Interesting New Gene) domain and U-box domain; RING ...
764-801 2.02e-07

The superfamily of RING finger (Really Interesting New Gene) domain and U-box domain; RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized as two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers. Some have different Cys/His pattern. Some lack a single Cys or His residues at typical Zn ligand positions. Especially, the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can indeed chelate Zn in a RING finger as well. C4C4-, C3HC3D-, C2H2C4-, and C3HC5-type RING fingers are closely related to RING-HC finger. In contrast, C4HC3- (RING-CH alias RINGv), C3H3C2-, C3H2C2D-, C3DHC3-, and C4HC2H-type RING fingers are close to RING-H2 finger. However, not all RING finger-containing proteins display regular RING finger features, and the RING finger family has turned out to be multifarious. The degenerated RING fingers from Siz/PIAS RING (SP-RING) family proteins and sporulation protein RMD5, are characterized by lacking the second, fifth, and sixth Zn2+ ion-coordinating residues. They bind only one Zn2+ ion. On the other hand, the RING fingers of the human APC11 and RBX1 proteins can bind a third Zn atom since they harbor four additional Zn ligands. U-box is a modified form of the RING finger domain that lacks metal chelating Cys and His. It resembles the cross-brace RING structure consisting of three beta-sheets and a single alpha-helix, which would be stabilized by salt bridges instead of chelated metal ions. U-box proteins are widely distributed among eukaryotic organisms and show a higher prevalence in plants than in other organisms. RING finger/U-box-containing proteins are a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serves as a scaffold for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enables efficient transfer of ubiquitin from E2 to the substrates.


Pssm-ID: 319361 [Multi-domain]  Cd Length: 40  Bit Score: 47.85  E-value: 2.02e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 341898957 764 CTVCHEDFSHPIKLE-CNHIFCKSCIETWL-DQKSTCPMC 801
Cdd:cd00162    1 CPICRELMKDPVVLPsCGHTFCYSCIARWLeSSDQTCPFC 40
RING-HC_TRIM25_C-IV cd16597
RING finger, HC subclass, found in tripartite motif-containing protein TRIM25 and similar ...
764-802 2.12e-07

RING finger, HC subclass, found in tripartite motif-containing protein TRIM25 and similar proteins; TRIM25, also known as estrogen-responsive finger protein (EFP), RING finger protein 147 (RNF147), or RING-type E3 ubiquitin transferase, is an E3 ubiquitin/ISG15 ligase that is induced by estrogen and is therefore particularly abundant in placenta and uterus. TRIM25 regulates various cellular processes through E3 ubiquitin ligase activity, transferring ubiquitin and ISG15 to target proteins. It mediates K63-linked polyubiquitination of retinoic acid inducible gene I (RIG-I) that is crucial for downstream antiviral interferon signaling. It is also required for melanoma differentiation-associated gene 5 (MDA5) and mitochondrial antiviral signaling (MAVS, also known as IPS-1, VISA, Cardiff) mediated activation of nuclear factor-kappaB (NF-kappaB) and interferon production. Upon UV irradiation, TRIM25 interacts with mono-ubiquitinated PCNA and promotes its ISG15 modification (ISGylation), suggesting a crucial role in termination of error-prone translesion DNA synthesis. TRIM25 also functions as a novel regulator of p53 and Mdm2. It enhances p53 and Mdm2 abundance by inhibiting their ubiquitination and degradation in 26S proteasomes. Meanwhile, it inhibits p53's transcriptional activity and dampens the response to DNA damage, and is essential for medaka development and this dependence is rescued by silencing of p53. Moreover, TRIM25 is involved in the host cellular innate immune response against retroviral infection. It interferes with the late stage of feline leukemia virus (FeLV) replication. Furthermore, TRIM25 acts as an oncogene in gastric cancer. Its blockade by RNA interference inhibits migration and invasion of gastric cancer cells through transforming growth factor-beta (TGF-beta) signaling, suggesting it presents a novel target for the detection and treatment of gastric cancer. In addition, TRIM25 acts as an RNA-specific activator for Lin28a/TuT4-mediated uridylation. TRIM25 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 319511 [Multi-domain]  Cd Length: 44  Bit Score: 47.57  E-value: 2.12e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 341898957 764 CTVCHEDFSHPIKLECNHIFCKSCI-ETWLDQKST--CPMCR 802
Cdd:cd16597    3 CSICLCLFDNPVTLPCGHNFCANCLeETWADQISSlfCPQCR 44
mRING-H2-C3H2C2D_ZSWM2 cd16486
Modified RING finger, H2 subclass (C3H2C2D-type), found in zinc finger SWIM domain-containing ...
763-802 2.23e-07

Modified RING finger, H2 subclass (C3H2C2D-type), found in zinc finger SWIM domain-containing protein 2 (ZSWIM2) and similar proteins; ZSWIM2, also known as MEKK1-related protein X (MEX) or ZZ-type zinc finger-containing protein 2, is a testis-specific E3 ubiquitin ligase that promotes death receptor-induced apoptosis through Fas, death receptor (DR) 3 and DR4 signaling. ZSWIM2 is self-ubiquitinated and targeted for degradation through the proteasome pathway. It also acts as an E3 ubiquitin ligase, through the E2, Ub-conjugating enzymes UbcH5a, UbcH5c, or UbcH6. ZSWIM2 contains four putative zinc-binding domains including an N-terminal SWIM (SWI2/SNF2 and MuDR) domain critical for its ubiquitination, and two modified RING-H2 fingers separated by a ZZ zinc finger domain, which was required for interaction with UbcH5a and its self-association. This family corresponds to the second RING-H2 finger, which is not a canonical C3H2C3-type, but a modified C3H2C2D-type.


Pssm-ID: 319400 [Multi-domain]  Cd Length: 44  Bit Score: 47.61  E-value: 2.23e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 341898957 763 QCTVCHEDFS---HPIKLECNHIFCKSCIETWL-DQKSTCPMCR 802
Cdd:cd16486    1 QCRICLRDFQagqVLRKLPCKHKFHRDCIDSWLtHSRPTCPLCG 44
RING-HC_RNF170 cd16553
RING finger, HC subclass, found in RING finger protein 170 (RNF170) and similar proteins; ...
764-802 2.26e-07

RING finger, HC subclass, found in RING finger protein 170 (RNF170) and similar proteins; RNF170, also known as putative LAG1-interacting protein, is an endoplasmic reticulum (ER) membrane-bound E3 ubiquitin-protein ligase that mediates ubiquitination-dependent degradation of type-I inositol 1,4,5-trisphosphate (IP3) receptors (ITPR1) via the endoplasmic-reticulum-associated protein degradation (ERAD) pathway. A point mutation (arginine to cysteine at position 199) of RNF170 gene is linked with autosomal-dominant sensory ataxia (ADSA), a disease characterized by neurodegeneration in the posterior columns of the spinal cord. RNF170 contains a C3HC4-type RING-HC finger.


Pssm-ID: 319467 [Multi-domain]  Cd Length: 44  Bit Score: 47.67  E-value: 2.26e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 341898957 764 CTVCHEDFSHPIKLECNHIFCKSCIETWLDQKST-----CPMCR 802
Cdd:cd16553    1 CPICLGDASYPVETNCGHIFCGNCIITYWRHGRWlgaisCPMCR 44
RING-HC_TRIM5_like-C-IV cd16591
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM5, TRIM6, TRIM22, ...
764-802 2.36e-07

RING finger, HC subclass, found in tripartite motif-containing proteins TRIM5, TRIM6, TRIM22, TRIM34 and similar proteins; TRIM5, TRIM6, TRIM22, and TRIM34, four closely related tripartite motif-containing proteins, belong to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. TRIM5, also known as RING finger protein 88 (RNF88), is a capsid-specific restriction factor that prevents infection from non-host-adapted retroviruses in a species-specific manner by binding to and destabilizing the retroviral capsid lattice before reverse transcription is completed. Its retroviral restriction activity correlates with the ability to activate TAK1-dependent innate immune signaling. TRIM5 also acts as a pattern recognition receptor that activates innate immune signaling in response to the retroviral capsid lattice. Moreover, TRIM5 plays a role in regulating autophagy through activation of autophagy regulator BECN1 by causing its dissociation from its inhibitors BCL2 and TAB2. It also plays a role in autophagy by acting as a selective autophagy receptor which recognizes and targets HIV-1 capsid protein p24 for autophagic destruction. TRIM6, also known as RING finger protein 89 (RNF89), is an E3-ubiquitin ligase that cooperates with the E2-ubiquitin conjugase UbE2K to catalyze the synthesis of unanchored K48-linked polyubiquitin chains, and further stimulates the interferon-I kappa B kinase epsilon (IKKepsilon) kinase-mediated antiviral response. It also regulates the transcriptional activity of Myc during the maintenance of embryonic stem (ES) cell pluripotency, and may act as a novel regulator for Myc-mediated transcription in ES cells. TRIM22, also known as 50 kDa-stimulated trans-acting factor (Staf-50) or RING finger protein 94 (RNF94), is an E3 ubiquitin-protein ligase that plays an integral role in the host innate immune response to viruses. It has been shown to inhibit the replication of a number of viruses, including HIV-1, hepatitis B, and influenza A. TRIM22 acts as a suppressor of basal HIV-1 long terminal repeat (LTR)-driven transcription by preventing the transcription factor specificity protein 1 (Sp1) binding to the HIV-1 promoter. It also controls FoxO4 activity and cell survival by directing Toll-like receptor 3 (TLR3)-stimulated cells toward type I interferon (IFN) type I gene induction or apoptosis. Moreover, TRIM22 can activate the noncanonical nuclear factor-kappaB (NF-kappaB) pathway by activating I kappa B kinase alpha (IKKalpha). It also regulates nucleotide binding oligomerization domain containing 2 (NOD2)-dependent activation of interferon-beta signaling and nuclear factor-kappaB. TRIM34, also known as interferon-responsive finger protein 1 or RING finger protein 21 (RNF21), may function as antiviral protein that contribute to the defense against retroviral infections.


Pssm-ID: 319505 [Multi-domain]  Cd Length: 49  Bit Score: 47.87  E-value: 2.36e-07
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gi 341898957 764 CTVCHEDFSHPIKLECNHIFCKSCI------ETWLDQKSTCPMCR 802
Cdd:cd16591    4 CPICLELLTEPLSLDCGHSFCRACItanhkeSVLTDGESSCPVCR 48
mRING-C3HGC3_RFWD3 cd16450
Modified RING finger, C3HGC3-type, found in RING finger and WD repeat domain-containing ...
760-802 2.47e-07

Modified RING finger, C3HGC3-type, found in RING finger and WD repeat domain-containing protein 3 (RFWD3) and similar proteins; RFWD3, also known as RING finger protein 201 (RNF201) or FLJ10520, is an E3 ubiquitin-protein ligase that forms a complex with Mdm2 and p53 to synergistically ubiquitinate p53 and acts as a positive regulator of p53 stability in response to DNA damage. It is phosphorylated by checkpoint kinase ATM/ATR and the phosphorylation mutant fails to stimulate p53 ubiquitination. RFWD3 also functions as a novel replication protein A (RPA)-associated protein involved in DNA replication checkpoint control. RFWD3 contains an N-terminal SQ-rich region followed by a RING finger domain that exhibits robust E3 ubiquitin ligase activity toward p53, a coiled-coil domain and three WD40 repeats in the C-terminus, the latter two of which may be responsible for protein-protein interaction. The RING finger in this family is a modified C3HGC3-type RING finger, but not a canonical C3H2C3-type RING-H2 finger or C3HC4-type RING-HC finger.


Pssm-ID: 319364 [Multi-domain]  Cd Length: 49  Bit Score: 47.66  E-value: 2.47e-07
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gi 341898957 760 DDNQCTVCHEDFS----HPI-KLECNHIFCKSCIETWL-DQKSTCPMCR 802
Cdd:cd16450    1 EGDTCPICFEPWTnsgsHRLcSLKCGHLFGRSCIEKWLkGQGGKCPQCN 49
RING-H2_PJA1_2 cd16465
RING finger, H2 subclass, found in protein E3 ubiquitin-protein ligase Praja-1, Praja-2, and ...
763-802 3.11e-07

RING finger, H2 subclass, found in protein E3 ubiquitin-protein ligase Praja-1, Praja-2, and similar proteins; The family includes two highly similar E3 ubiquitin-protein ligases Praja-1 and Praja-2. Praja-1, also known as RING finger protein 70, is a RING-H2 finger ubiquitin ligase encoded by gene PJA1, a novel human X chromosome gene abundantly expressed in brain. It has been implicated in bone and liver development, as well as memory formation and X-linked mental retardation (MRX). Praja-1 interacts with and activates the ubiquitin-conjugating enzyme UbcH5B, and shows E2-dependent E3 ubiquitin ligase activity. It is a 3-deazaneplanocin A (DZNep)-induced ubiquitin ligase that directly ubiquitinates individual polycomb repressive complex 2 (PRC2) subunits in a cell free system, which leads to their proteasomal degradation. It also plays an important role in neuronal plasticity, which is the basis for learning and memory. Moreover, Praja-1 ubiquitinates embryonic liver fodrin (ELF) and Smad3, but not Smad4, in a transforming growth factor-beta (TGF-beta)-dependent manner. It controls ELF abundance through ubiquitin-mediated degradation, and further regulates TGF-beta signaling, which plays a key role in the suppression of gastric carcinoma. Furthermore, Praja-1 regulates the transcription function of the homeodomain protein Dlx5 by controlling the stability of the Dlx/Msx-interacting MAGE/Necdin family protein, Dlxin-1, via an ubiquitin-dependent degradation pathway. Praja-2, also known as RING finger protein 131, or NEURODAP1, or KIAA0438, is an E2-dependent E3 ubiquitin ligase that interacts with and activates the ubiquitin-conjugating enzyme UbcH5B. It functions as an A-kinase anchoring protein (AKAP)-like E3 ubiquitin ligase that plays a critical role in controlling cyclic AMP (cAMP) dependent PKA activity and pro-survival signaling, and further promotes cell proliferation and growth. Praja-2 is also involved in protein sorting at the postsynaptic density region of axosomatic synapses and possibly plays a role in synaptic communication and plasticity. Moreover, Praja-2, together with the AMPK-related kinase SIK2 and the CDK5 activator CDK5R1/p35, forms a SIK2-p35-PJA2 complex that plays an essential role for glucose homeostasis in pancreatic beta cell functional compensation. Furthermore, Praja-2 ubiquitylates and degrades Mob, a core component of NDR/LATS kinase and a positive regulator of the tumor-suppressor Hippo signaling. Both Praja-1 and Praja-2 contain a potential nuclear localization signal (NLS) and a C-terminal C3H2C3-type RING-H2 motif.


Pssm-ID: 319379 [Multi-domain]  Cd Length: 46  Bit Score: 47.37  E-value: 3.11e-07
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gi 341898957 763 QCTVCHEDF---SHPIKLECNHIFCKSCIETWLDQKSTCPMCR 802
Cdd:cd16465    1 CCPICCCEYvkdEIATELPCHHLFHKLCITAWLQKSGTCPVCR 43
RING-H2_BRAP2 cd16457
RING finger, H2 subclass, found in BRCA1-associated protein (BRAP2) and similar proteins; ...
764-802 4.14e-07

RING finger, H2 subclass, found in BRCA1-associated protein (BRAP2) and similar proteins; BRAP2, also known as impedes mitogenic signal propagation (IMP), RING finger protein 52, or renal carcinoma antigen NY-REN-63, is a novel cytoplasmic protein interacting with the two functional nuclear localization signal (NLS) motifs of BRCA1, a nuclear protein linked to breast cancer. It also binds to the SV40 large T antigen NLS motif and the bipartite NLS motif found in mitosin. BRAP2 serves as a cytoplasmic retention protein and plays a role in in the regulation of nuclear protein transport. It contains an N-terminal RNA recognition motif (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), followed by a C3H2C3-type RING-H2 finger and a UBP-type zinc finger.


Pssm-ID: 319371 [Multi-domain]  Cd Length: 44  Bit Score: 46.89  E-value: 4.14e-07
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gi 341898957 764 CTVCHEDFSHPIK----LECNHIFCKSCIETWLDqkSTCPMCR 802
Cdd:cd16457    3 CPVCLERMDESVSgiltILCNHSFHCDCLKRWGD--STCPVCR 43
RING-HC_TRIM56_C-V cd16584
RING finger, HC subclass, found in tripartite motif-containing protein 56 (TRIM56) and similar ...
763-802 4.18e-07

RING finger, HC subclass, found in tripartite motif-containing protein 56 (TRIM56) and similar proteins; TRIM56, also known as RING finger protein 109 (RNF109), is a virus-inducible E3 ubiquitin ligase that restricts pestivirus infection. It positively regulates the Toll-like receptor 3 (TLR3) antiviral signaling pathway, and possesses antiviral activity against bovine viral diarrhea virus (BVDV), a ruminant pestivirus classified within the family Flaviviridae shared by tick-borne encephalitis virus (TBEV). It also possesses antiviral activity against two classical flaviviruses, yellow fever virus (YFV) and dengue virus (DENV), as well as a human coronavirus, HCoV-OC43, which is responsible for a significant share of common cold cases. It may do not act on positive-strand RNA viruses indiscriminately. Moreover, TRIM56 is an interferon-inducible E3 ubiquitin ligase that modulates STING to confer double-stranded DNA-mediated innate immune responses. TRIM56 belongs to the C-V subclass of TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as an uncharacterized region positioned C-terminal to the RBCC domain.


Pssm-ID: 319498 [Multi-domain]  Cd Length: 44  Bit Score: 47.00  E-value: 4.18e-07
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gi 341898957 763 QCTVCHEDFSHPIKLECNHIFCKSCIETWLDQKS---TCPMCR 802
Cdd:cd16584    2 NCPICLEHYTKPKSLPCLHTFCEDCLEQLIDHNSrrfSCPICR 44
RING-HC_DTX3 cd16711
RING finger, HC subclass, found in E3 ubiquitin-protein ligase Deltex3 (DTX3) and similar ...
763-802 4.28e-07

RING finger, HC subclass, found in E3 ubiquitin-protein ligase Deltex3 (DTX3) and similar proteins; DTX3, also known as RING finger protein 154 (RNF154), is an E3 ubiquitin-protein ligase that belongs to the Deltex (DTX) family. In contrast to other DTXs, DTX3 does not contain N-terminal two Notch-binding WWE domains, but a short unique N-terminal domain, suggesting it does not interact with intracellular domain of Notch. Its C-terminal region includes a C3HC4-type RING-HC finger, and a previously unidentified C-terminal domain.


Pssm-ID: 319625 [Multi-domain]  Cd Length: 41  Bit Score: 46.66  E-value: 4.28e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 341898957 763 QCTVCHEDFSHPIKLE-CNHIFCKSCIETWLDQKSTCPMCR 802
Cdd:cd16711    1 TCPICLGEIQNKKTLDkCKHSFCEDCITRALQVKKACPMCG 41
RING-HC_TRIM69_C-IV cd16611
RING finger, HC subclass, found in tripartite motif-containing protein 69 (TRIM69) and similar ...
764-802 7.57e-07

RING finger, HC subclass, found in tripartite motif-containing protein 69 (TRIM69) and similar proteins; TRIM69, also known as RFP-like domain-containing protein trimless or RING finger protein 36 (RNF36), is a testis E3 ubiquitin-protein ligase that plays a specific role in apoptosis and may also play an important role in germ cell homeostasis during spermatogenesis. TRIM69 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 319525 [Multi-domain]  Cd Length: 44  Bit Score: 46.29  E-value: 7.57e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 341898957 764 CTVCHEDFSHPIKLECNHIFCKSCIE-TWLDQKST-CPMCR 802
Cdd:cd16611    4 CPLCVEWFKDPVMLPCGHNFCRACIEdVWEGQSSFaCPECR 44
RING-HC_RAD16_like cd16567
RING finger, HC subclass, found in Saccharomyces cerevisiae DNA repair protein RAD16, ...
763-801 8.77e-07

RING finger, HC subclass, found in Saccharomyces cerevisiae DNA repair protein RAD16, Schizosaccharomyces pombe rhp16, and similar proteins; Budding yeast RAD16, also known as ATP-dependent helicase RAD16, is encoded by a yeast excision repair gene homologous to the recombinational repair gene RAD54 and to the SNF2 gene involved in transcriptional activation. It is a component of the global genome repair (GGR) complex which promotes global genome nucleotide excision repair (GG-NER) that removes DNA damage from non-transcribing DNA. RAD16 is involved in differential repair of DNA after UV damage, and repairs preferentially the MAT-alpha locus compared with the HML-alpha locus. Fission yeast rhp16, also known as ATP-dependent helicase rhp16, is a RAD16 homolog. It is involved in GGR via nucleotide excision repair (NER), in conjunction with rhp7, after UV irradiation. Both RAD16 and rhp16 contain a C3HC4-type RING-HC finger, as well as a DEAD-like helicase domain and a helicase superfamily C-terminal domain.


Pssm-ID: 319481 [Multi-domain]  Cd Length: 47  Bit Score: 45.90  E-value: 8.77e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 341898957 763 QCTVCHEDFSHPIKLECNHIFCKSCIETWLD----QKSTCPMC 801
Cdd:cd16567    1 VCGICNDPAEDPVVSRCHHAFCRLCVTEYIEsapgGEVTCPRC 43
RING-H2_RNF111_like cd16474
RING finger, H2 subclass, found in RING finger proteins RNF111, RNF165, and similar proteins; ...
764-802 8.77e-07

RING finger, H2 subclass, found in RING finger proteins RNF111, RNF165, and similar proteins; The family includes RING finger proteins RNF111, RNF165, and similar proteins. RNF111, also known as Arkadia, is a nuclear E3 ubiquitin-protein ligase that targets intracellular effectors and modulators of transforming growth factor beta (TGF-beta)/Nodal-related signaling for polyubiquitination and proteasome-dependent degradation. It also interacts with the clathrin-adaptor 2 (AP2) complex and regulates endocytosis of certain cell surface receptors, leading to modulation of epidermal growth factor (EGF) and possibly other signaling pathways. The N-terminal half of RNF111 harbors three SUMO-interacting motifs (SIMs). It thus functions as a SUMO-targeted ubiquitin ligase (STUbL) that directly links nonproteolytic ubiquitylation and SUMOylation in the DNA damage response, as well as triggers degradation of signal-induced polysumoylated proteins, such as the promyelocytic leukemia protein (PML). RNF165, also known as Arkadia-like 2, or Arkadia2, or Ark2C, is an E3 ubiquitin ligase with homology to C-terminal half of RNF111. It is expressed specifically in the nervous system, and can serve to amplify neuronal responses to specific signals. It thus acts as a positive regulator of bone morphogenetic protein (BMP)-Smad signaling that is involved in motor neuron (MN) axon elongation. Both RNF165 and RNF111 contain a C-terminal C3H2C3-type RING-H2 finger.


Pssm-ID: 319388 [Multi-domain]  Cd Length: 46  Bit Score: 46.15  E-value: 8.77e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 341898957 764 CTVCHEDFSHPI---KLECNHIFCKSCIETWLDQKSTCPMCR 802
Cdd:cd16474    3 CTICLSEFEDGEevrRLPCMHLFHQACVDQWLATNKRCPICR 44
RING-HC_RNF125 cd16542
RING finger, HC subclass, found in RING finger protein 125 (RNF125); RNF125, also known as ...
764-802 9.80e-07

RING finger, HC subclass, found in RING finger protein 125 (RNF125); RNF125, also known as T-cell RING activation protein 1 (TRAC-1), is an E3 ubiquitin-protein ligase that is predominantly expressed in lymphoid cells, and functions as a positive regulator of T cell activation. It also down-modulates HIV replication and inhibits pathogen-induced cytokine production. It negatively regulates type I interferon signaling, which conjugates Lys(48)-linked ubiquitination to retinoic acid-inducible gene-I (RIG-I) and subsequently leads to the proteasome-dependent degradation of RIG-I. Further, RNF125 conjugates ubiquitin to melanoma differentiation-associated gene 5 (MDA5), a family protein of RIG-I. It thus acts as a negative regulator of RIG-I signaling, and is a direct target of miR-15b in the context of Japanese encephalitis virus (JEV) infection. Moreover, RNF125 binds to and ubiquitinates JAK1, prompting its degradation and inhibition of receptor tyrosine kinase (RTK) expression. It also negatively regulates p53 function through physical interaction and ubiquitin-mediated proteasome degradation. Mutations in RNF125 may lead to overgrowth syndromes (OGS). RNF125, together with three closely related proteins: RNF114, RNF138 and RNF166, forms a novel family of ubiquitin ligases with a C3HC4-type RING-HC finger, a C2HC-, and two C2H2-type zinc fingers, as well as a ubiquitin interacting motif (UIM). The UIM of RNF125 binds K48-linked poly-ubiquitin chains and is, together with the RING domain, required for auto-ubiquitination.


Pssm-ID: 319456 [Multi-domain]  Cd Length: 42  Bit Score: 45.94  E-value: 9.80e-07
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gi 341898957 764 CTVCHEDFSHPIKLECNHIFCKSCIETWLDQKS-TCPMCR 802
Cdd:cd16542    3 CAICLEVLHQPVRTRCGHVFCRTCIITSLKNNTwTCPYCR 42
mRING-HC-C4C4_TRIM37_C-VIII cd16619
Modified RING finger, HC subclass (C4C4-type), found in tripartite motif-containing protein 37 ...
763-802 1.01e-06

Modified RING finger, HC subclass (C4C4-type), found in tripartite motif-containing protein 37 (TRIM37) and similar proteins; TRIM37, also known as mulibrey nanism protein, or MUL, is a peroxisomal E3 ubiquitin-protein ligase that is involved in the tumorigenesis of several cancer types, including pancreatic ductal adenocarcinoma (PDAC), hepatocellular carcinoma (HCC), breast cancer, and sporadic fibrothecoma. It mono-ubiquitinates histone H2A, a chromatin modification associated with transcriptional repression. Moreover, TRIM37 possesses anti-HIV-1 activity, and interferes with viral DNA synthesis. Mutations in the human TRIM37 gene (also known as MUL) cause Mulibrey (muscle-liver-brain-eye) nanism, a rare growth disorder of prenatal onset characterized by dysmorphic features, pericardial constriction, and hepatomegaly. TRIM37 belongs to the C-VIII subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C4C4-type RING finger, whose overall folding is similar to that of the typical C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a MATH (meprin and TRAF-C homology) domain positioned C-terminal to the RBCC domain. Its MATH domain has been shown to interact with the TRAF (TNF-Receptor-Associated Factor) domain of six known TRAFs in vitro.


Pssm-ID: 319533 [Multi-domain]  Cd Length: 43  Bit Score: 45.80  E-value: 1.01e-06
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gi 341898957 763 QCTVCHEDFSHPIKleCNH---IFCKSCIETWL-DQKSTCPMCR 802
Cdd:cd16619    2 RCFICMEKLRDARL--CPHcskLCCFSCIRRWLtEQRSQCPHCR 43
RING-HC_TRIM17_C-IV cd16595
RING finger, HC subclass, found in tripartite motif-containing protein TRIM17 and similar ...
764-802 1.36e-06

RING finger, HC subclass, found in tripartite motif-containing protein TRIM17 and similar proteins; TRIM17, also known as RING finger protein 16 (RNF16) or testis RING finger protein (Terf), is a crucial E3 ubiquitin ligase that is necessary and sufficient for neuronal apoptosis and contributes to Mcl-1 ubiquitination in cerebellar granule neurons (CGNs). It interacts in a SUMO-dependent manner with nuclear factor of activated T cell NFATc3 transcription factor, and thus inhibits the activity of NFATc3 by preventing its nuclear localization. In contrast, it binds to and inhibits NFATc4 transcription factor in a SUMO-independent manner. Moreover, TRIM17 stimulates degradation of kinetochore protein ZW10 interacting protein (ZWINT), a known component of the kinetochore complex required for the mitotic spindle checkpoint, and negatively regulates cell proliferation. TRIM17 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 319509 [Multi-domain]  Cd Length: 48  Bit Score: 45.53  E-value: 1.36e-06
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gi 341898957 764 CTVCHEDFSHPIKLECNHIFCKSCI------ETWLDQKSTCPMCR 802
Cdd:cd16595    4 CSICLDYFKDPVILRCGHNFCRACItqfwekQGGLQGKLTCPECR 48
HRD1 COG5243
HRD ubiquitin ligase complex, ER membrane component [Posttranslational modification, protein ...
726-808 1.51e-06

HRD ubiquitin ligase complex, ER membrane component [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227568 [Multi-domain]  Cd Length: 491  Bit Score: 51.51  E-value: 1.51e-06
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gi 341898957 726 KVGEIYRYSLFVKKSVKCLITdssvgTSVKILECDDNQCTVCHEDFSH-------------PIKLECNHIFCKSCIETWL 792
Cdd:COG5243  257 RIREHARFRRATKDLNAMYPT-----ATEEQLTNSDRTCTICMDEMFHpdheplprgldmtPKRLPCGHILHLHCLKNWL 331
                         90
                 ....*....|....*.
gi 341898957 793 DQKSTCPMCRAEVTKD 808
Cdd:COG5243  332 ERQQTCPICRRPVIFD 347
zf-RING_5 pfam14634
zinc-RING finger domain;
764-803 1.59e-06

zinc-RING finger domain;


Pssm-ID: 339304 [Multi-domain]  Cd Length: 43  Bit Score: 45.11  E-value: 1.59e-06
                          10        20        30        40
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gi 341898957  764 CTVCHEDFSHPIK---LECNHIFCKSCIETwLDQKSTCPMCRA 803
Cdd:pfam14634   2 CNKCFKPLSKTRPfylTSCGHIFCEECLTK-LLKERQCPICRK 43
RING-H2_RNF43 cd16798
RING finger, H2 subclass, found in RING finger protein 43 (RNF43) and similar proteins; RNF43 ...
764-801 1.81e-06

RING finger, H2 subclass, found in RING finger protein 43 (RNF43) and similar proteins; RNF43 is a transmembrane E3 ubiquitin-protein ligase that plays an important role in frizzled-dependent regulation of the Wnt/beta-catenin pathway. It functions as a tumor suppressor that inhibits Wnt/beta-catenin signaling by ubiquitinating Frizzled receptor and targeting it to the lysosomal pathway for degradation. miR-550a-5p directly targeted the 3?-UTR of gene RNF43 and regulated its expression. Moreover, RNF43 interacts with NEDD-4-like ubiquitin-protein ligase-1 (NEDL1) and regulates p53-mediated transcription. It may also be involved in cell growth control potentially through the interaction with HAP95, a chromatin-associated protein interfacing the nuclear envelope. Mutations of RNF43 have been identified in various tumors, including colorectal cancer (CRC), endometrial cancer, mucinous ovarian tumors, gastric adenocarcinoma, pancreatic ductal adenocarcinoma, liver fluke-associated cholangiocarcinoma, hepatocellular carcinoma, and glioma. RNF43 contains an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C3H2C3-type RING-H2 finger domain followed by a long C-terminal region.


Pssm-ID: 319712 [Multi-domain]  Cd Length: 47  Bit Score: 45.31  E-value: 1.81e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 341898957 764 CTVCHEDFSHPIKLE---CNHIFCKSCIETWLDQKSTCPMC 801
Cdd:cd16798    3 CAICLEEFSEGQELRiisCAHEFHRECVDPWLHQHRTCPLC 43
RING-HC_RNF5 cd16743
RING finger, HC subclass, found in RING finger protein 5 (RNF5) and similar proteins; RNF5, ...
763-803 2.10e-06

RING finger, HC subclass, found in RING finger protein 5 (RNF5) and similar proteins; RNF5, also known as protein G16 or Ram1, is an E3 ubiquitin-protein ligase anchored to the outer membrane of the endoplasmic reticulum (ER). It acts at early stages of cystic fibrosis (CF) transmembrane conductance regulator (CFTR) biosynthesis and functions as a target for therapeutic modalities to antagonize mutant CFTR proteins in CF patients carrying the F508del allele. It also regulates the turnover of specific G protein-coupled receptors by ubiquitinating JNK-associated membrane protein (JAMP) and preventing proteasome recruitment. RNF5 limits basal levels of autophagy and influences susceptibility to bacterial infection through the regulation of ATG4B stability. It is also involved in the degradation of Pendrin, a transmembrane chloride/anion exchanger highly expressed in thyroid, kidney, and inner ear. RNF5 plays an important role in cell adhesion and migration. It can modulate cell migration by ubiquitinating paxillin. Furthermore, RNF5 interacts with virus-induced signaling adaptor (VISA) at mitochondria in a viral infection-dependent manner, and further targets VISA at K362 and K461 for K48-linked ubiquitination and degradation after viral infection. It also negatively regulates virus-triggered signaling by targeting MITA, also known as STING, for ubiquitination and degradation at the mitochondria. In addition, RNF5 determines breast cancer response to ER stress-inducing chemotherapies through the regulation of the L-glutamine carrier proteins SLC1A5 and SLC38A2 (SLC1A5/38A2). It also has been implicated in muscle organization and in recognition and processing of misfolded proteins. RNF5 contains a C3HC4-type RING-HC finger.


Pssm-ID: 319657 [Multi-domain]  Cd Length: 46  Bit Score: 44.94  E-value: 2.10e-06
                         10        20        30        40
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gi 341898957 763 QCTVCHEDFSHPIKLECNHIFCKSCIETWLD---QKSTCPMCRA 803
Cdd:cd16743    2 ECNICLETAREAVVSLCGHLYCWPCLHQWLEtrpERQECPVCKA 45
RING-HC_RNF114 cd16540
RING finger, HC subclass, found in RING finger protein 114 (RNF114) and similar proteins; ...
764-802 2.19e-06

RING finger, HC subclass, found in RING finger protein 114 (RNF114) and similar proteins; RNF114, also known as zinc finger protein 228 (ZNF228) or zinc finger protein 313 (ZNF313), is a p21(WAF1)-targeting ubiquitin E3 ligase that interacts with X-linked inhibitor of apoptosis (XIAP)-associated factor 1 (XAF1) and may play a role in p53-mediated cell-fate decisions. It is involved in immune response to double-stranded RNA in disease pathogenesis. Moreover, RNF114 interacts with A20 and modulates its ubiquitylation. It negatively regulates nuclear factor-kappaB (NF-kappaB)-dependent transcription and positively regulates T-cell activation. RNF114 may play a putative role in the regulation of immune responses, since it corresponds to a novel psoriasis susceptibility gene, ZNF313. RNF114, together with three closely related proteins: RNF125, RNF138 and RNF166, forms a novel family of ubiquitin ligases with a C3HC4-type RING-HC finger, a C2HC-, and two C2H2-type zinc fingers, as well as a ubiquitin interacting motif (UIM).


Pssm-ID: 319454 [Multi-domain]  Cd Length: 42  Bit Score: 44.83  E-value: 2.19e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 341898957 764 CTVCHEDFSHPIKLECNHIFCKSCIETWLD-QKSTCPMCR 802
Cdd:cd16540    3 CPVCLEVFEKPVRVPCGHVFCSACLQECLKpKKPVCGVCR 42
RING-HC_BAR cd16497
RING finger, HC subclass, found in bifunctional apoptosis regulator (BAR); BAR, also known as ...
764-802 2.28e-06

RING finger, HC subclass, found in bifunctional apoptosis regulator (BAR); BAR, also known as RING finger protein 47, was originally identified as an inhibitor of Bax-induced apoptosis. It participates in the block of apoptosis induced by TNF-family death receptors (extrinsic pathway) and mitochondria-dependent apoptosis (intrinsic pathway). BAR is predominantly expressed by neurons in the central nervous system and is involved in the regulation of neuronal survival. It is an endoplasmic reticulum (ER)-associated RING-type E3 ubiquitin ligase that interacts with BI-1 protein and post-translationally regulates its stability as well as functions in ER stress. BAR contains an N-terminal C3HC4-type RING-HC finger, a SAM domain, a coiled-coil domain, and a C-terminal transmembrane (TM) domain. This family corresponds to the RING-HC finger responsible for the binding of ubiquitin conjugating enzymes (E2s).


Pssm-ID: 319411 [Multi-domain]  Cd Length: 46  Bit Score: 44.79  E-value: 2.28e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 341898957 764 CTVCHEDFSHPIKLECNHIFCKSCIETWLD--QKSTCPMCR 802
Cdd:cd16497    3 CHCCYDLLVNPTTLNCGHSFCRHCLALWWLssKKTECPECR 43
RING-H2_RNF6 cd16673
RING finger, H2 subclass, found in E3 ubiquitin-protein ligase RNF6 and similar proteins; RNF6 ...
764-802 2.29e-06

RING finger, H2 subclass, found in E3 ubiquitin-protein ligase RNF6 and similar proteins; RNF6 is an androgen receptor (AR)-associated protein that induces AR ubiquitination and promotes AR transcriptional activity. RNF6-induced ubiquitination may regulate AR transcriptional activity and specificity through modulating cofactor recruitment. RNF6 is overexpressed in hormone-refractory human prostate cancer tissues and required for prostate cancer cell growth under androgen-depleted conditions. Moreover, RNF6 regulates local serine/threonine kinase LIM kinase 1 (LIMK1) levels in axonal growth cones. RNF6-induced LIMK1 polyubiquitination is mediated via K48 of ubiquitin and leads to proteasomal degradation of the kinase. RNF6 also binds and upregulates the Inha promoter, and functions as a transcription regulatory protein in the mouse sertoli cell. Furthermore, RNF6 acts as a potential tumor suppressor gene involved in the pathogenesis of esophageal squamous cell carcinoma (ESCC). RNF6 contains an N-terminal coiled-coil domain, a Lys-X-X-Leu/Ile-X-X-Leu/Ile (KIL) motif, and a C-terminal C3H2C3-type RING-H2 finger which is responsible for its ubiquitin ligase activity. The KIL motif is present in a subset of RING-H2 proteins from organisms as evolutionarily diverse as human, mouse, chicken, Drosophila, Caenorhabditis elegans, and Arabidopsis thaliana.


Pssm-ID: 319587 [Multi-domain]  Cd Length: 45  Bit Score: 45.02  E-value: 2.29e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 341898957 764 CTVCHEDFSHPIKLE---CNHIFCKSCIETWLDQKSTCPMCR 802
Cdd:cd16673    3 CSVCINEYATGNKLRrlpCAHEFHIHCIDRWLSENSTCPICR 44
RING-HC_PCGF cd16525
RING finger, HC subclass, found in Polycomb Group RING finger homologs (PCGF1, 2, 3, 4, 5 and ...
764-802 2.30e-06

RING finger, HC subclass, found in Polycomb Group RING finger homologs (PCGF1, 2, 3, 4, 5 and 6), and similar proteins; The family includes six Polycomb Group (PcG) RING finger homologs (PCGF1/NSPc1, PCGF2/Mel-18, PCGF3, PCGF4/BMI1, PCGF5, and PCGF6/MBLR) that use epigenetic mechanisms to maintain or repress expression of their target genes. They were first discovered in fruit flies that can remodel chromatin such that epigenetic silencing of genes takes place, and are well known for silencing Hox genes through modulation of chromatin structure during embryonic development in fruit flies. PCGF homologs play important roles in cell proliferation, differentiation, and tumorigenesis. They all have been found to associate with ring finger protein 2 (RNF2). The RNF2-PCGF heterodimer is catalytically competent as an E3 ubiquitin transferase and is the scaffold for the assembly of additional components. Moreover, PCGF homologs are critical components in the assembly of distinct Polycomb Repression Complex 1 (PRC1) related complexes which is involved in the maintenance of gene repression and target different genes through distinct mechanisms. The Drosophila PRC1 core complex is formed by the Polycomb (Pc), Polyhomeotic (Ph), Posterior sex combs (Psc), and Sex combs extra (Sce, also known as Ring) subunits. In mammals, the composition of PRC1 is much more diverse and varies depending on the cellular context. All PRC1 complexes contain homologs of the Drosophila Ring protein. Ring1A/RNF1 and Ring1B/RNF2 are E3 ubiquitin ligases that mark lysine 119 of histone H2A with a single ubiquitin group (H2AK119ub). Mammalian homologs of the Drosophila Psc protein, such as PCGF2/Mel-18 or PCGF4/BMI1, regulate PRC1 enzymatic activity. PRC1 complexes can be divided into at least two classes according to the presence or absence of CBX proteins, which are homologs of Drosophila Pc. Canonical PRC1 complexes contain CBX proteins that recognize and bind H3K27me3, the mark deposited by PRC2. Therefore, canonical PRC1 complexes and PRC2 can act together to repress gene transcription and maintain this repression through cell division. Non-canonical PRC1 complexes, containing RYBP (together with additional proteins, such as L3mbtl2 or Kdm2b) rather than the CBX proteins have recently been described in mammals. PCGF homologs contain a C3HC4-type RING-HC finger.


Pssm-ID: 319439 [Multi-domain]  Cd Length: 42  Bit Score: 44.54  E-value: 2.30e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 341898957 764 CTVCHEDFSHPIKL-ECNHIFCKSCIETWLDQKSTCPMCR 802
Cdd:cd16525    3 CVLCKGYLIDATTItECLHSFCRSCIVRYLETSKYCPVCD 42
RING-HC_Cbl_like cd16502
RING finger, HC subclass, found in Casitas B-lineage lymphoma (Cbl) proteins; The Cbl adaptor ...
764-802 2.36e-06

RING finger, HC subclass, found in Casitas B-lineage lymphoma (Cbl) proteins; The Cbl adaptor proteins family contains a small class of RING-type E3 ubiquitin ligases with oncogenic activity, which is represented by three mammalian members, c-Cbl, Cbl-b and Cbl-c, as well as two invertebrate Cbl-family proteins, D-Cbl in Drosophila and Sli-1 in C. elegans. Cbl proteins function as potent negative regulators of various signaling cascades in a wide range of cell types. They play roles in ubiquitinating the activated tyrosine kinases and targeting them for degradation. D-Cbl associates with the Drosophila epidermal growth factor receptor (EGFR) and overexpression of D-Cbl in the eye of Drosophila embryos inhibits EGFR dependent photoreceptor cell development. Sli-1 is a negative regulator of the Let-23 receptor tyrosine kinase, an EGFR homolog, in vulva development. Cbl proteins in this family consist of a highly conserved N-terminal half that includes a tyrosine-kinase-binding domain (TKB, also known as the phosphotyrosine binding PTB domain, is composed of a four helix-bundle, a Ca2+ binding EF-hand and a highly variant SH2 domain) and a C3HC4-type RING-HC finger, both of which are required for Cbl-mediated downregulation of RTKs, and a divergent C-terminal region.


Pssm-ID: 319416 [Multi-domain]  Cd Length: 43  Bit Score: 44.65  E-value: 2.36e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 341898957 764 CTVCHEDFSHpIKLE-CNHIFCKSCIETWLDQ-KSTCPMCR 802
Cdd:cd16502    4 CKICAENDKD-VRIEpCGHLLCTPCLTSWQDSdGQTCPFCR 43
RING-HC_RNF135_like cd16543
RING finger, HC subclass, found in RING finger protein 135 (RNF135), tripartite ...
764-802 2.37e-06

RING finger, HC subclass, found in RING finger protein 135 (RNF135), tripartite motif-containing protein 15 (TRIM15) and similar proteins; RNF135, also known as RIG-I E3 ubiquitin ligase (REUL) or Riplet, is a widely expressed E3 ubiquitin-protein ligase that consists of an N-terminal C3HC4-type RING-HC finger and C-terminal B30.2/SPRY and PRY motifs, but lacks the B-box and coiled-coil domains that are also typically present in TRIM proteins. RNF135 serves as a specific retinoic acid-inducible gene-I (RIG-I)-interacting protein that ubiquitinates RIG-I and specifically stimulates RIG-I-mediated innate antiviral activity to produce antiviral type-I interferon (IFN) during the early phase of viral infection. It also has been identified as a bio-marker and therapy target of glioblastoma. It associates with the ERK signal transduction pathway and plays a role in glioblastoma cell proliferation, migration and cell cycle. TRIM15, also known as RING finger protein 93 (RNF93), zinc finger protein 178 (ZNF178), or zinc finger protein B7 (ZNFB7), is a focal adhesion protein that regulates focal adhesion disassembly. It localizes to focal contacts in a myosin-II-independent manner by an interaction between its coiled-coil domain and the LD2 motif of paxillin. TRIM15 can also associate with coronin 1B, cortactin, filamin binding LIM protein1, and vasodilator-stimulated phosphoprotein, which are involved in actin cytoskeleton dynamics. As an additional component of the integrin adhesome, it regulates focal adhesion turnover and cell migration. TRIM15 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a SPRY/B30.2 domain positioned C-terminal to the RBCC domain.


Pssm-ID: 319457 [Multi-domain]  Cd Length: 37  Bit Score: 44.75  E-value: 2.37e-06
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 341898957 764 CTVCHEDFSHPIKLECNHIFCKSCIETwlDQKSTCPMCR 802
Cdd:cd16543    1 CILCQGLLFDPVTIPCGHTFCRRCLER--LPSKLCPTCR 37
RING-HC_CHFR cd16503
RING finger, HC subclass, found in checkpoint with forkhead and RING finger domains protein ...
763-802 2.49e-06

RING finger, HC subclass, found in checkpoint with forkhead and RING finger domains protein (CHFR); CHFR, also known as RING finger protein 196 (RNF196), is a checkpoint protein that delays entry into mitosis in response to stress. It functions as an E3 ubiquitin ligase that ubiquitinates and degrades its target proteins, such as Aurora-A, Plk1, Kif22, and PARP-1, which are critical for proper mitotic transitions. It also plays an important role in cell cycle progression and tumor suppression, and is negatively regulated by SUMOylation-mediated proteasomal ubiquitylation. Moreover, CHFR is involved in the early stage of the DNA damage response, which mediates the crosstalk between ubiquitination and poly-ADP-ribosylation. CHFR contains a fork head associated- (FHA) and a C3HC4-type RING-HC finger.


Pssm-ID: 319417 [Multi-domain]  Cd Length: 44  Bit Score: 44.71  E-value: 2.49e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 341898957 763 QCTVCHEDFSHPIKLE-CNHIFCKSCIETWLDQKSTCPMCR 802
Cdd:cd16503    4 LCSICQDLLHDCVSLQpCMHNFCAGCYSEWMERSSLCPQCR 44
RING1-H2_RNF32 cd16677
RING finger 1, H2 subclass, found in RING finger protein 32 (RNF32) and similar proteins; ...
763-802 2.71e-06

RING finger 1, H2 subclass, found in RING finger protein 32 (RNF32) and similar proteins; RNF32 is mainly expressed in testis spermatogenesis, most likely in spermatocytes and/or in spermatids, suggesting a possible role in sperm formation. RNF32 contains two C3H2C3-type RING-H2 fingers separated by an IQ domain of unknown function. Although the biological function of RNF32 remains unclear, the protein with double RING-H2 fingers may act as a scaffold for binding several proteins that function in the same pathway. This family corresponds to the first RING-H2 finger.


Pssm-ID: 319591 [Multi-domain]  Cd Length: 44  Bit Score: 44.63  E-value: 2.71e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 341898957 763 QCTVCHEDF--SHPIKLECNHIFCKSCIETW--LDQKSTCPMCR 802
Cdd:cd16677    1 PCVICKEDFglQQQVLLSCSHVFHRACLESFerFSGKKTCPMCR 44
RING-HC_RNF222 cd16564
RING finger, HC subclass, found in RING finger protein 222 (RNF222) and similar proteins; ...
763-802 3.00e-06

RING finger, HC subclass, found in RING finger protein 222 (RNF222) and similar proteins; RNF222 is an uncharacterized C3HC4-type RING-HC finger-containing protein. It may function as an E3 ubiquitin-protein ligase.


Pssm-ID: 319478 [Multi-domain]  Cd Length: 47  Bit Score: 44.40  E-value: 3.00e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 341898957 763 QCTVCHEDFSH-PIKLECNHIFCKSCI-----ETWLDQKS-TCPMCR 802
Cdd:cd16564    1 ECPVCYEKFSAaARSLSCGHVFCHDCLvkyllSARVDKKRiVCPICR 47
RING-HC_TRIM9_like_C-I cd16576
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM9, TRIM36, TRIM46, ...
763-802 3.06e-06

RING finger, HC subclass, found in tripartite motif-containing proteins TRIM9, TRIM36, TRIM46, TRIM67, and similar proteins; Tripartite motif-containing proteins TRIM9, TRIM36, TRIM46, and TRIM67 belong to the C-I subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, consisting of three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. TRIM9 (the human ortholog of rat Spring), also known as RING finger protein 91 (RNF91), is a brain-specific E3 ubiquitin-protein ligase collaborating with an E2 ubiquitin conjugating enzyme UBCH5b. TRIM9 plays an important role in the regulation of neuronal functions and participates in the neurodegenerative disorders through its ligase activity. TRIM36 (the human ortholog of mouse Haprin), also known as RING finger protein 98 (RNF98), or zinc-binding protein Rbcc728, is an E3 ubiquitin-protein ligase expressed in the germ plasm. It has been implicated in acrosome reaction, fertilization, and embryogenesis, as well as in the carcinogenesis. TRIM46, also known as gene Y protein (GeneY) or tripartite, fibronectin type-III and C-terminal SPRY motif protein (TRIFIC), is a microtubule-associated protein that forms parallel microtubule bundles in the proximal axon and plays a crucial role for the establishment and maintenance of neuronal polarity. TRIM67, also known as TRIM9-like protein (TNL), is a protein selectively expressed in the cerebellum. It interacts with PRG-1, an important molecule in the control of hippocampal excitability dependent on presynaptic LPA2 receptor signaling, and 80K-H, also known as glucosidase II beta, a protein kinase C substrate.


Pssm-ID: 319490 [Multi-domain]  Cd Length: 42  Bit Score: 44.30  E-value: 3.06e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 341898957 763 QCTVCHEDFSHPIKLECNHIFCKSCIetwLDQKSTCPMCR 802
Cdd:cd16576    5 KCPVCREFYTCPVILPCSHSICLSCA---LEILLTCPQCR 41
RING-HC_ScPSH1_like cd16568
RING finger, HC subclass, found in Saccharomyces cerevisiae POB3/SPT16 histone-associated ...
764-802 3.24e-06

RING finger, HC subclass, found in Saccharomyces cerevisiae POB3/SPT16 histone-associated protein 1 (ScPSH1), Arabidopsis thaliana Protein KEEP ON GOING (AtKEG) and similar proteins; ScPSH1 is a Cse4-specific E3 ubiquitin ligase that interacts with the kinetochore protein Pat1 and targets the degradation of budding yeast centromeric histone H3 variant, CENP-ACse4, which is essential for faithful chromosome segregation. ScPSH1 contains a C3HC4-type RING-HC finger and a DNA directed RNA polymerase domain. AtKEG is an E3 ubiquitin ligase essential for Arabidopsis growth and development. It maintains low levels of ABSCISIC ACID-INSENSITIVE5 (ABI5) in the absence of stress and thus functions as a negative regulator of abscisic acid (ABA) signaling. AtKEG is a multidomain protein that includes a C3HC4-type RING-HC finger, a kinase domain, ankyrin repeats, and 12 HERC2-like (for HECT and RCC1-like) repeats.


Pssm-ID: 319482 [Multi-domain]  Cd Length: 45  Bit Score: 44.41  E-value: 3.24e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 341898957 764 CTVCHED-FSHPIKLECNHIFCKSCIETWL----DQKSTCPMCR 802
Cdd:cd16568    2 CSVCHDRlNEVPMMLPCGHGFCKKCLNKMFstssDKRLACPTCR 45
RING-H2_RNF32 cd16471
RING finger, H2 subclass, found in RING finger protein 32 (RNF32) and similar proteins; RNF32 ...
764-802 3.32e-06

RING finger, H2 subclass, found in RING finger protein 32 (RNF32) and similar proteins; RNF32 is mainly expressed in testis spermatogenesis, most likely in spermatocytes and/or in spermatids, suggesting a possible role in sperm formation. RNF32 contains two C3H2C3-type RING-H2 fingers separated by an IQ domain of unknown function. Although the biological function of RNF32 remains unclear, the protein with double RING-H2 fingers may act as a scaffold for binding several proteins that function in the same pathway.


Pssm-ID: 319385 [Multi-domain]  Cd Length: 49  Bit Score: 44.52  E-value: 3.32e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 341898957 764 CTVCHEDFS-HP-IKLECNHIFCKSCIETWL-------DQKSTCPMCR 802
Cdd:cd16471    2 CPICLEEFDqDSqARLSCSHVFHQACFLSYLayshserVSQTQCPMCR 49
mRING-HC-C3HC3D_Nrdp1 cd16634
Modified RING finger, HC subclass (C3HC3D-type), found in neuregulin receptor degradation ...
764-802 3.67e-06

Modified RING finger, HC subclass (C3HC3D-type), found in neuregulin receptor degradation protein-1 (Nrdp1) and similar proteins; Nrdp1 (referred to as FLRF in mice), also known as RING finger protein 41 (RNF41), is an E3 ubiquitin-protein ligase that plays a critical role in the regulation of cell growth and apoptosis, inflammation and production of reactive oxygen species (ROS), as well as in doxorubicin (DOX)-induced cardiac injury. It promoten and degradation of the epidermal growth factor receptor (EGFR/ErbB) family member, ErbB3, which is independent of growth factor stimulation. It also promotes M2 macrophage polarization by ubiquitinating and activating transcription factor CCAAT/enhancer-binding Protein beta (C/EBPbeta) via Lys-63-linked ubiquitination. Moreover, Nrdp1 interacts with and modulates activity of Parkin, a causative protein for early onset recessive juvenile parkinsonism (AR-JP). It also interacts with ubiquitin-specific protease 8 (USP8), which is involved in trafficking of various transmembrane proteins. Furthermore, Nrdp1 inhibits basal lysosomal degradation and enhances ectodomain shedding of JAK2-associated cytokine receptors. Its phosphorylation by the kinase Par-1b (also known as MARK2) is required for epithelial cell polarity. Nrdp1 contains an N-terminal modified C3HC3D-type RING-HC finger required for enhancing ErbB3 degradation, a B-box, a coiled-coil domain responsible for Nrdp1 oligomerization, and a C-terminal ErbB3-binding domain.


Pssm-ID: 319548 [Multi-domain]  Cd Length: 43  Bit Score: 44.34  E-value: 3.67e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 341898957 764 CTVCHEDFSHPIKL-ECNHIFCKSCIETWLDQKSTCPMCR 802
Cdd:cd16634    4 CPICSGVLEEPLQApHCEHAFCNACITEWLSRQQTCPVDR 43
RING-H2_RNF43_like cd16666
RING finger, H2 subclass, found in RING finger proteins RNF43, ZNRF3, and similar proteins; ...
763-802 3.69e-06

RING finger, H2 subclass, found in RING finger proteins RNF43, ZNRF3, and similar proteins; RNF43 and ZNRF3 (also known as RNF203) are transmembrane E3 ubiquitin-protein ligases that belong to the PA-TM-RING ubiquitin ligases family, which has been characterized by containing an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C3H2C3-type RING-H2 finger domain followed by a long C-terminal region. Both RNF43 and RNF203 function as tumor suppressors involved in the regulation of Wnt/beta-catenin signaling. They negatively regulate Wnt signaling through interacting with complexes of frizzled receptors (FZD) and low-density lipoprotein receptor-related protein (LRP) 5/6, which leads to ubiquitination of Frizzled receptors (FZD) and endocytosis of the Wnt receptor. Dishevelled (DVL), a positive Wnt regulator, is required for ZNRF3/RNF43-mediated ubiquitination and degradation of FZD. They also associate with R-spondin 1 (RSPO1). This interaction may block Frizzled ubiquitination and enhances Wnt signaling.


Pssm-ID: 319580 [Multi-domain]  Cd Length: 45  Bit Score: 44.35  E-value: 3.69e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 341898957 763 QCTVCHEDFSHPIKLE---CNHIFCKSCIETWLDQKSTCPMCR 802
Cdd:cd16666    1 VCAICLEEFKDGQELRvlpCSHEFHRHCVDPWLLQNRTCPLCL 43
RING-HC_TRIM13_like_C-V cd16581
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM13, TRIM59 and ...
764-802 3.95e-06

RING finger, HC subclass, found in tripartite motif-containing proteins TRIM13, TRIM59 and similar proteins; TRIM13 and TRIM59, two closely related tripartite motif-containing proteins, belong to the C-V subclass of TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, followed by a C-terminal transmembrane domain. TRIM13, also known as B-cell chronic lymphocytic leukemia tumor suppressor Leu5, leukemia-associated protein 5, putative tumor suppressor RFP2, RING finger protein 77 (RNF77), or Ret finger protein 2, is an endoplasmic reticulum (ER) membrane anchored E3 ubiquitin-protein ligase that interacts proteins localized to the ER, including valosin-containing protein (VCP), a protein indispensable for ER-associated degradation (ERAD). TRIM59, also known as RING finger protein 104 (RNF104) or tumor suppressor TSBF-1, is a putative E3 ubiquitin-protein ligase that functions as a novel multiple cancer biomarker for immunohistochemical detection of early tumorigenesis.


Pssm-ID: 319495 [Multi-domain]  Cd Length: 45  Bit Score: 43.98  E-value: 3.95e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 341898957 764 CTVCHEDFSHPIKLECNHIFCKSCIETWLDQKST--CPMCR 802
Cdd:cd16581    5 CSICLDIFNDPRVLPCLHTFCKNCLEGRAAESGPlkCPTCR 45
zf-C3HC4_4 pfam15227
zinc finger of C3HC4-type, RING; This is a family of primate-specific Ret finger protein-like ...
764-801 4.05e-06

zinc finger of C3HC4-type, RING; This is a family of primate-specific Ret finger protein-like (RFPL) zinc-fingers of the C3HC4 type. Ret finger protein-like proteins are primate-specific target genes of Pax6, a key transcription factor for pancreas, eye and neocortex development. This domain is likely to be DNA-binding. This zinc-finger domain together with the RDM domain, pfam11002, forms a large zinc-finger structure of the RING/U-Box superfamily. RING-containing proteins are known to exert an E3 ubiquitin protein ligase activity with the zinc-finger structure being mandatory for binding to the E2 ubiquitin-conjugating enzyme.


Pssm-ID: 317611 [Multi-domain]  Cd Length: 42  Bit Score: 43.93  E-value: 4.05e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 341898957  764 CTVCHEDFSHPIKLECNHIFCKSCI-ETWLDQKS---TCPMC 801
Cdd:pfam15227   1 CPICLDYLEKPVSIECGHNFCLSCInSLQKEPDGegfLCPLC 42
RING-HC_MKRN cd16521
RING finger, HC subclass, found in the makorin (MKRN) protein family; The MKRN protein family ...
764-802 4.22e-06

RING finger, HC subclass, found in the makorin (MKRN) protein family; The MKRN protein family includes the ribonucleoproteins that are characterized by a variety of zinc-finger motifs, including typical arrays of one to four C3H1-type zinc fingers and a C3HC4-type RING-HC finger. Another motif rich in Cys and His residues (CH), with so far unknown function, is also generally present in MKRN proteins. MKRN proteins may have E3 ubiquitin ligase activity.


Pssm-ID: 319435 [Multi-domain]  Cd Length: 51  Bit Score: 44.23  E-value: 4.22e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 341898957 764 CTVCHEDF-----SHPIKLECNHIFCKSCIETWLDQKS-------TCPMCR 802
Cdd:cd16521    1 CGICLEVVlpserRFGILPNCDHPFCLACIRDWRGSKDqektvvrACPICR 51
RING-HC_BRCA1 cd16498
RING finger, HC subclass, found in breast cancer type 1 susceptibility protein (BRCA1) and ...
763-802 4.67e-06

RING finger, HC subclass, found in breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; BRCA1, also known as RING finger protein 53 (RNF53), is a RING finger protein encoded by tumor suppressor gene BRCA1 that regulates all DNA double-strand break (DSB) repair pathways. BRCA1 is frequently mutated in in patients with hereditary breast and ovarian cancer (HBOC). Its mutation is also associated with an increased risk of pancreatic, stomach, laryngeal, fallopian tube, and prostate cancer. It plays an important role in the DNA damage response signaling and has been implicated in various cellular processes such as cell cycle regulation, transcriptional regulation, chromatin remodeling, DNA DSBs, and apoptosis. BRCA1 contains an N-terminal C3HC4-type RING-HC finger, and two BRCT (BRCA1 C-terminus domain) repeats at the C-terminus.


Pssm-ID: 319412 [Multi-domain]  Cd Length: 48  Bit Score: 43.93  E-value: 4.67e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 341898957 763 QCTVCHEDFSHPIKLECNHIFCKSCIETWLDQKST---CPMCR 802
Cdd:cd16498    6 ECPICLDLMKNPVSTKCDHQFCRFCILKLLSRKKGsapCPLCK 48
RING-HC_Topors cd16574
RING finger, HC subclass, found in topoisomerase I-binding arginine/serine-rich protein ...
764-802 4.76e-06

RING finger, HC subclass, found in topoisomerase I-binding arginine/serine-rich protein (Topors) and similar proteins; Topors, also known as topoisomerase I-binding RING finger protein, tumor suppressor p53- binding protein 3, or p53-binding protein 3 (p53BP3), is a ubiquitously expressed nuclear E3 ubiquitin-protein ligase that can ligate both ubiquitin and small ubiquitin-like modifier (SUMO) to substrate proteins in the nucleus. It contains an N-terminal C3HC4-type RING-HC finger which ligates ubiquitin to its target proteins including DNA topoisomerase I, p53, NKX3.1, H2AX, and the AAV-2 Rep78/68 proteins. As a RING-dependent E3 ubiquitin ligase, Topors works with the E2 enzymes UbcH5a, UbcH5c, and UbcH6, but not with UbcH7, CDC34, or UbcH2b. Topors acts as a tumor suppressor in various malignancies. It regulates p53 modification, suggesting it may be responsible for astrocyte elevated gene-1 (AEG-1, also known as metadherin, or LYRIC) ubiquitin modification. Plk1-mediated phosphorylation of Topors inhibits Topors-mediated sumoylation of p53, whereas p53 ubiquitination is enhanced, leading to p53 degradation. It also functions as a negative regulator of the prostate tumor suppressor NKX3.1. Moreover, Topors is associated with promyelocytic leukemia nuclear bodies, and may be involved in the cellular response to camptothecin. It also plays a key role in the turnover of H2AX protein, discriminating the type of DNA damaging stress. Furthermore, Topors is a cilia-centrosomal protein associated with autosomal dominant retinal degeneration. Mutations in TOPORS cause autosomal dominant retinitis pigmentosa (adRP).


Pssm-ID: 319488 [Multi-domain]  Cd Length: 40  Bit Score: 43.78  E-value: 4.76e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 341898957 764 CTVCHEDFSHPIKLE-CNHIFCKSCIETWLDQKSTCPMCR 802
Cdd:cd16574    1 CPICLGEFENKSFLDsCFHSFCFGCILEWSKVKAECPLCK 40
COG5152 COG5152
Uncharacterized conserved protein, contains RING and CCCH-type Zn-fingers [General function ...
764-815 4.87e-06

Uncharacterized conserved protein, contains RING and CCCH-type Zn-fingers [General function prediction only];


Pssm-ID: 227481 [Multi-domain]  Cd Length: 259  Bit Score: 48.53  E-value: 4.87e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 341898957 764 CTVCHEDFSHPIKLECNHIFCKSCIETWLDQKSTCPMC------RAEVTKDVDNEWKN 815
Cdd:COG5152  199 CGICKKDYESPVVTECGHSFCSLCAIRKYQKGDECGVCgkatygRFWVVSDLQKMLNK 256
RING-HC_TRIM10_C-IV cd16593
RING finger, HC subclass, found in tripartite motif-containing protein 10 (TRIM10) and similar ...
764-802 5.49e-06

RING finger, HC subclass, found in tripartite motif-containing protein 10 (TRIM10) and similar proteins; TRIM10, also known as B30-RING finger protein (RFB30), RING finger protein 9 (RNF9), or hematopoietic RING finger 1 (HERF1), is a novel hematopoiesis-specific RING finger protein required for terminal differentiation of erythroid cells. TRIM10 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 319507 [Multi-domain]  Cd Length: 49  Bit Score: 43.84  E-value: 5.49e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 341898957 764 CTVCHEDFSHPIKLECNHIFCKSCIETWLDQKS-------TCPMCR 802
Cdd:cd16593    4 CPICQGTLREPVTIDCGHNFCRACLTRYCEIPGpdleeppTCPLCK 49
RING-HC_TRIM47_C-IV cd16604
RING finger, HC subclass, found in tripartite motif-containing protein 47 (TRIM47) and similar ...
764-802 5.79e-06

RING finger, HC subclass, found in tripartite motif-containing protein 47 (TRIM47) and similar proteins; TRIM47, also known as gene overexpressed in astrocytoma protein (GOA) or RING finger protein 100 (RNF100), belongs a subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, a B-box, and two coiled coil domains, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. It plays an important role in the process of dedifferentiation that is associated with astrocytoma tumorigenesis.


Pssm-ID: 319518 [Multi-domain]  Cd Length: 47  Bit Score: 43.65  E-value: 5.79e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 341898957 764 CTVCHEDFSHPIKLECNHIFCKSCIETW------LDQKSTCPMCR 802
Cdd:cd16604    3 CPICLDALRDPVTLPCGHNYCLACLQHLwekngsRGGAYRCPECQ 47
RING-HC_RNF180 cd16554
RING finger, HC subclass, found in RING finger protein 180 (RNF180) and similar proteins; ...
763-802 5.87e-06

RING finger, HC subclass, found in RING finger protein 180 (RNF180) and similar proteins; RNF180, also known as Rines, is a membrane-bound E3 ubiquitin-protein ligase well conserved among vertebrates. It is a critical regulator of the monoaminergic system, as well as emotional and social behavior. It interacts with brain monoamine oxidase A (MAO-A) and targets it for ubiquitination and degradation. It also functions as a novel tumor suppressor in gastric carcinogenesis. The hypermethylated CpG site count of RNF180 DNA promoter can be used to predict the survival of gastric cancer. RNF180 contains a novel conserved dual specificity protein phosphatase Rines conserved (DSPRC) domain, a basic coiled-coil domain, a C3HC4-type RING-HC finger, and a C-terminal hydrophobic region that is predicted to be a transmembrane domain.


Pssm-ID: 319468 [Multi-domain]  Cd Length: 44  Bit Score: 43.50  E-value: 5.87e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 341898957 763 QCTVCHEDFSHPIKLE-CNHIFCKSCIETWLDQKST---CPMCR 802
Cdd:cd16554    1 TCPVCLDLYYDPYMCYpCGHIFCEPCLRQLAKSSPKntpCPLCR 44
RING-H2_RNF145 cd16684
RING finger, H2 subclass, found in RING finger protein 145 (RNF145) and similar proteins; ...
764-801 6.00e-06

RING finger, H2 subclass, found in RING finger protein 145 (RNF145) and similar proteins; RNF145 is an uncharacterized RING finger protein encoded by RNF145 gene, which is expressed in T lymphocytes, and its expression is altered in acute myelomonocytic and acute promyelocytic leukemias. Although its biological function remains unclear, RNF145 shows high sequence similarity with RNF139, an endoplasmic reticulum (ER)-resident multi-transmembrane protein that functions as a potent growth suppressor in mammalian cells, inducing G2/M arrest, decreased DNA synthesis and increased apoptosis. Like RNF139, RNF145 contains a C3H2C3-type RING-H2 finger with possible E3-ubiquitin ligase activity.


Pssm-ID: 319598 [Multi-domain]  Cd Length: 43  Bit Score: 43.51  E-value: 6.00e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 341898957 764 CTVCHEDFSHPIKLECNHIFCKSCIETWLDQKSTCPMC 801
Cdd:cd16684    5 CSICYQDMKSAVITPCSHFFHAGCLKKWLYVQETCPLC 42
mRING-HC-C3HC3D_LNX2 cd16780
Modified RING finger, HC subclass (C3HC3D-type), found in ligand of numb protein X 2 (LNX2); ...
760-803 6.46e-06

Modified RING finger, HC subclass (C3HC3D-type), found in ligand of numb protein X 2 (LNX2); LNX2, also known as numb-binding protein 2, or PDZ domain-containing RING finger protein 1 (PDZRN1), is a PDZ domain-containing RING-type E3 ubiquitin ligase responsible for the ubiquitination and degradation of Numb, a component of the Notch signaling pathway that functions in the specification of cell fates during development and is known to control cell numbers during neurogenesis in vertebrates. It interacts with contactin-associated protein 4 (Caspr4, also known as CNTNAP4) in a PDZ domain-dependent manner, which modulates the proliferation and neuronal differentiation of neural progenitor cells (NPCs). LNX2 contains an N-terminal modified C3HC3D-type RING-HC finger, a NPAF motif for Numb/ Numblike-LNX interaction, and four PDZ domains necessary for the binding of substrates, including ErbB2, RhoC, the presynaptic protein CAST, the melanoma/cancer-testis antigen MAGEB18 and several proteins associated with cell junctions, such as JAM4 and the Coxsackievirus and adenovirus receptor (CAR).


Pssm-ID: 319694 [Multi-domain]  Cd Length: 45  Bit Score: 43.71  E-value: 6.46e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 341898957 760 DDNQCTVCHEDFSHPIKLECNHIFCKSCIETWLDQKSTCPMCRA 803
Cdd:cd16780    2 DDLVCHICLQPLLQPLDTPCGHTFCFKCLRNFLQEKDFCPLDRK 45
RING-H2_RNF11 cd16468
RING finger, H2 subclass, found in RING finger protein 11 (RNF11) and similar proteins; RNF11 ...
763-801 7.26e-06

RING finger, H2 subclass, found in RING finger protein 11 (RNF11) and similar proteins; RNF11 is an E3 ubiquitin-protein ligase that acts both as an adaptor and a modulator of itch-mediated control of ubiquitination events underlying membrane traffic. It is the downstream of an enzymatic cascade for the ubiquitination of specific substrates. It is also a molecular adaptor of homologous to E6-associated protein C-terminus (HECT)-type ligases. RNF11 has been implicated in the regulation of several signaling pathways. It enhances the transforming growth factor receptor (TGFR) signaling by both abrogating Smurf2-mediated receptor ubiquitination and by promoting the Smurf2-mediated degradation of AMSH (associated molecule with the SH3 domain of STAM), a de-ubiquitinating enzyme that enhances transforming growth factor-beta (TGF-beta) signaling and epidermal growth factor receptor (EGFR) endosomal recycling. It also acts directly on Smad4 to enhance Smad4 function, and plays a role in prolonged TGF-beta signaling. Moreover, RNF11 functions as a critical component of the A20 ubiquitin-editing protein complex that negatively regulates tumor necrosis factor (TNF)-mediated nuclear factor (NF)-kappaB activation. It also interacts with Smad anchor for receptor activation (SARA) and the endosomal sorting complex required for transport (ESCRT)-0 complex, thus participating in the regulation of lysosomal degradation of EGFR. Furthermore, RNF11 acts as a novel GGA cargo actively participating in regulating the ubiquitination of the GGA protein family. In addition, RNF11 functions together with TAX1BP1 to target TANK-binding kinase 1 (TBK1)/IkappaB kinase IKKi, and further restricts antiviral signaling and type I interferon (IFN)-beta production. RNF11 contains an N-terminal PPPY motif that binds WW domain-containing proteins such as AIP4/itch, Nedd4 and Smurf1/2 (SMAD-specific E3 ubiquitin-protein ligase 1/2), and a C-terminal C3H2C3-type RING-H2 finger that functions as a scaffold for the coordinated transfer of ubiquitin to substrate proteins together with the E2 enzymes UbcH527 and Ubc13.


Pssm-ID: 319382 [Multi-domain]  Cd Length: 43  Bit Score: 43.19  E-value: 7.26e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 341898957 763 QCTVCHEDFS--HPIK-LECNHIFCKSCIETWLDQKSTCPMC 801
Cdd:cd16468    1 ECVICMNDFVygDPIRfLPCMHIYHKDCIDDWLMRSFTCPSC 42
RING-HC_TRIM60_like_C-IV cd16607
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM60, TRIM61 and ...
761-802 7.46e-06

RING finger, HC subclass, found in tripartite motif-containing proteins TRIM60, TRIM61 and similar proteins; TRIM60 and TRIM61 are two closely related tripartite motif-containing proteins. TRIM60, also known as RING finger protein 129 (RNF129) or RING finger protein 33 (RNF33), is a cytoplasmic protein expressed in the testis. It may play an important role in the spermatogenesis process, the development of the preimplantation embryo, and in testicular functions. RNF33 interacts with the cytoplasmic kinesin motor proteins KIF3A and KIF3B suggesting possible contribution to cargo movement along the microtubule in the expressed sites. It is also involved in spermatogenesis in Sertoli cells under the regulation of nuclear factor-kappaB (NF-kappaB). TRIM60 belongs the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, a B-box, and two coiled coil domains, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. In contrast to TRIM60, TRIM61 belongs to the C-V subclass of TRIM family that contains RBCC domains only. Its biological function remains unclear.


Pssm-ID: 319521 [Multi-domain]  Cd Length: 47  Bit Score: 43.43  E-value: 7.46e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 341898957 761 DNQCTVCHEDFSHPIKLECNHIFCKSCIE-TW--LDQKSTCPMCR 802
Cdd:cd16607    1 ESSCPICLEYLKDPVTINCGHNFCRSCLIvSWkdLDDTFPCPVCR 45
RING-HC_LNX4 cd16719
RING finger, HC subclass, found in ligand of numb protein X 4 (LNX4); LNX4, also known as PDZ ...
763-802 8.02e-06

RING finger, HC subclass, found in ligand of numb protein X 4 (LNX4); LNX4, also known as PDZ domain-containing RING finger protein 4 (PDZRN4), or SEMACAP3-like protein (SEMCAP3L), is an E3 ubiquitin-protein ligase responsible for the ubiquitination and degradation of Numb, a component of the Notch signaling pathway that functions in the specification of cell fates during development and is known to control cell numbers during neurogenesis in vertebrates. LNX4 contains an N-terminal typical C3HC4-type RING-HC finger, two PDZ domains, and a C-terminal LNX3 homology (LNX3H) domain.


Pssm-ID: 319633 [Multi-domain]  Cd Length: 42  Bit Score: 43.39  E-value: 8.02e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 341898957 763 QCTVCHEDFSHPIKLECNHIFCKSCIETWLDQKSTCPM-CR 802
Cdd:cd16719    1 KCKLCGKVLEEPLSTPCGHVFCAGCLLPWAVRRRRCPLqCQ 41
RING-HC_PCGF3 cd16735
RING finger found in polycomb group RING finger protein 3 (PCGF3) and similar proteins; PCGF3, ...
764-802 8.22e-06

RING finger found in polycomb group RING finger protein 3 (PCGF3) and similar proteins; PCGF3, also known as RING finger protein 3A (RNF3A), is one of six PcG RING finger (PCGF) homologs (PCGF1, PCGF2/Mel-18, PCGF3, PCGF4/BMI1, PCGF5, and PCGF6) and serves as the core component of a Polycomb repressive complex 1 (PRC1). Like other PCGF homologs, PCGF3 associates with ring finger protein 2 (RNF2) to form a RNF2-PCGF heterodimer, which is catalytically competent as an E3 ubiquitin transferase and is the scaffold for the assembly of additional components. PCGF3 contains a C3HC4-type RING-HC finger.


Pssm-ID: 319649 [Multi-domain]  Cd Length: 47  Bit Score: 43.23  E-value: 8.22e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 341898957 764 CTVCHEDFSHPIKL-ECNHIFCKSCIETWLDQKSTCPMCR 802
Cdd:cd16735    4 CRLCKGYLIDATTItECLHTFCKSCLVKYLEENNTCPTCG 43
RING-HC_RNF207 cd16558
RING finger, HC subclass, found in RING finger protein 207 (RNF207) and similar proteins; ...
763-801 9.23e-06

RING finger, HC subclass, found in RING finger protein 207 (RNF207) and similar proteins; RNF207 is a cardiac-specific E3 ubiquitin-protein ligase that plays an important role in the regulation of cardiac repolarization. It regulates action potential duration, likely via effects on human ether-a-go-go-related gene (HERG) trafficking and localization in a heat shock protein-dependent manner. RNF207 contains a C3HC4-type RING-HC finger, Bbox 1 and Bbox C-terminal (BBC), as well as a C-terminal non-homologous region (CNHR).


Pssm-ID: 319472 [Multi-domain]  Cd Length: 43  Bit Score: 43.15  E-value: 9.23e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 341898957 763 QCTVCHEDFSHPIKLECNHIFCKSCIE-TWLDQKSTCPMC 801
Cdd:cd16558    3 VCYLCNEQYEHPCLLDCYHTFCASCLRgRAADGRLSCPLC 42
RING-HC_TRIM62_C-IV cd16608
RING finger, HC subclass, found in tripartite motif-containing protein 62 (TRIM62) and similar ...
760-802 9.78e-06

RING finger, HC subclass, found in tripartite motif-containing protein 62 (TRIM62) and similar proteins; TRIM62, also known as Ductal Epithelium Associated Ring Chromosome 1 (DEAR1), is a cytoplasmic E3 ubiquitin-protein ligase that was identified as a dominant regulator of acinar morphogenesis in the mammary gland. It is implicated in the inflammatory response of immune cells by regulating the Toll-like receptor 4 (TLR4) signaling pathway, leading to increased activity of the activator protein 1 (AP-1) transcription factor in primary macrophages. It is also involved in muscular protein homeostasis, especially during inflammation-induced atrophy, and may play a role in the pathogenesis of ICU-acquired weakness (ICUAW) by activating and maintaining inflammation in myocytes. Moreover, TRIM62 facilitates K27-linked poly-ubiquitination of CARD9 and also regulates CARD9-mediated anti-fungal immunity and intestinal inflammation. Furthermore, TRIM62 is involved in the regulation of apical-basal polarity and acinar morphogenesis. It also functions as a chromosome 1p35 tumor suppressor and negatively regulates transforming growth factor beta (TGFbeta)-driven epithelial-mesenchymal transition (EMT) through binding to and promoting the ubiquitination of SMAD3, a major effector of TGFbeta-mediated EMT. TRIM62 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 319522 [Multi-domain]  Cd Length: 50  Bit Score: 43.13  E-value: 9.78e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 341898957 760 DDNQCTVCHEDFSHPIKLECNHIFCKSCI-ETWLDQKST----CPMCR 802
Cdd:cd16608    2 DELLCSICLSIYQDPVSFGCEHYFCRKCItEHWSRQEHQgtrdCPECR 49
RING-HC_UHRF cd16613
RING finger, HC subclass, found in ubiquitin-like PHD and RING finger domain-containing ...
763-804 1.05e-05

RING finger, HC subclass, found in ubiquitin-like PHD and RING finger domain-containing proteins, UHRF1 and UHRF2, and similar proteins; UHRF1 is a unique chromatin effector protein that integrates the recognition of both histone PTMs and DNA methylation. It is essential for cell proliferation and plays a critical role in the development and progression of many human carcinomas, such as laryngeal squamous cell carcinoma (LSCC), gastric cancer (GC), esophageal squamous cell carcinoma (ESCC), colorectal cancer, prostate cancer, and breast cancer. UHRF1 acts as a transcriptional repressor through its binding to histone H3 when it is unmodified at Arg2. Its overexpression in human lung fibroblasts results in downregulation of expression of the tumor suppressor pRB. It also plays a role in transcriptional repression of the cell cycle regulator p21. Moreover, UHRF1-dependent repression of transcription factors can facilitate the G1-S transition. It interacts with Tat-interacting protein of 60 kDa (TIP60) and induces degradation-independent ubiquitination of TIP60. It is also an N-methylpurine DNA glycosylase (MPG)-interacting protein that binds MPG in a p53 status-independent manner in the DNA base excision repair (BER) pathway. In addition, UHRF1 functions as an epigenetic regulator that is important for multiple aspects of epigenetic regulation, including maintenance of DNA methylation patterns and recognition of various histone modifications. UHRF2 was originally identified as a ubiquitin ligase acting as a small ubiquitin-like modifier (SUMO) E3 ligase that enhances zinc finger protein 131 (ZNF131) SUMOylation, but does not enhance ZNF131 ubiquitination. It also ubiquitinates PCNP, a PEST-containing nuclear protein. Moreover, UHRF2 functions as a nuclear protein involved in cell-cycle regulation and has been implicated in tumorigenesis. It interacts with cyclins, CDKs, p53, pRB, PCNA, HDAC1, DNMTs, G9a, methylated histone H3 lysine 9, and methylated DNA. It interacts with the cyclin E-CDK2 complex, ubiquitinates cyclins D1 and E1, induces G1 arrest, and is involved in the G1/S transition regulation. Furthermore, UHRF2 is a direct transcriptional target of the transcription factor E2F-1 in the induction of apoptosis. It recruits HDAC1 and binds to methyl-CpG. UHRF2 also participates in the maturation of Hepatitis B virus (HBV) by interacting with the HBV core protein and promoting its degradation. Both UHRF1 and UHRF2 contain an N-terminal ubiquitin-like domain (UBL), a tandem Tudor domain (TTD), a plant homeodomain (PHD) finger, a SET- and RING-associated (SRA) domain, and a C-terminal C3HC4-type RING-HC finger.


Pssm-ID: 319527 [Multi-domain]  Cd Length: 46  Bit Score: 43.15  E-value: 1.05e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 341898957 763 QCTVCHEDFSHPIKLECNHIFCKSCIetwldQKS------TCPMCRAE 804
Cdd:cd16613    2 TCICCQEVVYQPITTPCQHNVCKGCL-----QRSfkaevySCPACRHD 44
RING-H2_RNF38_like cd16472
RING finger, H2 subclass, found in RING finger proteins RNF38, RNF44, and similar proteins; ...
764-802 1.09e-05

RING finger, H2 subclass, found in RING finger proteins RNF38, RNF44, and similar proteins; The family includes RING finger proteins RNF38, RNF44, and similar proteins. RNF38 is a nuclear E3 ubiquitin protein ligase that plays a role in regulating p53. RNF44 is an uncharacterized RING finger protein that shows high sequence similarity with RNF38. Both RNF38 and RNF44 contain a coiled-coil motif, a KIL motif (Lys-X2-Ile/Leu-X2-Ile/Leu, X can be any amino acid), and a C3H2C3-type RING-H2 finger. In addition, RNF38 harbors two potential nuclear localization signals.


Pssm-ID: 319386 [Multi-domain]  Cd Length: 45  Bit Score: 42.85  E-value: 1.09e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 341898957 764 CTVCHEDF---SHPIKLECNHIFCKSCIETWLDQKSTCPMCR 802
Cdd:cd16472    4 CVVCMCDFearQLLRVLPCSHEFHAKCVDKWLKTNRTCPICR 45
mRING-HC-C3HC3D_TRAF5 cd16642
Modified RING finger, HC subclass (C3HC3D-type), found in tumor necrosis factor (TNF) ...
764-799 1.20e-05

Modified RING finger, HC subclass (C3HC3D-type), found in tumor necrosis factor (TNF) receptor-associated factor 5 (TRAF5) and similar proteins; TRAF5, also known as RING finger protein 84 (RNF84), is an important signal transducer for a wide range of TNF receptor superfamily members, including tumor necrosis factor receptor 1 (TNFR1), tumor necrosis factor receptor 2 (TNFR2), CD40, and other lymphocyte costimulatory receptors, RANK/TRANCE-R, ectodysplasin-A Receptor (EDAR), lymphotoxin-beta receptor (LT-betaR), latent membrane protein 1 (LMP1), and IRE1. It functions as an activator of NF-kappaB, MAPK, and JNK, and is involved in both RANKL- and TNFalpha-induced osteoclastogenesis. It mediates CD40 signaling through associating with the cytoplasmic tail of CD40. It also negatively regulates Toll-like receptor (TLR) signaling and functions as a negative regulator of the interleukin 6 (IL-6) receptor signaling pathway that limits the differentiation of inflammatory CD4(+) T cells. TRAF5 contains an N-terminal domain with a modified C3HC3D-type RING-HC finger and several zinc fingers, and a C-terminal TRAF domain that comprises a coiled coil domain and a conserved TRAF-C domain.


Pssm-ID: 319556 [Multi-domain]  Cd Length: 43  Bit Score: 42.83  E-value: 1.20e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 341898957 764 CTVCHEDFSHPIKLECNHIFCKSCIETWLDQKST--CP 799
Cdd:cd16642    3 CATCHFVLHNPHQTGCGHRFCEHCILVLLELNPTpaCP 40
RING-HC_TRIM8_C-V cd16580
RING finger, HC subclass, found in tripartite motif-containing protein 8 (TRIM8) and similar ...
764-801 1.22e-05

RING finger, HC subclass, found in tripartite motif-containing protein 8 (TRIM8) and similar proteins; TRIM8, also known as glioblastoma-expressed RING finger protein (GERP) or RING finger protein 27 (RNF27), is a probable E3 ubiquitin-protein ligase that may promote proteasomal degradation of suppressor of cytokine signaling 1 (SOCS1) and further regulate interferon-gamma signaling. It functions as a new p53 modulator that stabilizes p53 impairing its association with MDM2 and inducing the reduction of cell proliferation. TRIM8 deficit dramatically impairs p53 stabilization and activation in response to chemotherapeutic drugs. TRIM8 also modulates tumor necrosis factor-alpha (TNFalpha) and interleukin-1beta (IL-1beta)-triggered nuclear factor-kappaB (NF- kappa B) activation by targeting transforming growth factor beta (TGFbeta) activated kinase 1 (TAK1) for K63-linked polyubiquitination. Moreover, TRIM8 modulates translocation of phosphorylated STAT3 into the nucleus through interaction with Hsp90beta and consequently regulates transcription of Nanog in embryonic stem cells. It also interacts with protein inhibitor of activated STAT3 (PIAS3), which inhibits IL-6-dependent activation of STAT3. TRIM8 belongs to the C-V subclass of nuclear TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil domain, as well as an uncharacterized region positioned C-terminal to the RBCC domain. The coiled coil domain is required for homodimerization and the region immediately C-terminal to the RING motif is sufficient to mediate the interaction with SOCS1.


Pssm-ID: 319494 [Multi-domain]  Cd Length: 44  Bit Score: 42.64  E-value: 1.22e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 341898957 764 CTVCHEDFSHPIKLECNHIFCKSCI-ETWLDQK--STCPMC 801
Cdd:cd16580    3 CPICLHVFVEPVQLPCKHNFCRGCIgEAWAKEAglVRCPEC 43
RING-HC_BRE1_like cd16499
RING finger, HC subclass, found in yeast Bre1 and its homologs from eukaryotes; Bre1 is an E3 ...
763-802 1.30e-05

RING finger, HC subclass, found in yeast Bre1 and its homologs from eukaryotes; Bre1 is an E3 ubiquitin-protein ligase that catalyzes monoubiquitination of histone H2B in concert with the E2 ubiquitin-conjugating enzyme, Rad6. The Rad6-Bre1-mediated histone H2B ubiquitylation modulates the formation of double-strand breaks (DSBs) during meiosis in yeast. it is also required, indirectly, for the methylation of histone 3 on lysine 4 (H3K4) and 79. RNF20, also known as BRE1A and RNF40, also known as BRE1B, are the mammalian homologs of Bre1. They work together to form a heterodimeric Bre1 complex that facilitate the K120 monoubiquitination of histone H2B (H2Bub1), a DNA damage-induced histone modification that is crucial for recruitment of the chromatin remodeler SNF2h to DNA double-strand break (DSB) damage sites. Moreover, Bre1 complex acts as a tumor suppressor, augmenting expression of select tumor suppressor genes and suppressing select oncogenes. Deficiency in the mammalian histone H2B ubiquitin ligase Bre1 leads to replication stress and chromosomal instability. All family members contain a C3HC4-type RING-HC finger at its C-terminus.


Pssm-ID: 319413 [Multi-domain]  Cd Length: 42  Bit Score: 42.58  E-value: 1.30e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 341898957 763 QCTVCHEDFSHPIKLECNHIFCKSCIETWLDQKS-TCPMCR 802
Cdd:cd16499    2 KCSVCNDRQKDVILTKCGHVFCKECIQERLETRQrKCPSCN 42
RING-HC_TRIM59_C-V cd16763
RING finger, HC subclass, found in tripartite motif-containing protein 59 (TRIM59) and similar ...
760-802 1.40e-05

RING finger, HC subclass, found in tripartite motif-containing protein 59 (TRIM59) and similar proteins; TRIM59, also known as RING finger protein 104 (RNF104) or tumor suppressor TSBF-1, is a putative E3 ubiquitin-protein ligase that functions as a novel multiple cancer biomarker for immunohistochemical detection of early tumorigenesis. It is upregulated in gastric cancer and promotes gastric carcinogenesis by interacting with and targeting the P53 tumor suppressor for its ubiquitination and degradation. It also acts as a novel accessory molecule involved in cytotoxicity of BCG-activated macrophages (BAM). Moreover, TRIM59 may serve as a multifunctional regulator for innate immune signaling pathways. It interacts with ECSIT and negatively regulates nuclear factor-kappaB (NF- kappa B) and interferon regulatory factor (IRF)-3/7-mediated signal pathways. TRIM59 belongs to the C-V subclass of TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region. In addition, TRIM59 contains a C-terminal transmembrane domain.


Pssm-ID: 319677 [Multi-domain]  Cd Length: 56  Bit Score: 42.92  E-value: 1.40e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 341898957 760 DDNQCTVCHEDFSHPIKLECNHIFCKSCIETWLDQKST------------CPMCR 802
Cdd:cd16763    2 EELTCSVCYSIFEDPRVLPCSHTFCRNCLENVIQSSGNfslwrplraplkCPNCR 56
RING-HC_TRIM13_C-V cd16762
RING finger, HC subclass, found in tripartite motif-containing protein 13 (TRIM13) and similar ...
760-804 1.56e-05

RING finger, HC subclass, found in tripartite motif-containing protein 13 (TRIM13) and similar proteins; TRIM13, also known as B-cell chronic lymphocytic leukemia tumor suppressor Leu5, leukemia-associated protein 5, putative tumor suppressor RFP2, RING finger protein 77 (RNF77), or Ret finger protein 2, is an endoplasmic reticulum (ER) membrane anchored E3 ubiquitin-protein ligase that interacts proteins localized to the ER, including valosin-containing protein (VCP), a protein indispensable for ER-associated degradation (ERAD). It also targets the known ER proteolytic substrate CD3-delta, but not the N-end rule substrate Ub-R-YFP (yellow fluorescent protein) for its degradation. Moreover, TRIM13 regulates ubiquitination and degradation of NEMO to suppress tumor necrosis factor (TNF) induced nuclear factor-kappaB (NF- kappa B) activation. It is also involved in NF-kappaB p65 activation and nuclear factor of activated T-cells (NFAT)-dependent activation of c-Rel upon T-cell receptor engagement. Furthermore, TRIM13 negatively regulates lanoma differentiation-associated gene 5 (MDA5)-mediated type I interferon production. It also regulates caspase-8 ubiquitination, translocation to autophagosomes, and activation during ER stress induced cell death. Meanwhile, TRIM13 enhances ionizing radiation-induced apoptosis by increasing p53 stability and decreasing AKT kinase activity through MDM2 and AKT degradation. TRIM13 belongs to the C-V subclass of TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region. In addition, TRIM13 contains a C-terminal transmembrane domain.


Pssm-ID: 319676 [Multi-domain]  Cd Length: 57  Bit Score: 43.05  E-value: 1.56e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 341898957 760 DDNQCTVCHEDFSHPIKLECNHIFCKSCIETWLDQKST----------CPMCRAE 804
Cdd:cd16762    2 EDLTCPICCSLFDDPRVLPCSHNFCKKCLEGILEGNVRnmlwrpapfkCPTCRKE 56
PEX10 COG5574
RING-finger-containing E3 ubiquitin ligase [Posttranslational modification, protein turnover, ...
761-805 1.67e-05

RING-finger-containing E3 ubiquitin ligase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227861 [Multi-domain]  Cd Length: 271  Bit Score: 47.20  E-value: 1.67e-05
                         10        20        30        40
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gi 341898957 761 DNQCTVCHEDFSHPIKLECNHIFCKSCIETWLDQKST--CPMCRAEV 805
Cdd:COG5574  215 DYKCFLCLEEPEVPSCTPCGHLFCLSCLLISWTKKKYefCPLCRAKV 261
RING-HC_RNF224_like cd16565
RING finger, HC subclass, found in RING finger protein RNF224, RNF225 and similar proteins; ...
764-802 1.74e-05

RING finger, HC subclass, found in RING finger protein RNF224, RNF225 and similar proteins; Both RNF224 and RNF225 are uncharacterized C3HC4-type RING-HC finger-containing proteins. They may function as an E3 ubiquitin-protein ligase.


Pssm-ID: 319479 [Multi-domain]  Cd Length: 49  Bit Score: 42.53  E-value: 1.74e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 341898957 764 CTVCHEDFS----HPIKLECNHIFCKSCIETW-----LDQKSTCPMCR 802
Cdd:cd16565    2 CIICLSSYDlsgrLPRRLYCGHTFCQACLKRLdtvtnEQRWIPCPQCR 49
RING-H2_RNF38 cd16679
RING finger, H2 subclass, found in RING finger protein 38 (RNF38) and similar proteins; RNF38 ...
764-804 1.88e-05

RING finger, H2 subclass, found in RING finger protein 38 (RNF38) and similar proteins; RNF38 is a nuclear E3 ubiquitin protein ligase that is widely expressed throughout the body in human, especially highly expressed in the heart, brain, placenta and the testis. It recognizes p53 as a substrate for ubiquitination, and thus plays a role in regulating p53. The overexpression of RNF38 increases p53 ubiquitination and alters p53 localization. It is also capable of autoubiquitination. Moreover, RNF38 expression is negatively regulated by the serotonergic system. Induction of RNF38 may be involved in the anxiety-like behavior or non-cell autonomous by the decline of serotonin (5-HT) levels. RNF38 contains a coiled-coil motif, a KIL motif (Lys-X2-Ile/Leu-X2-Ile/Leu, X can be any amino acid), and a C3H2C3-type RING-H2 finger, as well as two potential nuclear localization signals.


Pssm-ID: 319593 [Multi-domain]  Cd Length: 49  Bit Score: 42.36  E-value: 1.88e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 341898957 764 CTVCHEDFSHPIKLE---CNHIFCKSCIETWLDQKSTCPMCRAE 804
Cdd:cd16679    5 CVVCMCDFESRQLLRvlpCNHEFHAKCVDKWLKANRTCPICRAD 48
RING-H2_RNF139 cd16683
RING finger, H2 subclass, found in RING finger protein 139 (RNF139) and similar proteins; ...
764-801 1.92e-05

RING finger, H2 subclass, found in RING finger protein 139 (RNF139) and similar proteins; RNF139, also known as translocation in renal carcinoma on chromosome 8 protein (TRC8), is an endoplasmic reticulum (ER)-resident multi-transmembrane protein that functions as a potent growth suppressor in mammalian cells, inducing G2/M arrest, decreased DNA synthesis and increased apoptosis. It is a tumor suppressor that has been implicated in a novel regulatory relationship linking the cholesterol/lipid biosynthetic pathway with cellular growth control. The mutation of RNF139 has been identified in families with hereditary renal (RCC) and thyroid cancers. RNF139 physically and functionally interacts with von Hippel-Lindau (VHL), which is part of an SCF related E3-ubiquitin ligase complex with "gatekeeper" function in renal carcinoma and is defective in most sporadic clear-cell renal cell carcinomas (ccRCC). It suppresses growth and functions with VHL in a common pathway. RNF139 also suppresses tumorigenesis through targeting heme oxygenase-1 for ubiquitination and degradation. Moreover, RNF139 is a target of Translin (TSN), a posttranscriptional regulator of genes transcribed by the transcription factor CREM-tau in postmeiotic male germ cells, suggesting a role of RNF139 in dysgerminoma. Furthermore, RNF139 physically and functionally interacts with von Hippel-Lindau (VHL), which is part of an SCF related E3-ubiquitin ligase complex with "gatekeeper" function in renal carcinoma and is defective in most sporadic clear-cell renal cell carcinomas (ccRCC). It suppresses growth and functions with VHL in a common pathway. In addition, RNF139 forms an integral part of a novel multi-protein ER complex, containing MHC I, US2, and signal peptide peptidase, which is associated with ER-associated degradation (ERAD) pathway. It is required for the ubiquitination of MHC class I molecules before dislocation from the ER. As a novel sterol-sensing ER membrane protein, RNF139 hinders sterol regulatory element-binding protein-2 (SREBP-2) processing through interaction with SREBP-2 and SREBP cleavage-activated protein (SCAP), regulating its own turnover rate via its E3 ubiquitin ligase activity. RNF139 shows two regions of similarity with the receptor for sonic hedgehog (SHH), Patched. The first region corresponds to the second extracellular domain of Patched, which is involved in binding SHH. The second region is a putative sterol-sensing domain (SSD). In addition, the C-terminal half of RNF139 contains a C3H2C3-type RING-H2 finger with E3-ubiquitin ligase activity in vitro.


Pssm-ID: 319597 [Multi-domain]  Cd Length: 42  Bit Score: 42.29  E-value: 1.92e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 341898957 764 CTVCHEDFSHPIKLE-CNHIFCKSCIETWLDQKSTCPMC 801
Cdd:cd16683    3 CAICYQEFTTSARITpCNHYFHALCLRKWLYIQDTCPMC 41
RING-HC_NHL-1_like cd16524
RING finger, HC subclass, found in Caenorhabditis elegans RING finger protein NHL-1 and ...
763-802 2.08e-05

RING finger, HC subclass, found in Caenorhabditis elegans RING finger protein NHL-1 and similar proteins; NHL-1 functions as an E3 ubiquitin-protein ligase in the presence of both UBC-13 and UBC-1 within the ubiquitin pathway of Caenorhabditis elegans. It acts in chemosensory neurons to promote stress resistance in distal tissues by the transcription factor DAF-16 activation but is dispensable for the activation of heat shock factor 1 (HSF-1). NHL-1 belongs to the TRIM (tripartite motif)-NHL family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil domain, as well as a NHL (named after proteins NCL-1, HT2A and Lin-41 that contain repeats folded into a six-bladed beta propeller) repeat domain positioned C-terminal to the RBCC domain.


Pssm-ID: 319438 [Multi-domain]  Cd Length: 45  Bit Score: 42.04  E-value: 2.08e-05
                         10        20        30        40
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gi 341898957 763 QCTVCHEDFSHPIKLECNHIFCKS-CIETWLD---QKSTCPMCR 802
Cdd:cd16524    2 TCAICLDRYRRPKLLPCQHTFCQSpCLEGLVDyvnRKLKCPECR 45
mRING-HC-C3HC3D_LNX1_like cd16637
Modified RING finger, HC subclass (C3HC3D-type), found in ligand of Numb protein LNX1, LNX2, ...
764-802 2.16e-05

Modified RING finger, HC subclass (C3HC3D-type), found in ligand of Numb protein LNX1, LNX2, and similar proteins; The ligand of Numb protein X (LNX) family, also known as PDZ and RING (PDZRN) family, includes LNX1-5, which can interact with Numb, a key regulator of neurogenesis and neuronal differentiation. LNX5 (also known as PDZK4 or PDZRN4L) shows high sequence homology to LNX3 and LNX4, but it lacks the RING domain. LNX1-4 proteins function as E3 ubiquitin ligases and have a unique domain architecture consisting of an N-terminal RING-HC finger for E3 ubiquitin ligase activity and either two or four PDZ domains necessary for the substrate-binding. This family corresponds to LNX1/LNX2-like proteins, which contains a modified C3HC3D-type RING-HC finger and four PDZ domains.


Pssm-ID: 319551 [Multi-domain]  Cd Length: 42  Bit Score: 41.94  E-value: 2.16e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 341898957 764 CTVCHEDFSHPIKLECNHIFCKSCIETWLDQKSTCPMCR 802
Cdd:cd16637    4 CHICLQPLVDPLDTPCGHTFCSRCLKNYLKVQKFCPIDR 42
RING-H2_RNF6_like cd16467
RING finger, H2 subclass, found in E3 ubiquitin-protein ligase RNF6, RNF12, and similar ...
763-802 2.23e-05

RING finger, H2 subclass, found in E3 ubiquitin-protein ligase RNF6, RNF12, and similar proteins; RNF6 is an androgen receptor (AR)-associated protein that induces AR ubiquitination and promotes AR transcriptional activity. RNF6-induced ubiquitination may regulate AR transcriptional activity and specificity through modulating cofactor recruitment. RNF6 is overexpressed in hormone-refractory human prostate cancer tissues and required for prostate cancer cell growth under androgen-depleted conditions. Moreover, RNF6 regulates local serine/threonine kinase LIM kinase 1 (LIMK1) levels in axonal growth cones. RNF6-induced LIMK1 polyubiquitination is mediated via K48 of ubiquitin and leads to proteasomal degradation of the kinase. RNF6 also binds and upregulates the Inha promoter, and functions as a transcription regulatory protein in the mouse sertoli cell. Furthermore, RNF6 acts as a potential tumor suppressor gene involved in the pathogenesis of esophageal squamous cell carcinoma (ESCC). RNF12, also known as LIM domain-interacting RING finger protein, or RING finger LIM domain-binding protein (R-LIM), is E3 ubiquitin-protein ligase encoded by gene RLIM that is crucial for normal embryonic development in some species and for normal X inactivation in mice. It thus functions as a major sex-specific epigenetic regulator of female mouse nurturing tissues. RNF12 is widely expressed during embryogenesis, and mainly localizes to the cell nucleus, where it regulates the levels of many proteins, including CLIM, LMO, HDAC2, TRF1, SMAD7, and REX1, by proteasomal degradation. Both RNF6 and RNF12 contain a well conserved C3H2C3-type RING-H2 finger.


Pssm-ID: 319381 [Multi-domain]  Cd Length: 43  Bit Score: 42.12  E-value: 2.23e-05
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gi 341898957 763 QCTVCHEDFSHPIKLE---CNHIFCKSCIETWLDQKSTCPMCR 802
Cdd:cd16467    1 TCSVCISEYVTGNKLRklpCSHEFHVHCIDRWLSENSTCPICR 43
RING-HC_TRIM3 cd16768
RING finger, HC subclass, found in tripartite motif-containing protein 3 (TRIM3); TRIM3, also ...
764-802 2.41e-05

RING finger, HC subclass, found in tripartite motif-containing protein 3 (TRIM3); TRIM3, also known as brain-expressed RING finger protein (BERP), RING finger protein 97 (RNF97), or RING finger protein 22 (RNF22), is an E3 ubiquitin-protein ligase involved in the pathogenesis of various cancers. It functions as a tumor suppressor that regulates asymmetric cell division in glioblastoma. It binds to the cdk inhibitor p21(WAF1/CIP1) and regulates its availability that promotes cyclin D1-cdk4 nuclear accumulation. Moreover, TRIM3 plays an important role in the central nervous system (CNS). It corresponds to gene BERP (brain-expressed RING finger protein), a unique p53-regulated gene that modulates seizure susceptibility and GABAAR cell surface expression. Furthermore, TRIM3 mediates activity-dependent turnover of postsynaptic density (PSD) scaffold proteins GKAP/SAPAP1 and is a negative regulator of dendritic spine morphology. In addition, TRIM3 may be involved in vesicular trafficking via its association with the cytoskeleton-associated-recycling or transport (CART) complex that is necessary for efficient transferrin receptor recycling, but not for epidermal growth factor receptor (EGFR) degradation. It also regulates the motility of the kinesin superfamily protein KIF21B. TRIM3 belongs to the C-VII subclass of TRIM (tripartite motif)-NHL family that is defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil domain, as well as a NHL (named after proteins NCL-1, HT2A and Lin-41 that contain repeats folded into a six-bladed beta propeller) repeat domain positioned C-terminal to the RBCC domain.


Pssm-ID: 319682 [Multi-domain]  Cd Length: 45  Bit Score: 41.91  E-value: 2.41e-05
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gi 341898957 764 CTVCHEDFSHPIKLECNHIFCKSCIETWLDQKS---TCPMCR 802
Cdd:cd16768    4 CSICLDRYHNPKVLPCLHTFCERCLQNYIPPQSltlSCPVCR 45
RING-HC_DTX3_like cd16506
RING finger, HC subclass, found in E3 ubiquitin-protein ligase Deltex3 (DTX3), Deltex-3-like ...
764-802 2.48e-05

RING finger, HC subclass, found in E3 ubiquitin-protein ligase Deltex3 (DTX3), Deltex-3-like (DTX3L) and similar proteins; The family contains Deltex3 (DTX3) and Deltex-3-like (DTX3L), both of which are E3 ubiquitin-protein ligases belonging to the Deltex (DTX) family. DTX3, also known as RING finger protein 154 (RNF154), has a biological function that remains unclear. DTX3L, also known as B-lymphoma- and BAL-associated protein (BBAP) or Rhysin-2 (Rhysin2), regulates endosomal sorting of the G protein-coupled receptor CXCR4 from endosomes to lysosomes. It also regulates subcellular localization of its partner protein, B aggressive lymphoma (BAL), by a dynamic nucleocytoplasmic trafficking mechanism. In contrast to other DTXs, both DTX3 and DTX3L contain a C3HC4-type RING-HC finger, and a previously unidentified C-terminal domain. DTX3L can associate with DTX1 through its unique N termini and further enhance self-ubiquitination.


Pssm-ID: 319420 [Multi-domain]  Cd Length: 41  Bit Score: 41.74  E-value: 2.48e-05
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gi 341898957 764 CTVCHEDFSHPIKLE-CNHIFCKSCIETWLDQKSTCPMCR 802
Cdd:cd16506    2 CPICLDTISNKKVLLkCKHSFCAPCINKALTVKPICPICQ 41
RING-HC_RNF5_like cd16534
RING finger, HC subclass, found in RING finger protein RNF5, RNF185 and similar proteins; RNF5 ...
763-802 2.73e-05

RING finger, HC subclass, found in RING finger protein RNF5, RNF185 and similar proteins; RNF5 and RNF185 are E3 ubiquitin-protein ligases that are anchored to the outer membrane of the endoplasmic reticulum (ER). RNF5 acts at early stages of cystic fibrosis (CF) transmembrane conductance regulator (CFTR) biosynthesis, and functions as a target for therapeutic modalities to antagonize mutant CFTR proteins in CF patients carrying the F508del allele. RNF185 controls the degradation of CFTR and CFTR F508del allele in a RING- and proteasome-dependent manner, but does not control that of other classical endoplasmic reticulum-associated degradation (ERAD) model substrates. Moreover, both RNF5 and RNF185 play important roles in cell adhesion and migration through the modulation of cell migration by ubiquitinating paxillin. Arabidopsis thaliana RING membrane-anchor proteins (AtRMAs) are also included in this family. They possess E3 ubiquitin-protein ligase activity and may play a role in the growth and development of Arabidopsis. All members in this family contain a C3HC4-type RING-HC finger.


Pssm-ID: 319448 [Multi-domain]  Cd Length: 43  Bit Score: 41.65  E-value: 2.73e-05
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gi 341898957 763 QCTVCHEDFSHPIKLECNHIFCKSCIETWLD---QKSTCPMCR 802
Cdd:cd16534    1 ECNICLDTAKDAVVSMCGHLFCWPCLHQWLEtrpDRPTCPVCK 43
RING-HC_TRIM26_C-IV cd16598
RING finger, HC subclass, found in tripartite motif-containing protein 26 (TRIM26) and similar ...
764-802 2.83e-05

RING finger, HC subclass, found in tripartite motif-containing protein 26 (TRIM26) and similar proteins; TRIM26, also known as acid finger protein (AFP), RING finger protein 95 (RNF95), or zinc finger protein 173 (ZNF173), is an E3 ubiquitin-protein ligase that negatively regulates interferon-beta production and antiviral response through polyubiquitination and degradation of nuclear transcription factor IRF3. It functions as an important regulator for RNA virus-triggered innate immune response by bridging TBK1 to NEMO (NF-kappaB essential modulator, also known as IKKgamma) and mediating TBK1 activation. It also acts as a novel tumor suppressor of hepatocellular carcinoma by regulating cancer cell proliferation, colony forming ability, migration, and invasion. TRIM26 belongs the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, a B-box, and two coiled coil domains, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 319512 [Multi-domain]  Cd Length: 45  Bit Score: 41.79  E-value: 2.83e-05
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gi 341898957 764 CTVCHEDFSHPIKLECNHIFCKSCI----ETWlDQKSTCPMCR 802
Cdd:cd16598    4 CSICLDYLRDPVTIDCGHVFCRSCTtdirPIS-GNRPVCPLCK 45
RING-H2_RNF12 cd16674
RING finger, H2 subclass, found in RING finger protein 12 (RNF12) and similar proteins; RNF12, ...
764-802 3.30e-05

RING finger, H2 subclass, found in RING finger protein 12 (RNF12) and similar proteins; RNF12, also known as LIM domain-interacting RING finger protein or RING finger LIM domain-binding protein (R-LIM), is an E3 ubiquitin-protein ligase encoded by gene RLIM that is crucial for normal embryonic development in some species and for normal X inactivation in mice. It thus functions as a major sex-specific epigenetic regulator of female mouse nurturing tissues. RNF12 is widely expressed during embryogenesis, and mainly localizes to the cell nucleus, where it regulates the levels of many proteins, including CLIM, LMO, HDAC2, TRF1, SMAD7, and REX1, by proteasomal degradation. Its functional activity is regulated by phosphorylation-dependent nucleocytoplasmic shuttling. It is negatively regulated by pluripotency factors in embryonic stem cells. p53 represses its transcription through Sp1. RNF12 is the primary factor responsible for X chromosome inactivation (XCI) in female placental mammals. It is an indispensable factor in up-regulation of Xist transcription, thereby leading to initiation of random XCI. It also targets REX1, an inhibitor of XCI, for proteasomal degradation. Moreover, RNF12 acts as a co-regulator of a range of transcription factors, particularly those containing a LIM homeodomain, and modulates the formation of transcriptional multiprotein complexes. It is a negative regulator of Smad7, which in turn negatively regulates the type I receptors in transforming growth factor beta (TGF-beta) superfamily signaling. In addition, paternal RNF12 is a critical survival factor for milk-producing alveolar cells. RNF12 contains an nuclear localization signal (NLS) and a C3H2C3-type RING-H2 finger.


Pssm-ID: 319588 [Multi-domain]  Cd Length: 45  Bit Score: 41.59  E-value: 3.30e-05
                         10        20        30        40
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gi 341898957 764 CTVCHEDFSHPIKLE---CNHIFCKSCIETWLDQKSTCPMCR 802
Cdd:cd16674    3 CSVCITEYTEGNKLRklpCSHEYHVHCIDRWLSENSTCPICR 44
RING-HC_TRIM2_like_C-VII cd16586
RING finger, HC subclass, found in tripartite motif-containing protein TRIM2, TRIM3, and ...
764-802 3.36e-05

RING finger, HC subclass, found in tripartite motif-containing protein TRIM2, TRIM3, and similar proteins; TRIM2, also known as RING finger protein 86 (RNF86), is an E3 ubiquitin-protein ligase that ubiquitinates the neurofilament light chain, a component of the intermediate filament in axons. Loss of function of TRIM2 results in early-onset axonal neuropathy. TRIM3, also known as brain-expressed RING finger protein (BERP), RING finger protein 97 (RNF97), or RING finger protein 22 (RNF22), is an E3 ubiquitin-protein ligase involved in the pathogenesis of various cancers. It also plays an important role in the central nervous system (CNS). In addition, TRIM3 may be involved in vesicular trafficking via its association with the cytoskeleton-associated-recycling or transport (CART) complex that is necessary for efficient transferrin receptor recycling, but not for epidermal growth factor receptor (EGFR) degradation. Both TRIM2 and TRIM3 belong to the C-VII subclass of TRIM (tripartite motif)-NHL family that is defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil domain, as well as a NHL (named after proteins NCL-1, HT2A and Lin-41 that contain repeats folded into a six-bladed beta propeller) repeat domain positioned C-terminal to the RBCC domain.


Pssm-ID: 319500 [Multi-domain]  Cd Length: 45  Bit Score: 41.63  E-value: 3.36e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 341898957 764 CTVCHEDFSHPIKLECNHIFCKSCIETWLDQKS---TCPMCR 802
Cdd:cd16586    4 CGICLERYKNPKVLPCLHTFCERCLQNYIPAESlslSCPVCR 45
RING-HC_RNF113A_B cd16539
RING finger, HC subclass, found in RING finger proteins RNF113A, RNF113B, and similar proteins; ...
764-801 3.38e-05

RING finger, HC subclass, found in RING finger proteins RNF113A, RNF113B, and similar proteins; RNF113A, also known as zinc finger protein 183 (ZNF183), is an E3 ubiquitin-protein ligase that physically interacts with the E2 protein, UBE2U. A nonsense mutation in RNF113A is associated with an X-linked trichothiodystrophy (TTD). Its yeast ortholog Cwc24p is predicted to have a spliceosome function and acts in a complex with Cef1p to participate in pre-U3 snoRNA splicing, indirectly affecting pre-rRNA processing. It is also important for the U2 snRNP binding to primary transcripts and co-migrates with spliceosomes. Moreover, the ortholog of RNF113A in fruit flies may also act as a spliceosome and is hypothesized to be involved in splicing, namely within the central nervous system. The ortholog in Caenorhabditis elegans is involved in DNA repair of inter-strand crosslinks. RNF113B, also known as zinc finger protein 183-like 1, shows high sequence similarity with RNF113A. Both RNF113A and RNF113B contain a CCCH-type zinc finger, which is commonly found in RNA-binding proteins involved in splicing, and a C3HC4-type RING-HC finger, which is frequently found in E3 ubiquitin ligases.


Pssm-ID: 319453 [Multi-domain]  Cd Length: 41  Bit Score: 41.45  E-value: 3.38e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 341898957 764 CTVCHEDFSHPIKLECNHIFCKSCIETWLDQKSTCPMC 801
Cdd:cd16539    3 CFICRKPFKNPVVTKCGHYFCEKCALKHYRKSKRCFVC 40
RING-H2_RNF165 cd16682
RING finger, H2 subclass, found in RING finger protein 165 (RNF165) and similar proteins; ...
763-805 4.11e-05

RING finger, H2 subclass, found in RING finger protein 165 (RNF165) and similar proteins; RNF165, also known as Arkadia-like 2, or Arkadia2, or Ark2C, is an E3 ubiquitin ligase with homology to C-terminal half of RNF111. It is expressed specifically in the nervous system, and can serve to amplify neuronal responses to specific signals. It thus acts as a positive regulator of bone morphogenetic protein (BMP)-Smad signaling that is involved in motor neuron (MN) axon elongation. RNF165 contains two serine rich domains, a nuclear localization signal, a NRG-TIER domain, and a C-terminal C3H2C3-type RING-H2 finger that is responsible for the enhancement of BMP-Smad1/5/8 signaling in the spinal cord.


Pssm-ID: 319596 [Multi-domain]  Cd Length: 51  Bit Score: 41.61  E-value: 4.11e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 341898957 763 QCTVCH---EDFSHPIKLECNHIFCKSCIETWLDQKSTCPMCRAEV 805
Cdd:cd16682    2 KCTICLsmlEDGEDVRRLPCMHLFHQLCVDQWLAMSKKCPICRVDI 47
RING-H2_RNF167 cd16797
RING finger, H2 subclass, found in RING finger protein 167 (RNF167) and similar proteins; ...
764-802 4.12e-05

RING finger, H2 subclass, found in RING finger protein 167 (RNF167) and similar proteins; RNF167, also known as RING105, is an endosomal/lysosomal E3 ubiquitin-protein ligase involved in alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) ubiquitination. It ubiquitinates GluA2 and regulates its surface expression, and thus acts as a selective regulator of AMPAR-mediated neurotransmission. It acts as an endosomal membrane protein which ubiquitylates vesicle-associated membrane protein 3 (VAMP3) and regulates endosomal trafficking. Moreover, RNF167 plays a role in the regulation of TSSC5 (tumor-suppressing subchromosomal transferable fragment cDNA, also known as ORCTL2/IMPT1/BWR1A/SLC22A1L), which can function in concert with the ubiquitin-conjugating enzyme UbcH6. RNF167 is widely conserved in metazoans and contains an N-terminal signal peptide, a protease-associated (PA) domain, two transmembrane domains (TM1 and TM2), and a C-terminal C3H2C3-type RING-H2 finger domain followed by a putative PEST sequence.


Pssm-ID: 319711 [Multi-domain]  Cd Length: 46  Bit Score: 41.18  E-value: 4.12e-05
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                 ....*....|....*....|....*....|....*....|...
gi 341898957 764 CTVCHEDFSHPIKLE---CNHIFCKSCIETWLDQ-KSTCPMCR 802
Cdd:cd16797    3 CAICLDEYEEGDKLRvlpCSHAYHSKCVDPWLTQtKKTCPVCK 45
mRING-HC-C3HC5_CGRF1_like cd16649
Modified RING finger, HC subclass (C3HC5-type), found in RING finger proteins, RNF26, RNF197 ...
763-802 4.32e-05

Modified RING finger, HC subclass (C3HC5-type), found in RING finger proteins, RNF26, RNF197 (CGRRF1), RNF156 (MGRN1), RNF157 and similar proteins; This family corresponds to a group of RING finger proteins containing a modified C3HC5-type RING-HC finger, which is distinguished from typical C3HC4 RING-HC finger due to the existence of the additional cysteine residue in the middle portion of the RING finger domain. Cell growth regulator with RING finger domain protein 1 (CGRRF1), also known as cell growth regulatory gene 19 protein (CGR19) or RING finger protein 197 (RNF197), functions as a novel biomarker of tissue monitor endometrial sensitivity and response to insulin-sensitizing drugs, such as metformin, in the context of obesity. RNF26 is an E3 ubiquitin ligase that temporally regulates virus-triggered type I interferon induction by increasing the stability of Mediator of IRF3 activation, MITA, also known as STING, through K11-linked polyubiquitination of MITA after viral infection and promoting degradation of IRF3, another important component required for virus-triggered interferon induction. Mahogunin ring finger-1 (MGRN1), also known as RING finger protein 156 (RNF156), is a cytosolic E3 ubiquitin-protein ligase that inhibits signaling through the G protein-coupled melanocortin receptors-1 (MC1R), -2 (MC2R) and -4 (MC4R) via ubiquitylation-dependent and -independent processes. It suppresses chaperone-associated misfolded protein aggregation and toxicity. RNF157 is a cytoplasmic E3 ubiquitin ligase predominantly expressed in brain. It is a homolog of the E3 ligase MGRN1. In cultured neurons, it promotes neuronal survival in an E3 ligase-dependent manner. In contrast, it supports growth and maintenance of dendrites independent of its E3 ligase activity. RNF157 interacts with and ubiquitinates the adaptor protein APBB1 (amyloid beta precursor protein-binding, family B, member 1 or Fe65), which regulates neuronal survival, but not dendritic growth downstream of RNF157. The nuclear localization of APBB1 together with its interaction partner RNA-binding protein SART3 (squamous cell carcinoma antigen recognized by T cells 3 or Tip110) is crucial to trigger apoptosis.


Pssm-ID: 319563  Cd Length: 41  Bit Score: 41.00  E-value: 4.32e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 341898957 763 QCTVCHEDFSHPIKLECNHI-FCKSCIETWLDQKSTCPMCR 802
Cdd:cd16649    1 DCVVCQNGTVNWLLLPCRHLcLCDGCVKYLQYQANNCPMCR 41
RING-HC_RNF138 cd16544
RING finger, HC subclass, found in RING finger protein 138 (RNF138) and similar proteins; ...
760-802 4.38e-05

RING finger, HC subclass, found in RING finger protein 138 (RNF138) and similar proteins; RNF138, also known as Nemo-like kinase-associated RING finger protein (NARF) or NLK-associated RING finger protein, is an E3 ubiquitin-protein ligase that plays an important role in glioma cell proliferation, apoptosis, and cell cycle. It specifically cooperates with the E2 conjugating enzyme E2-25K (Hip-2/UbcH1), regulates the ubiquitylation and degradation of T cell factor/lymphoid enhancer factor (TCF/LEF), and further suppresses Wnt-beta-catenin signaling. RNF138, together with three closely related proteins: RNF114, RNF125 and RNF166, forms a novel family of ubiquitin ligases with a C3HC4-type RING-HC finger, a C2HC-, and two C2H2-type zinc fingers, as well as a ubiquitin interacting motif (UIM).


Pssm-ID: 319458 [Multi-domain]  Cd Length: 46  Bit Score: 41.32  E-value: 4.38e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 341898957 760 DDNQCTVCHEDFSHPIKLE-CNHIFCKSCIET-WLDQKSTCPMCR 802
Cdd:cd16544    1 EDFSCPVCQEVLQTPIRTKkCRHVFCRKCFLLaMRRSGAHCPLCR 45
COG5540 COG5540
RING-finger-containing ubiquitin ligase [Posttranslational modification, protein turnover, ...
763-805 5.06e-05

RING-finger-containing ubiquitin ligase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227827 [Multi-domain]  Cd Length: 374  Bit Score: 46.14  E-value: 5.06e-05
                         10        20        30        40
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gi 341898957 763 QCTVCHEDFSHPIK---LECNHIFCKSCIETWL-DQKSTCPMCRAEV 805
Cdd:COG5540  325 ECAICMSNFIKNDRlrvLPCDHRFHVGCVDKWLlGYSNKCPVCRTAI 371
RING-HC_TIF1_C-VI cd16585
RING finger, HC subclass, found in the transcriptional inknown asiary factor 1 (TIF1) family ...
763-805 5.16e-05

RING finger, HC subclass, found in the transcriptional inknown asiary factor 1 (TIF1) family and similar proteins; This family corresponds to the TIF1 family of transcriptional cofactors including TIF1alpha (TRIM24), TIF1beta (TRIM28), and TIF1gamma (TRIM33), which belongs to the C-VI subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a plant homeodomain (PHD), and a bromodomain (Bromo) positioned C-terminal to the RBCC domain. TIF1 proteins couple chromatin modifications to transcriptional regulation, signaling, and tumor suppression. They exert a deacetylase-dependent silencing effect when tethered to a promoter region. TIF1alpha and TIF1beta can homodimerize and contain a PXVXL motif necessary and sufficient for heterochromatin protein 1(HP1) binding. They bind nuclear receptors and Kruppel-associated boxes (KRAB) specifically and respectively. TIF1gamma is structurally closely related to TIF1alpha and TIF1beta, but has very little functional features in common with them. It does not interact with the KRAB silencing domain of KOX1 or the heterochromatinic proteins HP1alpha, beta and gamma. It cannot bind to nuclear receptors (NRs). TIF1delta (TRIM66) doesn"t have RING-HC finger and is not included here.


Pssm-ID: 319499 [Multi-domain]  Cd Length: 61  Bit Score: 41.33  E-value: 5.16e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 341898957 763 QCTVCHEDFS--HPIKLECNHIFCKSCIETWLDQKST--------------CPMCRAEV 805
Cdd:cd16585    3 TCGVCKQDLRsrEPKLLPCLHSFCKRCLPAHLREASSpgsegyaeqvgvirCPVCKQEC 61
RING-H2_RNF44 cd16680
RING finger, H2 subclass, found in RING finger protein 44 (RNF44) and similar proteins; RNF44 ...
764-802 5.29e-05

RING finger, H2 subclass, found in RING finger protein 44 (RNF44) and similar proteins; RNF44 is an uncharacterized RING finger protein that shows high sequence similarity with RNF38, which is a nuclear E3 ubiquitin protein ligase that plays a role in regulating p53. RNF44 contains a coiled-coil motif, a KIL motif (Lys-X2-Ile/Leu-X2-Ile/Leu, X can be any amino acid), and a C3H2C2-type RING-H2 finger.


Pssm-ID: 319594 [Multi-domain]  Cd Length: 45  Bit Score: 41.20  E-value: 5.29e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 341898957 764 CTVCHEDFSHPIKLE---CNHIFCKSCIETWLDQKSTCPMCR 802
Cdd:cd16680    4 CVVCFSDFESRQLLRvlpCNHEFHTKCVDKWLKTNRTCPICR 45
RING-HC_TRIM39_C-IV cd16601
RING finger, HC subclass, found in tripartite motif-containing protein 39 (TRIM39) and similar ...
764-801 5.45e-05

RING finger, HC subclass, found in tripartite motif-containing protein 39 (TRIM39) and similar proteins; TRIM39, also known as RING finger protein 23 (RNF23) or testis-abundant finger protein, is an E3 ubiquitin-protein ligase that plays a role in controlling DNA damage-induced apoptosis through inhibition of the anaphase promoting complex (APC/C), a multiprotein ubiquitin ligase that controls multiple cell cycle regulators, including cyclins, geminin, and others. TRIM39 also functions as a regulator of several key processes in the proliferative cycle. It directly regulates p53 stability. It modulates cell cycle progression and DNA damage responses via stabilizing p21. Moreover, TRIM39 negatively regulates the nuclear factor kappaB (NFkappaB)-mediated signaling pathway through stabilization of Cactin, an inhibitor of NFkappaB- and Toll-like receptor (TLR)-mediated transcriptions, which is induced by inflammatory stimulants such as tumor necrosis factor alpha (TNFalpha). Furthermore, TRIM39 is a MOAP-1-binding protein that can promote apoptosis signaling through stabilization of MOAP-1 via the inhibition of its poly-ubiquitination process. TRIM39 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 319515 [Multi-domain]  Cd Length: 44  Bit Score: 40.81  E-value: 5.45e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 341898957 764 CTVCHEDFSHPIKLECNHIFCKSCIETW---LDQKSTCPMC 801
Cdd:cd16601    4 CSVCLEYLKEPVIIECGHNFCKACITRWwedLERDFPCPVC 44
RING-HC_malin cd16516
RING finger, HC subclass, found in malin and similar proteins; Malin ("mal" for seizure in ...
763-802 5.85e-05

RING finger, HC subclass, found in malin and similar proteins; Malin ("mal" for seizure in French), also known as NHL repeat-containing protein 1 (NHLRC1), or EPM2B, is a nuclear E3 ubiquitin-protein ligase that ubiquitinates and promotes the degradation of laforin (EPM2A encoding protein phosphatase). Malin and laforin operate as a functional complex that play key roles in regulating cellular functions such as glycogen metabolism, unfolded cellular stress response, and proteolytic processes. They act as pro-survival factors that negatively regulate the Hipk2-p53 cell death pathway. They also negatively regulate cellular glucose uptake by preventing plasma membrane targeting of glucose transporters. Moreover, they degrade polyglucosan bodies in concert with glycogen debranching enzyme and brain isoform glycogen phosphorylase. Furthermore, they, together with Hsp70, form a new functional complex that suppress the cellular toxicity of misfolded proteins by promoting their degradation through the ubiquitin-proteasome system. Defects in either malin or laforin may cause Lafora disease (LD), a fatal form of teenage-onset autosomal recessive progressive myoclonus epilepsy. In addition, malin may have function independent of laforin in lysosomal biogenesis and/or lysosomal glycogen disposal. Malin contains six NHL-repeat protein-protein interaction domains and a C3HC4-type RING-HC finger.


Pssm-ID: 319430 [Multi-domain]  Cd Length: 48  Bit Score: 40.97  E-value: 5.85e-05
                         10        20        30        40
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gi 341898957 763 QCTVCHEDFSH-----PIKLECNHIFCKSCIETWLDQKST---CPMCR 802
Cdd:cd16516    1 ECKVCFEKFSTqqqhrPRNLPCGHVLCQECVLALCHPNVSkleCPFCR 48
RING-H2_RNF150 cd16805
RING finger, H2 subclass, found in RING finger protein 150 (RNF150) and similar proteins; ...
762-807 6.10e-05

RING finger, H2 subclass, found in RING finger protein 150 (RNF150) and similar proteins; RNF150 is a RING finger protein that its polymorphisms may be associated with chronic obstructive pulmonary disease (COPD) risk in the Chinese population. Further studies with larger numbers of participants worldwide are needed for validation of the relationships between RNF150 genetic variants and the pathogenesis of COPD. RNF150 contains an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C-terminal C3H2C3-type RING-H2 finger domain followed by a putative PEST sequence.


Pssm-ID: 319719 [Multi-domain]  Cd Length: 49  Bit Score: 41.16  E-value: 6.10e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 341898957 762 NQCTVCHEDF--SHPIK-LECNHIFCKSCIETWLDQKSTCPMCRAEVTK 807
Cdd:cd16805    1 DNCAVCIEGYkpNDVVRiLPCRHLFHKSCVDPWLLDHRTCPMCKMNILK 49
RING-H2_RNF13_like cd16665
RING finger, H2 subclass, found in RING finger protein 13 (RNF13), RING finger protein 167 ...
764-802 6.81e-05

RING finger, H2 subclass, found in RING finger protein 13 (RNF13), RING finger protein 167 (RNF167), and similar proteins; This subfamily includes RING finger protein 13 (RNF13), RING finger protein 167 (RNF167), Zinc/RING finger protein 4 (ZNRF4), and similar proteins, which belong to a larger PA-TM-RING ubiquitin ligase family that has been characterized by containing an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane domain (TM), and a C-terminal C3H2C3-type RING-H2 finger domain followed by a putative PEST sequence. RNF13 is a widely expressed membrane-associated E3 ubiquitin-protein ligase that is functionally significant in the regulation of cancer development, muscle cell growth, and neuronal development. Its expression is developmentally regulated during myogenesis and is upregulated in various tumors. RNF13 negatively regulates cell proliferation through its E3 ligase activity. RNF167, also known as RING105, is an endosomal/lysosomal E3 ubiquitin-protein ligase involved in alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) ubiquitination. It acts as an endosomal membrane protein which ubiquitylates vesicle-associated membrane protein 3 (VAMP3) and regulates endosomal trafficking. Moreover, RNF167 plays a role in the regulation of TSSC5 (tumor-suppressing subchromosomal transferable fragment cDNA; also known as ORCTL2/IMPT1/BWR1A/SLC22A1L), which can function in concert with the ubiquitin-conjugating enzyme UbcH6. ZNRF4, also known as RING finger protein 204 (RNF204), or Nixin, is an endoplasmic reticulum (ER) membrane-anchored ubiquitin ligase that physically interacts with the ER-localized chaperone calnexin in a glycosylation-independent manner, induces calnexin ubiquitination, and p97-dependent degradation, indicating an ER-associated degradation-like mechanism of calnexin turnover. The murine protein sperizin (spermatid-specific ring zinc finger) is a homolog of human ZNRF4. It is specifically expressed in Haploid germ cells and involved in spermatogenesis.


Pssm-ID: 319579 [Multi-domain]  Cd Length: 46  Bit Score: 40.85  E-value: 6.81e-05
                         10        20        30        40
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gi 341898957 764 CTVCHEDFSHPIKLE---CNHIFCKSCIETWLDQ-KSTCPMCR 802
Cdd:cd16665    3 CAICLDDYEEGDKLRilpCSHAYHCKCIDPWLTQnRRTCPVCK 45
RING-HC_TRIM36 cd16756
RING finger, HC subclass, found in tripartite motif-containing protein 36 (TRIM36) and similar ...
763-805 6.86e-05

RING finger, HC subclass, found in tripartite motif-containing protein 36 (TRIM36) and similar proteins; TRIM36, human ortholog of mouse Haprin, also known as RING finger protein 98 (RNF98) or zinc-binding protein Rbcc728, is an E3 ubiquitin-protein ligase expressed in the germ plasm. It has been implicated in acrosome reaction, fertilization, and embryogenesis, as well as in the carcinogenesis. TRIM36 functions upstream of Wnt/beta-catenin activation, and plays a role in controlling the stability of proteins regulating microtubule polymerization during cortical rotation, and subsequently dorsal axis formation. It is also potentially associated with chromosome segregation through interacting with the kinetochore protein centromere protein-H (CENP-H), and colocalizing with the microtubule protein alpha-tubulin. Its overexpression may cause chromosomal instability and carcinogenesis. It is, thus, a novel regulator affecting cell cycle progression. Moreover, TRIM36 plays a critical role in the arrangement of somites during embryogenesis. TRIM36 belongs to the C-I subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 319670 [Multi-domain]  Cd Length: 49  Bit Score: 40.95  E-value: 6.86e-05
                         10        20        30        40
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gi 341898957 763 QCTVCHEDFSHPIKLECNHIFCKSCIETWLdQKSTCPMCRAEV 805
Cdd:cd16756    5 ICPACKELFTHPLILPCQHNICHRCAKELL-TSFPCPGCQHDV 46
RING-HC_RNF4 cd16533
RING finger, HC subclass, found in RING finger protein 4 (RNF4) and similar proteins; RNF4, ...
764-802 7.55e-05

RING finger, HC subclass, found in RING finger protein 4 (RNF4) and similar proteins; RNF4, also known as small nuclear ring finger protein (SNURF), is a SUMO-targeted E3 ubiquitin-protein ligase with a pivotal function in the DNA damage response (DDR) through interacting with the deubiquitinating enzyme ubiquitin-specific protease 11 (USP11), a known DDR-component, and further facilitating DNA repair. It plays a novel role in preventing the loss of intact chromosomes and ensures the maintenance of chromosome integrity. Moreover, RNF4 is responsible for the UbcH5A-catalyzed formation of K48 chains that target SUMO-modified promyelocytic leukemia (PML) protein for proteasomal degradation in response to arsenic treatment. It also interacts with telomeric repeat binding factor 2 (TRF2) in a small ubiquitin-like modifiers (SUMO)-dependent manner and preferentially targets SUMO-conjugated TRF2 for ubiquitination through SUMO-interacting motifs (SIMs). Furthermore, RNF4 can form a complex with a Ubc13-ubiquitin conjugate and Ube2V2. It catalyzes K63-linked polyubiquitination by the Ube2V2-Ubc13 (ubiquitin-loaded) complex. Meanwhile, RNF4 negatively regulates nuclear factor kappa B (NF-kappaB) signaling by down-regulating transforming growth factor beta (TGF-beta)-activated kinase 1 (TAK1)-TAK1-binding protein2 (TAB2). RNF4 contains four SIMs followed by a C3HC4-type RING-HC finger at the C-terminus.


Pssm-ID: 319447 [Multi-domain]  Cd Length: 54  Bit Score: 40.90  E-value: 7.55e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 341898957 764 CTVCHEDFS-------HPIKLECNHIFCKSCIETWLDQKSTCPMCR 802
Cdd:cd16533    6 CPICMDGYSeivqsgrLLVSTICGHVFCSQCIRDSIKNAHTCPTCR 51
RING-H2_RNF103 cd16473
RING finger, H2 subclass, found in RING finger protein 103 (RNF103) and similar proteins; ...
763-804 7.83e-05

RING finger, H2 subclass, found in RING finger protein 103 (RNF103) and similar proteins; RNF103, also known as KF-1, or zinc finger protein 103 homolog (Zfp-103), is an endoplasmic reticulum (ER)-resident E3 ubiquitin-protein ligase that is widely expressed in many different organs, including brain, heart, kidney, spleen, and lung. It is involved in the ER-associated degradation (ERAD) pathway through interacting with components of the ERAD pathway, including Derlin-1 and VCP. RNF103 contains several hydrophobic regions at its N-terminal and middle regions, as well as a C-terminal C3H2C3-type RING-H2 finger.


Pssm-ID: 319387 [Multi-domain]  Cd Length: 46  Bit Score: 40.35  E-value: 7.83e-05
                         10        20        30        40
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gi 341898957 763 QCTVCHEDF---SHPIKLECNHIFCKSCIETWLDQKS-TCPMCRAE 804
Cdd:cd16473    1 ECVICLENYeegCLLCGLPCGHVFHQNCIDVWLTRDNhCCPVCRWP 46
RING-HC_BARD1 cd16496
RING finger, HC subclass, found in BRCA1-associated RING domain protein 1 (BARD-1) and similar ...
763-803 9.47e-05

RING finger, HC subclass, found in BRCA1-associated RING domain protein 1 (BARD-1) and similar proteins; BARD-1 is a critical factor in BRCA1-mediated tumor suppression and may also serve as a target for tumorigenic lesions in some human cancers. It associates with BRCA1 (breast cancer-1) to form a heterodimeric BRCA1/BARD1 complex that is responsible for maintaining genomic stability through nuclear functions involving DNA damage signaling and repair, transcriptional regulation, and cell cycle control. The BRCA1/BARD1 complex catalyzes autoubiquitination of BRCA1 and trans ubiquitination of other protein substrates. Its E3 ligase activity is dramatically reduced in the presence of UBX domain protein 1 (UBXN1). BARD-1 contains an C3HC4-type RING-HC finger that binds BRCA1 at its N-terminus and three tandem ankyrin repeats and tandem BRCT repeat domains that bind CstF-50 (cleavage stimulation factor) to modulate mRNA processing and RNAP II stability in response to DNA damage at its C-terminus.


Pssm-ID: 319410 [Multi-domain]  Cd Length: 45  Bit Score: 40.43  E-value: 9.47e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 341898957 763 QCTVCHEDFSHPIKL-ECNHIFCKSCIETWLDQKstCPMCRA 803
Cdd:cd16496    3 SCSRCHGILREPVCLgGCEHVFCRSCVGDHLGNG--CPVCDA 42
RING-H2_APC11 cd16456
RING finger, H2 subclass, found in anaphase-promoting complex subunit 11 (APC11) and similar ...
778-804 1.10e-04

RING finger, H2 subclass, found in anaphase-promoting complex subunit 11 (APC11) and similar proteins; APC11, also known as cyclosome subunit 11, or hepatocellular carcinoma-associated RING finger protein, is a C3H2C3-type RING-H2 protein that facilitates ubiquitin chain formation by recruiting ubiquitin-charged ubiquitin conjugating enzymes (E2) through its RING-H2 domain. APC11 and its partner the cullin-like subunit APC2 form the dynamic catalytic core of the gigantic, multisubunit 1.2-MDa anaphase-promoting complex/cyclosome (APC), also known as the cyclosome, which is a ubiquitin-protein ligase (E3) composed of at least 12 subunits and controls cell division by ubiquitinating cell cycle regulators, such as cyclin B and securin, to drive their timely degradation. APC11 can be inhibited by hydrogen peroxide, which may contributes to the delay in cell cycle progression through mitosis that is characteristic of cells subjected to oxidative stress. APC11 contains a canonical RING-H2-finger domain, which includes one histidine and seven cysteine residues that coordinate two Zn2+ ions. In addition, it contains a third Zn2+-binding site and the third Zn2+ ion is not essential for its ligase activity.


Pssm-ID: 319370 [Multi-domain]  Cd Length: 63  Bit Score: 40.72  E-value: 1.10e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 341898957 778 ECNHIFCKSCIETWLDQ---KSTCPMCRAE 804
Cdd:cd16456   31 KCSHAFHMHCILKWLNSqqvQQQCPMCRQE 60
RING-HC_TRIM58_C-IV cd16606
RING finger, HC subclass, found in tripartite motif-containing protein TRIM58 and similar ...
761-803 1.10e-04

RING finger, HC subclass, found in tripartite motif-containing protein TRIM58 and similar proteins; TRIM58, also known as protein BIA2, is an erythroid E3 ubiquitin-protein ligase induced during late erythropoiesis. It binds and ubiquitinates the intermediate chain of the microtubule motor dynein (DYNC1LI1/DYNC1LI2), stimulating the degradation of the dynein holoprotein complex. It may participate in the erythroblast enucleation process through regulation of nuclear polarization. TRIM58 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 319520 [Multi-domain]  Cd Length: 51  Bit Score: 40.39  E-value: 1.10e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 341898957 761 DNQCTVCHEDFSHPIKLECNHIFCKSCIETWLDQKST-------CPMCRA 803
Cdd:cd16606    1 EARCPVCLDFLQEPVSVDCGHSFCLRCISEFCEKSDSaqggvyaCPQCRG 50
Prok-RING_4 pfam14447
Prokaryotic RING finger family 4; RING finger family domain found sporadically in bacteria. ...
764-808 1.12e-04

Prokaryotic RING finger family 4; RING finger family domain found sporadically in bacteria. The finger is fused to an N-terminal alpha-helical domain, ROT/Trove-like repeats and a C-terminal TerD domain. The architecture suggests a possible role in an RNA-processing complex.


Pssm-ID: 316929  Cd Length: 46  Bit Score: 40.04  E-value: 1.12e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 341898957  764 CTVCHEDFSHPIKLECNHIFCKSCIETWldQKSTCPMCRAEVTKD 808
Cdd:pfam14447   1 CVLCGRVGTVHILSPCGHLVCRDCFDGS--DYSGCPICHRRIDPD 43
RING-HC_TRIM2 cd16767
RING finger, HC subclass, found in tripartite motif-containing protein 2 (TRIM2); TRIM2, also ...
764-802 1.20e-04

RING finger, HC subclass, found in tripartite motif-containing protein 2 (TRIM2); TRIM2, also known as RING finger protein 86 (RNF86), is an E3 ubiquitin-protein ligase that ubiquitinates the neurofilament light chain, a component of the intermediate filament in axons. Loss of function of TRIM2 results in early-onset axonal neuropathy. TRIM2 also plays a role in mediating the p42/p44 MAPK-dependent ubiquitination of the cell death-promoting protein Bcl-2-interacting mediator of cell death (Bim) in rapid ischemic tolerance. TRIM2 belongs to the C-VII subclass of TRIM (tripartite motif)-NHL family that is defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil domain, as well as a NHL (named after proteins NCL-1, HT2A and Lin-41 that contain repeats folded into a six-bladed beta propeller) repeat domain positioned C-terminal to the RBCC domain.


Pssm-ID: 319681 [Multi-domain]  Cd Length: 46  Bit Score: 40.02  E-value: 1.20e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 341898957 764 CTVCHEDFSHPIKLECNHIFCKSCIETWLDQKS---TCPMCR 802
Cdd:cd16767    4 CSICLDRYKNPKVLPCLHTFCERCLQNYIPAHSltlSCPVCR 45
RING-H2_RNF122 cd16676
RING finger, H2 subclass, found in RING finger protein 122 (RNF122) and similar proteins; ...
764-805 1.22e-04

RING finger, H2 subclass, found in RING finger protein 122 (RNF122) and similar proteins; RNF122 is a RING finger protein associated with HEK 293T cell viability. It is localized to the endoplasmic reticulum (ER) and the Golgi apparatus, and overexpressed in anaplastic thyroid cancer cells. RNF122 functions as an E3 ubiquitin ligase that can ubiquitinate itself and undergoes degradation through its RING finger in a proteasome-dependent manner. It interacts with calcium-modulating cyclophilin ligand (CAML), which is not a substrate, but a stabilizer of RNF122. RNF122 contains an N-terminal transmembrane domain and a C-terminal C3H2C3-type RING-H2 finger.


Pssm-ID: 319590 [Multi-domain]  Cd Length: 47  Bit Score: 40.00  E-value: 1.22e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 341898957 764 CTVCHEDFSHPIKL---ECNHIFCKSCIETWLDQKSTCPMCRAEV 805
Cdd:cd16676    3 CAVCLEDFKVKDELgvlPCQHAFHRKCLVKWLEVRCVCPMCNKPI 47
RING-HC_Cbl cd16708
RING finger, HC subclass, found in E3 ubiquitin-protein ligase Cbl and similar proteins; Cbl, ...
764-805 1.35e-04

RING finger, HC subclass, found in E3 ubiquitin-protein ligase Cbl and similar proteins; Cbl, also known as Casitas B-lineage lymphoma proto-oncogene, proto-oncogene c-Cbl, RING finger protein 55 (RNF55), or signal transduction protein Cbl, is a multi-domain protein that acts as a key negative regulator of various receptor and non-receptor tyrosine kinases signaling. It contains a tyrosine kinase-binding domaina (TKB, also known as the phosphotyrosine binding PTB domain, is composed of a four helix-bundle, a Ca2+ binding EF-hand and a highly variant SH2 domain), a proline-rich domain, a C3HC4-type RING-HC finger, and an ubiquitin-associated (UBA) domain. TKB is responsible for the interactions with many tyrosine kinases, such as the colony-stimulating factor-1 (CSF-1) receptor, Syk/ZAP-70, and Src-family of protein tyrosine kinases. The proline-rich domain can recruit proteins with a SH3 domain. Moreover, Cbl functions as an E3 ubiquitin ligase that can bind ubiquitin-conjugating enzymes (E2s) through the RING-HC finger.


Pssm-ID: 319622  Cd Length: 57  Bit Score: 40.42  E-value: 1.35e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 341898957 764 CTVCHEDfSHPIKLE-CNHIFCKSCIETWLDQKST-CPMCRAEV 805
Cdd:cd16708    4 CKICAEN-DKDVKIEpCGHLMCTSCLTSWQESEGQgCPFCRCEI 46
RING-HC_SH3RF3 cd16750
RING finger, HC subclass, found in SH3 domain-containing RING finger protein 3 (SH3RF3) and ...
763-802 1.41e-04

RING finger, HC subclass, found in SH3 domain-containing RING finger protein 3 (SH3RF3) and similar proteins; SH3RF3, also known as plenty of SH3s 2 (POSH2) or SH3 multiple domains protein 4 (SH3MD4), is a scaffold protein with E3 ubiquitin-protein ligase activity. It was identified in the screen for interacting partners of p21-activated kinase 2 (PAK2). It may play a role in regulating c-Jun N-terminal kinase (JNK) mediated apoptosis in certain conditions. It also interacts with GTP-loaded Rac1. SH3RF3 is highly homologous to SH3RF1. Both of them contain an N-terminal C3HC4-type RING-HC finger responsible for the E3 ligase activity and four Src Homology 3 (SH3) domains that are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs.


Pssm-ID: 319664 [Multi-domain]  Cd Length: 46  Bit Score: 39.71  E-value: 1.41e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 341898957 763 QCTVCHEDFSHPIK-LECNHIFCKSCIETWLDQKST--CPMCR 802
Cdd:cd16750    4 ECSVCLERLDTTSKvLPCQHTFCRRCLEEIVSSRKElrCPECR 46
RING-HC_TRIM41_like_C-IV cd16602
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM41, TRIM52 and ...
764-802 1.49e-04

RING finger, HC subclass, found in tripartite motif-containing proteins TRIM41, TRIM52 and similar proteins; TRIM41 and TRIM52, two closely related tripartite motif-containing proteins, have dramatically expanded RING domains compared with the rest of the TRIM family proteins. TRIM41 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. In contrast, TRIM52 lacks the putative viral recognition SPRY/B30.2 domain, and thus has been classified to the C-V subclass of TRIM family that contains only RBCC domains. TRIM41, also known as RING finger-interacting protein with C kinase (RINCK), is an E3 ubiquitin-protein ligase that promotes the ubiquitination of protein kinase C (PKC) isozymes in cells. It specifically recognizes the C1 domain of PKC isozymes. It controls the amplitude of PKC signaling by controlling the amount of PKC in the cell. TRIM52, also known as RING finger protein 102 (RNF102), is encoded by a novel, noncanonical antiviral TRIM52 gene in primate genomes with unique specificity determined by the rapidly evolving RING domain.


Pssm-ID: 319516 [Multi-domain]  Cd Length: 41  Bit Score: 39.46  E-value: 1.49e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 341898957 764 CTVCHEDFSHPIKLECNHIFCKSCI-ETWLdqksTCPMCR 802
Cdd:cd16602    5 CAICLDYFRDPVSIGCGHNFCRVCVtQLWF----TCPQCR 40
mRING-CH-C4HC2H_ZNRF cd16489
Modified RING-CH finger, H2 subclass (C4HC2H-type), found in the ZNRF family; This ZNRF family ...
763-800 1.65e-04

Modified RING-CH finger, H2 subclass (C4HC2H-type), found in the ZNRF family; This ZNRF family includes zinc/RING finger proteins ZNRF1, ZNRF2, and similar proteins. It has been characterized by containing a unique combination zinc finger-RING finger motif in the C-terminal region, which is evolutionarily conserved in a wide range of species, including Caenorhabditis elegans and Drosophila. The ZNRF family of proteins function as an E3 ubiquitin ligase and are highly expressed in central nervous system (CNS) and peripheral nervous system (PNS) neurons, particularly during development and in adulthood. In neurons, ZNRF1 and ZNRF2 are differentially localized within the synaptic region. ZNRF1 is associated with synaptic vesicle membranes, whereas ZNRF2 is present in presynaptic plasma membranes. They are N-myrisotoylated and also located in the endosome-lysosome compartment in fibroblasts. ZNRF proteins may play a role in the establishment and maintenance of neuronal transmission and plasticity via their ubiquitin ligase activity, as well as in regulating Ca2+-dependent exocytosis. The RING fingers found in ZNRF proteins are modified as C4HC2H-type RING-CH finger, rather than the typical C4HC3-type RING-CH finger, which is a variant of RING-H2 finger.


Pssm-ID: 319403 [Multi-domain]  Cd Length: 43  Bit Score: 39.57  E-value: 1.65e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 341898957 763 QCTVCHEDFS--HPI-KLECNHIFCKSCIETWLDQKSTCPM 800
Cdd:cd16489    1 ECVICLEELLagDTIaRLPCLCIYHKKCIDDWFEVNRSCPE 41
RING-HC_RAG1 cd16530
RING finger, HC subclass, found in recombination activating gene-1 (RAG-1) and similar ...
764-802 1.87e-04

RING finger, HC subclass, found in recombination activating gene-1 (RAG-1) and similar proteins; RAG-1, also known as V(D)J recombination-activating protein 1, RING finger protein 74 (RNF74), or endonuclease RAG1, is the catalytic component of the RAG complex, a multiprotein complex that mediates the DNA cleavage phase during V(D)J recombination. RAG1 is the lymphoid-specific factor that mediates the DNA-binding to the conserved recombination signal sequences (RSS) and catalyzes the DNA cleavage activities by introducing a double-strand break between the RSS and the adjacent coding segment. It also functions as an E3 ubiquitin-protein ligase that mediates monoubiquitination of histone H3, which is required for the joining step of V(D)J recombination. RAG-1 contains an N-terminal C3HC4-type RING-HC finger that mediates monoubiquitylation of Histone H3, an adjacent C2H2-type zinc finger, and a nonamer binding (NBD) DNA-binding domain.


Pssm-ID: 319444 [Multi-domain]  Cd Length: 46  Bit Score: 39.35  E-value: 1.87e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 341898957 764 CTVCHEDFSHPIKLECNHIFCKSCIETWLD-QKSTCPMCR 802
Cdd:cd16530    5 CQVCEHILADPVQTPCKHLFCRTCILKCLKvMGSYCPSCR 44
RING-HC_TRIM72_C-IV cd16612
RING finger, HC subclass, found in tripartite motif-containing protein 72 (TRIM72) and similar ...
761-802 2.09e-04

RING finger, HC subclass, found in tripartite motif-containing protein 72 (TRIM72) and similar proteins; TRIM72, also known as Mitsugumin-53 (MG53), is a muscle-specific protein that plays a central role in cell membrane repair by nucleating the assembly of the repair machinery at muscle injury sites. It is required in repair of alveolar epithelial cells under plasma membrane stress failure. It interacts with dysferlin to regulate sarcolemmal repair. Upregulation of TRIM72 develops obesity, systemic insulin resistance, dyslipidemia, and hyperglycemia, as well as induces diabetic cardiomyopathy through transcriptional activation of peroxisome proliferation-activated receptor alpha (PPAR-alpha) signaling pathway. Compensation for the absence of AKT signaling by ERK signaling during TRIM72 overexpression leads to pathological hypertrophy. Moreover, TRIM72 functions as a novel negative feedback regulator of myogenesis via targeting insulin receptor substrate-1 (IRS-1). It is transcriptionally activated by the synergism of myogenin (MyoD) and myocyte enhancer factor 2 (MEF2). TRIM72 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 319526 [Multi-domain]  Cd Length: 47  Bit Score: 39.48  E-value: 2.09e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 341898957 761 DNQCTVCHEDFSHPIKLECNHIFCKSC---IETWLDQKST--CPMCR 802
Cdd:cd16612    1 DLSCPLCLELFRAPVTPECGHTFCQACltrVAKEQDQNGTtpCPTCQ 47
RING-H2_ZNRF3 cd16799
RING finger, H2 subclass, found in zinc/RING finger protein 3 (ZNRF3) and similar proteins; ...
764-802 2.19e-04

RING finger, H2 subclass, found in zinc/RING finger protein 3 (ZNRF3) and similar proteins; ZNRF3, also known as RING finger protein 203 (RNF203), is a homolog of Ring finger protein 43 (RNF43). It is a transmembrane E3 ubiquitin-protein ligase that is associated with the Wnt receptor complex, and negatively regulates Wnt signaling by promoting the turnover of frizzled and lipoprotein receptor-related protein LRP6 in an R-spondin-sensitive manner. It inhibits gastric cancer cell growth and promotes the cell apoptosis by affecting the Wnt/beta-catenin/TCF signaling pathway. ZNRF3 contains an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C3H2C3-type RING-H2 finger domain followed by a long C-terminal region.


Pssm-ID: 319713 [Multi-domain]  Cd Length: 45  Bit Score: 39.24  E-value: 2.19e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 341898957 764 CTVCHEDFSHPIKLE---CNHIFCKSCIETWLDQKSTCPMCR 802
Cdd:cd16799    2 CAICLEKYIDGEELRvipCTHRFHKKCVDPWLLQHHTCPHCR 43
APC11 COG5194
Component of SCF ubiquitin ligase and anaphase-promoting complex [Posttranslational ...
779-804 2.24e-04

Component of SCF ubiquitin ligase and anaphase-promoting complex [Posttranslational modification, protein turnover, chaperones / Cell division and chromosome partitioning];


Pssm-ID: 227521 [Multi-domain]  Cd Length: 88  Bit Score: 40.59  E-value: 2.24e-04
                         10        20
                 ....*....|....*....|....*.
gi 341898957 779 CNHIFCKSCIETWLDQKSTCPMCRAE 804
Cdd:COG5194   54 CNHAFHDHCIYRWLDTKGVCPLDRQT 79
RING-HC_RNF186 cd16557
RING finger, HC subclass, found in RING finger protein 186 (RNF186) and similar proteins; ...
761-802 2.45e-04

RING finger, HC subclass, found in RING finger protein 186 (RNF186) and similar proteins; RNF186 is an E3 ubiquitin-protein ligase with an N-terminal C3HC4-type RING-HC finger and two putative C-terminal transmembrane domains which enable it to localize in a certain organelle. It regulates RING-dependent self-ubiquitination, as well as endoplasmic reticulum (ER) stress-mediated apoptosis through interaction with the Bcl-2 family protein BNip1.


Pssm-ID: 319471 [Multi-domain]  Cd Length: 51  Bit Score: 39.43  E-value: 2.45e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 341898957 761 DNQCTVCHEDFSHPIK---LECNHIFCKSCIETWLDQKS-----TCPMCR 802
Cdd:cd16557    1 DLECLVCFNSYEFVRKpklLACQHAFCAICLKLILEEKDntwviTCPLCR 50
RING-HC_TRIM68_C-IV cd16610
RING finger, HC subclass, found in tripartite motif-containing protein 68 (TRIM68) and similar ...
764-802 2.50e-04

RING finger, HC subclass, found in tripartite motif-containing protein 68 (TRIM68) and similar proteins; TRIM68, also known as RING finger protein 137 (RNF137) or SSA protein SS-56 (SS-56), is an E3 ubiquitin-protein ligase that negatively regulates Toll-like receptor (TLR)- and RIG-I-like receptor (RLR)-driven type I interferon production by degrading TRK fused gene (TFG), a novel driver of IFN-beta downstream of anti-viral detection systems. It also functions as a cofactor for androgen receptor-mediated transcription through regulating ligand-dependent transcription of androgen receptor in prostate cancer cells. Moreover, TRIM68 is a cellular target of autoantibody responses in Sjogren"s syndrome (SS), as well as systemic lupus erythematosus (SLE). It is also an auto-antigen for T cells in SS and SLE. TRIM68 belongs the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, a B-box, and two coiled coil domains, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 319524 [Multi-domain]  Cd Length: 49  Bit Score: 39.14  E-value: 2.50e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 341898957 764 CTVCHEDFSHPIKLECNHIFCKSCIE-TW------LDQKSTCPMCR 802
Cdd:cd16610    4 CPICMTFLREPVSIDCGHSFCHSCLSgLWevpgesQNWGYTCPLCR 49
RING-H2_RNF111 cd16681
RING finger, H2 subclass, found in RING finger protein 111 (RNF111) and similar proteins; ...
763-804 2.58e-04

RING finger, H2 subclass, found in RING finger protein 111 (RNF111) and similar proteins; RNF111, also known as Arkadia, is a nuclear E3 ubiquitin-protein ligase that targets intracellular effectors and modulators of transforming growth factor beta (TGF-beta)/Nodal-related signaling for polyubiquitination and proteasome-dependent degradation. It acts as an amplifier of Nodal signals, and enhances the dorsalizing activity of limiting amounts of Xnr1, a Nodal homolog, and requires Nodal signaling for its function. The loss of RNF111 results in early embryonic lethality, with defects attributed to compromised Nodal signaling. Moreover, RNF111 regulates tumor metastasis by modulation of the TGF-beta pathway. Its ubiquitination can be modulated by the four and a half LIM-only protein 2 (FHL2) that activates TGF-beta signal transduction. Furthermore, RNF111 interacts with the clathrin-adaptor 2 (AP2) complex and regulates endocytosis of certain cell surface receptors, leading to modulation of epidermal growth factor (EGF) and possibly other signaling pathways. In addition, RNF111 has been identified as a small ubiquitin-like modifier (SUMO)-binding protein with clustered SUMO-interacting motifs (SIMs) that together form a SUMO-binding domain (SBD). It thus functions as a SUMO-targeted ubiquitin ligase (STUbL) that directly links nonproteolytic ubiquitylation and SUMOylation in the DNA damage response, as well as triggers degradation of signal-induced polysumoylated proteins, such as the promyelocytic leukemia protein (PML). The N-terminal half of RNF111 harbors three SIMs. Its C-terminal half show high sequence similarity with RING finger protein 165 (RNF165), where it contains two serine rich domains, two nuclear localization signals, a NRG-TIER domain, and a C-terminal C3H2C3-type RING-H2 finger that is required for polyubiqutination and proteasome-dependent degradation of phosphorylated forms of Smad2/3 and three major negative regulators of TGF-beta signaling, Smad7, SnoN and c-Ski.


Pssm-ID: 319595 [Multi-domain]  Cd Length: 46  Bit Score: 39.29  E-value: 2.58e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 341898957 763 QCTVCH---EDFSHPIKLECNHIFCKSCIETWLDQKSTCPMCRAE 804
Cdd:cd16681    2 KCTICLsilEEGEDVRRLPCMHLFHQVCVDQWLITNKKCPICRVD 46
RING-HC_RNF10 cd16536
RING finger, HC subclass, found in RING finger protein 10 (RNF10) and similar proteins; RNF10 ...
764-801 2.70e-04

RING finger, HC subclass, found in RING finger protein 10 (RNF10) and similar proteins; RNF10 is an E3 ubiquitin-protein ligase that interacts with mesenchyme Homeobox 2 (MEOX2) transcription factor, a regulator of the proliferation, differentiation and migration of vascular smooth muscle cells and cardiomyocytes, and enhances Meox2 activation of the p21 promoter. It also regulates the expression of myelin-associated glycoprotein (MAG) genes and is required for myelin production in Schwann cells of peripheral nervous system. Moreover, RNF10 regulates retinoic acid-induced neuronal differentiation and the cell cycle exit of P19 embryonic carcinoma cells. RNF10 contains a C3HC4-type RING-HC finger and three putative nuclear localization signals.


Pssm-ID: 319450 [Multi-domain]  Cd Length: 43  Bit Score: 39.08  E-value: 2.70e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 341898957 764 CTVCHEDFSHPIKLECNHIFCKSCIETWL----DQKSTCPMC 801
Cdd:cd16536    1 CPICLEPPVAPRITKCGHIFCWPCILHYLslseKAWRKCPIC 42
RING-H2_RNF24 cd16675
RING finger, H2 subclass, found in RING finger protein 24 (RNF24) and similar proteins; RNF24 ...
764-805 2.90e-04

RING finger, H2 subclass, found in RING finger protein 24 (RNF24) and similar proteins; RNF24 is an intrinsic membrane protein localized in the Golgi apparatus. It specifically interacts with the ankyrin-repeats domains (ARDs) of TRPC1, ?3, ?4, ?5, ?6, and ?7, and affects TRPC intracellular trafficking without affecting their activity. RNF24 contains an N-terminal transmembrane domain and a C-terminal C3H2C3-type RING-H2 finger.


Pssm-ID: 319589 [Multi-domain]  Cd Length: 47  Bit Score: 38.83  E-value: 2.90e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 341898957 764 CTVCHEDFSHPIKL---ECNHIFCKSCIETWLDQKSTCPMCRAEV 805
Cdd:cd16675    3 CAVCLEEFKPKDELgicPCKHAFHRKCLIKWL