DNAJB2

From Wikipedia, the free encyclopedia

DnaJ (Hsp40) homolog, subfamily B, member 2

Identifiers

DNAJB2; HSJ1; HSPF3

External IDs

OMIM: 604139 MGI: 1928739 HomoloGene: 4902

Gene ontology
Molecular Function:	• heat shock protein binding • unfolded protein binding
Biological Process:	• protein folding • response to unfolded protein

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001039550 (mRNA)
NP_001034639 (protein)

NM_020266 (mRNA)
NP_064662 (protein)

Location

Chr 2: 219.85 - 219.86 Mb

Chr 1: 75.12 - 75.13 Mb

Pubmed search

[1]

[2]

DnaJ (Hsp40) homolog, subfamily B, member 2, also known as DNAJB2, is a human gene.^[1]

[edit] References

^ Entrez Gene: DNAJB2 DnaJ (Hsp40) homolog, subfamily B, member 2.

[edit] Further reading

Cheetham ME, Brion JP, Anderton BH (1992). "Human homologues of the bacterial heat-shock protein DnaJ are preferentially expressed in neurons.". Biochem. J. 284 ( Pt 2): 469–76. PMID 1599432.
Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. PMID 8889548.
Chapple JP, Hardcastle AJ, Kurzik-Dumke U, et al. (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. PMID 10516435.
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. PMID 11147971.
Wistow G, Bernstein SL, Wyatt MK, et al. (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, 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. doi:10.1073/pnas.242603899. 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, et al. (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. 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. PMID 14759258.
Colland F, Jacq X, Trouplin V, et al. (2004). "Functional proteomics mapping of a human signaling pathway.". Genome Res. 14 (7): 1324–32. doi:10.1101/gr.2334104. PMID 15231748.
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. PMID 15489334.
Westhoff B, Chapple JP, van der Spuy J, et al. (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, et al. (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, et al. (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. PMID 16604191.
Adaimy L, Chouery E, Megarbane H, et al. (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. PMID 17847007.