##gff-version 3 O14713 UniProtKB Chain 1 200 . . . ID=PRO_0000084264;Note=Integrin beta-1-binding protein 1 O14713 UniProtKB Domain 58 200 . . . Note=PID O14713 UniProtKB Region 1 56 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O14713 UniProtKB Region 136 139 . . . Note=Interaction with KRIT1 O14713 UniProtKB Region 139 141 . . . Note=Interaction with ITGB1 O14713 UniProtKB Motif 6 7 . . . Note=Nuclear localization signal O14713 UniProtKB Compositional bias 12 56 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O14713 UniProtKB Modified residue 38 38 . . . Note=Phosphothreonine%3B by CaMK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9813144;Dbxref=PMID:9813144 O14713 UniProtKB Modified residue 41 41 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O35671 O14713 UniProtKB Alternative sequence 128 177 . . . ID=VSP_003898;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:9281591;Dbxref=PMID:9281591 O14713 UniProtKB Mutagenesis 6 7 . . . Note=Abolishes nuclear import and transcriptional activity. KK->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15703214;Dbxref=PMID:15703214 O14713 UniProtKB Mutagenesis 38 38 . . . Note=Stimulates cell spreading on fibronectin to a similar extent as inhibition of CaMKII. T->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11741908,ECO:0000269|PubMed:9813144;Dbxref=PMID:11741908,PMID:9813144 O14713 UniProtKB Mutagenesis 38 38 . . . Note=Changes in cell spreading. T->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11741908,ECO:0000269|PubMed:9813144;Dbxref=PMID:11741908,PMID:9813144 O14713 UniProtKB Mutagenesis 38 38 . . . Note=Strong defect in cell spreading. T->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11741908,ECO:0000269|PubMed:9813144;Dbxref=PMID:11741908,PMID:9813144 O14713 UniProtKB Mutagenesis 82 82 . . . Note=Reduces ITGB1 binding. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11741908;Dbxref=PMID:11741908 O14713 UniProtKB Mutagenesis 82 82 . . . Note=No effect on ITGB1 binding. L->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11741908;Dbxref=PMID:11741908 O14713 UniProtKB Mutagenesis 86 86 . . . Note=No effect on ITGB1 binding. L->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11741908;Dbxref=PMID:11741908 O14713 UniProtKB Mutagenesis 89 89 . . . Note=Reduces KRIT1 binding. No effect on ITGB1 binding. I->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.19 O14713 UniProtKB Mutagenesis 93 93 . . . Note=Abolishes KRIT1 binding%3B when associated with A-96. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.19 O14713 UniProtKB Mutagenesis 96 96 . . . Note=Abolishes KRIT1 binding%3B when associated with A-93. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.19 O14713 UniProtKB Mutagenesis 135 139 . . . Note=Reduces KRIT1 and ITGB1 binding. LYLII->AYAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.19 O14713 UniProtKB Mutagenesis 135 135 . . . Note=Abolishes ITGB1 binding. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11741908;Dbxref=PMID:11741908 O14713 UniProtKB Mutagenesis 138 138 . . . Note=Abolishes ITGB1 binding. I->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11741908,ECO:0000269|PubMed:15703214;Dbxref=PMID:11741908,PMID:15703214 O14713 UniProtKB Mutagenesis 139 139 . . . Note=Abolishes ITGB1 binding. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11741908;Dbxref=PMID:11741908 O14713 UniProtKB Mutagenesis 144 144 . . . Note=Abolishes ITGB1 binding. Y->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11741908;Dbxref=PMID:11741908 O14713 UniProtKB Mutagenesis 184 184 . . . Note=Reduces KRIT1 and ITGB1 binding. C->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.19 O14713 UniProtKB Sequence conflict 150 150 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 O14713 UniProtKB Beta strand 61 74 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JIF O14713 UniProtKB Helix 85 97 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JIF O14713 UniProtKB Beta strand 99 101 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4DX9 O14713 UniProtKB Beta strand 109 115 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JIF O14713 UniProtKB Beta strand 118 123 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JIF O14713 UniProtKB Beta strand 129 134 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JIF O14713 UniProtKB Helix 135 137 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JIF O14713 UniProtKB Beta strand 138 145 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JIF O14713 UniProtKB Beta strand 148 150 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JIF O14713 UniProtKB Beta strand 153 160 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JIF O14713 UniProtKB Beta strand 167 175 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JIF O14713 UniProtKB Helix 177 192 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JIF