DNAJB2

Protein-coding gene in the species Homo sapiens
DNAJB2
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2LGW

Identifiers
AliasesDNAJB2, DSMA5, HSJ-1, HSJ1, HSPF3, CMT2T, DnaJ heat shock protein family (Hsp40) member B2
External IDsOMIM: 604139; MGI: 1928739; HomoloGene: 4902; GeneCards: DNAJB2; OMA:DNAJB2 - orthologs
Gene location (Human)
Chromosome 2 (human)
Chr.Chromosome 2 (human)[1]
Chromosome 2 (human)
Genomic location for DNAJB2
Genomic location for DNAJB2
Band2q35Start219,279,342 bp[1]
End219,286,898 bp[1]
Gene location (Mouse)
Chromosome 1 (mouse)
Chr.Chromosome 1 (mouse)[2]
Chromosome 1 (mouse)
Genomic location for DNAJB2
Genomic location for DNAJB2
Band1|1 C4Start75,236,406 bp[2]
End75,245,692 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • C1 segment

  • right hemisphere of cerebellum

  • right frontal lobe

  • anterior pituitary

  • amygdala

  • cingulate gyrus

  • anterior cingulate cortex

  • prefrontal cortex

  • Brodmann area 9

  • tibial nerve
Top expressed in
  • motor neuron

  • lens

  • spermatid

  • neural layer of retina

  • supraoptic nucleus

  • retinal pigment epithelium

  • spermatocyte

  • muscle of thigh

  • aortic valve

  • blood
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • polyubiquitin modification-dependent protein binding
  • proteasome binding
  • chaperone binding
  • protein binding
  • ubiquitin protein ligase binding
  • ATPase activator activity
  • Hsp70 protein binding
  • unfolded protein binding
  • ubiquitin binding
  • ubiquitin-dependent protein binding
Cellular component
  • inclusion body
  • proteasome complex
  • cytosol
  • nucleus
  • cytoplasm
  • endoplasmic reticulum
  • endoplasmic reticulum membrane
  • membrane
  • intrinsic component of endoplasmic reticulum membrane
  • nuclear membrane
Biological process
  • response to unfolded protein
  • negative regulation of protein deubiquitination
  • positive regulation of protein ubiquitination
  • positive regulation of proteasomal ubiquitin-dependent protein catabolic process
  • ubiquitin-dependent ERAD pathway
  • protein refolding
  • negative regulation of inclusion body assembly
  • regulation of protein localization
  • regulation of protein ubiquitination
  • negative regulation of protein binding
  • positive regulation of ATP-dependent activity
  • proteasome-mediated ubiquitin-dependent protein catabolic process
  • chaperone-mediated protein folding
  • regulation of chaperone-mediated protein folding
  • negative regulation of cell population proliferation
  • negative regulation of cell growth
  • neuron cellular homeostasis
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

3300

56812

Ensembl

ENSG00000135924

ENSMUSG00000026203

UniProt

P25686

Q9QYI5

RefSeq (mRNA)

NM_006736
NM_001039550

NM_001159883
NM_001159884
NM_001159885
NM_020266
NM_178055

RefSeq (protein)

NP_001034639
NP_006727

NP_001153355
NP_001153356
NP_001153357
NP_064662
NP_835156

Location (UCSC)Chr 2: 219.28 – 219.29 MbChr 1: 75.24 – 75.25 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

DnaJ homolog subfamily B member 2 is a protein that in humans is encoded by the DNAJB2 gene.[5][6][7]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000135924 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000026203 – 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. ^ Cheetham ME, Brion JP, Anderton BH (Jul 1992). "Human homologues of the bacterial heat-shock protein DnaJ are preferentially expressed in neurons". Biochem J. 284 ( Pt 2) (Pt 2): 469–76. doi:10.1042/bj2840469. PMC 1132662. PMID 1599432.
  6. ^ Chapple JP, Hardcastle AJ, Kurzik-Dumke U, Collier DA, Cheetham ME (Oct 1999). "Assignment of the neuronal cochaperone, HSJ1, to human chromosome bands 2q32→q34 between D2S295 and D2S339 by in situ hybridization and somatic cell and radiation hybrids". Cytogenet Cell Genet. 86 (1): 62–3. doi:10.1159/000015411. PMID 10516435. S2CID 46545726.
  7. ^ "Entrez Gene: DNAJB2 DnaJ (Hsp40) homolog, subfamily B, member 2".

Further reading

  • Bonaldo 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.
  • Ohtsuka K, Hata M (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 2024-03-28). PMC 312896. PMID 11147971.{{cite journal}}: CS1 maint: DOI inactive as of March 2024 (link)
  • Wistow G, Bernstein SL, Wyatt MK (2002). "Expressed sequence tag analysis of human RPE/choroid for the NEIBank Project: over 6000 non-redundant transcripts, novel genes and splice variants". Mol. Vis. 8: 205–20. PMID 12107410.
  • Strausberg RL, Feingold EA, Grouse LH (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.
  • Chapple JP, Cheetham ME (2003). "The chaperone environment at the cytoplasmic face of the endoplasmic reticulum can modulate rhodopsin processing and inclusion formation". J. Biol. Chem. 278 (21): 19087–94. doi:10.1074/jbc.M212349200. PMID 12754272.
  • Janket ML, Manickam P, Majumder B (2004). "Differential regulation of host cellular genes by HIV-1 viral protein R (Vpr): cDNA microarray analysis using isogenic virus". Biochem. Biophys. Res. Commun. 314 (4): 1126–32. doi:10.1016/j.bbrc.2004.01.008. PMID 14751250.
  • Hillman RT, Green RE, Brenner SE (2005). "An unappreciated role for RNA surveillance". Genome Biol. 5 (2): R8. doi:10.1186/gb-2004-5-2-r8. PMC 395752. PMID 14759258.
  • Colland F, Jacq X, Trouplin V (2004). "Functional Proteomics Mapping of a Human Signaling Pathway". Genome Res. 14 (7): 1324–32. doi:10.1101/gr.2334104. PMC 442148. PMID 15231748.
  • Gerhard DS, Wagner L, Feingold EA (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.
  • Westhoff B, Chapple JP, van der Spuy J (2005). "HSJ1 is a neuronal shuttling factor for the sorting of chaperone clients to the proteasome". Curr. Biol. 15 (11): 1058–64. Bibcode:2005CBio...15.1058W. doi:10.1016/j.cub.2005.04.058. PMID 15936278. S2CID 8599003.
  • Rual JF, Venkatesan K, Hao T (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.
  • Borrell-Pagès M, Canals JM, Cordelières FP (2006). "Cystamine and cysteamine increase brain levels of BDNF in Huntington disease via HSJ1b and transglutaminase" (PDF). J. Clin. Invest. 116 (5): 1410–24. doi:10.1172/JCI27607. PMC 1430359. PMID 16604191.
  • Adaimy L, Chouery E, Megarbane H (2007). "Mutation in WNT10A Is Associated with an Autosomal Recessive Ectodermal Dysplasia: The Odonto-onycho-dermal Dysplasia". Am. J. Hum. Genet. 81 (4): 821–8. doi:10.1086/520064. PMC 1973944. PMID 17847007.
  • 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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