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Conserved domains on  [gi|975830193|ref|NP_001305998|]
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integrin beta-1-binding protein 1 isoform 3 [Homo sapiens]

Protein Classification

PH domain-containing protein( domain architecture ID 106840)

Pleckstrin homology (PH) domain-containing protein may be involved in targeting a protein to the appropriate cellular location or interacting with a binding partner

CATH:  2.30.29.30
Gene Ontology:  GO:0005515
PubMed:  22728242|17233582|15493994

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 7-156 3.50e-118

Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins.


The actual alignment was detected with superfamily member pfam10480:

Pssm-ID: 473070  Cd Length: 200  Bit Score: 331.65  E-value: 3.50e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830193    7 GQSNNNSDTCAEFRIKYVGAIEKLKLSEGKGLEGPLDLINYIDVAQQDGKLPFVPPEEEFIMGVSKYGIKVSTSDQYDVL 86
Cdd:pfam10480  51 GQSNANSDACAEFRIKYVGAIEKLKFDEGKGLEEPLDLINYIDAAQQDGKLPFVPGDEEFILGVSKYGIKVASLDQCDVL 130

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830193   87 HRHALYLIIRMVCYDDGLGAGKSLLALKTTDASNEEYSLWVYQCNSLEQAQAICKVLSTAFDSVLTSEKP 156
Cdd:pfam10480 131 HRHALYLIIRMLCYDDGLGAGKNLLALKTTDAKNEECSIWVYQCNSAEHAQAICKVLSSAFDCALASEKP 200
 
Name Accession Description Interval E-value
ICAP-1_inte_bdg pfam10480
Beta-1 integrin binding protein; ICAP-1 is a serine/threonine-rich protein that binds to the ...
 7-156 3.50e-118

Beta-1 integrin binding protein; ICAP-1 is a serine/threonine-rich protein that binds to the cytoplasmic domains of beta-1 integrins in a highly specific manner, binding to a NPXY sequence motif on the beta-1 integrin. The cytoplasmic domains of integrins are essential for cell adhesion, and the fact that phosphorylation of ICAP-1 by interaction with the cell-matrix implies an important role of ICAP-1 during integrin-dependent cell adhesion. Overexpression of ICAP-1 strongly reduces the integrin-mediated cell spreading on extracellular matrix and inhibits both Cdc42 and Rac1. In addition, ICAP-1 induces release of Cdc42 from cellular membranes and prevents the dissociation of GDP from this GTPase. An additional function of ICAP-1 is to promote differentiation of osteoprogenitors by supporting their condensation through modulating the integrin high affinity state,


Pssm-ID: 119000  Cd Length: 200  Bit Score: 331.65  E-value: 3.50e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830193    7 GQSNNNSDTCAEFRIKYVGAIEKLKLSEGKGLEGPLDLINYIDVAQQDGKLPFVPPEEEFIMGVSKYGIKVSTSDQYDVL 86
Cdd:pfam10480  51 GQSNANSDACAEFRIKYVGAIEKLKFDEGKGLEEPLDLINYIDAAQQDGKLPFVPGDEEFILGVSKYGIKVASLDQCDVL 130

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830193   87 HRHALYLIIRMVCYDDGLGAGKSLLALKTTDASNEEYSLWVYQCNSLEQAQAICKVLSTAFDSVLTSEKP 156
Cdd:pfam10480 131 HRHALYLIIRMLCYDDGLGAGKNLLALKTTDAKNEECSIWVYQCNSAEHAQAICKVLSSAFDCALASEKP 200
PTB_ICAP1 cd13163
Integrin beta-1-binding protein 1 Phosphotyrosine-binding (PTB) PH-like fold; ICAP1 (also ...
 17-147 2.70e-82

Integrin beta-1-binding protein 1 Phosphotyrosine-binding (PTB) PH-like fold; ICAP1 (also called Integrin cytoplasmic domain-associated protein 1) binds specifically to the beta1 integrin subunit cytoplasmic domain and the cerebral cavernous malformation (CCM) protein CCM1. It regulates beta1 integrin-dependent cell migration by affecting the pattern of focal adhesion formation. ICAP1 recruits CCM1 to the cell membrane and activates CCM1 by changing its conformation. Since CCM1 plays role in cardiovascular development, it is hypothesized ICAP1 is involved in vascular differentiation. ICAP-1 has an N-terminal domain that rich in serine and threonine and a C-terminal PTB domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 269985  Cd Length: 129  Bit Score: 238.12  E-value: 2.70e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830193  17 AEFRIKYVGAIEKLKLSeGKGLEGPLDLINYIDVAQQDGKLPFVPPEEEFIMGVSKYGIKVSTSDQYDVLHRHALYLIIR 96
Cdd:cd13163    1 AEFRVKYVGVIENLEGL-SHSLEGPLDLINAIDVAQQDGKLPFVAIEEEVILGLSKYGIKVTELNQPVVLKRHPLYSIIR 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 975830193  97 MVCYDDGLGaGKSLLALKTTDASNEEYSLWVYQCNSLEQAQAICKVLSTAF 147
Cdd:cd13163   80 MVCYDDGLG-GKSLLAVKTGDPGEEVYSLLAYQCNSQEQAIEICKTLSTAF 129
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 14-156 5.33e-21

Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain structure similar to those of pleckstrin homology (PH) and IRS-1-like PTB domains.


Pssm-ID: 214675  Cd Length: 134  Bit Score: 82.75  E-value: 5.33e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830193    14 DTCAEFRIKYVGAIEklkLSEGKGLEGPLDLINYIDVAQqdgkLPFVPPEEEFIMGVSKYGIKVSTSDQYDVLHRHALYL 93
Cdd:smart00462   1 GSGVSFRVKYLGSVE---VPEARGLQVVQEAIRKLRAAQ----GSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRR 73

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 975830193    94 IIRMVCYDDGLgagkSLLALKTTDASNEEYSLWVYQCNSL--EQAQAICKVLSTAFDSVLTSEKP 156
Cdd:smart00462  74 ISFCAVGPDDL----DVFGYIARDPGSSRFACHVFRCEKAaeDIALAIGQAFQLAYELKLKARSE 134
 
Name Accession Description Interval E-value
ICAP-1_inte_bdg pfam10480
Beta-1 integrin binding protein; ICAP-1 is a serine/threonine-rich protein that binds to the ...
 7-156 3.50e-118

Beta-1 integrin binding protein; ICAP-1 is a serine/threonine-rich protein that binds to the cytoplasmic domains of beta-1 integrins in a highly specific manner, binding to a NPXY sequence motif on the beta-1 integrin. The cytoplasmic domains of integrins are essential for cell adhesion, and the fact that phosphorylation of ICAP-1 by interaction with the cell-matrix implies an important role of ICAP-1 during integrin-dependent cell adhesion. Overexpression of ICAP-1 strongly reduces the integrin-mediated cell spreading on extracellular matrix and inhibits both Cdc42 and Rac1. In addition, ICAP-1 induces release of Cdc42 from cellular membranes and prevents the dissociation of GDP from this GTPase. An additional function of ICAP-1 is to promote differentiation of osteoprogenitors by supporting their condensation through modulating the integrin high affinity state,


Pssm-ID: 119000  Cd Length: 200  Bit Score: 331.65  E-value: 3.50e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830193    7 GQSNNNSDTCAEFRIKYVGAIEKLKLSEGKGLEGPLDLINYIDVAQQDGKLPFVPPEEEFIMGVSKYGIKVSTSDQYDVL 86
Cdd:pfam10480  51 GQSNANSDACAEFRIKYVGAIEKLKFDEGKGLEEPLDLINYIDAAQQDGKLPFVPGDEEFILGVSKYGIKVASLDQCDVL 130

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830193   87 HRHALYLIIRMVCYDDGLGAGKSLLALKTTDASNEEYSLWVYQCNSLEQAQAICKVLSTAFDSVLTSEKP 156
Cdd:pfam10480 131 HRHALYLIIRMLCYDDGLGAGKNLLALKTTDAKNEECSIWVYQCNSAEHAQAICKVLSSAFDCALASEKP 200
PTB_ICAP1 cd13163
Integrin beta-1-binding protein 1 Phosphotyrosine-binding (PTB) PH-like fold; ICAP1 (also ...
 17-147 2.70e-82

Integrin beta-1-binding protein 1 Phosphotyrosine-binding (PTB) PH-like fold; ICAP1 (also called Integrin cytoplasmic domain-associated protein 1) binds specifically to the beta1 integrin subunit cytoplasmic domain and the cerebral cavernous malformation (CCM) protein CCM1. It regulates beta1 integrin-dependent cell migration by affecting the pattern of focal adhesion formation. ICAP1 recruits CCM1 to the cell membrane and activates CCM1 by changing its conformation. Since CCM1 plays role in cardiovascular development, it is hypothesized ICAP1 is involved in vascular differentiation. ICAP-1 has an N-terminal domain that rich in serine and threonine and a C-terminal PTB domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 269985  Cd Length: 129  Bit Score: 238.12  E-value: 2.70e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830193  17 AEFRIKYVGAIEKLKLSeGKGLEGPLDLINYIDVAQQDGKLPFVPPEEEFIMGVSKYGIKVSTSDQYDVLHRHALYLIIR 96
Cdd:cd13163    1 AEFRVKYVGVIENLEGL-SHSLEGPLDLINAIDVAQQDGKLPFVAIEEEVILGLSKYGIKVTELNQPVVLKRHPLYSIIR 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 975830193  97 MVCYDDGLGaGKSLLALKTTDASNEEYSLWVYQCNSLEQAQAICKVLSTAF 147
Cdd:cd13163   80 MVCYDDGLG-GKSLLAVKTGDPGEEVYSLLAYQCNSQEQAIEICKTLSTAF 129
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 14-156 5.33e-21

Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain structure similar to those of pleckstrin homology (PH) and IRS-1-like PTB domains.


Pssm-ID: 214675  Cd Length: 134  Bit Score: 82.75  E-value: 5.33e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830193    14 DTCAEFRIKYVGAIEklkLSEGKGLEGPLDLINYIDVAQqdgkLPFVPPEEEFIMGVSKYGIKVSTSDQYDVLHRHALYL 93
Cdd:smart00462   1 GSGVSFRVKYLGSVE---VPEARGLQVVQEAIRKLRAAQ----GSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRR 73

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 975830193    94 IIRMVCYDDGLgagkSLLALKTTDASNEEYSLWVYQCNSL--EQAQAICKVLSTAFDSVLTSEKP 156
Cdd:smart00462  74 ISFCAVGPDDL----DVFGYIARDPGSSRFACHVFRCEKAaeDIALAIGQAFQLAYELKLKARSE 134
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 17-147 4.05e-12

Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to bind peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains.


Pssm-ID: 269911  Cd Length: 120  Bit Score: 59.44  E-value: 4.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830193  17 AEFRIKYVGAIEKLKLSEGKGLEGPLDLINYIdVAQQDGKLPfvppeeEFIMGVSKYGIKVSTSDQYDVLHRHALYlIIR 96
Cdd:cd00934    1 ASFQVKYLGSVEVGSSRGVDVVEEALKALAAA-LKSSKRKPG------PVLLEVSSKGVKLLDLDTKELLLRHPLH-RIS 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 975830193  97 MVCYDDGlgaGKSLLALKTTDASNEEYSLWVYQCNSLEQAQAICKVLSTAF 147
Cdd:cd00934   73 YCGRDPD---NPNVFAFIAGEEGGSGFRCHVFQCEDEEEAEEILQAIGQAF 120
 
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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