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O14713 (ITBP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Integrin beta-1-binding protein 1
Alternative name(s):
Integrin cytoplasmic domain-associated protein 1
Short name=ICAP-1
Gene names
Name:ITGB1BP1
Synonyms:ICAP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length200 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.7 Ref.10 Ref.11 Ref.12 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18

Subunit structure

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. Ref.1 Ref.2 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.15 Ref.17 Ref.18

Subcellular location

Nucleus. Cytoplasm. Cytoplasmcytoskeleton By similarity. Cell membrane By similarity. Cell projectionlamellipodium. Cell projectionruffle. 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. Ref.10 Ref.12 Ref.14

Tissue specificity

Expressed in endothelial cells and fibroblasts (at protein level). Ubiquitously expressed. Expressed in intestine, colon, testis, ovary, thymus, spleen and prostate. Ref.1 Ref.2

Post-translational modification

Phosphorylation at Thr-38 seems to enhance integrin alpha5beta1-mediated cell adhesion. The degree of phosphorylation is regulated by integrin-dependent cell-matrix interaction.

Sequence similarities

Contains 1 PID domain.

Ontologies

Keywords
   Biological processAngiogenesis
Biomineralization
Cell adhesion
Differentiation
Notch signaling pathway
Transcription
Transcription regulation
   Cellular componentCell membrane
Cell projection
Cytoplasm
Cytoskeleton
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
   Molecular functionMitogen
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processNotch signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

activation of protein kinase B activity

Inferred from direct assay Ref.16. Source: UniProtKB

biomineral tissue development

Inferred from electronic annotation. Source: UniProtKB-KW

blood vessel endothelial cell proliferation involved in sprouting angiogenesis

Inferred from direct assay Ref.16. Source: UniProtKB

cell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

cell migration

Traceable author statement Ref.10. Source: HGNC

cell-matrix adhesion

Inferred from direct assay Ref.1. Source: UniProtKB

cellular response to fibroblast growth factor stimulus

Inferred from direct assay Ref.16. Source: UniProtKB

cellular response to vascular endothelial growth factor stimulus

Inferred from direct assay Ref.16. Source: UniProtKB

integrin activation

Inferred from sequence or structural similarity. Source: UniProtKB

integrin-mediated signaling pathway

Inferred from direct assay Ref.10Ref.14. Source: UniProtKB

intracellular signal transduction

Traceable author statement Ref.6. Source: ProtInc

myoblast migration

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of ERK1 and ERK2 cascade

Inferred from direct assay Ref.16. Source: UniProtKB

negative regulation of cell adhesion involved in substrate-bound cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell migration involved in sprouting angiogenesis

Inferred from direct assay Ref.16. Source: UniProtKB

negative regulation of cell proliferation

Inferred from direct assay Ref.16. Source: UniProtKB

negative regulation of fibroblast migration

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of focal adhesion assembly

Inferred from direct assay Ref.12. Source: UniProtKB

negative regulation of protein binding

Inferred from direct assay Ref.12. Source: UniProtKB

negative regulation of protein kinase activity

Inferred from direct assay Ref.16. Source: UniProtKB

negative regulation of protein targeting to membrane

Inferred from direct assay Ref.11. Source: UniProtKB

negative regulation of substrate adhesion-dependent cell spreading

Inferred from direct assay Ref.11. Source: UniProtKB

positive regulation of Notch signaling pathway

Inferred from direct assay Ref.16. Source: UniProtKB

positive regulation of cell division

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of cell proliferation

Inferred from direct assay Ref.14. Source: UniProtKB

positive regulation of endothelial cell migration

Inferred from direct assay Ref.16. Source: UniProtKB

positive regulation of focal adhesion assembly

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein kinase B signaling

Inferred from direct assay Ref.16. Source: UniProtKB

positive regulation of protein targeting to membrane

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of stress fiber assembly

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.14Ref.16. Source: UniProtKB

protein transport

Inferred from direct assay Ref.15. Source: UniProtKB

receptor clustering

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of Cdc42 GTPase activity

Inferred from direct assay Ref.11. Source: UniProtKB

regulation of blood vessel size

Inferred from direct assay Ref.16. Source: UniProtKB

regulation of cell adhesion mediated by integrin

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of integrin-mediated signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

tube formation

Inferred from direct assay Ref.16. Source: UniProtKB

   Cellular_componentcell periphery

Inferred from direct assay Ref.10. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.10Ref.12Ref.14. Source: UniProtKB

cytoskeleton

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Inferred from direct assay Ref.10. Source: HGNC

lamellipodium

Inferred from direct assay Ref.10. Source: HGNC

membrane

Non-traceable author statement Ref.1. Source: UniProtKB

nucleus

Inferred from direct assay Ref.12Ref.14. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from direct assay Ref.10. Source: UniProtKB

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

ruffle

Inferred from direct assay Ref.10. Source: HGNC

   Molecular_functionGDP-dissociation inhibitor activity

Inferred from direct assay Ref.11. Source: UniProtKB

integrin binding

Inferred from direct assay Ref.14. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.11Ref.14Ref.15Ref.1. Source: UniProtKB

protein complex binding

Inferred from direct assay Ref.15. Source: UniProtKB

protein transporter activity

Inferred from direct assay Ref.15. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NME2P223927EBI-2127367,EBI-713693

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O14713-1)

Also known as: ICAP1-alpha;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Isoform 2 (identifier: O14713-2)

Also known as: ICAP1-beta;

The sequence of this isoform differs from the canonical sequence as follows:
     128-177: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 200200Integrin beta-1-binding protein 1
PRO_0000084264

Regions

Domain58 – 200143PID
Region136 – 1394Interaction with KRIT1
Region139 – 1413Interaction with ITGB1
Motif6 – 72Nuclear localization signal
Compositional bias10 – 5748Ser/Thr-rich

Amino acid modifications

Modified residue381Phosphothreonine; by CaMK2 Ref.6

Natural variations

Alternative sequence128 – 17750Missing in isoform 2.
VSP_003898

Experimental info

Mutagenesis6 – 72KK → AA: Abolishes nuclear import and transcriptional activity.
Mutagenesis381T → A: Stimulates cell spreading on fibronectin to a similar extent as inhibition of CaMKII. Ref.6 Ref.9
Mutagenesis381T → D: Changes in cell spreading. Ref.6 Ref.9
Mutagenesis381T → D: Strong defect in cell spreading. Ref.6 Ref.9
Mutagenesis821L → A: Reduces ITGB1 binding. Ref.9
Mutagenesis821L → Q: No effect on ITGB1 binding. Ref.9
Mutagenesis861L → Q: No effect on ITGB1 binding. Ref.9
Mutagenesis891I → R: Reduces KRIT1 binding. No effect on ITGB1 binding. Ref.18
Mutagenesis931D → A: Abolishes KRIT1 binding; when associated with A-96. Ref.18
Mutagenesis961Q → A: Abolishes KRIT1 binding; when associated with A-93. Ref.18
Mutagenesis135 – 1395LYLII → AYAA: Reduces KRIT1 and ITGB1 binding. Ref.9 Ref.18
Mutagenesis1351L → A: Abolishes ITGB1 binding. Ref.9
Mutagenesis1381I → A: Abolishes ITGB1 binding. Ref.9 Ref.14
Mutagenesis1391I → A: Abolishes ITGB1 binding. Ref.9
Mutagenesis1441Y → T: Abolishes ITGB1 binding. Ref.9
Mutagenesis1841C → D: Reduces KRIT1 and ITGB1 binding. Ref.18
Sequence conflict1501A → V in AAH12264. Ref.4

Secondary structure

....................... 200
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (ICAP1-alpha) [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 0F041238E68FBE23

FASTA20021,782
        10         20         30         40         50         60 
MFRKGKKRHS SSSSQSSEIS TKSKSVDSSL GGLSRSSTVA SLDTDSTKSS GQSNNNSDTC 

        70         80         90        100        110        120 
AEFRIKYVGA IEKLKLSEGK GLEGPLDLIN YIDVAQQDGK LPFVPPEEEF IMGVSKYGIK 

       130        140        150        160        170        180 
VSTSDQYDVL HRHALYLIIR MVCYDDGLGA GKSLLALKTT DASNEEYSLW VYQCNSLEQA 

       190        200 
QAICKVLSTA FDSVLTSEKP 

« Hide

Isoform 2 (ICAP1-beta) [UniParc].

Checksum: FC6E3D387878DB81
Show »

FASTA15016,140

References

« Hide 'large scale' references
[1]"ICAP-1, a novel beta1 integrin cytoplasmic domain-associated protein, binds to a conserved and functionally important NPXY sequence motif of beta1 integrin."
Chang D.D., Wong C., Smith H., Liu J.
J. Cell Biol. 138:1149-1157(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), INTERACTION WITH ITGB1, PHOSPHORYLATION, TISSUE SPECIFICITY.
Tissue: Cervix carcinoma.
[2]"Interaction of the integrin beta1 cytoplasmic domain with ICAP-1 protein."
Zhang X.A., Hemler M.E.
J. Biol. Chem. 274:11-19(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH ITGB1, PHOSPHORYLATION, TISSUE SPECIFICITY.
[3]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
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. expand/collapse author list , 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.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Ovary.
[6]"Calcium/calmodulin-dependent protein kinase II controls integrin alpha5beta1-mediated cell adhesion through the integrin cytoplasmic domain associated protein-1alpha."
Bouvard D., Block M.R.
Biochem. Biophys. Res. Commun. 252:46-50(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-38, MUTAGENESIS OF THR-38.
[7]"Interaction between krit1 and icap1alpha infers perturbation of integrin beta1-mediated angiogenesis in the pathogenesis of cerebral cavernous malformation."
Zhang J., Clatterbuck R.E., Rigamonti D., Chang D.D., Dietz H.C.
Hum. Mol. Genet. 10:2953-2960(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ITGB1 AND KRIT1.
[8]"KRIT1 association with the integrin-binding protein ICAP-1: a new direction in the elucidation of cerebral cavernous malformations (CCM1) pathogenesis."
Zawistowski J.S., Serebriiskii I.G., Lee M.F., Golemis E.A., Marchuk D.A.
Hum. Mol. Genet. 11:389-396(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KRIT1.
[9]"Molecular basis for interaction between Icap1alpha PTB domain and beta 1 integrin."
Chang D.D., Hoang B.Q., Liu J., Springer T.A.
J. Biol. Chem. 277:8140-8145(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ITGB1, MUTAGENESIS OF THR-38; LEU-82; LEU-86; LEU-135; ILE-138; ILE-139 AND TYR-144, 3D-STRUCTURE MODELING.
[10]"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."
Fournier H.N., Dupe-Manet S., Bouvard D., Lacombe M.L., Marie C., Block M.R., Albiges-Rizo C.
J. Biol. Chem. 277:20895-20902(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH NME2, SUBCELLULAR LOCATION.
[11]"The integrin cytoplasmic domain-associated protein ICAP-1 binds and regulates Rho family GTPases during cell spreading."
Degani S., Balzac F., Brancaccio M., Guazzone S., Retta S.F., Silengo L., Eva A., Tarone G.
J. Cell Biol. 156:377-387(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CDC42; ITGB1 AND RAC1.
[12]"Disruption of focal adhesions by integrin cytoplasmic domain-associated protein-1 alpha."
Bouvard D., Vignoud L., Dupe-Manet S., Abed N., Fournier H.N., Vincent-Monegat C., Retta S.F., Fassler R., Block M.R.
J. Biol. Chem. 278:6567-6574(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ITGB1, SUBCELLULAR LOCATION.
[13]"An unappreciated role for RNA surveillance."
Hillman R.T., Green R.E., Brenner S.E.
Genome Biol. 5:R8.1-R8.16(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
[14]"Nuclear translocation of integrin cytoplasmic domain-associated protein 1 stimulates cellular proliferation."
Fournier H.N., Dupe-Manet S., Bouvard D., Luton F., Degani S., Block M.R., Retta S.F., Albiges-Rizo C.
Mol. Biol. Cell 16:1859-1871(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF 6-LYS-LYS-7 AND ILE-138.
[15]"Krit 1 interactions with microtubules and membranes are regulated by Rap1 and integrin cytoplasmic domain associated protein-1."
Beraud-Dufour S., Gautier R., Albiges-Rizo C., Chardin P., Faurobert E.
FEBS J. 274:5518-5532(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH KRIT1 AND RAP1A, INTERACTION WITH KRIT1.
[16]"Integrin cytoplasmic domain-associated protein-1 attenuates sprouting angiogenesis."
Brutsch R., Liebler S.S., Wustehube J., Bartol A., Herberich S.E., Adam M.G., Telzerow A., Augustin H.G., Fischer A.
Circ. Res. 107:592-601(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[17]"Osteoblast mineralization requires beta1 integrin/ICAP-1-dependent fibronectin deposition."
Brunner M., Millon-Fremillon A., Chevalier G., Nakchbandi I.A., Mosher D., Block M.R., Albiges-Rizo C., Bouvard D.
J. Cell Biol. 194:307-322(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ITGB1 AND FERMT2.
[18]"Mechanism for KRIT1 release of ICAP1-mediated suppression of integrin activation."
Liu W., Draheim K.M., Zhang R., Calderwood D.A., Boggon T.J.
Mol. Cell 0:0-0(2013)
Cited for: X-RAY CRYSTALLOGRAPHY (2.54 ANGSTROMS) OF 49-200 IN COMPLEXES WITH KRIT1 AND ITGB1, FUNCTION, INTERACTION WITH KRIT1 AND ITGB1, MUTAGENESIS OF ILE-89; ASP-93; GLN-96; 135-LEU--ILE-139 AND CYS-184.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF012023 mRNA. Translation: AAB88671.1.
AF012024 mRNA. Translation: AAB88672.1.
CH471053 Genomic DNA. Translation: EAX00992.1.
CH471053 Genomic DNA. Translation: EAX00995.1.
CH471053 Genomic DNA. Translation: EAX01000.1.
CH471053 Genomic DNA. Translation: EAX01001.1.
AC080162 Genomic DNA. Translation: AAY14857.1.
CH471053 Genomic DNA. Translation: EAX00993.1.
CH471053 Genomic DNA. Translation: EAX00997.1.
BC012264 mRNA. Translation: AAH12264.1.
CCDSCCDS1662.1. [O14713-1]
CCDS1663.1. [O14713-2]
RefSeqNP_004754.1. NM_004763.3. [O14713-1]
NP_071729.1. NM_022334.3. [O14713-2]
XP_005246240.1. XM_005246183.2. [O14713-1]
XP_005246241.1. XM_005246184.2. [O14713-1]
XP_005246242.1. XM_005246185.2. [O14713-1]
XP_005246243.1. XM_005246186.2. [O14713-1]
XP_005246244.1. XM_005246187.2. [O14713-1]
XP_005246246.1. XM_005246189.2. [O14713-2]
XP_006711966.1. XM_006711903.1. [O14713-1]
UniGeneHs.467662.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1K11model-A58-196[»]
4DX8X-ray2.54A/B/D/E49-200[»]
4DX9X-ray3.000/1/2/3/4/5/A/C/E/G/I/K/M/O/Q/S/U/W/Y/a/c/e/g/i/k/m/o/q/s/u/w/y49-200[»]
4JIFX-ray1.70A49-200[»]
ProteinModelPortalO14713.
SMRO14713. Positions 55-196.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114689. 10 interactions.
IntActO14713. 7 interactions.
STRING9606.ENSP00000347504.

PTM databases

PhosphoSiteO14713.

Proteomic databases

MaxQBO14713.
PaxDbO14713.
PRIDEO14713.

Protocols and materials databases

DNASU9270.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000238091; ENSP00000238091; ENSG00000119185. [O14713-2]
ENST00000355346; ENSP00000347504; ENSG00000119185. [O14713-1]
ENST00000360635; ENSP00000353850; ENSG00000119185. [O14713-1]
ENST00000488451; ENSP00000419524; ENSG00000119185. [O14713-2]
GeneID9270.
KEGGhsa:9270.
UCSCuc002qzj.3. human. [O14713-1]
uc002qzk.3. human. [O14713-2]

Organism-specific databases

CTD9270.
GeneCardsGC02M009496.
HGNCHGNC:23927. ITGB1BP1.
MIM607153. gene.
neXtProtNX_O14713.
PharmGKBPA134913590.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG45114.
HOGENOMHOG000015089.
HOVERGENHBG052155.
InParanoidO14713.
OMARMLCYDD.
OrthoDBEOG7WT447.
PhylomeDBO14713.
TreeFamTF105393.

Gene expression databases

ArrayExpressO14713.
BgeeO14713.
CleanExHS_ITGB1BP1.
GenevestigatorO14713.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
InterProIPR019517. Integrin-bd_ICAP-1.
IPR011993. PH_like_dom.
IPR006020. PTB/PI_dom.
[Graphical view]
PfamPF10480. ICAP-1_inte_bdg. 1 hit.
[Graphical view]
SMARTSM00462. PTB. 1 hit.
[Graphical view]
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Other

ChiTaRSITGB1BP1. human.
GeneWikiITGB1BP1.
GenomeRNAi9270.
NextBio34745.
PROO14713.
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Entry information

Entry nameITBP1_HUMAN
AccessionPrimary (citable) accession number: O14713
Secondary accession number(s): D6W4Y9, O14714, Q53RS0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM