CCT3

Protein-coding gene in the species Homo sapiens

CCT3
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1GML, 1GN1

Identifiers
AliasesCCT3, CCT-gamma, CCTG, PIG48, TCP-1-gamma, TRIC5, chaperonin containing TCP1 subunit 3
External IDsOMIM: 600114; MGI: 104708; HomoloGene: 4373; GeneCards: CCT3; OMA:CCT3 - orthologs
Gene location (Human)
Chromosome 1 (human)
Chr.Chromosome 1 (human)[1]
Chromosome 1 (human)
Genomic location for CCT3
Genomic location for CCT3
Band1q22Start156,308,968 bp[1]
End156,367,873 bp[1]
Gene location (Mouse)
Chromosome 3 (mouse)
Chr.Chromosome 3 (mouse)[2]
Chromosome 3 (mouse)
Genomic location for CCT3
Genomic location for CCT3
Band3 F1|3 38.79 cMStart88,204,423 bp[2]
End88,229,074 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • gonad

  • embryo

  • islet of Langerhans

  • ventricular zone

  • ganglionic eminence

  • right adrenal gland

  • smooth muscle tissue

  • right testis

  • left testis

  • right adrenal cortex
Top expressed in
  • primitive streak

  • otic placode

  • Paneth cell

  • maxillary prominence

  • saccule

  • mandibular prominence

  • otic vesicle

  • condyle

  • somite

  • spermatocyte
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • nucleotide binding
  • protein folding chaperone activity
  • protein binding
  • ATP binding
  • unfolded protein binding
  • RNA binding
Cellular component
  • cell body
  • myelin sheath
  • plasma membrane
  • zona pellucida receptor complex
  • chaperonin-containing T-complex
  • microtubule
  • cytoskeleton
  • extracellular exosome
  • cytoplasm
  • cytosol
Biological process
  • positive regulation of protein localization to Cajal body
  • pore complex assembly
  • protein stabilization
  • positive regulation of telomere maintenance via telomerase
  • toxin transport
  • protein folding
  • positive regulation of telomerase RNA localization to Cajal body
  • binding of sperm to zona pellucida
  • 'de novo' protein folding
  • chaperone-mediated protein folding
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

7203

12462

Ensembl

ENSG00000163468

ENSMUSG00000001416

UniProt

P49368
Q5SZW8

P80318

RefSeq (mRNA)

NM_001008800
NM_001008883
NM_005998

NM_009836

RefSeq (protein)

NP_001008800
NP_005989

NP_033966

Location (UCSC)Chr 1: 156.31 – 156.37 MbChr 3: 88.2 – 88.23 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

T-complex protein 1 subunit gamma is a protein that in humans is encoded by the CCT3 gene.[5][6]

Function

This gene encodes a molecular chaperone that is member of the TRiC complex. This complex consists of two identical stacked rings, each containing eight different proteins. Unfolded polypeptides enter the central cavity of the complex and are folded in an ATP-dependent manner. The complex folds various proteins, including actin and tubulin. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.[6]

Interactions

CCT3 has been shown to interact with PPP4C.[7][8]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000163468 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000001416 – 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. ^ Joly EC, Sévigny G, Todorov IT, Bibor-Hardy V (Mar 1994). "cDNA encoding a novel TCP1-related protein". Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1217 (2): 224–6. doi:10.1016/0167-4781(94)90041-8. PMID 8110840.
  6. ^ a b "Entrez Gene: CCT3 chaperonin containing TCP1, subunit 3 (gamma)".
  7. ^ Chen GI, Tisayakorn S, Jorgensen C, D'Ambrosio LM, Goudreault M, Gingras AC (Oct 2008). "PP4R4/KIAA1622 forms a novel stable cytosolic complex with phosphoprotein phosphatase 4". The Journal of Biological Chemistry. 283 (43): 29273–84. doi:10.1074/jbc.M803443200. PMC 2662017. PMID 18715871.
  8. ^ Gingras AC, Caballero M, Zarske M, Sanchez A, Hazbun TR, Fields S, Sonenberg N, Hafen E, Raught B, Aebersold R (Nov 2005). "A novel, evolutionarily conserved protein phosphatase complex involved in cisplatin sensitivity". Molecular & Cellular Proteomics. 4 (11): 1725–40. doi:10.1074/mcp.M500231-MCP200. PMID 16085932.

Further reading

  • Kubota H, Hynes G, Carne A, Ashworth A, Willison K (Feb 1994). "Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperonin". Current Biology. 4 (2): 89–99. Bibcode:1994CBio....4...89K. doi:10.1016/S0960-9822(94)00024-2. PMID 7953530. S2CID 31300131.
  • Sévigny G, Joly EC, Bibor-Hardy V, Lemieux N (Aug 1994). "Assignment of the human homologue of the mTRiC-P5 gene (TRIC5) to band 1q23 by fluorescence in situ hybridization". Genomics. 22 (3): 634–6. doi:10.1006/geno.1994.1438. PMID 8001976.
  • Walkley NA, Demaine AG, Malik AN (Jan 1996). "Cloning, structure and mRNA expression of human Cctg, which encodes the chaperonin subunit CCT gamma". The Biochemical Journal. 313 (Pt 2): 381–9. doi:10.1042/bj3130381. PMC 1216920. PMID 8573069.
  • Feldman DE, Thulasiraman V, Ferreyra RG, Frydman J (Dec 1999). "Formation of the VHL-elongin BC tumor suppressor complex is mediated by the chaperonin TRiC". Molecular Cell. 4 (6): 1051–61. doi:10.1016/S1097-2765(00)80233-6. PMID 10635329.
  • Wong N, Chan A, Lee SW, Lam E, To KF, Lai PB, Li XN, Liew CT, Johnson PJ (Mar 2003). "Positional mapping for amplified DNA sequences on 1q21-q22 in hepatocellular carcinoma indicates candidate genes over-expression". Journal of Hepatology. 38 (3): 298–306. doi:10.1016/S0168-8278(02)00412-9. PMID 12586295.
  • Yuryev A, Wennogle LP (Feb 2003). "Novel raf kinase protein-protein interactions found by an exhaustive yeast two-hybrid analysis". Genomics. 81 (2): 112–25. doi:10.1016/S0888-7543(02)00008-3. PMID 12620389.
  • Reuter TY, Medhurst AL, Waisfisz Q, Zhi Y, Herterich S, Hoehn H, Gross HJ, Joenje H, Hoatlin ME, Mathew CG, Huber PA (Oct 2003). "Yeast two-hybrid screens imply involvement of Fanconi anemia proteins in transcription regulation, cell signaling, oxidative metabolism, and cellular transport". Experimental Cell Research. 289 (2): 211–21. doi:10.1016/S0014-4827(03)00261-1. PMID 14499622.
  • Imai Y, Soda M, Murakami T, Shoji M, Abe K, Takahashi R (Dec 2003). "A product of the human gene adjacent to parkin is a component of Lewy bodies and suppresses Pael receptor-induced cell death". The Journal of Biological Chemistry. 278 (51): 51901–10. doi:10.1074/jbc.M309655200. PMID 14532270.
  • Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 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.
  • v
  • t
  • e
  • 1gml: CRYSTAL STRUCTURE OF THE MOUSE CCT GAMMA APICAL DOMAIN (TRICLINIC)
    1gml: CRYSTAL STRUCTURE OF THE MOUSE CCT GAMMA APICAL DOMAIN (TRICLINIC)
  • 1gn1: CRYSTAL STRUCTURE OF THE MOUSE CCT GAMMA APICAL DOMAIN (MONOCLINIC)
    1gn1: CRYSTAL STRUCTURE OF THE MOUSE CCT GAMMA APICAL DOMAIN (MONOCLINIC)


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