PARVA

For other uses, see Parva.

Alpha-parvin is a protein that in humans is encoded by the PARVA gene.

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	OMIM: 608120; MGI: 1931144; HomoloGene: 10077; GeneCards: PARVA; OMA:PARVA - orthologs
Gene location (Human) Chr. Chromosome 11 (human) Band 11p15.3 Start 12,377,563 bp End 12,535,356 bp
Gene location (Mouse) Chr. Chromosome 7 (mouse) Band 7|7 F1 Start 112,026,712 bp End 112,190,899 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in smooth muscle tissue stromal cell of endometrium epithelium of colon myometrium muscle layer of sigmoid colon saphenous vein gastric mucosa glomerulus tail of epididymis metanephric glomerulus Top expressed in superior cervical ganglion sciatic nerve umbilical cord uterus carotid body Epithelium of choroid plexus external carotid artery olfactory epithelium right lung lobe tunica media of zone of aorta More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein binding actin binding cadherin binding Cellular component cytoplasm cytosol membrane plasma membrane cell junction Z discdkac cytoskeleton focal adhesion actin cytoskeleton nucleus lamellipodium Biological process actin cytoskeleton reorganization cilium assembly 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 cell projection assembly Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 55742 57342 Ensembl ENSG00000197702 ENSMUSG00000030770 UniProt Q9NVD7 Q9EPC1 RefSeq (mRNA) NM_018222 NM_020606 RefSeq (protein) NP_060692 NP_065631 Location (UCSC) Chr 11: 12.38 – 12.54 Mb Chr 7: 112.03 – 112.19 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

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

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. S2CID 13630628.
• 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.
• 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. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
• 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.