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DNAJB11

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From Wikipedia, the free encyclopedia

Protein-coding gene in the species Homo sapiens

DNAJB11

Identifiers

Aliases

DNAJB11, ABBP-2, ABBP2, DJ9, Dj-9, EDJ, ERdj3, ERj3, ERj3p, PRO1080, UNQ537, DnaJ heat shock protein family (Hsp40) member B11, PKD6

External IDs

OMIM:611341;MGI:1915088;HomoloGene:9464;GeneCards:DNAJB11;OMA:DNAJB11 - orthologs

Gene location (Human)

Chr.	Chromosome 3 (human)^[1]

Band	3q27.3	Start	186,567,403bp^[1]
Band	3q27.3	End	186,585,800bp^[1]

Gene location (Mouse)

Chr.	Chromosome 16 (mouse)^[2]

Band	16\|16 B1	Start	22,676,595bp^[2]
Band	16\|16 B1	End	22,698,384bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

Achilles tendon

right lobe of liver

colon

body of pancreas

adrenal gland

thyroid gland

testicle

Top expressed in

Ileal epithelium

tail of embryo

molar

right kidney

aortic valve

ascending aorta

yolk sac

genital tubercle

seminal vesicula

spermatocyte

More reference expression data

BioGPS

n/a

Gene ontology
Molecular function	unfolded protein binding protein binding
Cellular component	endoplasmic reticulum lumen endoplasmic reticulum membrane nucleus cytoplasm endoplasmic reticulum chaperone complex
Biological process	IRE1-mediated unfolded protein response positive regulation of ATP-dependent activity protein folding mRNA modification protein maturation
Sources:Amigo /QuickGO

Orthologs

Species

Human

Mouse

Entrez


51726


67838

Ensembl


ENSG00000090520


ENSMUSG00000004460

UniProt


Q9UBS4


Q99KV1

RefSeq (mRNA)


NM_016306


NM_001190804 NM_001190805 NM_026400

RefSeq (protein)


NP_057390 NP_001365380


NP_001177733 NP_001177734 NP_080676

Location (UCSC)

Chr 3: 186.57 – 186.59 Mb

Chr 16: 22.68 – 22.7 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

DnaJ homolog subfamily B member 11 is aprotein that in humans is encoded by theDNAJB11gene.^[5]^[6]^[7]

References

[edit]

^^a ^b ^cGRCh38: Ensembl release 89: ENSG00000090520 –Ensembl, May 2017
^^a ^b ^cGRCm38: Ensembl release 89: ENSMUSG00000004460 –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.
^Yu M, Haslam RH, Haslam DB (Sep 2000)."HEDJ, an Hsp40 co-chaperone localized to the endoplasmic reticulum of human cells".J Biol Chem.275 (32):24984–92.doi:10.1074/jbc.M000739200.PMID 10827079.
^Ohtsuka K, Hata M (Jan 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).ISSN 1466-1268.PMC 312896.PMID 11147971.{{cite journal}}: CS1 maint: DOI inactive as of July 2025 (link)
^"Entrez Gene: DNAJB11 DnaJ (Hsp40) homolog, subfamily B, member 11".

Lau PP, Villanueva H, Kobayashi K, et al. (2002)."A DnaJ protein, apobec-1-binding protein-2, modulates apolipoprotein B mRNA editing".J. Biol. Chem.276 (49):46445–52.doi:10.1074/jbc.M109215200.PMID 11584023.
Meunier L, Usherwood YK, Chung KT, Hendershot LM (2003)."A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins".Mol. Biol. Cell.13 (12):4456–69.doi:10.1091/mbc.E02-05-0311.PMC 138646.PMID 12475965.
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.Bibcode:2002PNAS...9916899M.doi:10.1073/pnas.242603899.PMC 139241.PMID 12477932.
Clark HF, Gurney AL, Abaya E, et al. (2003)."The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment".Genome Res.13 (10):2265–70.doi:10.1101/gr.1293003.PMC 403697.PMID 12975309.
Ota T, Suzuki Y, Nishikawa T, et al. (2004)."Complete sequencing and characterization of 21,243 full-length human cDNAs".Nat. Genet.36 (1):40–5.doi:10.1038/ng1285.PMID 14702039.
Bies C, Blum R, Dudek J, et al. (2005). "Characterization of pancreatic ERj3p, a homolog of yeast DnaJ-like protein Scj1p".Biol. Chem.385 (5):389–95.doi:10.1515/BC.2004.043.PMID 15195998.S2CID 11097339.
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.PMC 528928.PMID 15489334.
Shen Y, Hendershot LM (2005)."ERdj3, a stress-inducible endoplasmic reticulum DnaJ homologue, serves as a cofactor for BiP's interactions with unfolded substrates".Mol. Biol. Cell.16 (1):40–50.doi:10.1091/mbc.E04-05-0434.PMC 539150.PMID 15525676.
Nakanishi K, Kamiguchi K, Torigoe T, et al. (2005)."Localization and function in endoplasmic reticulum stress tolerance of ERdj3, a new member of Hsp40 family protein".Cell Stress Chaperones.9 (3):253–64.doi:10.1379/CSC-52.1 (inactive 12 July 2025).PMC 1065284.PMID 15544163.{{cite journal}}: CS1 maint: DOI inactive as of July 2025 (link)
Bruneel A, Labas V, Mailloux A, et al. (2006). "Proteomics of human umbilical vein endothelial cells applied to etoposide-induced apoptosis".Proteomics.5 (15):3876–84.doi:10.1002/pmic.200401239.PMID 16130169.S2CID 26007149.
Stelzl U, Worm U, Lalowski M, et al. (2005). "A human protein–protein interaction network: a resource for annotating the proteome".Cell.122 (6):957–68.doi:10.1016/j.cell.2005.08.029.hdl:11858/00-001M-0000-0010-8592-0.PMID 16169070.S2CID 8235923.
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.Bibcode:2005Natur.437.1173R.doi:10.1038/nature04209.PMID 16189514.S2CID 4427026.
Guo D, Han J, Adam BL, et al. (2005). "Proteomic analysis of SUMO4 substrates in HEK293 cells under serum starvation-induced stress".Biochem. Biophys. Res. Commun.337 (4):1308–18.doi:10.1016/j.bbrc.2005.09.191.PMID 16236267.
Otsuki T, Ota T, Nishikawa T, et al. (2007)."Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries".DNA Res.12 (2):117–26.doi:10.1093/dnares/12.2.117.PMID 16303743.
Ewing RM, Chu P, Elisma F, et al. (2007)."Large-scale mapping of human protein–protein interactions by mass spectrometry".Mol. Syst. Biol.3 (1): 89.doi:10.1038/msb4100134.PMC 1847948.PMID 17353931.

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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