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DNAJB2

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From Wikipedia, the free encyclopedia

Protein-coding gene in the species Homo sapiens

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	219,279,342bp^[1]
Band	2q35	End	219,286,898bp^[1]

Gene location (Mouse)

Chr.	Chromosome 1 (mouse)^[2]

Band	1\|1 C4	Start	75,236,406bp^[2]
Band	1\|1 C4	End	75,245,692bp^[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 aprotein that in humans is encoded by theDNAJB2gene.^[5]^[6]^[7]

References

[edit]

^^a ^b ^cGRCh38: Ensembl release 89: ENSG00000135924 –Ensembl, May 2017
^^a ^b ^cGRCm38: 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.doi:10.1379/1466-1268(2000)005<0098:mhdhco>2.0.co;2 (inactive 12 July 2025).PMC 312896.PMID 11147971.{{cite journal}}: CS1 maint: DOI inactive as of July 2025 (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.

Posttranslational modification

Chaperones/
protein folding

Heat shock proteins/ Chaperonins	Hsp10/GroES Hsp27 Hsp47 HSP60/GroEL Hsp40/DnaJ A1 A2 A3 B1 B2 B11 B4 B6 B9 C1 C3 C5 C6 C7 C10 C11 C13 C14 C19 Hsp70 1A 1B 1L 2 4 4L 5 6 7 8 9 12A 14 Hsp90 α₁ α₂ β ER TRAP1
Other	Alpha crystallin Clusterin Survival of motor neuron SMN1 SMN2

Protein targeting

Ubiquitin
(ubiquitylation)

E1Ubiquitin-activating enzyme
- UBA1
- UBA2
- UBA3
- UBA5
- UBA6
- UBA7
- ATG7
- NAE1
- SAE1

E2Ubiquitin-conjugating enzyme
- A
- B
- C
- D1
- D2
- D3
- E1
- E2
- E3
- G1
- G2
- H
- I
- J1
- J2
- K
- L1
- L2
- L3
- L4
- L6
- M
- N
- O
- Q1
- Q2
- R1 (CDC34)
- R2
- S
- V1
- V2
- Z

E3Ubiquitin ligase
- VHL
- Cullin
- CBL
- MDM2
- FANCL
- UBR1

Ubiquitin-like proteins
(UBL)

SUMO protein (SUMOylation)	E1 SUMO-activating enzyme SAE1 SAE2 E2 SUMO-conjugating enzyme UBC9 E3 SUMO ligase PIAS1 PIAS2 PIAS3 PIAS4
Other	ISG15 URM1 UFM1 NEDD8 (neddylation) FAT10 ATG8 ATG12 FUB1 MUB UBL5 Prokaryotic ubiquitin-like protein

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