DNAJC7

Protein-coding gene in the species Homo sapiens
DNAJC7
Identifiers
AliasesDNAJC7, DJ11, DJC7, TPR2, TTC2, DnaJ heat shock protein family (Hsp40) member C7
External IDsOMIM: 601964; MGI: 1928373; HomoloGene: 68306; GeneCards: DNAJC7; OMA:DNAJC7 - orthologs
Gene location (Human)
Chromosome 17 (human)
Chr.Chromosome 17 (human)[1]
Chromosome 17 (human)
Genomic location for DNAJC7
Genomic location for DNAJC7
Band17q21.2Start41,976,421 bp[1]
End42,021,376 bp[1]
Gene location (Mouse)
Chromosome 11 (mouse)
Chr.Chromosome 11 (mouse)[2]
Chromosome 11 (mouse)
Genomic location for DNAJC7
Genomic location for DNAJC7
Band11 D|11 63.47 cMStart100,473,644 bp[2]
End100,511,014 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • nucleus accumbens

  • caudate nucleus

  • right frontal lobe

  • anterior pituitary

  • monocyte

  • mucosa of transverse colon

  • apex of heart

  • cingulate gyrus

  • Brodmann area 9

  • anterior cingulate cortex
Top expressed in
  • tail of embryo

  • neural layer of retina

  • ventricular zone

  • genital tubercle

  • superior frontal gyrus

  • thymus

  • ganglionic eminence

  • cerebellar cortex

  • primary visual cortex

  • trigeminal ganglion
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • protein binding
  • heat shock protein binding
  • ATPase activator activity
Cellular component
  • cytoplasm
  • extracellular exosome
  • cytoskeleton
  • membrane
  • nucleus
  • nucleoplasm
  • cytosol
Biological process
  • regulation of cellular response to heat
  • protein folding
  • positive regulation of ATP-dependent activity
  • chaperone cofactor-dependent protein refolding
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

7266

56354

Ensembl

ENSG00000168259

ENSMUSG00000014195

UniProt

Q99615

Q9QYI3

RefSeq (mRNA)

NM_001144766
NM_003315

NM_019795
NM_001378962
NM_001378963

RefSeq (protein)

NP_001138238
NP_003306

NP_062769
NP_001365891
NP_001365892

Location (UCSC)Chr 17: 41.98 – 42.02 MbChr 11: 100.47 – 100.51 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

DnaJ homolog subfamily C member 7 is a protein that in humans is encoded by the DNAJC7 gene.[5][6][7]

Interactions

DNAJC7 has been shown to interact with RAD9A.[8]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000168259 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000014195 – 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. ^ Murthy AE, Bernards A, Church D, Wasmuth J, Gusella JF (Nov 1996). "Identification and characterization of two novel tetratricopeptide repeat-containing genes". DNA Cell Biol. 15 (9): 727–35. doi:10.1089/dna.1996.15.727. PMID 8836031.
  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 2024-03-06). PMC 312896. PMID 11147971.{{cite journal}}: CS1 maint: DOI inactive as of March 2024 (link)
  7. ^ "Entrez Gene: DNAJC7 DnaJ (Hsp40) homolog, subfamily C, member 7".
  8. ^ Xiang SL, Kumano T, Iwasaki SI, Sun X, Yoshioka K, Yamamoto KC (2001). "The J domain of Tpr2 regulates its interaction with the proapoptotic and cell-cycle checkpoint protein, Rad9". Biochem. Biophys. Res. Commun. 287 (4): 932–40. doi:10.1006/bbrc.2001.5685. hdl:2297/1794. PMID 11573955. S2CID 20694221.

Further reading

  • Hartley JL, Temple GF, Brasch MA (2001). "DNA Cloning Using In Vitro Site-Specific Recombination". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
  • Wiemann S, Weil B, Wellenreuther R, et al. (2001). "Toward a Catalog of Human Genes and Proteins: Sequencing and Analysis of 500 Novel Complete Protein Coding Human cDNAs". Genome Res. 11 (3): 422–35. doi:10.1101/gr.GR1547R. PMC 311072. PMID 11230166.
  • Xiang SL, Kumano T, Iwasaki SI, et al. (2001). "The J domain of Tpr2 regulates its interaction with the proapoptotic and cell-cycle checkpoint protein, Rad9". Biochem. Biophys. Res. Commun. 287 (4): 932–40. doi:10.1006/bbrc.2001.5685. hdl:2297/1794. PMID 11573955. S2CID 20694221.
  • 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.
  • Brychzy A, Rein T, Winklhofer KF, et al. (2003). "Cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone system". EMBO J. 22 (14): 3613–23. doi:10.1093/emboj/cdg362. PMC 165632. PMID 12853476.
  • 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.
  • Wiemann S, Arlt D, Huber W, et al. (2004). "From ORFeome to Biology: A Functional Genomics Pipeline". Genome Res. 14 (10B): 2136–44. doi:10.1101/gr.2576704. PMC 528930. PMID 15489336.
  • Rush J, Moritz A, Lee KA, et al. (2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells". Nat. Biotechnol. 23 (1): 94–101. doi:10.1038/nbt1046. PMID 15592455. S2CID 7200157.
  • 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.
  • Mehrle A, Rosenfelder H, Schupp I, et al. (2006). "The LIFEdb database in 2006". Nucleic Acids Res. 34 (Database issue): D415–8. doi:10.1093/nar/gkj139. PMC 1347501. PMID 16381901.
  • v
  • t
  • e
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


Stub icon

This article on a gene on human chromosome 17 is a stub. You can help Wikipedia by expanding it.

  • v
  • t
  • e