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Integrin beta-1-binding protein 1 (Integrin cytoplasmic domain-associated protein 1) (ICAP-1)

 ITBP1_HUMAN             Reviewed;         200 AA.
O14713; D6W4Y9; O14714; Q53RS0;
16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
27-SEP-2017, entry version 151.
RecName: Full=Integrin beta-1-binding protein 1;
AltName: Full=Integrin cytoplasmic domain-associated protein 1;
Short=ICAP-1;
Name=ITGB1BP1; Synonyms=ICAP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), INTERACTION WITH ITGB1,
PHOSPHORYLATION, AND TISSUE SPECIFICITY.
TISSUE=Cervix carcinoma;
PubMed=9281591; DOI=10.1083/jcb.138.5.1149;
Chang D.D., Wong C., Smith H., Liu J.;
"ICAP-1, a novel beta1 integrin cytoplasmic domain-associated protein,
binds to a conserved and functionally important NPXY sequence motif of
beta1 integrin.";
J. Cell Biol. 138:1149-1157(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH ITGB1,
PHOSPHORYLATION, AND TISSUE SPECIFICITY.
PubMed=9867804; DOI=10.1074/jbc.274.1.11;
Zhang X.A., Hemler M.E.;
"Interaction of the integrin beta1 cytoplasmic domain with ICAP-1
protein.";
J. Biol. Chem. 274:11-19(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Ovary;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PHOSPHORYLATION AT THR-38, AND MUTAGENESIS OF THR-38.
PubMed=9813144; DOI=10.1006/bbrc.1998.9592;
Bouvard D., Block M.R.;
"Calcium/calmodulin-dependent protein kinase II controls integrin
alpha5beta1-mediated cell adhesion through the integrin cytoplasmic
domain associated protein-1alpha.";
Biochem. Biophys. Res. Commun. 252:46-50(1998).
[7]
FUNCTION, AND INTERACTION WITH ITGB1 AND KRIT1.
PubMed=11741838; DOI=10.1093/hmg/10.25.2953;
Zhang J., Clatterbuck R.E., Rigamonti D., Chang D.D., Dietz H.C.;
"Interaction between krit1 and icap1alpha infers perturbation of
integrin beta1-mediated angiogenesis in the pathogenesis of cerebral
cavernous malformation.";
Hum. Mol. Genet. 10:2953-2960(2001).
[8]
INTERACTION WITH KRIT1.
PubMed=11854171; DOI=10.1093/hmg/11.4.389;
Zawistowski J.S., Serebriiskii I.G., Lee M.F., Golemis E.A.,
Marchuk D.A.;
"KRIT1 association with the integrin-binding protein ICAP-1: a new
direction in the elucidation of cerebral cavernous malformations
(CCM1) pathogenesis.";
Hum. Mol. Genet. 11:389-396(2002).
[9]
INTERACTION WITH ITGB1, MUTAGENESIS OF THR-38; LEU-82; LEU-86;
LEU-135; ILE-138; ILE-139 AND TYR-144, AND 3D-STRUCTURE MODELING.
PubMed=11741908; DOI=10.1074/jbc.M109031200;
Chang D.D., Hoang B.Q., Liu J., Springer T.A.;
"Molecular basis for interaction between Icap1alpha PTB domain and
beta 1 integrin.";
J. Biol. Chem. 277:8140-8145(2002).
[10]
FUNCTION, INTERACTION WITH NME2, AND SUBCELLULAR LOCATION.
PubMed=11919189; DOI=10.1074/jbc.M200200200;
Fournier H.N., Dupe-Manet S., Bouvard D., Lacombe M.L., Marie C.,
Block M.R., Albiges-Rizo C.;
"Integrin cytoplasmic domain-associated protein 1alpha (ICAP-1alpha)
interacts directly with the metastasis suppressor nm23-H2, and both
proteins are targeted to newly formed cell adhesion sites upon
integrin engagement.";
J. Biol. Chem. 277:20895-20902(2002).
[11]
FUNCTION, AND INTERACTION WITH CDC42; ITGB1 AND RAC1.
PubMed=11807099; DOI=10.1083/jcb.200108030;
Degani S., Balzac F., Brancaccio M., Guazzone S., Retta S.F.,
Silengo L., Eva A., Tarone G.;
"The integrin cytoplasmic domain-associated protein ICAP-1 binds and
regulates Rho family GTPases during cell spreading.";
J. Cell Biol. 156:377-387(2002).
[12]
FUNCTION, INTERACTION WITH ITGB1, AND SUBCELLULAR LOCATION.
PubMed=12473654; DOI=10.1074/jbc.M211258200;
Bouvard D., Vignoud L., Dupe-Manet S., Abed N., Fournier H.N.,
Vincent-Monegat C., Retta S.F., Fassler R., Block M.R.;
"Disruption of focal adhesions by integrin cytoplasmic domain-
associated protein-1 alpha.";
J. Biol. Chem. 278:6567-6574(2003).
[13]
SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
Hillman R.T., Green R.E., Brenner S.E.;
"An unappreciated role for RNA surveillance.";
Genome Biol. 5:R8.1-R8.16(2004).
[14]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 6-LYS-LYS-7 AND
ILE-138.
PubMed=15703214; DOI=10.1091/mbc.E04-08-0744;
Fournier H.N., Dupe-Manet S., Bouvard D., Luton F., Degani S.,
Block M.R., Retta S.F., Albiges-Rizo C.;
"Nuclear translocation of integrin cytoplasmic domain-associated
protein 1 stimulates cellular proliferation.";
Mol. Biol. Cell 16:1859-1871(2005).
[15]
FUNCTION, IDENTIFICATION IN A COMPLEX WITH KRIT1 AND RAP1A, AND
INTERACTION WITH KRIT1.
PubMed=17916086; DOI=10.1111/j.1742-4658.2007.06068.x;
Beraud-Dufour S., Gautier R., Albiges-Rizo C., Chardin P.,
Faurobert E.;
"Krit 1 interactions with microtubules and membranes are regulated by
Rap1 and integrin cytoplasmic domain associated protein-1.";
FEBS J. 274:5518-5532(2007).
[16]
FUNCTION.
PubMed=20616313; DOI=10.1161/CIRCRESAHA.110.217257;
Brutsch R., Liebler S.S., Wustehube J., Bartol A., Herberich S.E.,
Adam M.G., Telzerow A., Augustin H.G., Fischer A.;
"Integrin cytoplasmic domain-associated protein-1 attenuates sprouting
angiogenesis.";
Circ. Res. 107:592-601(2010).
[17]
FUNCTION, AND INTERACTION WITH ITGB1 AND FERMT2.
PubMed=21768292; DOI=10.1083/jcb.201007108;
Brunner M., Millon-Fremillon A., Chevalier G., Nakchbandi I.A.,
Mosher D., Block M.R., Albiges-Rizo C., Bouvard D.;
"Osteoblast mineralization requires beta1 integrin/ICAP-1-dependent
fibronectin deposition.";
J. Cell Biol. 194:307-322(2011).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[19]
X-RAY CRYSTALLOGRAPHY (2.54 ANGSTROMS) OF 49-200 IN COMPLEXES WITH
KRIT1 AND ITGB1, FUNCTION, INTERACTION WITH KRIT1 AND ITGB1, AND
MUTAGENESIS OF ILE-89; ASP-93; GLN-96; 135-LEU--ILE-139 AND CYS-184.
DOI=10.1016/j.molcel.2012.12.005;
Liu W., Draheim K.M., Zhang R., Calderwood D.A., Boggon T.J.;
"Mechanism for KRIT1 release of ICAP1-mediated suppression of integrin
activation.";
Mol. Cell 0:0-0(2013).
-!- 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}.
-!- SUBUNIT: Interacts (via N-terminus and PTB domain) with ROCK1 (By
similarity). Found in a complex, at least composed of ITGB1BP1,
KRIT1 and RAP1A. Interacts (via C-terminal region) with ITGB1 (via
C-terminal cytoplasmic tail); the interaction prevents talin TLN1
binding to ITGB1 and KRIT1 and ITGB1 compete for the same binding
site. Interacts with KRIT1 (via N-terminal NPXY motif); the
interaction induces the opening conformation of KRIT1 and KRIT1
and ITGB1 compete for the same binding site. Isoform 2 does not
interact with ITGB1. Interacts with CDC42 (GTP- or GDP-bound
form); the interaction is increased with the CDC42-membrane bound
forms and prevents both CDC42 activation and cell spreading.
Interacts (via C-terminal domain region) with NME2. Interacts with
FERMT2 and RAC1. {ECO:0000250, ECO:0000269|PubMed:11741838,
ECO:0000269|PubMed:11741908, ECO:0000269|PubMed:11807099,
ECO:0000269|PubMed:11854171, ECO:0000269|PubMed:11919189,
ECO:0000269|PubMed:12473654, ECO:0000269|PubMed:17916086,
ECO:0000269|PubMed:21768292, ECO:0000269|PubMed:9281591,
ECO:0000269|PubMed:9867804, ECO:0000269|Ref.19}.
-!- INTERACTION:
Q6PIW4:FIGNL1; NbExp=3; IntAct=EBI-2127319, EBI-8468390;
O00522:KRIT1; NbExp=4; IntAct=EBI-2127319, EBI-1573121;
P22392:NME2; NbExp=7; IntAct=EBI-2127367, EBI-713693;
-!- 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.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=ICAP1-alpha;
IsoId=O14713-1; Sequence=Displayed;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
Name=2; Synonyms=ICAP1-beta;
IsoId=O14713-2; Sequence=VSP_003898;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
-!- TISSUE SPECIFICITY: Expressed in endothelial cells and fibroblasts
(at protein level). Ubiquitously expressed. Expressed in
intestine, colon, testis, ovary, thymus, spleen and prostate.
{ECO:0000269|PubMed:9281591, ECO:0000269|PubMed:9867804}.
-!- 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}.
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EMBL; AF012023; AAB88671.1; -; mRNA.
EMBL; AF012024; AAB88672.1; -; mRNA.
EMBL; CH471053; EAX00992.1; -; Genomic_DNA.
EMBL; CH471053; EAX00995.1; -; Genomic_DNA.
EMBL; CH471053; EAX01000.1; -; Genomic_DNA.
EMBL; CH471053; EAX01001.1; -; Genomic_DNA.
EMBL; AC080162; AAY14857.1; -; Genomic_DNA.
EMBL; CH471053; EAX00993.1; -; Genomic_DNA.
EMBL; CH471053; EAX00997.1; -; Genomic_DNA.
EMBL; BC012264; AAH12264.1; -; mRNA.
CCDS; CCDS1662.1; -. [O14713-1]
CCDS; CCDS1663.1; -. [O14713-2]
RefSeq; NP_001305995.1; NM_001319066.1. [O14713-1]
RefSeq; NP_001305996.1; NM_001319067.1. [O14713-1]
RefSeq; NP_001305997.1; NM_001319068.1. [O14713-1]
RefSeq; NP_004754.1; NM_004763.4. [O14713-1]
RefSeq; NP_071729.1; NM_022334.4. [O14713-2]
RefSeq; XP_005246240.1; XM_005246183.4. [O14713-1]
RefSeq; XP_005246241.1; XM_005246184.4. [O14713-1]
RefSeq; XP_005246242.1; XM_005246185.4. [O14713-1]
RefSeq; XP_005246246.1; XM_005246189.4. [O14713-2]
RefSeq; XP_006711966.1; XM_006711903.3. [O14713-1]
RefSeq; XP_011508718.1; XM_011510416.2. [O14713-1]
RefSeq; XP_016860756.1; XM_017005267.1. [O14713-1]
RefSeq; XP_016860757.1; XM_017005268.1. [O14713-1]
RefSeq; XP_016860758.1; XM_017005269.1. [O14713-2]
RefSeq; XP_016860759.1; XM_017005270.1. [O14713-2]
UniGene; Hs.467662; -.
PDB; 1K11; Model; -; A=58-196.
PDB; 4DX8; X-ray; 2.54 A; A/B/D/E=49-200.
PDB; 4DX9; X-ray; 2.99 A; 0/1/2/3/4/5/A/C/E/G/I/K/M/O/Q/S/U/W/Y/a/c/e/g/i/k/m/o/q/s/u=49-200.
PDB; 4JIF; X-ray; 1.70 A; A=49-200.
PDBsum; 1K11; -.
PDBsum; 4DX8; -.
PDBsum; 4DX9; -.
PDBsum; 4JIF; -.
ProteinModelPortal; O14713; -.
SMR; O14713; -.
BioGrid; 114689; 15.
CORUM; O14713; -.
IntAct; O14713; 10.
STRING; 9606.ENSP00000347504; -.
iPTMnet; O14713; -.
PhosphoSitePlus; O14713; -.
BioMuta; ITGB1BP1; -.
EPD; O14713; -.
MaxQB; O14713; -.
PaxDb; O14713; -.
PeptideAtlas; O14713; -.
PRIDE; O14713; -.
DNASU; 9270; -.
Ensembl; ENST00000238091; ENSP00000238091; ENSG00000119185. [O14713-2]
Ensembl; ENST00000355346; ENSP00000347504; ENSG00000119185. [O14713-1]
Ensembl; ENST00000360635; ENSP00000353850; ENSG00000119185. [O14713-1]
Ensembl; ENST00000488451; ENSP00000419524; ENSG00000119185. [O14713-2]
GeneID; 9270; -.
KEGG; hsa:9270; -.
UCSC; uc002qzj.4; human. [O14713-1]
CTD; 9270; -.
DisGeNET; 9270; -.
EuPathDB; HostDB:ENSG00000119185.12; -.
GeneCards; ITGB1BP1; -.
HGNC; HGNC:23927; ITGB1BP1.
HPA; HPA071538; -.
MIM; 607153; gene.
neXtProt; NX_O14713; -.
OpenTargets; ENSG00000119185; -.
PharmGKB; PA134913590; -.
eggNOG; ENOG410IFN6; Eukaryota.
eggNOG; ENOG4111GWT; LUCA.
GeneTree; ENSGT00390000003990; -.
HOGENOM; HOG000015089; -.
HOVERGEN; HBG052155; -.
InParanoid; O14713; -.
KO; K20058; -.
OMA; RMLCYDD; -.
OrthoDB; EOG091G16AY; -.
PhylomeDB; O14713; -.
TreeFam; TF105393; -.
SIGNOR; O14713; -.
ChiTaRS; ITGB1BP1; human.
GeneWiki; ITGB1BP1; -.
GenomeRNAi; 9270; -.
PRO; PR:O14713; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000119185; -.
CleanEx; HS_ITGB1BP1; -.
ExpressionAtlas; O14713; baseline and differential.
Genevisible; O14713; HS.
GO; GO:0071944; C:cell periphery; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HGNC.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0030027; C:lamellipodium; IDA:HGNC.
GO; GO:0016020; C:membrane; NAS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0001726; C:ruffle; IDA:HGNC.
GO; GO:0005092; F:GDP-dissociation inhibitor activity; IDA:UniProtKB.
GO; GO:0005178; F:integrin binding; IDA:UniProtKB.
GO; GO:0032403; F:protein complex binding; IDA:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0008565; F:protein transporter activity; IDA:UniProtKB.
GO; GO:0032148; P:activation of protein kinase B activity; IDA:UniProtKB.
GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
GO; GO:0002043; P:blood vessel endothelial cell proliferation involved in sprouting angiogenesis; IDA:UniProtKB.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0016477; P:cell migration; TAS:HGNC.
GO; GO:0007160; P:cell-matrix adhesion; IDA:UniProtKB.
GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IDA:UniProtKB.
GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; IDA:UniProtKB.
GO; GO:0033622; P:integrin activation; ISS:UniProtKB.
GO; GO:0007229; P:integrin-mediated signaling pathway; IDA:UniProtKB.
GO; GO:0035556; P:intracellular signal transduction; TAS:ProtInc.
GO; GO:0051451; P:myoblast migration; ISS:UniProtKB.
GO; GO:0006933; P:negative regulation of cell adhesion involved in substrate-bound cell migration; ISS:UniProtKB.
GO; GO:0090051; P:negative regulation of cell migration involved in sprouting angiogenesis; IDA:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
GO; GO:0010764; P:negative regulation of fibroblast migration; ISS:UniProtKB.
GO; GO:0051895; P:negative regulation of focal adhesion assembly; IDA:UniProtKB.
GO; GO:0032091; P:negative regulation of protein binding; IDA:UniProtKB.
GO; GO:0006469; P:negative regulation of protein kinase activity; IDA:UniProtKB.
GO; GO:0090315; P:negative regulation of protein targeting to membrane; IDA:UniProtKB.
GO; GO:1900025; P:negative regulation of substrate adhesion-dependent cell spreading; IDA:UniProtKB.
GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0010595; P:positive regulation of endothelial cell migration; IDA:UniProtKB.
GO; GO:0051894; P:positive regulation of focal adhesion assembly; IEA:Ensembl.
GO; GO:0045747; P:positive regulation of Notch signaling pathway; IDA:UniProtKB.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:UniProtKB.
GO; GO:0090314; P:positive regulation of protein targeting to membrane; ISS:UniProtKB.
GO; GO:0051496; P:positive regulation of stress fiber assembly; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0015031; P:protein transport; IDA:UniProtKB.
GO; GO:0043113; P:receptor clustering; ISS:UniProtKB.
GO; GO:0050880; P:regulation of blood vessel size; IDA:UniProtKB.
GO; GO:0033628; P:regulation of cell adhesion mediated by integrin; ISS:UniProtKB.
GO; GO:0043087; P:regulation of GTPase activity; IDA:UniProtKB.
GO; GO:2001044; P:regulation of integrin-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0035148; P:tube formation; IDA:UniProtKB.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR019517; Integrin-bd_ICAP-1.
InterPro; IPR011993; PH_dom-like.
InterPro; IPR006020; PTB/PI_dom.
PANTHER; PTHR32055; PTHR32055; 1.
Pfam; PF10480; ICAP-1_inte_bdg; 1.
SMART; SM00462; PTB; 1.
SUPFAM; SSF50729; SSF50729; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Angiogenesis; Biomineralization;
Cell adhesion; Cell membrane; Cell projection; Complete proteome;
Cytoplasm; Cytoskeleton; Differentiation; Membrane; Mitogen;
Notch signaling pathway; Nucleus; Phosphoprotein; Reference proteome;
Transcription; Transcription regulation.
CHAIN 1 200 Integrin beta-1-binding protein 1.
/FTId=PRO_0000084264.
DOMAIN 58 200 PID.
REGION 136 139 Interaction with KRIT1.
REGION 139 141 Interaction with ITGB1.
MOTIF 6 7 Nuclear localization signal.
COMPBIAS 10 57 Ser/Thr-rich.
MOD_RES 38 38 Phosphothreonine; by CaMK2.
{ECO:0000269|PubMed:9813144}.
MOD_RES 41 41 Phosphoserine.
{ECO:0000250|UniProtKB:O35671}.
VAR_SEQ 128 177 Missing (in isoform 2).
{ECO:0000303|PubMed:9281591}.
/FTId=VSP_003898.
MUTAGEN 6 7 KK->AA: Abolishes nuclear import and
transcriptional activity.
{ECO:0000269|PubMed:15703214}.
MUTAGEN 38 38 T->A: Stimulates cell spreading on
fibronectin to a similar extent as
inhibition of CaMKII.
{ECO:0000269|PubMed:11741908,
ECO:0000269|PubMed:9813144}.
MUTAGEN 38 38 T->D: Changes in cell spreading.
{ECO:0000269|PubMed:11741908,
ECO:0000269|PubMed:9813144}.
MUTAGEN 38 38 T->D: Strong defect in cell spreading.
{ECO:0000269|PubMed:11741908,
ECO:0000269|PubMed:9813144}.
MUTAGEN 82 82 L->A: Reduces ITGB1 binding.
{ECO:0000269|PubMed:11741908}.
MUTAGEN 82 82 L->Q: No effect on ITGB1 binding.
{ECO:0000269|PubMed:11741908}.
MUTAGEN 86 86 L->Q: No effect on ITGB1 binding.
{ECO:0000269|PubMed:11741908}.
MUTAGEN 89 89 I->R: Reduces KRIT1 binding. No effect on
ITGB1 binding. {ECO:0000269|Ref.19}.
MUTAGEN 93 93 D->A: Abolishes KRIT1 binding; when
associated with A-96.
{ECO:0000269|Ref.19}.
MUTAGEN 96 96 Q->A: Abolishes KRIT1 binding; when
associated with A-93.
{ECO:0000269|Ref.19}.
MUTAGEN 135 139 LYLII->AYAA: Reduces KRIT1 and ITGB1
binding. {ECO:0000269|Ref.19}.
MUTAGEN 135 135 L->A: Abolishes ITGB1 binding.
{ECO:0000269|PubMed:11741908}.
MUTAGEN 138 138 I->A: Abolishes ITGB1 binding.
{ECO:0000269|PubMed:11741908,
ECO:0000269|PubMed:15703214}.
MUTAGEN 139 139 I->A: Abolishes ITGB1 binding.
{ECO:0000269|PubMed:11741908}.
MUTAGEN 144 144 Y->T: Abolishes ITGB1 binding.
{ECO:0000269|PubMed:11741908}.
MUTAGEN 184 184 C->D: Reduces KRIT1 and ITGB1 binding.
{ECO:0000269|Ref.19}.
CONFLICT 150 150 A -> V (in Ref. 4; AAH12264).
{ECO:0000305}.
STRAND 61 74 {ECO:0000244|PDB:4JIF}.
HELIX 85 97 {ECO:0000244|PDB:4JIF}.
STRAND 99 101 {ECO:0000244|PDB:4DX9}.
STRAND 109 115 {ECO:0000244|PDB:4JIF}.
STRAND 118 123 {ECO:0000244|PDB:4JIF}.
STRAND 129 134 {ECO:0000244|PDB:4JIF}.
HELIX 135 137 {ECO:0000244|PDB:4JIF}.
STRAND 138 145 {ECO:0000244|PDB:4JIF}.
STRAND 148 150 {ECO:0000244|PDB:4JIF}.
STRAND 153 160 {ECO:0000244|PDB:4JIF}.
STRAND 167 175 {ECO:0000244|PDB:4JIF}.
HELIX 177 192 {ECO:0000244|PDB:4JIF}.
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


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