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 27-MAR-2024, entry version 227. 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=8; 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 7TRG; EM; 3.00 A; H=1-545. DR PDB; 7TTN; EM; 3.30 A; H=1-545. DR PDB; 7TTT; EM; 2.90 A; H=1-545. DR PDB; 7TUB; EM; 3.60 A; H=1-545. DR PDB; 7WU7; EM; 3.85 A; C/K=1-545. DR PDB; 7WZ3; EM; 4.10 A; G/g=1-545. DR PDB; 7X0A; EM; 3.10 A; G/g=1-545. DR PDB; 7X0S; EM; 3.10 A; G/N=1-545. DR PDB; 7X0V; EM; 3.20 A; G/N=1-545. DR PDB; 7X3J; EM; 4.20 A; G/g=1-545. DR PDB; 7X3U; EM; 3.30 A; G/g=1-545. DR PDB; 7X6Q; EM; 4.50 A; G/N=1-545. DR PDB; 7X7Y; EM; 3.80 A; G/g=1-545. DR PDB; 8SFE; EM; 3.36 A; G/g=3-530. DR PDB; 8SFF; EM; 3.20 A; G/g=3-530. DR PDB; 8SG8; EM; 3.00 A; G/g=3-530. DR PDB; 8SG9; EM; 2.90 A; G/g=3-530. DR PDB; 8SGC; EM; 2.90 A; G/g=3-530. DR PDB; 8SGL; EM; 2.90 A; G/g=3-530. DR PDB; 8SGQ; EM; 3.70 A; G/g=3-530. DR PDB; 8SH9; EM; 2.70 A; G/g=3-530. DR PDB; 8SHA; EM; 3.00 A; G/g=3-530. DR PDB; 8SHD; EM; 2.90 A; G/g=3-530. DR PDB; 8SHE; EM; 2.80 A; G/g=3-530. DR PDB; 8SHF; EM; 3.00 A; G/g=3-530. DR PDB; 8SHG; EM; 2.80 A; G/g=3-530. DR PDB; 8SHL; EM; 3.00 A; G/g=3-530. DR PDB; 8SHN; EM; 2.80 A; G/g=3-530. DR PDB; 8SHO; EM; 3.00 A; G/g=3-530. DR PDB; 8SHP; EM; 3.00 A; G/g=3-530. DR PDB; 8SHQ; EM; 2.90 A; G/g=3-530. DR PDB; 8SHT; EM; 3.00 A; G/g=3-530. 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 PDBsum; 7TRG; -. DR PDBsum; 7TTN; -. DR PDBsum; 7TTT; -. DR PDBsum; 7TUB; -. DR PDBsum; 7WU7; -. DR PDBsum; 7WZ3; -. DR PDBsum; 7X0A; -. DR PDBsum; 7X0S; -. DR PDBsum; 7X0V; -. DR PDBsum; 7X3J; -. DR PDBsum; 7X3U; -. DR PDBsum; 7X6Q; -. DR PDBsum; 7X7Y; -. DR PDBsum; 8SFE; -. DR PDBsum; 8SFF; -. DR PDBsum; 8SG8; -. DR PDBsum; 8SG9; -. DR PDBsum; 8SGC; -. DR PDBsum; 8SGL; -. DR PDBsum; 8SGQ; -. DR PDBsum; 8SH9; -. DR PDBsum; 8SHA; -. DR PDBsum; 8SHD; -. DR PDBsum; 8SHE; -. DR PDBsum; 8SHF; -. DR PDBsum; 8SHG; -. DR PDBsum; 8SHL; -. DR PDBsum; 8SHN; -. DR PDBsum; 8SHO; -. DR PDBsum; 8SHP; -. DR PDBsum; 8SHQ; -. DR PDBsum; 8SHT; -. DR AlphaFoldDB; P49368; -. DR EMDB; EMD-0490; -. DR EMDB; EMD-0491; -. DR EMDB; EMD-0492; -. DR EMDB; EMD-0493; -. DR EMDB; EMD-0494; -. DR EMDB; EMD-0495; -. DR EMDB; EMD-12605; -. DR EMDB; EMD-12606; -. DR EMDB; EMD-12607; -. DR EMDB; EMD-12608; -. DR EMDB; EMD-13754; -. DR EMDB; EMD-23522; -. DR EMDB; EMD-23526; -. DR EMDB; EMD-26089; -. DR EMDB; EMD-26120; -. DR EMDB; EMD-26123; -. DR EMDB; EMD-26131; -. DR EMDB; EMD-32823; -. DR EMDB; EMD-32903; -. DR EMDB; EMD-32922; -. DR EMDB; EMD-32923; -. DR EMDB; EMD-32926; -. DR EMDB; EMD-32989; -. DR EMDB; EMD-32993; -. DR EMDB; EMD-33025; -. DR EMDB; EMD-33053; -. DR EMDB; EMD-40439; -. DR EMDB; EMD-40440; -. DR EMDB; EMD-40452; -. DR EMDB; EMD-40453; -. DR EMDB; EMD-40454; -. DR EMDB; EMD-40461; -. DR EMDB; EMD-40464; -. DR EMDB; EMD-40481; -. DR EMDB; EMD-40482; -. DR EMDB; EMD-40484; -. DR EMDB; EMD-40485; -. DR EMDB; EMD-40486; -. DR EMDB; EMD-40487; -. DR EMDB; EMD-40488; -. DR EMDB; EMD-40489; -. DR EMDB; EMD-40490; -. DR EMDB; EMD-40491; -. DR EMDB; EMD-40492; -. DR EMDB; EMD-40494; -. DR EMDB; EMD-4489; -. DR SMR; P49368; -. DR BioGRID; 113054; 617. DR ComplexPortal; CPX-6030; Chaperonin-containing T-complex. DR CORUM; P49368; -. DR DIP; DIP-32970N; -. DR IntAct; P49368; 309. 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 CPTAC; CPTAC-474; -. DR CPTAC; CPTAC-475; -. DR EPD; P49368; -. DR jPOST; P49368; -. DR MassIVE; P49368; -. DR MaxQB; P49368; -. DR PaxDb; 9606-ENSP00000295688; -. DR PeptideAtlas; P49368; -. DR PRIDE; P49368; -. DR ProteomicsDB; 55998; -. [P49368-1] DR ProteomicsDB; 55999; -. [P49368-2] DR Pumba; P49368; -. DR TopDownProteomics; P49368-1; -. [P49368-1] DR Antibodypedia; 1677; 270 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 AGR; HGNC:1616; -. 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; CGGSTIR; -. DR OrthoDB; 212971at2759; -. 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 SIGNOR; P49368; -. DR BioGRID-ORCS; 7203; 829 hits in 1120 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 primordial germ cell in gonad and 219 other cell types or tissues. DR ExpressionAtlas; P49368; baseline and differential. 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: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 CDD; cd03337; TCP1_gamma; 1. DR Gene3D; 3.50.7.10; GroEL; 1. DR Gene3D; 1.10.560.10; GroEL-like equatorial domain; 1. DR Gene3D; 3.30.260.10; TCP-1-like chaperonin intermediate domain; 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 NCBIfam; TIGR02344; chap_CCT_gamma; 1. DR NCBIfam; NF041082; thermosome_alpha; 1. DR NCBIfam; NF041083; thermosome_beta; 1. DR PANTHER; PTHR11353; CHAPERONIN; 1. DR PANTHER; PTHR11353:SF24; T-COMPLEX PROTEIN 1 SUBUNIT GAMMA; 1. DR Pfam; PF00118; Cpn60_TCP1; 1. DR PRINTS; PR00304; TCOMPLEXTCP1. DR SUPFAM; SSF52029; GroEL apical domain-like; 1. DR SUPFAM; SSF48592; GroEL equatorial domain-like; 1. DR SUPFAM; SSF54849; GroEL-intermediate domain like; 1. DR PROSITE; PS00750; TCP1_1; 1. DR PROSITE; PS00751; TCP1_2; 1. DR PROSITE; PS00995; TCP1_3; 1. DR SWISS-2DPAGE; P49368; -. DR Genevisible; P49368; HS. 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" FT STRAND 15..18 FT /evidence="ECO:0007829|PDB:7X0S" FT HELIX 20..37 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 38..40 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 42..44 FT /evidence="ECO:0007829|PDB:7NVO" FT STRAND 47..51 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 53..55 FT /evidence="ECO:0007829|PDB:7NVO" FT STRAND 57..60 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 63..69 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 75..90 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 92..94 FT /evidence="ECO:0007829|PDB:7X0A" FT HELIX 97..114 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 119..140 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 149..160 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 161..163 FT /evidence="ECO:0007829|PDB:7X0S" FT HELIX 164..168 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 169..183 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 184..189 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 191..193 FT /evidence="ECO:0007829|PDB:7NVL" FT TURN 195..197 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 198..207 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 209..211 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 213..217 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 219..221 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 231..235 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 238..243 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 263..283 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 288..294 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 298..306 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 310..312 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 317..327 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 335..337 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 340..342 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 350..355 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 358..362 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 372..379 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 381..403 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 407..409 FT /evidence="ECO:0007829|PDB:7NVL" FT TURN 410..412 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 413..426 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 434..443 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 446..455 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 459..469 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 472..474 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 478..480 FT /evidence="ECO:0007829|PDB:7NVL" FT TURN 482..484 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 487..489 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 490..493 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 496..498 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 499..518 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 519..524 FT /evidence="ECO:0007829|PDB:7NVL" 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 //