DNAJA2

Protein-coding gene in the species Homo sapiens
DNAJA2
Identifiers
AliasesDNAJA2, CPR3, DJ3, DJA2, DNAJ, DNJ3, HIRIP4, PRO3015, RDJ2, DnaJ heat shock protein family (Hsp40) member A2
External IDsOMIM: 611322 MGI: 1931882 HomoloGene: 21193 GeneCards: DNAJA2
Gene location (Human)
Chromosome 16 (human)
Chr.Chromosome 16 (human)[1]
Chromosome 16 (human)
Genomic location for DNAJA2
Genomic location for DNAJA2
Band16q11.2Start46,955,362 bp[1]
End46,973,674 bp[1]
Gene location (Mouse)
Chromosome 8 (mouse)
Chr.Chromosome 8 (mouse)[2]
Chromosome 8 (mouse)
Genomic location for DNAJA2
Genomic location for DNAJA2
Band8|8 C3Start86,264,262 bp[2]
End86,281,973 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • Achilles tendon

  • gastrocnemius muscle

  • endothelial cell

  • sperm

  • germinal epithelium

  • prefrontal cortex

  • retinal pigment epithelium

  • monocyte

  • left ventricle

  • islet of Langerhans
Top expressed in
  • triceps brachii muscle

  • sternocleidomastoid muscle

  • medial ganglionic eminence

  • temporal muscle

  • digastric muscle

  • urothelium

  • abdominal wall

  • atrioventricular valve

  • primitive streak

  • calvaria
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • unfolded protein binding
  • chaperone binding
  • protein binding
  • ATP binding
  • heat shock protein binding
  • metal ion binding
  • ATPase activator activity
Cellular component
  • extracellular exosome
  • membrane
  • cytosol
Biological process
  • response to heat
  • protein folding
  • protein refolding
  • positive regulation of cell population proliferation
  • positive regulation of ATP-dependent activity
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

10294

56445

Ensembl

ENSG00000069345

ENSMUSG00000031701

UniProt

O60884

Q9QYJ0

RefSeq (mRNA)

NM_005880

NM_019794

RefSeq (protein)

NP_005871

NP_062768

Location (UCSC)Chr 16: 46.96 – 46.97 MbChr 8: 86.26 – 86.28 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

DnaJ homolog subfamily A member 2 is a protein that in humans is encoded by the DNAJA2 gene.[5][6][7]

The protein encoded by this gene shares sequence similarity with Hir1p and Hir2p, the two corepressors of histone gene transcription characterized in the yeast, Saccharomyces cerevisiae. The structural features of this protein suggest that it may function as part of a multiprotein complex. Several cDNAs encoding interacting proteins, HIRIPs, have been identified. HIRIP4 was isolated by virtue of its interaction with this protein; however, its exact function is not known. The sequence of HIRIP4 protein is highly homologous to the human DNJ3/CPR3, mouse Dj3 and rat Dj2 gene products.[7]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000069345 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000031701 – 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. ^ Lorain S, Quivy JP, Monier-Gavelle F, Scamps C, Lecluse Y, Almouzni G, Lipinski M (Sep 1998). "Core histones and HIRIP3, a novel histone-binding protein, directly interact with WD repeat protein HIRA". Mol Cell Biol. 18 (9): 5546–56. doi:10.1128/MCB.18.9.5546. PMC 109139. PMID 9710638.
  6. ^ Ohtsuka K, Hata M (Jan 2001). "Mammalian HSP40/DNAJ homologs: cloning of novel cDNAs and a proposal for their classification and nomenclature". Cell Stress & Chaperones. 5 (2): 98–112. doi:10.1379/1466-1268(2000)005<0098:mhdhco>2.0.co;2 (inactive 2024-03-06). ISSN 1466-1268. PMC 312896. PMID 11147971.{{cite journal}}: CS1 maint: DOI inactive as of March 2024 (link)
  7. ^ a b "Entrez Gene: DNAJA2 DnaJ (Hsp40) homolog, subfamily A, member 2".

Further reading

  • Bonwaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
  • Edwards MC, Liegeois N, Horecka J, et al. (1998). "Human CPR (cell cycle progression restoration) genes impart a Far- phenotype on yeast cells". Genetics. 147 (3): 1063–76. doi:10.1093/genetics/147.3.1063. PMC 1208234. PMID 9383053.
  • Scanlan MJ, Gordan JD, Williamson B, et al. (1999). "Antigens recognized by autologous antibody in patients with renal-cell carcinoma". Int. J. Cancer. 83 (4): 456–64. doi:10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5. PMID 10508479. S2CID 21839750.
  • Diefenbach J, Kindl H (2000). "The membrane-bound DnaJ protein located at the cytosolic site of glyoxysomes specifically binds the cytosolic isoform 1 of Hsp70 but not other Hsp70 species". Eur. J. Biochem. 267 (3): 746–54. doi:10.1046/j.1432-1327.2000.01053.x. PMID 10651811.
  • Terada K, Mori M (2000). "Human DnaJ homologs dj2 and dj3, and bag-1 are positive cochaperones of hsc70". J. Biol. Chem. 275 (32): 24728–34. doi:10.1074/jbc.M002021200. PMID 10816573.
  • 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.
  • Willingham S, Outeiro TF, DeVit MJ, et al. (2003). "Yeast genes that enhance the toxicity of a mutant huntingtin fragment or alpha-synuclein". Science. 302 (5651): 1769–72. Bibcode:2003Sci...302.1769W. doi:10.1126/science.1090389. PMID 14657499. S2CID 43221047.
  • Kho Y, Kim SC, Jiang C, et al. (2004). "A tagging-via-substrate technology for detection and proteomics of farnesylated proteins". Proc. Natl. Acad. Sci. U.S.A. 101 (34): 12479–84. Bibcode:2004PNAS..10112479K. doi:10.1073/pnas.0403413101. PMC 515085. PMID 15308774.
  • 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.
  • Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
  • Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983. S2CID 7827573.

External links

  • v
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Chaperones/
protein folding
Heat shock proteins/
Chaperonins
Other
Protein targetingUbiquitin
(ubiquitylation)Ubiquitin-like proteins
(UBL)
SUMO protein
(SUMOylation)
  • E1 SUMO-activating enzyme
  • E2 SUMO-conjugating enzyme
Other


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