DNAJC10

DnaJ (Hsp40) homolog, subfamily C, member 10

Identifiers

DNAJC10; DKFZp434J1813; ERdj5; JPDI; MGC104194

External IDs

OMIM: 607987 MGI: 1914111 HomoloGene: 10358 GeneCards: DNAJC10 Gene

Gene Ontology
Molecular function	• ATPase activator activity • protein binding • electron carrier activity • protein disulfide oxidoreductase activity • disulfide oxidoreductase activity • heat shock protein binding • unfolded protein binding • chaperone binding • ATPase binding • misfolded protein binding
Cellular component	• extracellular region • endoplasmic reticulum • endoplasmic reticulum lumen • microsome • endoplasmic reticulum chaperone complex
Biological process	• negative regulation of protein phosphorylation • protein folding • glycerol ether metabolic process • ER-associated protein catabolic process • positive regulation of ATPase activity • response to endoplasmic reticulum stress • cell redox homeostasis • apoptosis in response to endoplasmic reticulum stress
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

n/a

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 2:
183.58 – 183.65 Mb

Chr 2:
80.16 – 80.19 Mb

PubMed search

[1]

[2]

DnaJ homolog subfamily C member 10 is a protein that in humans is encoded by the DNAJC10 gene.^[1]^[2]^[3]

References

^ Cunnea PM, Miranda-Vizuete A, Bertoli G, Simmen T, Damdimopoulos AE, Hermann S, Leinonen S, Huikko MP, Gustafsson JA, Sitia R, Spyrou G (Jan 2003). "ERdj5, an endoplasmic reticulum (ER)-resident protein containing DnaJ and thioredoxin domains, is expressed in secretory cells or following ER stress". J Biol Chem 278 (2): 1059–66. doi:10.1074/jbc.M206995200. PMID 12411443.
^ Hosoda A, Kimata Y, Tsuru A, Kohno K (Jan 2003). "JPDI, a novel endoplasmic reticulum-resident protein containing both a BiP-interacting J-domain and thioredoxin-like motifs". J Biol Chem 278 (4): 2669–76. doi:10.1074/jbc.M208346200. PMID 12446677.
^ "Entrez Gene: DNAJC10 DnaJ (Hsp40) homolog, subfamily C, member 10". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=54431.

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.
Gu SH, Chen JZ, Ying K, et al. (2004). "Cloning and identification of a novel cDNA which encodes a putative protein with a DnaJ domain and a thioredoxin active motif, human macrothioredoxin.". Biochem. Genet. 41 (7-8): 245–53. doi:10.1023/A:1025510502147. PMID 14587667.
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.
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.
Hillier LW, Graves TA, Fulton RS, et al. (2005). "Generation and annotation of the DNA sequences of human chromosomes 2 and 4.". Nature 434 (7034): 724–31. doi:10.1038/nature03466. PMID 15815621.
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.
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.

Posttranslational modification

Chaperones/
protein folding

Heat shock proteins/ Chaperonins	Hsp10/GroES (Early pregnancy factor) · 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

Signal peptide

Ubiquitin

E1 Ubiquitin-activating enzyme (UBA1, UBA2, UBA3, UBA5, UBA6, UBA7, ATG7, NAE1, SAE1)

E2 Ubiquitin-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)

E3 Ubiquitin ligase (VHL, Cullin, CBL, MDM2, FANCL, UBR1)

Deubiquitinating enzyme: Ataxin 3 • USP6 • CYLD

ATG3 • BIRC6 • UFC1

Other

SUMO protein

see also posttranslational modification disorders
B bsyn: dna (repl, cycl, reco, repr) · tscr (fact, tcrg, nucl, rnat, rept, ptts) · tltn (risu, pttl, nexn) · dnab, rnab/runp · stru (domn, 1°, 2°, 3°, 4°)

DNAJC10

References

Further reading