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Conserved domains on  [gi|1034675132|ref|XP_016885275|]
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actin nucleation-promoting factor WAS isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WH1 pfam00568
WH1 domain; WASp Homology domain 1 (WH1) domain. WASP is the protein that is defective in ...
 36-145 8.43e-54

WH1 domain; WASp Homology domain 1 (WH1) domain. WASP is the protein that is defective in Wiskott-Aldrich syndrome (WAS). The majority of point mutations occur within the amino- terminal WH1 domain. The metabotropic glutamate receptors mGluR1alpha and mGluR5 bind a protein called homer, which is a WH1 domain homolog. A subset of WH1 domains has been termed a "EVH1" domain and appear to bind a polyproline motif.


:

Pssm-ID: 395450  Cd Length: 111  Bit Score: 178.41  E-value: 8.43e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034675132  36 FEMLGRKCLTLATAVVQLYLALPPGAEHWTK-EHCGAVCFVKDNPQKSYFIRLYGLQAGRLLWEQELYSQLVYSTPTPFF 114
Cdd:pfam00568   1 FSALGKKCQTICTAVAQVYLADPDNKRHWIKaKHSGVVCFVKDSPQNSYFIRLVDIQDGKVIWNQEIYPNMEYNQARPFF 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1034675132 115 HTFAGDDCQAGLNFADEDEAQAFRALVQEKI 145
Cdd:pfam00568  81 HTFADSRCVYGLNFASEEEATKFAKAVQEAL 111
PBD pfam00786
P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also ...
 237-294 5.03e-16

P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also known as the Cdc42/Rac interactive binding (CRIB).


:

Pssm-ID: 395634  Cd Length: 59  Bit Score: 72.34  E-value: 5.03e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034675132 237 DIGAPSGFKHVSHVGWDPQNGFDVnNLDPDLRSLFSRAGISEAQLTDAETSKLIYDFI 294
Cdd:pfam00786   1 MISAPTNFKHTVHVGFDPDTGFFT-GLPPEWAKLLDSSGITEDEQKENPKAVLDVLKF 57
WH2 super family cl41728
Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif), and similar proteins; This ...
 434-448 9.18e-03

Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif), and similar proteins; This family contains the Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) as well as thymosin-beta (Tbeta; also called beta-thymosin or betaT) domains that are small, widespread intrinsically disordered actin-binding peptides displaying significant sequence variability and different regulations of actin self-assembly in motile and morphogenetic processes. These WH2/betaT peptides are identified by a central consensus actin-binding motif LKKT/V flanked by variable N-terminal and C-terminal extensions; the betaT shares a more extended and conserved C-terminal half than WH2. These single or repeated domains are found in actin-binding proteins (ABPs) such as the hematopoietic-specific protein WASP, its ubiquitously expressed ortholog neural-WASP (N-WASP), WASP-interacting protein (WAS/WASL-interacting protein family members 1 and 2), and WASP-family verprolin homologous protein (WAVE/SCAR) isoforms: WAVE1, WAVE2, and WAVE3. Also included are the WH2 domains found in inverted formin FH2 domain-containing protein (INF2), Cordon bleu (Cobl) protein, vasodilator-stimulated phosphoprotein (VASP) homology protein and actobindin (found in amoebae). These ABPs are commonly multidomain proteins that contain signaling domains and structurally conserved actin-binding motifs, the most important being the WH2 domain motif through which they bind actin in order to direct the location, rate, and timing for actin assembly in the cell into different structures, such as filopodia, lamellipodia, stress fibers, and focal adhesions. The WH2 domain motif is one of the most abundant actin-binding motifs in Wiskott-Aldrich syndrome proteins (WASPs) where they activate Arp2/3-dependent actin nucleation and branching in response to signals mediated by Rho-family GTPases. The thymosin beta (Tbeta) domains in metazoans act in cells as major actin-sequestering peptides; their complex with monomeric ATP-actin (G-ATP-actin) cannot polymerize at either filament (F-actin) end.


The actual alignment was detected with superfamily member cd22075:

Pssm-ID: 425359  Cd Length: 25  Bit Score: 33.97  E-value: 9.18e-03
                          10
                  ....*....|....*
gi 1034675132 434 LLDQIRQGIQLNKTP 448
Cdd:cd22075     9 LLDQIRQGIQLKSVP 23
 
Name Accession Description Interval E-value
WH1 pfam00568
WH1 domain; WASp Homology domain 1 (WH1) domain. WASP is the protein that is defective in ...
 36-145 8.43e-54

WH1 domain; WASp Homology domain 1 (WH1) domain. WASP is the protein that is defective in Wiskott-Aldrich syndrome (WAS). The majority of point mutations occur within the amino- terminal WH1 domain. The metabotropic glutamate receptors mGluR1alpha and mGluR5 bind a protein called homer, which is a WH1 domain homolog. A subset of WH1 domains has been termed a "EVH1" domain and appear to bind a polyproline motif.


Pssm-ID: 395450  Cd Length: 111  Bit Score: 178.41  E-value: 8.43e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034675132  36 FEMLGRKCLTLATAVVQLYLALPPGAEHWTK-EHCGAVCFVKDNPQKSYFIRLYGLQAGRLLWEQELYSQLVYSTPTPFF 114
Cdd:pfam00568   1 FSALGKKCQTICTAVAQVYLADPDNKRHWIKaKHSGVVCFVKDSPQNSYFIRLVDIQDGKVIWNQEIYPNMEYNQARPFF 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1034675132 115 HTFAGDDCQAGLNFADEDEAQAFRALVQEKI 145
Cdd:pfam00568  81 HTFADSRCVYGLNFASEEEATKFAKAVQEAL 111
EVH1_WASP-like cd01205
WASP family proteins EVH1 domain; The Wiskott-Aldrich Syndrome Protein (WASP; also called ...
 45-145 2.79e-51

WASP family proteins EVH1 domain; The Wiskott-Aldrich Syndrome Protein (WASP; also called Bee1p) and its homolog N (neuronal)-WASP are signal transduction proteins that promote actin polymerization in response to upstream intracellular signals. WAS is an X-linked recessive disease, characterized by eczema, immunodeficiency, and thrombocytopenia. The majority of patients with WAS, or a milder version of the disorder, X-linked thrombocytopenia (XLT), have point mutations in the EVH1 domain of WASP. WASP is an actin regulatory protein consisting of an N-terminal EVH1 domain called WH1 which binds LPPPEP peptides, a basic region (B), a GTP binding domain (GBP), a proline rich region, a WH2 domain, and a verprolin-cofilin-acidic motif (VCA) which activates the actin-related protein (Arp)2/3 actin nucleating complex. The B, GBD, and the proline-rich region are involved in autoinhibitory interactions that repress or block the activity of the VCA. Yeast members lack the GTP binding domain. The EVH1 domains are part of the PH domain superamily. There are 5 EVH1 subfamilies: Enables/VASP, Homer/Vesl, WASP, Dcp1, and Spred. Ligands are known for three of the EVH1 subfamilies, all of which bind proline-rich sequences: the Enabled/VASP family binds to FPPPP peptides, the Homer/Vesl family binds PPxxF peptides, and the WASP family binds LPPPEP peptides. EVH1 has a PH-like fold, despite having minimal sequence similarity to PH or PTB domains.


Pssm-ID: 269916  Cd Length: 101  Bit Score: 171.17  E-value: 2.79e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034675132  45 TLATAVVQLYLALPPgAEHWTK-EHCGAVCFVKDNPQKSYFIRLYGLQAGRLLWEQELYSQLVYSTPTPFFHTFAGDDCQ 123
Cdd:cd01205     1 ILAAAVARLYYAEPD-PDSWSYtGLTGALCFVKDNAKRSYFFRLVDLKTRGVVWEQELYEGFEYNQDRPFFHTFEGDECM 79

                          90       100
                  ....*....|....*....|..
gi 1034675132 124 AGLNFADEDEAQAFRALVQEKI 145
Cdd:cd01205    80 IGLNFADEDEAAAFYKKVQEKL 101
WH1 smart00461
WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains ...
 39-145 5.97e-38

WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains point mutations in the majority of patients with WAS. Unknown function. Ena-like WH1 domains bind polyproline-containing peptides, and that Homer contains a WH1 domain.


Pssm-ID: 214674  Cd Length: 106  Bit Score: 135.56  E-value: 5.97e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034675132   39 LGRKCLTLATAVVQLYLALPPGaehWTKEHCG-AVCFVKDNPQKSYFIRLYGLQAG-RLLWEQELYSQLVYSTPTPFFHT 116
Cdd:smart00461   1 LGSQCIILARAVVQLYDADTKK---WVPTGEGgAANLVIDKNQRSYFFRIVGIKGQdKVIWNQELYKNFKYNQATPTFHQ 77

                           90       100
                   ....*....|....*....|....*....
gi 1034675132  117 FAGDDCQAGLNFADEDEAQAFRALVQEKI 145
Cdd:smart00461  78 WADDKCVYGLNFASEEEAKKFRKKVLKAL 106
PBD pfam00786
P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also ...
 237-294 5.03e-16

P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also known as the Cdc42/Rac interactive binding (CRIB).


Pssm-ID: 395634  Cd Length: 59  Bit Score: 72.34  E-value: 5.03e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034675132 237 DIGAPSGFKHVSHVGWDPQNGFDVnNLDPDLRSLFSRAGISEAQLTDAETSKLIYDFI 294
Cdd:pfam00786   1 MISAPTNFKHTVHVGFDPDTGFFT-GLPPEWAKLLDSSGITEDEQKENPKAVLDVLKF 57
CRIB cd00132
PAK (p21 activated kinase) Binding Domain (PBD), binds Cdc42p- and/or Rho-like small GTPases; ...
 236-278 8.81e-14

PAK (p21 activated kinase) Binding Domain (PBD), binds Cdc42p- and/or Rho-like small GTPases; also known as the Cdc42/Rac interactive binding (CRIB) motif; has been shown to inhibit transcriptional activation and cell transformation mediated by the Ras-Rac pathway. CRIB-containing effector proteins are functionally diverse and include serine/threonine kinases, tyrosine kinases, actin-binding proteins, and adapter molecules.


Pssm-ID: 238077  Cd Length: 42  Bit Score: 65.54  E-value: 8.81e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1034675132 236 ADIGAPSGFKHVSHVGWDPQnGFDVNNLDPDLRSLFSRAGISE 278
Cdd:cd00132     1 MEISTPTDFKHISHVGWDGV-GFDGANLPPDLQSLFQTAGISA 42
PBD smart00285
P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also ...
 238-273 9.69e-08

P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also known as the Cdc42/Rac interactive binding (CRIB).


Pssm-ID: 197628  Cd Length: 36  Bit Score: 48.36  E-value: 9.69e-08
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1034675132  238 IGAPSGFKHVSHVGWDPQNGfDVNNLDPDLRSLFSR 273
Cdd:smart00285   1 ISTPTNFKHIAHVGFDGQTG-GFTGLPTEWKSLLKT 35
WH2_hN-WASP_r2_like cd22075
second tandem Wiskott Aldrich syndrome homology region 2 (WH2 motif) repeat found in human ...
 434-448 9.18e-03

second tandem Wiskott Aldrich syndrome homology region 2 (WH2 motif) repeat found in human Neural Wiskott-Aldrich syndrome protein (N-WASP) and related domains; This subfamily includes the second tandem Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) found in human Neural Wiskott-Aldrich syndrome protein (N-WASP or Neural WASP). N-WASP integrates various extracellular signals to control actin dynamics and cytoskeletal reorganization through activation of the actin related protein (Arp)2/3 complex. It interacts with actin via the WH2 domain. N-WASP plays an important role in the deactivation or attenuation of B cell receptor signaling. N-WASP regulates filopodia formation and membrane invagination, as compared to WAVE proteins that serve as Rac1 effectors in the formation of lamellipodia. Filopodia are thin, actin-rich surface projections that are extended and maintained by N-WASP together with CDC42. N-WASP also plays a role in the nucleus by regulating gene transcription, probably by promoting nuclear actin polymerization. It binds to HSF1/HSTF1 and forms a complex on heat shock promoter elements (HSE) that negatively regulates HSP90 expression. It also plays a role in dendrite spine morphogenesis. Unphosphorylated N-WASP is preferentially localized in the nucleus and in the cytoplasm when phosphorylated; it is exported from the nucleus by a nuclear export signal (NES)-dependent mechanism to the cytoplasm. This subfamily includes both tandem WH2 domains of mouse N-WASP.


Pssm-ID: 409218  Cd Length: 25  Bit Score: 33.97  E-value: 9.18e-03
                          10
                  ....*....|....*
gi 1034675132 434 LLDQIRQGIQLNKTP 448
Cdd:cd22075     9 LLDQIRQGIQLKSVP 23
 
Name Accession Description Interval E-value
WH1 pfam00568
WH1 domain; WASp Homology domain 1 (WH1) domain. WASP is the protein that is defective in ...
 36-145 8.43e-54

WH1 domain; WASp Homology domain 1 (WH1) domain. WASP is the protein that is defective in Wiskott-Aldrich syndrome (WAS). The majority of point mutations occur within the amino- terminal WH1 domain. The metabotropic glutamate receptors mGluR1alpha and mGluR5 bind a protein called homer, which is a WH1 domain homolog. A subset of WH1 domains has been termed a "EVH1" domain and appear to bind a polyproline motif.


Pssm-ID: 395450  Cd Length: 111  Bit Score: 178.41  E-value: 8.43e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034675132  36 FEMLGRKCLTLATAVVQLYLALPPGAEHWTK-EHCGAVCFVKDNPQKSYFIRLYGLQAGRLLWEQELYSQLVYSTPTPFF 114
Cdd:pfam00568   1 FSALGKKCQTICTAVAQVYLADPDNKRHWIKaKHSGVVCFVKDSPQNSYFIRLVDIQDGKVIWNQEIYPNMEYNQARPFF 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1034675132 115 HTFAGDDCQAGLNFADEDEAQAFRALVQEKI 145
Cdd:pfam00568  81 HTFADSRCVYGLNFASEEEATKFAKAVQEAL 111
EVH1_WASP-like cd01205
WASP family proteins EVH1 domain; The Wiskott-Aldrich Syndrome Protein (WASP; also called ...
 45-145 2.79e-51

WASP family proteins EVH1 domain; The Wiskott-Aldrich Syndrome Protein (WASP; also called Bee1p) and its homolog N (neuronal)-WASP are signal transduction proteins that promote actin polymerization in response to upstream intracellular signals. WAS is an X-linked recessive disease, characterized by eczema, immunodeficiency, and thrombocytopenia. The majority of patients with WAS, or a milder version of the disorder, X-linked thrombocytopenia (XLT), have point mutations in the EVH1 domain of WASP. WASP is an actin regulatory protein consisting of an N-terminal EVH1 domain called WH1 which binds LPPPEP peptides, a basic region (B), a GTP binding domain (GBP), a proline rich region, a WH2 domain, and a verprolin-cofilin-acidic motif (VCA) which activates the actin-related protein (Arp)2/3 actin nucleating complex. The B, GBD, and the proline-rich region are involved in autoinhibitory interactions that repress or block the activity of the VCA. Yeast members lack the GTP binding domain. The EVH1 domains are part of the PH domain superamily. There are 5 EVH1 subfamilies: Enables/VASP, Homer/Vesl, WASP, Dcp1, and Spred. Ligands are known for three of the EVH1 subfamilies, all of which bind proline-rich sequences: the Enabled/VASP family binds to FPPPP peptides, the Homer/Vesl family binds PPxxF peptides, and the WASP family binds LPPPEP peptides. EVH1 has a PH-like fold, despite having minimal sequence similarity to PH or PTB domains.


Pssm-ID: 269916  Cd Length: 101  Bit Score: 171.17  E-value: 2.79e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034675132  45 TLATAVVQLYLALPPgAEHWTK-EHCGAVCFVKDNPQKSYFIRLYGLQAGRLLWEQELYSQLVYSTPTPFFHTFAGDDCQ 123
Cdd:cd01205     1 ILAAAVARLYYAEPD-PDSWSYtGLTGALCFVKDNAKRSYFFRLVDLKTRGVVWEQELYEGFEYNQDRPFFHTFEGDECM 79

                          90       100
                  ....*....|....*....|..
gi 1034675132 124 AGLNFADEDEAQAFRALVQEKI 145
Cdd:cd01205    80 IGLNFADEDEAAAFYKKVQEKL 101
WH1 smart00461
WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains ...
 39-145 5.97e-38

WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains point mutations in the majority of patients with WAS. Unknown function. Ena-like WH1 domains bind polyproline-containing peptides, and that Homer contains a WH1 domain.


Pssm-ID: 214674  Cd Length: 106  Bit Score: 135.56  E-value: 5.97e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034675132   39 LGRKCLTLATAVVQLYLALPPGaehWTKEHCG-AVCFVKDNPQKSYFIRLYGLQAG-RLLWEQELYSQLVYSTPTPFFHT 116
Cdd:smart00461   1 LGSQCIILARAVVQLYDADTKK---WVPTGEGgAANLVIDKNQRSYFFRIVGIKGQdKVIWNQELYKNFKYNQATPTFHQ 77

                           90       100
                   ....*....|....*....|....*....
gi 1034675132  117 FAGDDCQAGLNFADEDEAQAFRALVQEKI 145
Cdd:smart00461  78 WADDKCVYGLNFASEEEAKKFRKKVLKAL 106
EVH1_family cd00837
EVH1 (Drosophila Enabled (Ena)/Vasodilator-stimulated phosphoprotein (VASP) homology 1) domain; ...
 45-145 4.76e-22

EVH1 (Drosophila Enabled (Ena)/Vasodilator-stimulated phosphoprotein (VASP) homology 1) domain; The EVH1 domains are part of the PH domain superfamily. EVH1 subfamilies include Enables/VASP, Homer/Vesl, WASP, and Spred. Ligands are known for three of the EVH1 subfamilies, all of which bind proline-rich sequences: the Enabled/VASP family binds to FPPPP peptides, the Homer/Vesl family binds PPxxF peptides, and the WASP family binds LPPPEP peptides. EVH1 has a PH-like fold, despite having minimal sequence similarity to PH or PTB domains.


Pssm-ID: 269909  Cd Length: 103  Bit Score: 90.98  E-value: 4.76e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034675132  45 TLATAVVQLYlALPPGAEHWTK---EHCGAVCFVKDNPQKSYFIRLYGLQAGRLLWEQELYSQLVYSTPTPFFHTFAGDD 121
Cdd:cd00837     1 SIFSARAHVM-QIDDSNKNWVPaggKGASRVSYFKDTTRNSFRIIGVDIKDKKVVINCTITKNLVYNKATQTFHQWADDR 79

                          90       100
                  ....*....|....*....|....
gi 1034675132 122 CQAGLNFADEDEAQAFRALVQEKI 145
Cdd:cd00837    80 TVFGLNFASEEDATKFAEAVQEAL 103
PBD pfam00786
P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also ...
 237-294 5.03e-16

P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also known as the Cdc42/Rac interactive binding (CRIB).


Pssm-ID: 395634  Cd Length: 59  Bit Score: 72.34  E-value: 5.03e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034675132 237 DIGAPSGFKHVSHVGWDPQNGFDVnNLDPDLRSLFSRAGISEAQLTDAETSKLIYDFI 294
Cdd:pfam00786   1 MISAPTNFKHTVHVGFDPDTGFFT-GLPPEWAKLLDSSGITEDEQKENPKAVLDVLKF 57
CRIB cd00132
PAK (p21 activated kinase) Binding Domain (PBD), binds Cdc42p- and/or Rho-like small GTPases; ...
 236-278 8.81e-14

PAK (p21 activated kinase) Binding Domain (PBD), binds Cdc42p- and/or Rho-like small GTPases; also known as the Cdc42/Rac interactive binding (CRIB) motif; has been shown to inhibit transcriptional activation and cell transformation mediated by the Ras-Rac pathway. CRIB-containing effector proteins are functionally diverse and include serine/threonine kinases, tyrosine kinases, actin-binding proteins, and adapter molecules.


Pssm-ID: 238077  Cd Length: 42  Bit Score: 65.54  E-value: 8.81e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1034675132 236 ADIGAPSGFKHVSHVGWDPQnGFDVNNLDPDLRSLFSRAGISE 278
Cdd:cd00132     1 MEISTPTDFKHISHVGWDGV-GFDGANLPPDLQSLFQTAGISA 42
PBD smart00285
P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also ...
 238-273 9.69e-08

P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also known as the Cdc42/Rac interactive binding (CRIB).


Pssm-ID: 197628  Cd Length: 36  Bit Score: 48.36  E-value: 9.69e-08
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1034675132  238 IGAPSGFKHVSHVGWDPQNGfDVNNLDPDLRSLFSR 273
Cdd:smart00285   1 ISTPTNFKHIAHVGFDGQTG-GFTGLPTEWKSLLKT 35
CRIB_PAK_like cd01093
PAK (p21 activated kinase) Binding Domain (PBD), binds Cdc42p- and/or Rho-like small GTPases; ...
 238-257 1.14e-04

PAK (p21 activated kinase) Binding Domain (PBD), binds Cdc42p- and/or Rho-like small GTPases; also known as the Cdc42/Rac interactive binding (CRIB) motif; has been shown to inhibit transcriptional activation and cell transformation mediated by the Ras-Rac pathway. This subgroup of CRIB/PBD-domains is found N-terminal of Serine/Threonine kinase domains in PAK and PAK-like proteins.


Pssm-ID: 238526  Cd Length: 46  Bit Score: 39.95  E-value: 1.14e-04
                          10        20
                  ....*....|....*....|
gi 1034675132 238 IGAPSGFKHVSHVGWDPQNG 257
Cdd:cd01093     3 ISSPTNFKHRVHVGFDPQTG 22
WH2_hN-WASP_r2_like cd22075
second tandem Wiskott Aldrich syndrome homology region 2 (WH2 motif) repeat found in human ...
 434-448 9.18e-03

second tandem Wiskott Aldrich syndrome homology region 2 (WH2 motif) repeat found in human Neural Wiskott-Aldrich syndrome protein (N-WASP) and related domains; This subfamily includes the second tandem Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) found in human Neural Wiskott-Aldrich syndrome protein (N-WASP or Neural WASP). N-WASP integrates various extracellular signals to control actin dynamics and cytoskeletal reorganization through activation of the actin related protein (Arp)2/3 complex. It interacts with actin via the WH2 domain. N-WASP plays an important role in the deactivation or attenuation of B cell receptor signaling. N-WASP regulates filopodia formation and membrane invagination, as compared to WAVE proteins that serve as Rac1 effectors in the formation of lamellipodia. Filopodia are thin, actin-rich surface projections that are extended and maintained by N-WASP together with CDC42. N-WASP also plays a role in the nucleus by regulating gene transcription, probably by promoting nuclear actin polymerization. It binds to HSF1/HSTF1 and forms a complex on heat shock promoter elements (HSE) that negatively regulates HSP90 expression. It also plays a role in dendrite spine morphogenesis. Unphosphorylated N-WASP is preferentially localized in the nucleus and in the cytoplasm when phosphorylated; it is exported from the nucleus by a nuclear export signal (NES)-dependent mechanism to the cytoplasm. This subfamily includes both tandem WH2 domains of mouse N-WASP.


Pssm-ID: 409218  Cd Length: 25  Bit Score: 33.97  E-value: 9.18e-03
                          10
                  ....*....|....*
gi 1034675132 434 LLDQIRQGIQLNKTP 448
Cdd:cd22075     9 LLDQIRQGIQLKSVP 23
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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