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; OMA:DNAJB2 - orthologs
Gene location (Human) Chr. Chromosome 2 (human) [1] Band 2q35 Start 219,279,342 bp [1] End 219,286,898 bp [1]
Gene location (Mouse) Chr. Chromosome 1 (mouse) [2] Band 1|1 C4 Start 75,236,406 bp [2] End 75,245,692 bp [2]
RNA expression pattern Bgee Human Mouse (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 Species Human Mouse 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 Mb Chr 1: 75.24 – 75.25 Mb PubMed search [3] [4]
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

1. GRCh38: Ensembl release 89: ENSG00000135924 – Ensembl, May 2017
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.
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 (inactive 2024-08-01). 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.
• 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.