NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|975830189|ref|NP_001305996|]
View 

integrin beta-1-binding protein 1 isoform 1 [Homo sapiens]

Protein Classification

integrin beta-1-binding protein 1( domain architecture ID 11187036)

integrin beta-1-binding protein 1 (ITGB1BP1) is a key regulator of the integrin-mediated cell-matrix interaction signaling by binding to the ITGB1 cytoplasmic tail and preventing the activation of integrin alpha-5/beta-1 (heterodimer of ITGA5 and ITGB1) by talin or FERMT1

Gene Symbol:  ITGB1BP1
Gene Ontology:  GO:0005515|GO:2001044|GO:0043087|GO:0019901|GO:0005092
PubMed:  15567406|8987385|10610414

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 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 ...
 1-200 2.09e-137

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: 382.12  E-value: 2.09e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830189    1 MFRKGKKRHSSSSSQSSEISTKSKSVDSSLGGLSRSSTVASLDTDSTKSSGQSNNNSDTCAEFRIKYVGAIEKLKLSEGK 80
Cdd:pfam10480   1 MFRKGKKRHSSSSSQSSEISTKSKSVDSSLGGLSRSSTVASLDTDSTKSSGQSNANSDACAEFRIKYVGAIEKLKFDEGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830189   81 GLEGPLDLINYIDVAQQDGKLPFVPPEEEFIMGVSKYGIKVSTSDQYDVLHRHALYLIIRMVCYDDGLGAGKSLLALKTT 160
Cdd:pfam10480  81 GLEEPLDLINYIDAAQQDGKLPFVPGDEEFILGVSKYGIKVASLDQCDVLHRHALYLIIRMLCYDDGLGAGKNLLALKTT 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 975830189  161 DASNEEYSLWVYQCNSLEQAQAICKVLSTAFDSVLTSEKP 200
Cdd:pfam10480 161 DAKNEECSIWVYQCNSAEHAQAICKVLSSAFDCALASEKP 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 ...
 1-200 2.09e-137

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: 382.12  E-value: 2.09e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830189    1 MFRKGKKRHSSSSSQSSEISTKSKSVDSSLGGLSRSSTVASLDTDSTKSSGQSNNNSDTCAEFRIKYVGAIEKLKLSEGK 80
Cdd:pfam10480   1 MFRKGKKRHSSSSSQSSEISTKSKSVDSSLGGLSRSSTVASLDTDSTKSSGQSNANSDACAEFRIKYVGAIEKLKFDEGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830189   81 GLEGPLDLINYIDVAQQDGKLPFVPPEEEFIMGVSKYGIKVSTSDQYDVLHRHALYLIIRMVCYDDGLGAGKSLLALKTT 160
Cdd:pfam10480  81 GLEEPLDLINYIDAAQQDGKLPFVPGDEEFILGVSKYGIKVASLDQCDVLHRHALYLIIRMLCYDDGLGAGKNLLALKTT 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 975830189  161 DASNEEYSLWVYQCNSLEQAQAICKVLSTAFDSVLTSEKP 200
Cdd:pfam10480 161 DAKNEECSIWVYQCNSAEHAQAICKVLSSAFDCALASEKP 200
PTB_ICAP1 cd13163
Integrin beta-1-binding protein 1 Phosphotyrosine-binding (PTB) PH-like fold; ICAP1 (also ...
 61-191 9.10e-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: 238.89  E-value: 9.10e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830189  61 AEFRIKYVGAIEKLKLSeGKGLEGPLDLINYIDVAQQDGKLPFVPPEEEFIMGVSKYGIKVSTSDQYDVLHRHALYLIIR 140
Cdd:cd13163    1 AEFRVKYVGVIENLEGL-SHSLEGPLDLINAIDVAQQDGKLPFVAIEEEVILGLSKYGIKVTELNQPVVLKRHPLYSIIR 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 975830189 141 MVCYDDGLGaGKSLLALKTTDASNEEYSLWVYQCNSLEQAQAICKVLSTAF 191
Cdd:cd13163   80 MVCYDDGLG-GKSLLAVKTGDPGEEVYSLLAYQCNSQEQAIEICKTLSTAF 129
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 58-200 5.15e-20

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: 81.59  E-value: 5.15e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830189    58 DTCAEFRIKYVGAIEklkLSEGKGLEGPLDLINYIDVAQqdgkLPFVPPEEEFIMGVSKYGIKVSTSDQYDVLHRHALYL 137
Cdd:smart00462   1 GSGVSFRVKYLGSVE---VPEARGLQVVQEAIRKLRAAQ----GSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRR 73

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 975830189   138 IIRMVCYDDGLgagkSLLALKTTDASNEEYSLWVYQCNSL--EQAQAICKVLSTAFDSVLTSEKP 200
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 ...
 1-200 2.09e-137

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: 382.12  E-value: 2.09e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830189    1 MFRKGKKRHSSSSSQSSEISTKSKSVDSSLGGLSRSSTVASLDTDSTKSSGQSNNNSDTCAEFRIKYVGAIEKLKLSEGK 80
Cdd:pfam10480   1 MFRKGKKRHSSSSSQSSEISTKSKSVDSSLGGLSRSSTVASLDTDSTKSSGQSNANSDACAEFRIKYVGAIEKLKFDEGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830189   81 GLEGPLDLINYIDVAQQDGKLPFVPPEEEFIMGVSKYGIKVSTSDQYDVLHRHALYLIIRMVCYDDGLGAGKSLLALKTT 160
Cdd:pfam10480  81 GLEEPLDLINYIDAAQQDGKLPFVPGDEEFILGVSKYGIKVASLDQCDVLHRHALYLIIRMLCYDDGLGAGKNLLALKTT 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 975830189  161 DASNEEYSLWVYQCNSLEQAQAICKVLSTAFDSVLTSEKP 200
Cdd:pfam10480 161 DAKNEECSIWVYQCNSAEHAQAICKVLSSAFDCALASEKP 200
PTB_ICAP1 cd13163
Integrin beta-1-binding protein 1 Phosphotyrosine-binding (PTB) PH-like fold; ICAP1 (also ...
 61-191 9.10e-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: 238.89  E-value: 9.10e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830189  61 AEFRIKYVGAIEKLKLSeGKGLEGPLDLINYIDVAQQDGKLPFVPPEEEFIMGVSKYGIKVSTSDQYDVLHRHALYLIIR 140
Cdd:cd13163    1 AEFRVKYVGVIENLEGL-SHSLEGPLDLINAIDVAQQDGKLPFVAIEEEVILGLSKYGIKVTELNQPVVLKRHPLYSIIR 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 975830189 141 MVCYDDGLGaGKSLLALKTTDASNEEYSLWVYQCNSLEQAQAICKVLSTAF 191
Cdd:cd13163   80 MVCYDDGLG-GKSLLAVKTGDPGEEVYSLLAYQCNSQEQAIEICKTLSTAF 129
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 58-200 5.15e-20

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: 81.59  E-value: 5.15e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830189    58 DTCAEFRIKYVGAIEklkLSEGKGLEGPLDLINYIDVAQqdgkLPFVPPEEEFIMGVSKYGIKVSTSDQYDVLHRHALYL 137
Cdd:smart00462   1 GSGVSFRVKYLGSVE---VPEARGLQVVQEAIRKLRAAQ----GSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRR 73

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 975830189   138 IIRMVCYDDGLgagkSLLALKTTDASNEEYSLWVYQCNSL--EQAQAICKVLSTAFDSVLTSEKP 200
Cdd:smart00462  74 ISFCAVGPDDL----DVFGYIARDPGSSRFACHVFRCEKAaeDIALAIGQAFQLAYELKLKARSE 134
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 61-191 1.67e-11

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: 59.06  E-value: 1.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830189  61 AEFRIKYVGAIEKLKLSEGKGLEGPLDLINYIdVAQQDGKLPfvppeeEFIMGVSKYGIKVSTSDQYDVLHRHALYlIIR 140
Cdd:cd00934    1 ASFQVKYLGSVEVGSSRGVDVVEEALKALAAA-LKSSKRKPG------PVLLEVSSKGVKLLDLDTKELLLRHPLH-RIS 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 975830189 141 MVCYDDGlgaGKSLLALKTTDASNEEYSLWVYQCNSLEQAQAICKVLSTAF 191
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH