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 25-MAY-2022, entry version 181. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 25. 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; 206 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. DR Ensembl; ENST00000360635.7; ENSP00000353850.3; ENSG00000119185.13. 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 caudate nucleus and 247 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 //