TCPG_HUMAN
ID TCPG_HUMAN Reviewed; 545 AA.
AC P49368; A6NE14; Q5SZY1; Q9BR64;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 4.
DT 03-AUG-2022, entry version 218.
DE RecName: Full=T-complex protein 1 subunit gamma;
DE Short=TCP-1-gamma;
DE AltName: Full=CCT-gamma;
DE AltName: Full=hTRiC5;
GN Name=CCT3; Synonyms=CCTG, TRIC5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lymph node;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 1-15; 32-38; 49-85; 129-138; 182-191; 238-248; 295-306;
RP 382-389; 428-449 AND 508-528, ACETYLATION AT MET-1, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Hepatoma;
RA Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.;
RL Submitted (JUL-2007) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-545.
RC TISSUE=Kidney;
RX PubMed=8573069; DOI=10.1042/bj3130381;
RA Walkley N.A., Demaine A.G., Malik A.N.;
RT "Cloning, structure and mRNA expression of human Cctg, which encodes the
RT chaperonin subunit CCT gamma.";
RL Biochem. J. 313:381-389(1996).
RN [7]
RP PROTEIN SEQUENCE OF 204-216; 331-353 AND 508-518, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Vishwanath V.;
RL Submitted (MAR-2007) to UniProtKB.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 345-544.
RX PubMed=8001976; DOI=10.1006/geno.1994.1438;
RA Sevigny G., Joly E., Bibor-Hardy V., Lemieux N.;
RT "Assignment of the human homologue of the mTRiC-P5 gene (TRIC5) to band
RT 1q23 by fluorescence in situ hybridization.";
RL Genomics 22:634-636(1994).
RN [9]
RP INTERACTION WITH PACRG.
RX PubMed=14532270; DOI=10.1074/jbc.m309655200;
RA Imai Y., Soda M., Murakami T., Shoji M., Abe K., Takahashi R.;
RT "A product of the human gene adjacent to parkin is a component of Lewy
RT bodies and suppresses Pael receptor-induced cell death.";
RL J. Biol. Chem. 278:51901-51910(2003).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-222, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [14]
RP FUNCTION, AND IDENTIFICATION IN THE CHAPERONIN-CONTAINING T-COMPLEX.
RX PubMed=20080638; DOI=10.1073/pnas.0910268107;
RA Seo S., Baye L.M., Schulz N.P., Beck J.S., Zhang Q., Slusarski D.C.,
RA Sheffield V.C.;
RT "BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family chaperonins and
RT mediate BBSome assembly.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:1488-1493(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP FUNCTION, AND IDENTIFICATION IN THE CHAPERONIN-CONTAINING T-COMPLEX.
RX PubMed=25467444; DOI=10.1016/j.cell.2014.10.059;
RA Freund A., Zhong F.L., Venteicher A.S., Meng Z., Veenstra T.D., Frydman J.,
RA Artandi S.E.;
RT "Proteostatic control of telomerase function through TRiC-mediated folding
RT of TCAB1.";
RL Cell 159:1389-1403(2014).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-243; TYR-247;
RP SER-252; THR-430 AND THR-459, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-381, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [22]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-15; LYS-248 AND LYS-249, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [23]
RP INTERACTION WITH DLEC1.
RX PubMed=33144677; DOI=10.1038/s41598-020-75957-y;
RA Okitsu Y., Nagano M., Yamagata T., Ito C., Toshimori K., Dohra H.,
RA Fujii W., Yogo K.;
RT "Dlec1 is required for spermatogenesis and male fertility in mice.";
RL Sci. Rep. 10:18883-18883(2020).
CC -!- FUNCTION: Component of the chaperonin-containing T-complex (TRiC), a
CC molecular chaperone complex that assists the folding of proteins upon
CC ATP hydrolysis (PubMed:25467444). The TRiC complex mediates the folding
CC of WRAP53/TCAB1, thereby regulating telomere maintenance
CC (PubMed:25467444). As part of the TRiC complex may play a role in the
CC assembly of BBSome, a complex involved in ciliogenesis regulating
CC transports vesicles to the cilia (PubMed:20080638). The TRiC complex
CC plays a role in the folding of actin and tubulin (Probable).
CC {ECO:0000269|PubMed:20080638, ECO:0000269|PubMed:25467444,
CC ECO:0000305}.
CC -!- SUBUNIT: Component of the chaperonin-containing T-complex (TRiC), a
CC heterooligomeric complex of about 850 to 900 kDa that forms two stacked
CC rings, 12 to 16 nm in diameter (PubMed:20080638, PubMed:25467444).
CC Interacts with PACRG (PubMed:14532270). Interacts with DNAAF4 (By
CC similarity). Interacts with DLEC1 (PubMed:33144677).
CC {ECO:0000250|UniProtKB:P80318, ECO:0000269|PubMed:14532270,
CC ECO:0000269|PubMed:20080638, ECO:0000269|PubMed:25467444,
CC ECO:0000269|PubMed:33144677}.
CC -!- INTERACTION:
CC P49368; O75140-2: DEPDC5; NbExp=3; IntAct=EBI-356673, EBI-12366971;
CC P49368; O75530: EED; NbExp=2; IntAct=EBI-356673, EBI-923794;
CC P49368; P57678: GEMIN4; NbExp=3; IntAct=EBI-356673, EBI-356700;
CC P49368; Q8TD10: MIPOL1; NbExp=6; IntAct=EBI-356673, EBI-2548751;
CC P49368; Q13371: PDCL; NbExp=6; IntAct=EBI-356673, EBI-5772890;
CC P49368; O15160: POLR1C; NbExp=3; IntAct=EBI-356673, EBI-1055079;
CC P49368; P04049: RAF1; NbExp=5; IntAct=EBI-356673, EBI-365996;
CC P49368; Q9H832: UBE2Z; NbExp=3; IntAct=EBI-356673, EBI-720977;
CC P49368; O60232: ZNRD2; NbExp=6; IntAct=EBI-356673, EBI-741415;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P49368-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P49368-2; Sequence=VSP_042026;
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH08019.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK293477; BAG56968.1; -; mRNA.
DR EMBL; AL833197; CAI46192.1; -; mRNA.
DR EMBL; AL589685; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006501; AAH06501.3; -; mRNA.
DR EMBL; BC008019; AAH08019.1; ALT_INIT; mRNA.
DR EMBL; X74801; CAA52808.1; -; mRNA.
DR EMBL; U17104; AAC50068.1; -; mRNA.
DR CCDS; CCDS1140.2; -. [P49368-1]
DR CCDS; CCDS30888.1; -. [P49368-2]
DR PIR; S61529; A38983.
DR RefSeq; NP_001008800.1; NM_001008800.2. [P49368-2]
DR RefSeq; NP_005989.3; NM_005998.4. [P49368-1]
DR PDB; 6NR8; EM; 7.80 A; C/K=13-525.
DR PDB; 6NR9; EM; 8.50 A; C/K=13-525.
DR PDB; 6NRA; EM; 7.70 A; C/K=13-525.
DR PDB; 6NRB; EM; 8.70 A; C/K=13-525.
DR PDB; 6NRC; EM; 8.30 A; C/K=13-525.
DR PDB; 6NRD; EM; 8.20 A; C/K=13-525.
DR PDB; 6QB8; EM; 3.97 A; G/g=2-545.
DR PDB; 7LUM; EM; 4.50 A; H/P=1-545.
DR PDB; 7LUP; EM; 6.20 A; H/P=1-545.
DR PDB; 7NVL; EM; 2.50 A; G/g=1-545.
DR PDB; 7NVM; EM; 3.10 A; G/g=1-545.
DR PDB; 7NVN; EM; 3.00 A; G/g=1-545.
DR PDB; 7NVO; EM; 3.50 A; G/g=1-545.
DR PDBsum; 6NR8; -.
DR PDBsum; 6NR9; -.
DR PDBsum; 6NRA; -.
DR PDBsum; 6NRB; -.
DR PDBsum; 6NRC; -.
DR PDBsum; 6NRD; -.
DR PDBsum; 6QB8; -.
DR PDBsum; 7LUM; -.
DR PDBsum; 7LUP; -.
DR PDBsum; 7NVL; -.
DR PDBsum; 7NVM; -.
DR PDBsum; 7NVN; -.
DR PDBsum; 7NVO; -.
DR AlphaFoldDB; P49368; -.
DR SMR; P49368; -.
DR BioGRID; 113054; 513.
DR ComplexPortal; CPX-6030; Chaperonin-containing T-complex.
DR CORUM; P49368; -.
DR DIP; DIP-32970N; -.
DR IntAct; P49368; 307.
DR MINT; P49368; -.
DR STRING; 9606.ENSP00000295688; -.
DR DrugBank; DB11638; Artenimol.
DR DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester.
DR GlyGen; P49368; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P49368; -.
DR MetOSite; P49368; -.
DR PhosphoSitePlus; P49368; -.
DR SwissPalm; P49368; -.
DR BioMuta; CCT3; -.
DR DMDM; 66774185; -.
DR DOSAC-COBS-2DPAGE; P49368; -.
DR OGP; P49368; -.
DR SWISS-2DPAGE; P49368; -.
DR CPTAC; CPTAC-474; -.
DR CPTAC; CPTAC-475; -.
DR EPD; P49368; -.
DR jPOST; P49368; -.
DR MassIVE; P49368; -.
DR MaxQB; P49368; -.
DR PaxDb; P49368; -.
DR PeptideAtlas; P49368; -.
DR PRIDE; P49368; -.
DR ProteomicsDB; 55998; -. [P49368-1]
DR ProteomicsDB; 55999; -. [P49368-2]
DR TopDownProteomics; P49368-1; -. [P49368-1]
DR Antibodypedia; 1677; 251 antibodies from 34 providers.
DR DNASU; 7203; -.
DR Ensembl; ENST00000295688.8; ENSP00000295688.3; ENSG00000163468.15. [P49368-1]
DR Ensembl; ENST00000368259.6; ENSP00000357242.2; ENSG00000163468.15. [P49368-2]
DR GeneID; 7203; -.
DR KEGG; hsa:7203; -.
DR MANE-Select; ENST00000295688.8; ENSP00000295688.3; NM_005998.5; NP_005989.3.
DR UCSC; uc001fol.3; human. [P49368-1]
DR CTD; 7203; -.
DR DisGeNET; 7203; -.
DR GeneCards; CCT3; -.
DR HGNC; HGNC:1616; CCT3.
DR HPA; ENSG00000163468; Low tissue specificity.
DR MIM; 600114; gene.
DR neXtProt; NX_P49368; -.
DR OpenTargets; ENSG00000163468; -.
DR PharmGKB; PA26180; -.
DR VEuPathDB; HostDB:ENSG00000163468; -.
DR eggNOG; KOG0364; Eukaryota.
DR GeneTree; ENSGT00570000079224; -.
DR HOGENOM; CLU_008891_7_3_1; -.
DR InParanoid; P49368; -.
DR OMA; RYCRIEK; -.
DR PhylomeDB; P49368; -.
DR TreeFam; TF105649; -.
DR BRENDA; 3.6.4.B10; 2681.
DR PathwayCommons; P49368; -.
DR Reactome; R-HSA-389957; Prefoldin mediated transfer of substrate to CCT/TriC.
DR Reactome; R-HSA-389960; Formation of tubulin folding intermediates by CCT/TriC.
DR Reactome; R-HSA-390450; Folding of actin by CCT/TriC.
DR Reactome; R-HSA-390471; Association of TriC/CCT with target proteins during biosynthesis.
DR Reactome; R-HSA-5620922; BBSome-mediated cargo-targeting to cilium.
DR Reactome; R-HSA-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR SignaLink; P49368; -.
DR BioGRID-ORCS; 7203; 794 hits in 1042 CRISPR screens.
DR ChiTaRS; CCT3; human.
DR GeneWiki; CCT3; -.
DR GenomeRNAi; 7203; -.
DR Pharos; P49368; Tbio.
DR PRO; PR:P49368; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P49368; protein.
DR Bgee; ENSG00000163468; Expressed in embryo and 217 other tissues.
DR ExpressionAtlas; P49368; baseline and differential.
DR Genevisible; P49368; HS.
DR GO; GO:0044297; C:cell body; IEA:Ensembl.
DR GO; GO:0005832; C:chaperonin-containing T-complex; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0002199; C:zona pellucida receptor complex; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0044183; F:protein folding chaperone; IDA:FlyBase.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IEA:Ensembl.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IDA:ComplexPortal.
DR GO; GO:0046931; P:pore complex assembly; IEA:Ensembl.
DR GO; GO:1904851; P:positive regulation of establishment of protein localization to telomere; IMP:BHF-UCL.
DR GO; GO:1904871; P:positive regulation of protein localization to Cajal body; HMP:BHF-UCL.
DR GO; GO:1904874; P:positive regulation of telomerase RNA localization to Cajal body; HMP:BHF-UCL.
DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; IMP:BHF-UCL.
DR GO; GO:0006457; P:protein folding; IDA:FlyBase.
DR GO; GO:0050821; P:protein stabilization; IMP:BHF-UCL.
DR GO; GO:1901998; P:toxin transport; IEA:Ensembl.
DR CDD; cd03337; TCP1_gamma; 1.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR InterPro; IPR012719; Chap_CCT_gamma.
DR InterPro; IPR017998; Chaperone_TCP-1.
DR InterPro; IPR002194; Chaperonin_TCP-1_CS.
DR InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR InterPro; IPR027413; GROEL-like_equatorial_sf.
DR InterPro; IPR027410; TCP-1-like_intermed_sf.
DR PANTHER; PTHR11353; PTHR11353; 1.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR PRINTS; PR00304; TCOMPLEXTCP1.
DR SUPFAM; SSF48592; SSF48592; 1.
DR SUPFAM; SSF52029; SSF52029; 1.
DR SUPFAM; SSF54849; SSF54849; 1.
DR TIGRFAMs; TIGR02344; chap_CCT_gamma; 1.
DR PROSITE; PS00750; TCP1_1; 1.
DR PROSITE; PS00751; TCP1_2; 1.
DR PROSITE; PS00995; TCP1_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; Chaperone;
KW Cytoplasm; Direct protein sequencing; Disulfide bond; Isopeptide bond;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..545
FT /note="T-complex protein 1 subunit gamma"
FT /id="PRO_0000128321"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 526..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:19413330"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P80318"
FT MOD_RES 222
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 247
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 430
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 459
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT DISULFID 366..372
FT /evidence="ECO:0000250"
FT CROSSLNK 15
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 248
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 249
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 381
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25114211"
FT VAR_SEQ 32..69
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042026"
FT VARIANT 391
FT /note="L -> F (in dbSNP:rs2230194)"
FT /id="VAR_052265"
FT CONFLICT 251
FT /note="E -> G (in Ref. 6; CAA52808)"
FT /evidence="ECO:0000305"
FT CONFLICT 345
FT /note="T -> A (in Ref. 8; AAC50068)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 545 AA; 60534 MW; 0A528762EF24F36B CRC64;
MMGHRPVLVL SQNTKRESGR KVQSGNINAA KTIADIIRTC LGPKSMMKML LDPMGGIVMT
NDGNAILREI QVQHPAAKSM IEISRTQDEE VGDGTTSVII LAGEMLSVAE HFLEQQMHPT
VVISAYRKAL DDMISTLKKI SIPVDISDSD MMLNIINSSI TTKAISRWSS LACNIALDAV
KMVQFEENGR KEIDIKKYAR VEKIPGGIIE DSCVLRGVMI NKDVTHPRMR RYIKNPRIVL
LDSSLEYKKG ESQTDIEITR EEDFTRILQM EEEYIQQLCE DIIQLKPDVV ITEKGISDLA
QHYLMRANIT AIRRVRKTDN NRIARACGAR IVSRPEELRE DDVGTGAGLL EIKKIGDEYF
TFITDCKDPK ACTILLRGAS KEILSEVERN LQDAMQVCRN VLLDPQLVPG GGASEMAVAH
ALTEKSKAMT GVEQWPYRAV AQALEVIPRT LIQNCGASTI RLLTSLRAKH TQENCETWGV
NGETGTLVDM KELGIWEPLA VKLQTYKTAV ETAVLLLRID DIVSGHKKKG DDQSRQGGAP
DAGQE
