ID ITP1_HUMAN STANDARD; PRT; 200 AA. AC O14713; O14714; DT 01-MAR-2002 (Rel. 41, Created) DT 01-MAR-2002 (Rel. 41, Last sequence update) DT 01-MAR-2002 (Rel. 41, Last annotation update) DE Integrin beta-1 binding protein 1 (Integrin cytoplasmic domain- DE associated protein 1) (ICAP-1). GN ITGB1BP1 OR ICAP1. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS 1 AND 2). RC TISSUE=Cervical carcinoma; RX MEDLINE=97428321; PubMed=9281591; 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 SEQUENCE FROM N.A. (ISOFORM 1). RC TISSUE=Ovary; RA Strausberg R.; RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases. 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 PubMed=11741908; 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). 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: Cytoplasmic. CC -!- ALTERNATIVE PRODUCTS: 2 isoforms; 1/ICAP1-alpha (shown here) and CC 2/ICAP1-beta; are produced by alternative splicing. 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; -. DR EMBL; AF012024; AAB88672.1; -. DR EMBL; BC012264; AAH12264.1; -. DR PDB; 1K11; 20-MAR-02. DR InterPro; IPR000050; PID_domain. DR SMART; SM00462; PTB; 1. DR PROSITE; PS01179; PID; FALSE_NEG. KW Alternative splicing; Phosphorylation; 3D-structure. FT DOMAIN 10 57 SER/THR-RICH. FT DOMAIN 58 200 PID. FT VARSPLIC 128 177 MISSING (IN ISOFORM 2). 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 THR-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 THR-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). 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 //