ITGB1BP1

ITGB1BP1
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	4DX8, 4DX9, 4JIF
Identifiers
Aliases	ITGB1BP1, ICAP-1A, ICAP-1B, ICAP-1alpha, ICAP1, ICAP1A, ICAP1B, integrin subunit beta 1 binding protein 1
External IDs	MGI: 1306802 HomoloGene: 3496 GeneCards: ITGB1BP1
Gene location (Human)
Chr.	Chromosome 2 (human)[1]
End	9,423,547 bp[1]
Gene location (Mouse)
Chr.	Chromosome 12 (mouse)[2]
End	21,286,284 bp[2]
RNA expression pattern
	; ;
	More reference expression data
Gene ontology
Molecular function	• protein transporter activity; • integrin binding; • kinase binding; • protein binding; • GDP-dissociation inhibitor activity; • protein kinase binding; • macromolecular complex binding;
Cellular component	• cytoplasm; • cytosol; • cell projection; • membrane; • focal adhesion; • ruffle; • plasma membrane; • perinuclear region of cytoplasm; • cytoskeleton; • cell nucleus; • lamellipodium; • cell periphery; • nucleoplasm; • microtubule organizing center; • nuclear body;
Biological process	• Notch signaling pathway; • positive regulation of protein targeting to membrane; • cell differentiation; • activation of protein kinase B activity; • myoblast migration; • negative regulation of fibroblast migration; • regulation of cell adhesion mediated by integrin; • intracellular signal transduction; • regulation of blood vessel size; • positive regulation of protein kinase B signaling; • regulation of transcription, DNA-templated; • negative regulation of protein kinase activity; • regulation of GTPase activity; • biomineral tissue development; • negative regulation of protein binding; • cellular response to fibroblast growth factor stimulus; • receptor clustering; • blood vessel endothelial cell proliferation involved in sprouting angiogenesis; • transcription, DNA-templated; • positive regulation of endothelial cell migration; • negative regulation of cell adhesion involved in substrate-bound cell migration; • negative regulation of cell migration involved in sprouting angiogenesis; • negative regulation of protein targeting to membrane; • tube formation; • regulation of integrin-mediated signaling pathway; • cell adhesion; • angiogenesis; • positive regulation of cell proliferation; • protein transport; • integrin-mediated signaling pathway; • negative regulation of ERK1 and ERK2 cascade; • positive regulation of focal adhesion assembly; • cellular response to vascular endothelial growth factor stimulus; • integrin activation; • cell-matrix adhesion; • negative regulation of substrate adhesion-dependent cell spreading; • cell migration; • negative regulation of focal adhesion assembly; • positive regulation of cell division; • positive regulation of stress fiber assembly; • positive regulation of Notch signaling pathway; • negative regulation of cell proliferation; • positive regulation of transcription from RNA polymerase II promoter;
	Sources:Amigo / QuickGO
Orthologs
	9270
	16413
	ENSG00000119185
	ENSMUSG00000062352
	O14713
	O35671
NM_004763; NM_022334; NM_001319066; NM_001319067; NM_001319068;
	NM_001319069; NM_001319070
	NM_008403; NM_001355609
NP_001305995; NP_001305996; NP_001305997; NP_001305998; NP_001305999;
	NP_004754; NP_071729
	NP_032429; NP_001342538
	Wikidata
View/Edit Human	View/Edit Mouse

Integrin beta-1-binding protein 1 is a protein that in humans is encoded by the ITGB1BP1 gene.^[5]^[6]^[7]

The cytoplasmic domains of integrins are essential for cell adhesion. The protein encoded by this gene binds to the beta1 integrin cytoplasmic domain. The interaction between this protein and beta1 integrin is highly specific. Two isoforms of this protein are derived from alternatively spliced transcripts. The shorter form of this protein does not interact with the beta1 integrin cytoplasmic domain. The longer form is a phosphoprotein and the extent of its phosphorylation is regulated by the cell-matrix interaction, suggesting an important role of this protein during integrin-dependent cell adhesion.^[7]

Interactions

ITGB1BP1 has been shown to interact with KRIT1,^[5]^[8] LRP2,^[9] CD29^[6]^[10] and LRP1.^[9]

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000119185 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000062352 - Ensembl, May 2017
↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
1 2 Zawistowski JS, Serebriiskii IG, Lee MF, Golemis EA, Marchuk DA (March 2002). "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 (4): 389–96. doi:10.1093/hmg/11.4.389. PMID 11854171.
1 2 Chang DD, Wong C, Smith H, Liu J (October 1997). "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 (5): 1149–57. doi:10.1083/jcb.138.5.1149. PMC 2136751. PMID 9281591.
1 2 "Entrez Gene: ITGB1BP1 integrin beta 1 binding protein 1".
↑ Zhang, J; Clatterbuck R E; Rigamonti D; Chang D D; Dietz H C (December 2001). "Interaction between krit1 and icap1alpha infers perturbation of integrin beta1-mediated angiogenesis in the pathogenesis of cerebral cavernous malformation". Hum. Mol. Genet. England. 10 (25): 2953–60. doi:10.1093/hmg/10.25.2953. ISSN 0964-6906. PMID 11741838.
1 2 Gotthardt, M; Trommsdorff M; Nevitt M F; Shelton J; Richardson J A; Stockinger W; Nimpf J; Herz J (August 2000). "Interactions of the low density lipoprotein receptor gene family with cytosolic adaptor and scaffold proteins suggest diverse biological functions in cellular communication and signal transduction". J. Biol. Chem. UNITED STATES. 275 (33): 25616–24. doi:10.1074/jbc.M000955200. ISSN 0021-9258. PMID 10827173.
↑ Chang, David D; Hoang Bao Q; Liu Jenny; Springer Timothy A (March 2002). "Molecular basis for interaction between Icap1 alpha PTB domain and beta 1 integrin". J. Biol. Chem. United States. 277 (10): 8140–5. doi:10.1074/jbc.M109031200. ISSN 0021-9258. PMID 11741908.

Andersson B, Wentland MA, Ricafrente JY, et al. (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
Yu W, Andersson B, Worley KC, et al. (1997). "Large-scale concatenation cDNA sequencing". Genome Res. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.
Bouvard D, Block MR (1998). "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 (1): 46–50. doi:10.1006/bbrc.1998.9592. PMID 9813144.
Gotthardt M, Trommsdorff M, Nevitt MF, et al. (2000). "Interactions of the low density lipoprotein receptor gene family with cytosolic adaptor and scaffold proteins suggest diverse biological functions in cellular communication and signal transduction". J. Biol. Chem. 275 (33): 25616–24. doi:10.1074/jbc.M000955200. PMID 10827173.
Zhang J, Clatterbuck RE, Rigamonti D, et al. (2002). "Interaction between krit1 and icap1alpha infers perturbation of integrin beta1-mediated angiogenesis in the pathogenesis of cerebral cavernous malformation". Hum. Mol. Genet. 10 (25): 2953–60. doi:10.1093/hmg/10.25.2953. PMID 11741838.
Chang DD, Hoang BQ, Liu J, Springer TA (2002). "Molecular basis for interaction between Icap1 alpha PTB domain and beta 1 integrin". J. Biol. Chem. 277 (10): 8140–5. doi:10.1074/jbc.M109031200. PMID 11741908.
Fournier HN, Dupé-Manet S, Bouvard D, et al. (2002). "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 (23): 20895–902. doi:10.1074/jbc.M200200200. PMID 11919189.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Hillman RT, Green RE, Brenner SE (2005). "An unappreciated role for RNA surveillance". Genome Biol. 5 (2): R8. doi:10.1186/gb-2004-5-2-r8. PMC 395752. PMID 14759258.
Xia H, Nho RS, Kahm J, et al. (2004). "Focal adhesion kinase is upstream of phosphatidylinositol 3-kinase/Akt in regulating fibroblast survival in response to contraction of type I collagen matrices via a beta 1 integrin viability signaling pathway". J. Biol. Chem. 279 (31): 33024–34. doi:10.1074/jbc.M313265200. PMID 15166238.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Fournier HN, Dupé-Manet S, Bouvard D, et al. (2005). "Nuclear translocation of integrin cytoplasmic domain-associated protein 1 stimulates cellular proliferation". Mol. Biol. Cell. 16 (4): 1859–71. doi:10.1091/mbc.E04-08-0744. PMC 1073667. PMID 15703214.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514.
Oh JH, Yang JO, Hahn Y, et al. (2006). "Transcriptome analysis of human gastric cancer". Mamm. Genome. 16 (12): 942–54. doi:10.1007/s00335-005-0075-2. PMID 16341674.
Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
Stroeken PJ, Alvarez B, Van Rheenen J, et al. (2006). "Integrin cytoplasmic domain-associated protein-1 (ICAP-1) interacts with the ROCK-I kinase at the plasma membrane". J. Cell. Physiol. 208 (3): 620–8. doi:10.1002/jcp.20699. PMID 16741948.
Furusu A, Nakayama K, Xu Q, et al. (2007). "MAP kinase-dependent, NF-kappaB-independent regulation of inhibitor of apoptosis protein genes by TNF-alpha". J. Cell. Physiol. 210 (3): 703–10. doi:10.1002/jcp.20881. PMID 17133355.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000119185 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000062352 - Ensembl, May 2017

[3] "Human PubMed Reference:".

[4] "Mouse PubMed Reference:".

[pmid11854171-5] 1 2 Zawistowski JS, Serebriiskii IG, Lee MF, Golemis EA, Marchuk DA (March 2002). "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 (4): 389–96. doi:10.1093/hmg/11.4.389. PMID 11854171.

[pmid9281591-6] 1 2 Chang DD, Wong C, Smith H, Liu J (October 1997). "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 (5): 1149–57. doi:10.1083/jcb.138.5.1149. PMC 2136751. PMID 9281591.

[entrez-7] 1 2 "Entrez Gene: ITGB1BP1 integrin beta 1 binding protein 1".

[pmid11741838-8] Zhang, J; Clatterbuck R E; Rigamonti D; Chang D D; Dietz H C (December 2001). "Interaction between krit1 and icap1alpha infers perturbation of integrin beta1-mediated angiogenesis in the pathogenesis of cerebral cavernous malformation". Hum. Mol. Genet. England. 10 (25): 2953–60. doi:10.1093/hmg/10.25.2953. ISSN 0964-6906. PMID 11741838.

[pmid10827173-9] 1 2 Gotthardt, M; Trommsdorff M; Nevitt M F; Shelton J; Richardson J A; Stockinger W; Nimpf J; Herz J (August 2000). "Interactions of the low density lipoprotein receptor gene family with cytosolic adaptor and scaffold proteins suggest diverse biological functions in cellular communication and signal transduction". J. Biol. Chem. UNITED STATES. 275 (33): 25616–24. doi:10.1074/jbc.M000955200. ISSN 0021-9258. PMID 10827173.

[pmid11741908-10] Chang, David D; Hoang Bao Q; Liu Jenny; Springer Timothy A (March 2002). "Molecular basis for interaction between Icap1 alpha PTB domain and beta 1 integrin". J. Biol. Chem. United States. 277 (10): 8140–5. doi:10.1074/jbc.M109031200. ISSN 0021-9258. PMID 11741908.

ITGB1BP1

Interactions

References

Further reading