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 21-MAR-2012, entry version 103. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Cervix carcinoma; RX MEDLINE=97428321; 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 [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., RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., RA 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., RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., RA 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., RA Waterston R.H., Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 RT and 4."; RL Nature 434:724-731(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [4] 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP MUTAGENESIS OF THR-38; LEU-82; LEU-86; LEU-135; ILE-138; ILE-139 AND RP TYR-144, AND 3D-STRUCTURE MODELING. RX MEDLINE=21864153; 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 RT beta 1 integrin."; RL J. Biol. Chem. 277:8140-8145(2002). RN [6] 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 [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41, AND MASS RP SPECTROMETRY. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). CC -!- FUNCTION: May play a role in the recruitment of beta-1 integrins CC to the focal contacts during integrin-dependent cell adhesion. CC Isoform 2 does not bind the integrin cytoplasmic domain-associated CC protein-1. CC -!- SUBUNIT: Interacts specifically with the beta-1 integrin CC cytoplasmic domain-associated protein-1. CC -!- INTERACTION: CC P22392:NME2; NbExp=7; IntAct=EBI-2127367, EBI-713693; CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=ICAP1-alpha; CC IsoId=O14713-1; Sequence=Displayed; CC Note=May be produced at very low levels due to a premature stop CC codon in the mRNA, leading to nonsense-mediated mRNA decay; CC Name=2; Synonyms=ICAP1-beta; CC IsoId=O14713-2; Sequence=VSP_003898; CC Note=May be produced at very low levels due to a premature stop CC codon in the mRNA, leading to nonsense-mediated mRNA decay; CC -!- TISSUE SPECIFICITY: Expressed in intestine, colon, testis, ovary, CC thymus, spleen and prostate. CC -!- PTM: Isoform 1 appears to be phosphorylated. The degree of CC phosphorylation is regulated by integrin-dependent cell-matrix CC interaction. CC -!- SIMILARITY: Contains 1 PID domain. 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 IPI; IPI00006265; -. DR IPI; IPI00219566; -. DR RefSeq; NP_004754.1; NM_004763.3. DR RefSeq; NP_071729.1; NM_022334.3. DR UniGene; Hs.467662; -. DR PDB; 1K11; Model; -; A=58-196. DR PDBsum; 1K11; -. DR ProteinModelPortal; O14713; -. DR IntAct; O14713; 2. DR STRING; O14713; -. DR PhosphoSite; O14713; -. DR PRIDE; O14713; -. DR DNASU; 9270; -. DR Ensembl; ENST00000355346; ENSP00000347504; ENSG00000119185. DR Ensembl; ENST00000360635; ENSP00000353850; ENSG00000119185. DR GeneID; 9270; -. DR KEGG; hsa:9270; -. DR UCSC; uc002qzj.1; human. DR UCSC; uc002qzk.1; human. DR CTD; 9270; -. DR GeneCards; GC02M009496; -. DR H-InvDB; HIX0001808; -. DR HGNC; HGNC:23927; ITGB1BP1. DR MIM; 607153; gene. DR neXtProt; NX_O14713; -. DR PharmGKB; PA134913590; -. DR eggNOG; NOG45114; -. DR GeneTree; ENSGT00390000003990; -. DR HOGENOM; HBG713132; -. DR HOVERGEN; HBG052155; -. DR InParanoid; O14713; -. DR OMA; LDTCAEF; -. DR OrthoDB; EOG483D5W; -. DR PhylomeDB; O14713; -. DR NextBio; 34745; -. DR ArrayExpress; O14713; -. DR Bgee; O14713; -. DR CleanEx; HS_ITGB1BP1; -. DR Genevestigator; O14713; -. DR GermOnline; ENSG00000119185; Homo sapiens. DR GO; GO:0005829; C:cytosol; IDA:HGNC. DR GO; GO:0030027; C:lamellipodium; IDA:HGNC. DR GO; GO:0016020; C:membrane; NAS:UniProtKB. DR GO; GO:0001726; C:ruffle; IDA:HGNC. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0016477; P:cell migration; TAS:HGNC. DR GO; GO:0007160; P:cell-matrix adhesion; IDA:UniProtKB. DR GO; GO:0007243; P:intracellular protein kinase cascade; TAS:ProtInc. DR InterPro; IPR019517; Integrin-bd_ICAP-1. DR InterPro; IPR011993; PH_like_dom. DR InterPro; IPR006020; PTyr_interaction_dom. DR Gene3D; G3DSA:2.30.29.30; PH_type; 1. DR Pfam; PF10480; ICAP-1_inte_bdg; 1. DR SMART; SM00462; PTB; 1. DR PROSITE; PS01179; PID; FALSE_NEG. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Complete proteome; Cytoplasm; KW Phosphoprotein; Reference proteome. FT CHAIN 1 200 Integrin beta-1-binding protein 1. FT /FTId=PRO_0000084264. FT DOMAIN 58 200 PID. FT COMPBIAS 10 57 Ser/Thr-rich. FT MOD_RES 41 41 Phosphoserine. FT VAR_SEQ 128 177 Missing (in isoform 2). FT /FTId=VSP_003898. FT MUTAGEN 38 38 T->D: Changes in cell spreading. FT MUTAGEN 82 82 L->A: Decrease in binding to beta 1 FT integrin; when associated with T-144 no FT binding to beta 1 integrin. FT MUTAGEN 82 82 L->Q: No change in binding to beta 1 FT integrin. FT MUTAGEN 86 86 L->Q: No change in binding to beta 1 FT integrin; when associated with T-144 no FT binding to beta 1 integrin. FT MUTAGEN 135 135 L->A: No binding to beta 1 integrin. FT MUTAGEN 138 138 I->A: No binding to beta 1 integrin. FT MUTAGEN 139 139 I->A: No binding to beta 1 integrin. FT MUTAGEN 144 144 Y->T: No binding to beta 1 integrin. FT CONFLICT 150 150 A -> V (in Ref. 4; AAH12264). FT STRAND 61 73 FT HELIX 80 97 FT STRAND 109 114 FT STRAND 116 123 FT TURN 124 126 FT STRAND 129 134 FT TURN 135 137 FT STRAND 138 144 FT STRAND 154 160 FT STRAND 162 165 FT STRAND 167 174 FT HELIX 176 193 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 //