DNAJB11

DnaJ (Hsp40) homolog, subfamily B, member 11
Identifiers
Symbols	DNAJB11; ABBP-2; ABBP2; DJ9; EDJ; ERdj3; ERj3; HEDJ; PRO1080; UNQ537; hDj9
External IDs	OMIM: 611341 MGI: 1915088 HomoloGene: 9464 GeneCards: DNAJB11 Gene
Gene Ontology Molecular function • protein binding • heat shock protein binding • unfolded protein binding Cellular component • nucleus • cytoplasm • endoplasmic reticulum • endoplasmic reticulum • endoplasmic reticulum lumen Biological process • protein folding • mRNA modification Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	51726	67838
Ensembl	ENSG00000090520	ENSMUSG00000004460
UniProt	Q9UBS4	Q8BK79
RefSeq (mRNA)	NM_016306	NM_026400
RefSeq (protein)	NP_057390	NP_080676
Location (UCSC)	Chr 3: 186.29 – 186.32 Mb	Chr 16: 22.86 – 22.88 Mb
PubMed search	[1]	[2]

DnaJ homolog subfamily B member 11 is a protein that in humans is encoded by the DNAJB11 gene.^[1][2][3]

References

1. ^ 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. 
2. ^ 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. ISSN 1466-1268. PMC 312896. PMID 11147971. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=312896. 
3. ^ "Entrez Gene: DNAJB11 DnaJ (Hsp40) homolog, subfamily B, member 11". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51726. 

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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=138646. 
• 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. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=403697. 
• 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. 
• 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928. 
• 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=539150. 
• 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. PMC 1065284. PMID 15544163. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1065284. 
• 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. 
• 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. PMID 16169070. 
• 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. 
• 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1847948.