DNAJB2

DNAJB2
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2LGW
Identifiers
Aliases	DNAJB2, DSMA5, HSJ-1, HSJ1, HSPF3, CMT2T, DnaJ heat shock protein family (Hsp40) member B2
External IDs	OMIM: 604139 MGI: 1928739 HomoloGene: 4902 GeneCards: DNAJB2
Gene location (Human)
Chr.	Chromosome 2 (human)[1]
End	219,286,898 bp[1]
Gene location (Mouse)
Chr.	Chromosome 1 (mouse)[2]
End	75,245,692 bp[2]
RNA expression pattern
	Top expressed in
	anterior pituitary; ; amygdala; ; cingulate gyrus; ; prefrontal cortex; ; Brodmann area 9; ; tibial nerve; ; nucleus accumbens; ; right adrenal gland; ; corpus callosum; ; hypothalamus;
	Top expressed in
	motor neuron; ; mirror; ; spermatid; ; supraoptic nucleus; ; retinal pigment epithelium; ; spermatocyte; ; aortic valve; ; blood; ; suprachiasmatic nucleus; ; ciliary body;
	More reference expression data
	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
	3300
	56812
	ENSG00000135924
	ENSMUSG00000026203
	P25686
	Q9QYI5
	NM_006736; NM_001039550
	NM_001159883; NM_001159884; NM_001159885; NM_020266; NM_178055
	NP_001034639; NP_006727
	NP_001153355; NP_001153356; NP_001153357; NP_064662; NP_835156
	Wikidata
View/Edit Human	View/Edit Mouse

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

References

GRCh38: Ensembl release 89: ENSG00000135924 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000026203 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
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.
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.
"Entrez Gene: DNAJB2 DnaJ (Hsp40) homolog, subfamily B, member 2".

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. PMC 312896. PMID 11147971.
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. 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.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000135924 - Ensembl, May 2017

[refGRCm38Ensembl-2] 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.

[pmid1599432-5] 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.

[pmid10516435-6] 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.

[entrez-7] "Entrez Gene: DNAJB2 DnaJ (Hsp40) homolog, subfamily B, member 2".

DNAJB2

References

Further reading