PARVA

Parvin, alpha

Rendering based on PDB 2K2R.

Available structures
PDB	2K2R, 2VZC, 2VZD, 2VZG, 2VZI, 3KMU, 3KMW

Identifiers

PARVA; CH-ILKBP; FLJ10793; FLJ12254; FLJ25106; FLJ46049; MXRA2

External IDs

OMIM: 608120 MGI: 1931144 HomoloGene: 10077 GeneCards: PARVA Gene

Gene Ontology
Molecular function	• actin binding • protein binding
Cellular component	• cytoplasm • cytosol • cytosol • plasma membrane • focal adhesion • actin cytoskeleton • cell junction • protein complex
Biological process	• cell adhesion • cell projection organization • actin cytoskeleton organization • cell junction assembly • protein heterooligomerization • cilium morphogenesis
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

ENSG00000197702

ENSMUSG00000030770

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 11:
12.4 – 12.55 Mb

Chr 7:
119.57 – 119.74 Mb

PubMed search

Alpha-parvin is a protein that in humans is encoded by the PARVA gene.^[1]^[2]

Members of the parvin family, including PARVA, are actin-binding proteins associated with focal contacts.[supplied by OMIM]^[2]

References

^ 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.
^ ^a ^b "Entrez Gene: PARVA parvin, alpha". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=55742.

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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2150668.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2190577.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1134064.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2172128.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1847948.