ID ITBP1_HUMAN STANDARD; PRT; 200 AA. AC O14713; O14714; DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 19-SEP-2006, entry version 55. DE Integrin beta-1-binding protein 1 (Integrin cytoplasmic domain- DE associated protein 1) (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 MRNA] (ISOFORM 1). RC TISSUE=Ovary; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). RN [3] 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 [4] 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:RESEARCH008.1-RESEARCH008.16(2004). 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 -!- 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; BC012264; AAH12264.1; -; mRNA. DR UniGene; Hs.467662; -. DR PDB; 1K11; Model; A=58-196. DR Ensembl; ENSG00000119185; Homo sapiens. DR KEGG; hsa:9270; -. DR H-InvDB; HIX0001808; -. DR HGNC; HGNC:23927; ITGB1BP1. DR MIM; 607153; gene. DR LinkHub; O14713; -. DR ArrayExpress; O14713; -. DR RZPD-ProtExp; Q0228; -. DR RZPD-ProtExp; RZPDo834G015; -. DR GO; GO:0016020; C:membrane; NAS. DR GO; GO:0008022; F:protein C-terminus binding; TAS. DR GO; GO:0007155; P:cell adhesion; TAS. DR GO; GO:0007160; P:cell-matrix adhesion; IDA. DR GO; GO:0007243; P:protein kinase cascade; TAS. DR InterPro; IPR006020; PTB_PID. DR SMART; SM00462; PTB; 1. DR PROSITE; PS01179; PID; FALSE_NEG. KW 3D-structure; Alternative splicing; Phosphorylation. 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 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. 2). FT STRAND 61 73 FT TURN 78 79 FT HELIX 80 97 FT STRAND 109 114 FT STRAND 118 123 FT TURN 124 126 FT STRAND 129 134 FT TURN 135 137 FT STRAND 138 144 FT STRAND 154 160 FT STRAND 167 174 FT HELIX 176 193 FT TURN 194 194 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 //