ITGB1BP1
entrez
9270
canonical
uniprot
O14713
canonical
ensembl
ENSG00000119185
resolver
ensp
ENSP00000238091
resolver
ensp
ENSP00000347504
resolver
ensp
ENSP00000353850
resolver
ensp
ENSP00000536012
resolver
ensp
ENSP00000536013
resolver
ensp
ENSP00000536014
resolver
ensp
ENSP00000536017
resolver
ensp
ENSP00000536022
resolver
ensp
ENSP00000536025
resolver
ensp
ENSP00000536038
resolver
ensp
ENSP00000536039
resolver
ensp
ENSP00000536042
resolver
ensp
ENSP00000591639
resolver
ensp
ENSP00000591642
resolver
ensp
ENSP00000620041
resolver
ensp
ENSP00000620047
resolver
genesymbol
ITGB1BP1
resolver
genesymbol_syn
ICAP1
resolver
hgnc
HGNC:23927
resolver
uniprot
B4DQY5
resolver
uniprot
D6W4Y9
resolver
uniprot
O14714
resolver
uniprot
Q53RS0
resolver
uniprot_entry
B4DQY5_HUMAN
resolver
uniprot_entry
ITBP1_HUMAN
resolver
uniprot_sec
D6W4Y9
resolver
uniprot_sec
O14714
resolver
uniprot_sec
Q53RS0
resolver
amino_acid_sequence
MFRKGKKRHSSSSSQSSEISTKSKSVDSSLGGLSRSSTVASLDTDSTKSSGQSNNNSDTCAEFRIKYVGAIEKLKLSEGKGLEGPLDLINYIDVAQQDGKLPFVPPEEEFIMGVSKYGIKVSTSDQYDVLHRHALYLIIRMVCYDDGLGAGKSLLALKTTDASNEEYSLWVYQCNSLEQAQAICKVLSTAFDSVLTSEKP
uniprot
proteins
function
FUNCTION: Key regulator of the integrin-mediated cell-matrix interaction signaling by binding to the ITGB1 cytoplasmic tail and preventing the activation of integrin alpha-5/beta-1 (heterodimer of ITGA5 and ITGB1) by talin or FERMT1. Plays a role in cell proliferation, differentiation, spreading, adhesion and migration in the context of mineralization and bone development and angiogenesis. Stimulates cellular proliferation in a fibronectin-dependent manner. Involved in the regulation of beta-1 integrin-containing focal adhesion (FA) site dynamics by controlling its assembly rate during cell adhesion; inhibits beta-1 integrin clustering within FA by directly competing with talin TLN1, and hence stimulates osteoblast spreading and migration in a fibronectin- and/or collagen-dependent manner. Acts as a guanine nucleotide dissociation inhibitor (GDI) by regulating Rho family GTPases during integrin-mediated cell matrix adhesion; reduces the level of active GTP-bound form of both CDC42 and RAC1 GTPases upon cell adhesion to fibronectin. Stimulates the release of active CDC42 from the membranes to maintain it in an inactive cytoplasmic pool. Participates in the translocation of the Rho-associated protein kinase ROCK1 to membrane ruffles at cell leading edges of the cell membrane, leading to an increase of myoblast cell migration on laminin. Plays a role in bone mineralization at a late stage of osteoblast differentiation; modulates the dynamic formation of focal adhesions into fibrillar adhesions, which are adhesive structures responsible for fibronectin deposition and fibrillogenesis. Plays a role in blood vessel development; acts as a negative regulator of angiogenesis by attenuating endothelial cell proliferation and migration, lumen formation and sprouting angiogenesis by promoting AKT phosphorylation and inhibiting ERK1/2 phosphorylation through activation of the Notch signaling pathway. Promotes transcriptional activity of the MYC promoter. {ECO:0000269|PubMed:11741838, ECO:0000269|PubMed:11807099, ECO:0000269|PubMed:11919189, ECO:0000269|PubMed:12473654, ECO:0000269|PubMed:15703214, ECO:0000269|PubMed:17916086, ECO:0000269|PubMed:20616313, ECO:0000269|PubMed:21768292, ECO:0000269|Ref.19}.
uniprot
proteins
mass_dalton
21782
uniprot
proteins
mutagenesis
MUTAGEN 6..7; /note="KK->AA: Abolishes nuclear import and transcriptional activity."; /evidence="ECO:0000269|PubMed:15703214"; MUTAGEN 38; /note="T->A: Stimulates cell spreading on fibronectin to a similar extent as inhibition of CaMKII."; /evidence="ECO:0000269|PubMed:11741908, ECO:0000269|PubMed:9813144"; MUTAGEN 38; /note="T->D: Changes in cell spreading."; /evidence="ECO:0000269|PubMed:11741908, ECO:0000269|PubMed:9813144"; MUTAGEN 38; /note="T->D: Strong defect in cell spreading."; /evidence="ECO:0000269|PubMed:11741908, ECO:0000269|PubMed:9813144"; MUTAGEN 82; /note="L->A: Reduces ITGB1 binding."; /evidence="ECO:0000269|PubMed:11741908"; MUTAGEN 82; /note="L->Q: No effect on ITGB1 binding."; /evidence="ECO:0000269|PubMed:11741908"; MUTAGEN 86; /note="L->Q: No effect on ITGB1 binding."; /evidence="ECO:0000269|PubMed:11741908"; MUTAGEN 89; /note="I->R: Reduces KRIT1 binding. No effect on ITGB1 binding."; /evidence="ECO:0000269|Ref.19"; MUTAGEN 93; /note="D->A: Abolishes KRIT1 binding; when associated with A-96."; /evidence="ECO:0000269|Ref.19"; MUTAGEN 96; /note="Q->A: Abolishes KRIT1 binding; when associated with A-93."; /evidence="ECO:0000269|Ref.19"; MUTAGEN 135..139; /note="LYLII->AYAA: Reduces KRIT1 and ITGB1 binding."; /evidence="ECO:0000269|Ref.19"; MUTAGEN 135; /note="L->A: Abolishes ITGB1 binding."; /evidence="ECO:0000269|PubMed:11741908"; MUTAGEN 138; /note="I->A: Abolishes ITGB1 binding."; /evidence="ECO:0000269|PubMed:11741908, ECO:0000269|PubMed:15703214"; MUTAGEN 139; /note="I->A: Abolishes ITGB1 binding."; /evidence="ECO:0000269|PubMed:11741908"; MUTAGEN 144; /note="Y->T: Abolishes ITGB1 binding."; /evidence="ECO:0000269|PubMed:11741908"; MUTAGEN 184; /note="C->D: Reduces KRIT1 and ITGB1 binding."; /evidence="ECO:0000269|Ref.19
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Thr-38 seems to enhance integrin alpha5beta1-mediated cell adhesion. The degree of phosphorylation is regulated by integrin-dependent cell-matrix interaction. {ECO:0000269|PubMed:9281591, ECO:0000269|PubMed:9813144, ECO:0000269|PubMed:9867804}.
uniprot
proteins
pubmed
11741838
uniprot
proteins
pubmed
11741908
uniprot
proteins
pubmed
11807099
uniprot
proteins
pubmed
11854171
uniprot
proteins
pubmed
11919189
uniprot
proteins
pubmed
12473654
uniprot
proteins
pubmed
14759258
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15703214
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
17916086
uniprot
proteins
pubmed
20616313
uniprot
proteins
pubmed
21768292
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
9281591
uniprot
proteins
pubmed
9813144
uniprot
proteins
pubmed
9867804
uniprot
proteins
sequence_length
200
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasm, cytoskeleton {ECO:0000250}. Cell membrane {ECO:0000250}. Cell projection, lamellipodium. Cell projection, ruffle. Note=Nucleocytoplasmic shuttling protein; shuttles between nucleus and cytoplasm in a integrin-dependent manner; probably sequestered in the cytosol by ITGB1. Its localization is dependent on the stage of cell spreading on fibronectin; cytoplasmic in case of round cells, corresponding to the initial step of cell spreading, or nuclear in case of well spread cells. Colocalizes with ROCK1 and NME2 at beta-1 integrin engagement sites. Together with ITGB1 and NME2 is recruited to beta-1 integrin-rich peripheral ruffles and lamellipodia during initial cell spreading on fibronectin and/or collagen.
uniprot
proteins