DNAJB11

Protein-coding gene in the species Homo sapiens
DNAJB11
Identifiers
AliasesDNAJB11, ABBP-2, ABBP2, DJ9, Dj-9, EDJ, ERdj3, ERj3, ERj3p, PRO1080, UNQ537, DnaJ heat shock protein family (Hsp40) member B11, PKD6
External IDsOMIM: 611341; MGI: 1915088; HomoloGene: 9464; GeneCards: DNAJB11; OMA:DNAJB11 - orthologs
Gene location (Human)
Chromosome 3 (human)
Chr.Chromosome 3 (human)[1]
Chromosome 3 (human)
Genomic location for DNAJB11
Genomic location for DNAJB11
Band3q27.3Start186,567,403 bp[1]
End186,585,800 bp[1]
Gene location (Mouse)
Chromosome 16 (mouse)
Chr.Chromosome 16 (mouse)[2]
Chromosome 16 (mouse)
Genomic location for DNAJB11
Genomic location for DNAJB11
Band16|16 B1Start22,676,595 bp[2]
End22,698,384 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • Achilles tendon

  • right lobe of liver

  • colon

  • body of pancreas

  • adrenal gland

  • thyroid gland

  • testicle
Top expressed in
  • molar

  • aortic valve

  • ascending aorta

  • yolk sac

  • seminal vesicula

  • spermatocyte

  • duodenum

  • left lobe of liver

  • primitive streak

  • lacrimal gland
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
SpeciesHumanMouse
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 MbChr 16: 22.68 – 22.7 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

DnaJ homolog subfamily B member 11 is a protein that in humans is encoded by the DNAJB11 gene.[5][6][7]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000090520 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000004460 – 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. ^ 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.
  6. ^ 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 2024-03-28). ISSN 1466-1268. PMC 312896. PMID 11147971.{{cite journal}}: CS1 maint: DOI inactive as of March 2024 (link)
  7. ^ "Entrez Gene: DNAJB11 DnaJ (Hsp40) homolog, subfamily B, member 11".

Further reading

  • 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 2024-04-11). PMC 1065284. PMID 15544163.{{cite journal}}: CS1 maint: DOI inactive as of April 2024 (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.
  • v
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Chaperones/
protein folding
Heat shock proteins/
Chaperonins
Other
Protein targetingUbiquitin
(ubiquitylation)Ubiquitin-like proteins
(UBL)
SUMO protein
(SUMOylation)
  • E1 SUMO-activating enzyme
  • E2 SUMO-conjugating enzyme
Other


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