PARVA

Protein-coding gene in the species Homo sapiens
PARVA
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2K2R, 2VZC, 2VZD, 2VZG, 2VZI, 3KMU, 3KMW, 3REP

Identifiers
AliasesPARVA, CH-ILKBP, MXRA2, parvin alpha
External IDsOMIM: 608120; MGI: 1931144; HomoloGene: 10077; GeneCards: PARVA; OMA:PARVA - orthologs
Gene location (Human)
Chromosome 11 (human)
Chr.Chromosome 11 (human)[1]
Chromosome 11 (human)
Genomic location for PARVA
Genomic location for PARVA
Band11p15.3Start12,377,563 bp[1]
End12,535,356 bp[1]
Gene location (Mouse)
Chromosome 7 (mouse)
Chr.Chromosome 7 (mouse)[2]
Chromosome 7 (mouse)
Genomic location for PARVA
Genomic location for PARVA
Band7|7 F1Start112,026,712 bp[2]
End112,190,899 bp[2]
RNA expression pattern
Bgee
HumanMouse (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

  • belly 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
SpeciesHumanMouse
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 MbChr 7: 112.03 – 112.19 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Alpha-parvin is a protein that in humans is encoded by the PARVA gene.[5][6]

Members of the parvin family, including PARVA, PARVB and PARVG, are actin-binding proteins associated with focal contacts.[supplied by OMIM][6]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000197702 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000030770 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ 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. doi:10.1242/jcs.114.3.525. PMID 11171322.
  6. ^ a b "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. 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.


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