- DNAJC7
-
DnaJ (Hsp40) homolog, subfamily C, member 7 Identifiers Symbols DNAJC7; DJ11; DJC7; TPR2; TTC2 External IDs OMIM: 601964 MGI: 1928373 HomoloGene: 68306 GeneCards: DNAJC7 Gene Gene Ontology Molecular function • binding
• heat shock protein binding
• unfolded protein bindingCellular component • nucleus
• nucleolus
• cytoplasm
• cytoskeletonBiological process • protein folding
• chaperone cofactor-dependent protein refoldingSources: Amigo / QuickGO RNA expression pattern More reference expression data Orthologs Species Human Mouse Entrez 7266 56354 Ensembl ENSG00000168259 ENSMUSG00000014195 UniProt Q99615 Q3UL32 RefSeq (mRNA) NM_001144766.2 NM_019795.4 RefSeq (protein) NP_001138238.1 NP_062769.2 Location (UCSC) Chr 17:
40.13 – 40.17 MbChr 11:
100.44 – 100.48 MbPubMed search [1] [2] DnaJ homolog subfamily C member 7 is a protein that in humans is encoded by the DNAJC7 gene.[1][2][3]
Interactions
DNAJC7 has been shown to interact with RAD9A.[4]
References
- ^ 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.
- ^ 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. PMC 312896. PMID 11147971. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=312896.
- ^ "Entrez Gene: DNAJC7 DnaJ (Hsp40) homolog, subfamily C, member 7". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7266.
- ^ Xiang, S L; Kumano T, Iwasaki S I, Sun X, Yoshioka K, Yamamoto K C (Oct. 2001). "The J domain of Tpr2 regulates its interaction with the proapoptotic and cell-cycle checkpoint protein, Rad9". Biochem. Biophys. Res. Commun. (United States) 287 (4): 932–40. doi:10.1006/bbrc.2001.5685. ISSN 0006-291X. PMID 11573955.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=310948.
- 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=311072.
- 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. PMID 11573955.
- 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.
- 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=165632.
- 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.
- 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528930.
- 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.
- 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.
- 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1347501.
Chaperones/
protein foldingOtherProtein targeting 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 • UFC1Other 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°)Categories:- Human proteins
- Chromosome 17 gene stubs
- Heat shock proteins
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