DNAJC10

Protein-coding gene in the species Homo sapiens
DNAJC10
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

3APO, 3APQ, 3APS

Identifiers
AliasesDNAJC10, ERdj5, JPDI, MTHr, PDIA19, DnaJ heat shock protein family (Hsp40) member C10
External IDsOMIM: 607987; MGI: 1914111; HomoloGene: 10358; GeneCards: DNAJC10; OMA:DNAJC10 - orthologs
Gene location (Human)
Chromosome 2 (human)
Chr.Chromosome 2 (human)[1]
Chromosome 2 (human)
Genomic location for DNAJC10
Genomic location for DNAJC10
Band2q32.1Start182,716,255 bp[1]
End182,794,464 bp[1]
Gene location (Mouse)
Chromosome 2 (mouse)
Chr.Chromosome 2 (mouse)[2]
Chromosome 2 (mouse)
Genomic location for DNAJC10
Genomic location for DNAJC10
Band2|2 C3Start80,145,810 bp[2]
End80,184,387 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • corpus epididymis

  • right uterine tube

  • bronchial epithelial cell

  • stromal cell of endometrium

  • tail of epididymis

  • Achilles tendon

  • caput epididymis

  • seminal vesicula

  • mucosa of paranasal sinus

  • islet of Langerhans
Top expressed in
  • spermatocyte

  • seminal vesicula

  • spermatid

  • medullary collecting duct

  • renal corpuscle

  • ureter

  • pyloric antrum

  • calvaria

  • tail of embryo

  • Paneth cell
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • ATPase binding
  • misfolded protein binding
  • Hsp70 protein binding
  • protein binding
  • oxidoreductase activity
  • chaperone binding
  • ATPase activator activity
  • disulfide oxidoreductase activity
  • oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor
  • protein-disulfide reductase activity
Cellular component
  • membrane
  • endoplasmic reticulum chaperone complex
  • endoplasmic reticulum lumen
  • endoplasmic reticulum
Biological process
  • negative regulation of protein phosphorylation
  • cell redox homeostasis
  • response to endoplasmic reticulum stress
  • intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress
  • ubiquitin-dependent ERAD pathway
  • positive regulation of ATP-dependent activity
  • protein folding in endoplasmic reticulum
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

54431

66861

Ensembl

ENSG00000077232

ENSMUSG00000027006

UniProt

Q8IXB1

Q9DC23

RefSeq (mRNA)

NM_001271581
NM_018981

NM_024181

RefSeq (protein)

NP_001258510
NP_061854

NP_077143

Location (UCSC)Chr 2: 182.72 – 182.79 MbChr 2: 80.15 – 80.18 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

DnaJ homolog subfamily C member 10 is a protein that in humans is encoded by the DNAJC10 gene.[5][6][7]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000077232 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000027006 – 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. ^ 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.
  6. ^ 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.
  7. ^ "Entrez Gene: DNAJC10 DnaJ (Hsp40) homolog, subfamily C, member 10".

Further reading

  • 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.
  • 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. S2CID 13635128.
  • 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.
  • 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. Bibcode:2005Natur.434..724H. 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. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
  • 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.

External links

  • PDBe-KB provides an overview of all the structure information available in the PDB for Mouse DnaJ homolog subfamily C member 10 (DNAJC10)
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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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