DNAJB2

DnaJ (Hsp40) homolog, subfamily B, member 2
Identifiers
Symbols	DNAJB2; HSJ1; HSPF3
External IDs	OMIM: 604139 MGI: 1928739 HomoloGene: 4902 GeneCards: DNAJB2 Gene
Gene Ontology Molecular function • protein binding • Hsp70 protein binding • heat shock protein binding • polyubiquitin binding • unfolded protein binding • proteasome binding Cellular component • proteasome complex • inclusion body Biological process • protein folding • response to unfolded protein • negative regulation of cell proliferation • negative regulation of cell growth • ER-associated protein catabolic process • positive regulation of protein ubiquitination • positive regulation of proteasomal ubiquitin-dependent protein catabolic process • negative regulation of inclusion body assembly • negative regulation of protein deubiquitination Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	3300	56812
Ensembl	ENSG00000135924	ENSMUSG00000026203
UniProt	P25686	Q9QYI5
RefSeq (mRNA)	NM_001039550.1	NM_020266
RefSeq (protein)	NP_001034639.1	NP_064662
Location (UCSC)	Chr 2: 220.14 – 220.15 Mb	Chr 1: 75.23 – 75.24 Mb
PubMed search	[1]	[2]

DnaJ homolog subfamily B member 2 is a protein that in humans is encoded by the DNAJB2 gene.^[1][2][3]

References

1. ^ 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. PMC 1132662. PMID 1599432. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1132662. 
2. ^ 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. 
3. ^ "Entrez Gene: DNAJB2 DnaJ (Hsp40) homolog, subfamily B, member 2". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3300. 

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. PMC 312896. PMID 11147971. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=312896. 
• 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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=395752. 
• 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=442148. 
• 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928. 
• 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. 
• Rual JF, Venkatesan K, Hao T (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514. 
• Borrell-Pagès M, Canals JM, Cordelières FP (2006). "Cystamine and cysteamine increase brain levels of BDNF in Huntington disease via HSJ1b and transglutaminase". J. Clin. Invest. 116 (5): 1410–24. doi:10.1172/JCI27607. PMC 1430359. PMID 16604191. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1430359. 
• 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1973944.