ITBP1_HUMAN
ID ITBP1_HUMAN Reviewed; 200 AA.
AC O14713; D6W4Y9; O14714; Q53RS0;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Integrin beta-1-binding protein 1;
DE AltName: Full=Integrin cytoplasmic domain-associated protein 1;
DE Short=ICAP-1;
GN Name=ITGB1BP1; Synonyms=ICAP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), INTERACTION WITH ITGB1,
RP PHOSPHORYLATION, AND TISSUE SPECIFICITY.
RC TISSUE=Cervix carcinoma;
RX PubMed=9281591; DOI=10.1083/jcb.138.5.1149;
RA Chang D.D., Wong C., Smith H., Liu J.;
RT "ICAP-1, a novel beta1 integrin cytoplasmic domain-associated protein,
RT binds to a conserved and functionally important NPXY sequence motif of
RT beta1 integrin.";
RL J. Cell Biol. 138:1149-1157(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH ITGB1,
RP PHOSPHORYLATION, AND TISSUE SPECIFICITY.
RX PubMed=9867804; DOI=10.1074/jbc.274.1.11;
RA Zhang X.A., Hemler M.E.;
RT "Interaction of the integrin beta1 cytoplasmic domain with ICAP-1
RT protein.";
RL J. Biol. Chem. 274:11-19(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PHOSPHORYLATION AT THR-38, AND MUTAGENESIS OF THR-38.
RX PubMed=9813144; DOI=10.1006/bbrc.1998.9592;
RA Bouvard D., Block M.R.;
RT "Calcium/calmodulin-dependent protein kinase II controls integrin
RT alpha5beta1-mediated cell adhesion through the integrin cytoplasmic domain
RT associated protein-1alpha.";
RL Biochem. Biophys. Res. Commun. 252:46-50(1998).
RN [7]
RP FUNCTION, AND INTERACTION WITH ITGB1 AND KRIT1.
RX PubMed=11741838; DOI=10.1093/hmg/10.25.2953;
RA Zhang J., Clatterbuck R.E., Rigamonti D., Chang D.D., Dietz H.C.;
RT "Interaction between krit1 and icap1alpha infers perturbation of integrin
RT beta1-mediated angiogenesis in the pathogenesis of cerebral cavernous
RT malformation.";
RL Hum. Mol. Genet. 10:2953-2960(2001).
RN [8]
RP INTERACTION WITH KRIT1.
RX PubMed=11854171; DOI=10.1093/hmg/11.4.389;
RA Zawistowski J.S., Serebriiskii I.G., Lee M.F., Golemis E.A., Marchuk D.A.;
RT "KRIT1 association with the integrin-binding protein ICAP-1: a new
RT direction in the elucidation of cerebral cavernous malformations (CCM1)
RT pathogenesis.";
RL Hum. Mol. Genet. 11:389-396(2002).
RN [9]
RP INTERACTION WITH ITGB1, MUTAGENESIS OF THR-38; LEU-82; LEU-86; LEU-135;
RP ILE-138; ILE-139 AND TYR-144, AND 3D-STRUCTURE MODELING.
RX PubMed=11741908; DOI=10.1074/jbc.m109031200;
RA Chang D.D., Hoang B.Q., Liu J., Springer T.A.;
RT "Molecular basis for interaction between Icap1alpha PTB domain and beta 1
RT integrin.";
RL J. Biol. Chem. 277:8140-8145(2002).
RN [10]
RP FUNCTION, INTERACTION WITH NME2, AND SUBCELLULAR LOCATION.
RX PubMed=11919189; DOI=10.1074/jbc.m200200200;
RA Fournier H.N., Dupe-Manet S., Bouvard D., Lacombe M.L., Marie C.,
RA Block M.R., Albiges-Rizo C.;
RT "Integrin cytoplasmic domain-associated protein 1alpha (ICAP-1alpha)
RT interacts directly with the metastasis suppressor nm23-H2, and both
RT proteins are targeted to newly formed cell adhesion sites upon integrin
RT engagement.";
RL J. Biol. Chem. 277:20895-20902(2002).
RN [11]
RP FUNCTION, AND INTERACTION WITH CDC42; ITGB1 AND RAC1.
RX PubMed=11807099; DOI=10.1083/jcb.200108030;
RA Degani S., Balzac F., Brancaccio M., Guazzone S., Retta S.F., Silengo L.,
RA Eva A., Tarone G.;
RT "The integrin cytoplasmic domain-associated protein ICAP-1 binds and
RT regulates Rho family GTPases during cell spreading.";
RL J. Cell Biol. 156:377-387(2002).
RN [12]
RP FUNCTION, INTERACTION WITH ITGB1, AND SUBCELLULAR LOCATION.
RX PubMed=12473654; DOI=10.1074/jbc.m211258200;
RA Bouvard D., Vignoud L., Dupe-Manet S., Abed N., Fournier H.N.,
RA Vincent-Monegat C., Retta S.F., Fassler R., Block M.R.;
RT "Disruption of focal adhesions by integrin cytoplasmic domain-associated
RT protein-1 alpha.";
RL J. Biol. Chem. 278:6567-6574(2003).
RN [13]
RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA Hillman R.T., Green R.E., Brenner S.E.;
RT "An unappreciated role for RNA surveillance.";
RL Genome Biol. 5:R8.1-R8.16(2004).
RN [14]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 6-LYS-LYS-7 AND ILE-138.
RX PubMed=15703214; DOI=10.1091/mbc.e04-08-0744;
RA Fournier H.N., Dupe-Manet S., Bouvard D., Luton F., Degani S., Block M.R.,
RA Retta S.F., Albiges-Rizo C.;
RT "Nuclear translocation of integrin cytoplasmic domain-associated protein 1
RT stimulates cellular proliferation.";
RL Mol. Biol. Cell 16:1859-1871(2005).
RN [15]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH KRIT1 AND RAP1A, AND INTERACTION
RP WITH KRIT1.
RX PubMed=17916086; DOI=10.1111/j.1742-4658.2007.06068.x;
RA Beraud-Dufour S., Gautier R., Albiges-Rizo C., Chardin P., Faurobert E.;
RT "Krit 1 interactions with microtubules and membranes are regulated by Rap1
RT and integrin cytoplasmic domain associated protein-1.";
RL FEBS J. 274:5518-5532(2007).
RN [16]
RP FUNCTION.
RX PubMed=20616313; DOI=10.1161/circresaha.110.217257;
RA Brutsch R., Liebler S.S., Wustehube J., Bartol A., Herberich S.E.,
RA Adam M.G., Telzerow A., Augustin H.G., Fischer A.;
RT "Integrin cytoplasmic domain-associated protein-1 attenuates sprouting
RT angiogenesis.";
RL Circ. Res. 107:592-601(2010).
RN [17]
RP FUNCTION, AND INTERACTION WITH ITGB1 AND FERMT2.
RX PubMed=21768292; DOI=10.1083/jcb.201007108;
RA Brunner M., Millon-Fremillon A., Chevalier G., Nakchbandi I.A., Mosher D.,
RA Block M.R., Albiges-Rizo C., Bouvard D.;
RT "Osteoblast mineralization requires beta1 integrin/ICAP-1-dependent
RT fibronectin deposition.";
RL J. Cell Biol. 194:307-322(2011).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.54 ANGSTROMS) OF 49-200 IN COMPLEXES WITH KRIT1
RP AND ITGB1, FUNCTION, INTERACTION WITH KRIT1 AND ITGB1, AND MUTAGENESIS OF
RP ILE-89; ASP-93; GLN-96; 135-LEU--ILE-139 AND CYS-184.
RX DOI=10.1016/j.molcel.2012.12.005;
RA Liu W., Draheim K.M., Zhang R., Calderwood D.A., Boggon T.J.;
RT "Mechanism for KRIT1 release of ICAP1-mediated suppression of integrin
RT activation.";
RL Mol. Cell 0:0-0(2013).
CC -!- FUNCTION: Key regulator of the integrin-mediated cell-matrix
CC interaction signaling by binding to the ITGB1 cytoplasmic tail and
CC preventing the activation of integrin alpha-5/beta-1 (heterodimer of
CC ITGA5 and ITGB1) by talin or FERMT1. Plays a role in cell
CC proliferation, differentiation, spreading, adhesion and migration in
CC the context of mineralization and bone development and angiogenesis.
CC Stimulates cellular proliferation in a fibronectin-dependent manner.
CC Involved in the regulation of beta-1 integrin-containing focal adhesion
CC (FA) site dynamics by controlling its assembly rate during cell
CC adhesion; inhibits beta-1 integrin clustering within FA by directly
CC competing with talin TLN1, and hence stimulates osteoblast spreading
CC and migration in a fibronectin- and/or collagen-dependent manner. Acts
CC as a guanine nucleotide dissociation inhibitor (GDI) by regulating Rho
CC family GTPases during integrin-mediated cell matrix adhesion; reduces
CC the level of active GTP-bound form of both CDC42 and RAC1 GTPases upon
CC cell adhesion to fibronectin. Stimulates the release of active CDC42
CC from the membranes to maintain it in an inactive cytoplasmic pool.
CC Participates in the translocation of the Rho-associated protein kinase
CC ROCK1 to membrane ruffles at cell leading edges of the cell membrane,
CC leading to an increase of myoblast cell migration on laminin. Plays a
CC role in bone mineralization at a late stage of osteoblast
CC differentiation; modulates the dynamic formation of focal adhesions
CC into fibrillar adhesions, which are adhesive structures responsible for
CC fibronectin deposition and fibrillogenesis. Plays a role in blood
CC vessel development; acts as a negative regulator of angiogenesis by
CC attenuating endothelial cell proliferation and migration, lumen
CC formation and sprouting angiogenesis by promoting AKT phosphorylation
CC and inhibiting ERK1/2 phosphorylation through activation of the Notch
CC signaling pathway. Promotes transcriptional activity of the MYC
CC promoter. {ECO:0000269|PubMed:11741838, ECO:0000269|PubMed:11807099,
CC ECO:0000269|PubMed:11919189, ECO:0000269|PubMed:12473654,
CC ECO:0000269|PubMed:15703214, ECO:0000269|PubMed:17916086,
CC ECO:0000269|PubMed:20616313, ECO:0000269|PubMed:21768292,
CC ECO:0000269|Ref.19}.
CC -!- SUBUNIT: Interacts (via N-terminus and PTB domain) with ROCK1 (By
CC similarity). Found in a complex, at least composed of ITGB1BP1, KRIT1
CC and RAP1A. Interacts (via C-terminal region) with ITGB1 (via C-terminal
CC cytoplasmic tail); the interaction prevents talin TLN1 binding to ITGB1
CC and KRIT1 and ITGB1 compete for the same binding site. Interacts with
CC KRIT1 (via N-terminal NPXY motif); the interaction induces the opening
CC conformation of KRIT1 and KRIT1 and ITGB1 compete for the same binding
CC site. Isoform 2 does not interact with ITGB1. Interacts with CDC42
CC (GTP- or GDP-bound form); the interaction is increased with the CDC42-
CC membrane bound forms and prevents both CDC42 activation and cell
CC spreading. Interacts (via C-terminal domain region) with NME2.
CC Interacts with FERMT2 and RAC1. {ECO:0000250,
CC ECO:0000269|PubMed:11741838, ECO:0000269|PubMed:11741908,
CC ECO:0000269|PubMed:11807099, ECO:0000269|PubMed:11854171,
CC ECO:0000269|PubMed:11919189, ECO:0000269|PubMed:12473654,
CC ECO:0000269|PubMed:17916086, ECO:0000269|PubMed:21768292,
CC ECO:0000269|PubMed:9281591, ECO:0000269|PubMed:9867804,
CC ECO:0000269|Ref.19}.
CC -!- INTERACTION:
CC O14713; P54253: ATXN1; NbExp=3; IntAct=EBI-2127319, EBI-930964;
CC O14713; P09622: DLD; NbExp=3; IntAct=EBI-2127319, EBI-353366;
CC O14713; Q6PIW4: FIGNL1; NbExp=3; IntAct=EBI-2127319, EBI-8468390;
CC O14713; O00522: KRIT1; NbExp=4; IntAct=EBI-2127319, EBI-1573121;
CC O14713; Q15669: RHOH; NbExp=3; IntAct=EBI-2127319, EBI-1244971;
CC O14713; P37840: SNCA; NbExp=3; IntAct=EBI-2127319, EBI-985879;
CC O14713; P00441: SOD1; NbExp=3; IntAct=EBI-2127319, EBI-990792;
CC O14713-1; P22392: NME2; NbExp=7; IntAct=EBI-2127367, EBI-713693;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Cell membrane {ECO:0000250}. Cell projection,
CC lamellipodium. Cell projection, ruffle. Note=Nucleocytoplasmic
CC shuttling protein; shuttles between nucleus and cytoplasm in a
CC integrin-dependent manner; probably sequestered in the cytosol by
CC ITGB1. Its localization is dependent on the stage of cell spreading on
CC fibronectin; cytoplasmic in case of round cells, corresponding to the
CC initial step of cell spreading, or nuclear in case of well spread
CC cells. Colocalizes with ROCK1 and NME2 at beta-1 integrin engagement
CC sites. Together with ITGB1 and NME2 is recruited to beta-1 integrin-
CC rich peripheral ruffles and lamellipodia during initial cell spreading
CC on fibronectin and/or collagen.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=ICAP1-alpha;
CC IsoId=O14713-1; Sequence=Displayed;
CC Name=2; Synonyms=ICAP1-beta;
CC IsoId=O14713-2; Sequence=VSP_003898;
CC -!- TISSUE SPECIFICITY: Expressed in endothelial cells and fibroblasts (at
CC protein level). Ubiquitously expressed. Expressed in intestine, colon,
CC testis, ovary, thymus, spleen and prostate.
CC {ECO:0000269|PubMed:9281591, ECO:0000269|PubMed:9867804}.
CC -!- PTM: Phosphorylation at Thr-38 seems to enhance integrin alpha5beta1-
CC mediated cell adhesion. The degree of phosphorylation is regulated by
CC integrin-dependent cell-matrix interaction.
CC {ECO:0000269|PubMed:9281591, ECO:0000269|PubMed:9813144,
CC ECO:0000269|PubMed:9867804}.
CC -!- MISCELLANEOUS: [Isoform 1]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
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DR EMBL; AF012023; AAB88671.1; -; mRNA.
DR EMBL; AF012024; AAB88672.1; -; mRNA.
DR EMBL; CH471053; EAX00992.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00995.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX01000.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX01001.1; -; Genomic_DNA.
DR EMBL; AC080162; AAY14857.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00993.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00997.1; -; Genomic_DNA.
DR EMBL; BC012264; AAH12264.1; -; mRNA.
DR CCDS; CCDS1662.1; -. [O14713-1]
DR CCDS; CCDS1663.1; -. [O14713-2]
DR RefSeq; NP_001305995.1; NM_001319066.1. [O14713-1]
DR RefSeq; NP_001305996.1; NM_001319067.1. [O14713-1]
DR RefSeq; NP_001305997.1; NM_001319068.1. [O14713-1]
DR RefSeq; NP_004754.1; NM_004763.4. [O14713-1]
DR RefSeq; NP_071729.1; NM_022334.4. [O14713-2]
DR RefSeq; XP_005246240.1; XM_005246183.4.
DR RefSeq; XP_005246241.1; XM_005246184.4.
DR RefSeq; XP_005246242.1; XM_005246185.4.
DR RefSeq; XP_005246246.1; XM_005246189.4.
DR RefSeq; XP_006711966.1; XM_006711903.3. [O14713-1]
DR RefSeq; XP_011508718.1; XM_011510416.2.
DR RefSeq; XP_016860756.1; XM_017005267.1. [O14713-1]
DR RefSeq; XP_016860757.1; XM_017005268.1.
DR RefSeq; XP_016860758.1; XM_017005269.1.
DR RefSeq; XP_016860759.1; XM_017005270.1. [O14713-2]
DR PDB; 4DX8; X-ray; 2.54 A; A/B/D/E=49-200.
DR PDB; 4DX9; X-ray; 2.99 A; 0/1/2/3/4/5/A/C/E/G/I/K/M/O/Q/S/U/W/Y/a/c/e/g/i/k/m/o/q/s/u=49-200.
DR PDB; 4JIF; X-ray; 1.70 A; A=49-200.
DR PDBsum; 4DX8; -.
DR PDBsum; 4DX9; -.
DR PDBsum; 4JIF; -.
DR AlphaFoldDB; O14713; -.
DR SMR; O14713; -.
DR BioGRID; 114689; 27.
DR ComplexPortal; CPX-983; ICAP1-KRIT1 integrin activation complex.
DR CORUM; O14713; -.
DR IntAct; O14713; 18.
DR MINT; O14713; -.
DR STRING; 9606.ENSP00000353850; -.
DR iPTMnet; O14713; -.
DR PhosphoSitePlus; O14713; -.
DR BioMuta; ITGB1BP1; -.
DR EPD; O14713; -.
DR jPOST; O14713; -.
DR MassIVE; O14713; -.
DR MaxQB; O14713; -.
DR PaxDb; O14713; -.
DR PeptideAtlas; O14713; -.
DR PRIDE; O14713; -.
DR ProteomicsDB; 48172; -. [O14713-1]
DR ProteomicsDB; 48173; -. [O14713-2]
DR Antibodypedia; 26528; 223 antibodies from 28 providers.
DR DNASU; 9270; -.
DR Ensembl; ENST00000238091.8; ENSP00000238091.4; ENSG00000119185.13. [O14713-2]
DR Ensembl; ENST00000355346.9; ENSP00000347504.4; ENSG00000119185.13. [O14713-1]
DR Ensembl; ENST00000360635.7; ENSP00000353850.3; ENSG00000119185.13. [O14713-1]
DR Ensembl; ENST00000488451.5; ENSP00000419524.1; ENSG00000119185.13. [O14713-2]
DR GeneID; 9270; -.
DR KEGG; hsa:9270; -.
DR MANE-Select; ENST00000355346.9; ENSP00000347504.4; NM_004763.5; NP_004754.1.
DR UCSC; uc002qzj.4; human. [O14713-1]
DR CTD; 9270; -.
DR DisGeNET; 9270; -.
DR GeneCards; ITGB1BP1; -.
DR HGNC; HGNC:23927; ITGB1BP1.
DR HPA; ENSG00000119185; Low tissue specificity.
DR MIM; 607153; gene.
DR neXtProt; NX_O14713; -.
DR OpenTargets; ENSG00000119185; -.
DR PharmGKB; PA134913590; -.
DR VEuPathDB; HostDB:ENSG00000119185; -.
DR eggNOG; ENOG502QS6V; Eukaryota.
DR GeneTree; ENSGT00390000003990; -.
DR InParanoid; O14713; -.
DR OMA; QCHSLEQ; -.
DR OrthoDB; 1409828at2759; -.
DR PhylomeDB; O14713; -.
DR TreeFam; TF105393; -.
DR PathwayCommons; O14713; -.
DR SignaLink; O14713; -.
DR SIGNOR; O14713; -.
DR BioGRID-ORCS; 9270; 21 hits in 1077 CRISPR screens.
DR ChiTaRS; ITGB1BP1; human.
DR GeneWiki; ITGB1BP1; -.
DR GenomeRNAi; 9270; -.
DR Pharos; O14713; Tbio.
DR PRO; PR:O14713; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; O14713; protein.
DR Bgee; ENSG00000119185; Expressed in endocervix and 205 other tissues.
DR ExpressionAtlas; O14713; baseline and differential.
DR Genevisible; O14713; HS.
DR GO; GO:0071944; C:cell periphery; IDA:UniProtKB.
DR GO; GO:0034451; C:centriolar satellite; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HGNC-UCL.
DR GO; GO:0030027; C:lamellipodium; IDA:HGNC-UCL.
DR GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0001726; C:ruffle; IDA:HGNC-UCL.
DR GO; GO:0005092; F:GDP-dissociation inhibitor activity; IDA:UniProtKB.
DR GO; GO:0005178; F:integrin binding; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0032148; P:activation of protein kinase B activity; IDA:UniProtKB.
DR GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
DR GO; GO:0097746; P:blood vessel diameter maintenance; IDA:UniProtKB.
DR GO; GO:0002043; P:blood vessel endothelial cell proliferation involved in sprouting angiogenesis; IDA:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; TAS:HGNC-UCL.
DR GO; GO:0007160; P:cell-matrix adhesion; IDA:UniProtKB.
DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IDA:UniProtKB.
DR GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; IDA:UniProtKB.
DR GO; GO:0033622; P:integrin activation; IDA:ComplexPortal.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; TAS:ProtInc.
DR GO; GO:0051451; P:myoblast migration; ISS:UniProtKB.
DR GO; GO:0006933; P:negative regulation of cell adhesion involved in substrate-bound cell migration; ISS:UniProtKB.
DR GO; GO:0090051; P:negative regulation of cell migration involved in sprouting angiogenesis; IDA:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
DR GO; GO:0010764; P:negative regulation of fibroblast migration; ISS:UniProtKB.
DR GO; GO:0051895; P:negative regulation of focal adhesion assembly; IDA:UniProtKB.
DR GO; GO:0032091; P:negative regulation of protein binding; IDA:UniProtKB.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IDA:UniProtKB.
DR GO; GO:0090315; P:negative regulation of protein targeting to membrane; IDA:UniProtKB.
DR GO; GO:1900025; P:negative regulation of substrate adhesion-dependent cell spreading; IDA:UniProtKB.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; IDA:UniProtKB.
DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; IEA:Ensembl.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; IDA:UniProtKB.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:UniProtKB.
DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; ISS:UniProtKB.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; IDA:GO_Central.
DR GO; GO:0043113; P:receptor clustering; ISS:UniProtKB.
DR GO; GO:0033628; P:regulation of cell adhesion mediated by integrin; ISS:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; IDA:UniProtKB.
DR GO; GO:2001044; P:regulation of integrin-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0035148; P:tube formation; IDA:UniProtKB.
DR DisProt; DP01836; -.
DR InterPro; IPR019517; Integrin-bd_ICAP-1.
DR InterPro; IPR006020; PTB/PI_dom.
DR PANTHER; PTHR32055; PTHR32055; 1.
DR Pfam; PF10480; ICAP-1_inte_bdg; 1.
DR SMART; SM00462; PTB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Angiogenesis; Biomineralization;
KW Cell adhesion; Cell membrane; Cell projection; Cytoplasm; Cytoskeleton;
KW Differentiation; Membrane; Mitogen; Notch signaling pathway; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..200
FT /note="Integrin beta-1-binding protein 1"
FT /id="PRO_0000084264"
FT DOMAIN 58..200
FT /note="PID"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..139
FT /note="Interaction with KRIT1"
FT REGION 139..141
FT /note="Interaction with ITGB1"
FT MOTIF 6..7
FT /note="Nuclear localization signal"
FT COMPBIAS 12..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 38
FT /note="Phosphothreonine; by CaMK2"
FT /evidence="ECO:0000269|PubMed:9813144"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35671"
FT VAR_SEQ 128..177
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9281591"
FT /id="VSP_003898"
FT MUTAGEN 6..7
FT /note="KK->AA: Abolishes nuclear import and transcriptional
FT activity."
FT /evidence="ECO:0000269|PubMed:15703214"
FT MUTAGEN 38
FT /note="T->A: Stimulates cell spreading on fibronectin to a
FT similar extent as inhibition of CaMKII."
FT /evidence="ECO:0000269|PubMed:11741908,
FT ECO:0000269|PubMed:9813144"
FT MUTAGEN 38
FT /note="T->D: Changes in cell spreading."
FT /evidence="ECO:0000269|PubMed:11741908,
FT ECO:0000269|PubMed:9813144"
FT MUTAGEN 38
FT /note="T->D: Strong defect in cell spreading."
FT /evidence="ECO:0000269|PubMed:11741908,
FT ECO:0000269|PubMed:9813144"
FT MUTAGEN 82
FT /note="L->A: Reduces ITGB1 binding."
FT /evidence="ECO:0000269|PubMed:11741908"
FT MUTAGEN 82
FT /note="L->Q: No effect on ITGB1 binding."
FT /evidence="ECO:0000269|PubMed:11741908"
FT MUTAGEN 86
FT /note="L->Q: No effect on ITGB1 binding."
FT /evidence="ECO:0000269|PubMed:11741908"
FT MUTAGEN 89
FT /note="I->R: Reduces KRIT1 binding. No effect on ITGB1
FT binding."
FT /evidence="ECO:0000269|Ref.19"
FT MUTAGEN 93
FT /note="D->A: Abolishes KRIT1 binding; when associated with
FT A-96."
FT /evidence="ECO:0000269|Ref.19"
FT MUTAGEN 96
FT /note="Q->A: Abolishes KRIT1 binding; when associated with
FT A-93."
FT /evidence="ECO:0000269|Ref.19"
FT MUTAGEN 135..139
FT /note="LYLII->AYAA: Reduces KRIT1 and ITGB1 binding."
FT /evidence="ECO:0000269|Ref.19"
FT MUTAGEN 135
FT /note="L->A: Abolishes ITGB1 binding."
FT /evidence="ECO:0000269|PubMed:11741908"
FT MUTAGEN 138
FT /note="I->A: Abolishes ITGB1 binding."
FT /evidence="ECO:0000269|PubMed:11741908,
FT ECO:0000269|PubMed:15703214"
FT MUTAGEN 139
FT /note="I->A: Abolishes ITGB1 binding."
FT /evidence="ECO:0000269|PubMed:11741908"
FT MUTAGEN 144
FT /note="Y->T: Abolishes ITGB1 binding."
FT /evidence="ECO:0000269|PubMed:11741908"
FT MUTAGEN 184
FT /note="C->D: Reduces KRIT1 and ITGB1 binding."
FT /evidence="ECO:0000269|Ref.19"
FT CONFLICT 150
FT /note="A -> V (in Ref. 4; AAH12264)"
FT /evidence="ECO:0000305"
FT STRAND 61..74
FT /evidence="ECO:0007829|PDB:4JIF"
FT HELIX 85..97
FT /evidence="ECO:0007829|PDB:4JIF"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:4DX9"
FT STRAND 109..115
FT /evidence="ECO:0007829|PDB:4JIF"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:4JIF"
FT STRAND 129..134
FT /evidence="ECO:0007829|PDB:4JIF"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:4JIF"
FT STRAND 138..145
FT /evidence="ECO:0007829|PDB:4JIF"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:4JIF"
FT STRAND 153..160
FT /evidence="ECO:0007829|PDB:4JIF"
FT STRAND 167..175
FT /evidence="ECO:0007829|PDB:4JIF"
FT HELIX 177..192
FT /evidence="ECO:0007829|PDB:4JIF"
SQ SEQUENCE 200 AA; 21782 MW; 0F041238E68FBE23 CRC64;
MFRKGKKRHS SSSSQSSEIS TKSKSVDSSL GGLSRSSTVA SLDTDSTKSS GQSNNNSDTC
AEFRIKYVGA IEKLKLSEGK GLEGPLDLIN YIDVAQQDGK LPFVPPEEEF IMGVSKYGIK
VSTSDQYDVL HRHALYLIIR MVCYDDGLGA GKSLLALKTT DASNEEYSLW VYQCNSLEQA
QAICKVLSTA FDSVLTSEKP
