PARVA

From Wikipedia, the free encyclopedia


Parvin, alpha
Identifiers
Symbol(s) PARVA; FLJ10793; FLJ12254; MXRA2
External IDs OMIM: 608120 MGI1931144 HomoloGene10077
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 55742 57342
Ensembl ENSG00000197702 ENSMUSG00000030770
Uniprot Q9NVD7 Q3UF75
Refseq NM_018222 (mRNA)
NP_060692 (protein)
NM_020606 (mRNA)
NP_065631 (protein)
Location Chr 11: 12.36 - 12.51 Mb Chr 7: 112.22 - 112.38 Mb
Pubmed search [1] [2]

Alpha parvin, also known as PARVA, is a human gene.[1]

Members of the parvin family, including PARVA, are actin-binding proteins associated with focal contacts.[supplied by OMIM][1]

[edit] References

[edit] 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. PMID 11134073. 
  • Olski TM, Noegel AA, Korenbaum E (2001). "Parvin, a 42 kDa focal adhesion protein, related to the alpha-actinin superfamily.". J. Cell. Sci. 114 (Pt 3): 525–38. PMID 11171322. 
  • 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. 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. 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. 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. 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. 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. 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. 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: 89. doi:10.1038/msb4100134. PMID 17353931.