PARVA

PARVA
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2K2R, 2VZC, 2VZD, 2VZG, 2VZI, 3KMU, 3KMW, 3REP
Identifiers
Aliases	PARVA, CH-ILKBP, MXRA2, parvin alpha
External IDs	MGI: 1931144 HomoloGene: 10077 GeneCards: PARVA
Gene ontology Molecular function • protein binding • actin binding • cadherin binding involved in cell-cell adhesion Cellular component • cytoplasm • cytosol • membrane • plasma membrane • cell junction • Z disc • cytoskeleton • focal adhesion • cell-cell adherens junction • actin cytoskeleton Biological process • actin cytoskeleton reorganization • cilium morphogenesis • smooth muscle cell chemotaxis • heterotypic cell-cell adhesion • sprouting angiogenesis • outflow tract septum morphogenesis • establishment or maintenance of cell polarity • chemotaxis • actin-mediated cell contraction • cell adhesion • cell projection organization • angiogenesis • regulation of cell shape • substrate adhesion-dependent cell spreading Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	55742	57342
Ensembl	ENSG00000197702	ENSMUSG00000030770
UniProt	Q9NVD7	Q9EPC1
RefSeq (mRNA)	NM_018222	NM_020606
RefSeq (protein)	NP_060692.2	NP_065631.3
Location (UCSC)	Chr 11: 12.38 – 12.53 Mb	Chr 7: 112.43 – 112.59 Mb
PubMed search	[1]	[2]
Wikidata

View/Edit Human

View/Edit Mouse

Alpha-parvin is a protein that in humans is encoded by the PARVA gene.^[3][4]

Members of the parvin family, including PARVA, PARVB and PARVG, are actin-binding proteins associated with focal contacts.[supplied by OMIM]^[4]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. Olski TM, Noegel AA, Korenbaum E (Feb 2001). "Parvin, a 42 kDa focal adhesion protein, related to the alpha-actinin superfamily". J Cell Sci. 114 (Pt 3): 525–38. PMID 11171322.
4. "Entrez Gene: PARVA parvin, alpha".

Further reading

• Nikolopoulos SN, Turner CE (2001). "Actopaxin, a new focal adhesion protein that binds paxillin LD motifs and actin and regulates cell adhesion.". J. Cell Biol. 151 (7): 1435–48. doi:10.1083/jcb.151.7.1435. PMC 2150668. PMID 11134073.
• Tu Y, Huang Y, Zhang Y, et al. (2001). "A new focal adhesion protein that interacts with integrin-linked kinase and regulates cell adhesion and spreading.". J. Cell Biol. 153 (3): 585–98. doi:10.1083/jcb.153.3.585. PMC 2190577. PMID 11331308.
• Nikolopoulos SN, Turner CE (2002). "Molecular dissection of actopaxin-integrin-linked kinase-Paxillin interactions and their role in subcellular localization.". J. Biol. Chem. 277 (2): 1568–75. doi:10.1074/jbc.M108612200. PMID 11694518.
• Korenbaum E, Olski TM, Noegel AA (2002). "Genomic organization and expression profile of the parvin family of focal adhesion proteins in mice and humans.". Gene. 279 (1): 69–79. doi:10.1016/S0378-1119(01)00743-0. PMID 11722847.
• Zhang Y, Chen K, Tu Y, et al. (2003). "Assembly of the PINCH-ILK-CH-ILKBP complex precedes and is essential for localization of each component to cell-matrix adhesion sites.". J. Cell. Sci. 115 (Pt 24): 4777–86. doi:10.1242/jcs.00166. PMID 12432066.
• 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. 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.
• Aboulaich N, Vainonen JP, Strålfors P, Vener AV (2005). "Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes.". Biochem. J. 383 (Pt 2): 237–48. doi:10.1042/BJ20040647. PMC 1134064. PMID 15242332.
• Zhang Y, Chen K, Tu Y, Wu C (2004). "Distinct roles of two structurally closely related focal adhesion proteins, alpha-parvins and beta-parvins, in regulation of cell morphology and survival.". J. Biol. Chem. 279 (40): 41695–705. doi:10.1074/jbc.M401563200. PMID 15284246.
• Clarke DM, Brown MC, LaLonde DP, Turner CE (2004). "Phosphorylation of actopaxin regulates cell spreading and migration.". J. Cell Biol. 166 (6): 901–12. doi:10.1083/jcb.200404024. PMC 2172128. PMID 15353548.
• 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.
• LaLonde DP, Brown MC, Bouverat BP, Turner CE (2005). "Actopaxin interacts with TESK1 to regulate cell spreading on fibronectin.". J. Biol. Chem. 280 (22): 21680–8. doi:10.1074/jbc.M500752200. PMID 15817463.
• 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. doi:10.1038/nature04209. PMID 16189514.
• Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry.". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.