ID TCPQ_HUMAN Reviewed; 548 AA. AC P50990; A6NN54; B4DEM7; B4DQH4; Q4VBP8; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 27-MAR-2024, entry version 221. DE RecName: Full=T-complex protein 1 subunit theta; DE Short=TCP-1-theta; DE AltName: Full=CCT-theta; DE AltName: Full=Chaperonin containing T-complex polypeptide 1 subunit 8; DE AltName: Full=Renal carcinoma antigen NY-REN-15; GN Name=CCT8; Synonyms=C21orf112, CCTQ, KIAA0002; 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 1). RC TISSUE=Bone marrow; RX PubMed=7584026; DOI=10.1093/dnares/1.1.27; RA Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S., RA Nagase T., Seki N., Ishikawa K., Tabata S.; RT "Prediction of the coding sequences of unidentified human genes. I. The RT coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of RT randomly sampled cDNA clones from human immature myeloid cell line KG-1."; RL DNA Res. 1:27-35(1994). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8590283; DOI=10.1093/dnares/2.4.187; RA Yamazaki M., Ono A., Watanabe K., Sasaki K., Tashiro H., Nomura T.; RT "Nucleotide sequence surrounding the locus marker D21S246 on human RT chromosome 21."; RL DNA Res. 2:187-189(1995). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Taudien S., Dagand E., Delabar J., Nordsiek G., Drescher B., Weber J., RA Schattevoy R., Menzel U., Yaspo M.-L., Rosenthal A.; RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10830953; DOI=10.1038/35012518; RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U., RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.; RT "The DNA sequence of human chromosome 21."; RL Nature 405:311-319(2000). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Chondrosarcoma, and Liver; 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 [7] RP PROTEIN SEQUENCE OF 2-16; 55-74; 156-165; 172-181; 283-296; 408-421; RP 441-450 AND 510-520, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT RP ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=B-cell lymphoma; RA Bienvenut W.V.; RL Submitted (OCT-2004) to UniProtKB. RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 33-65 (ISOFORM 1/2). RX PubMed=7890169; DOI=10.1016/0378-1119(94)00880-2; RA Kubota H., Hynes G., Willison K.; RT "The eighth Cct gene, Cctq, encoding the theta subunit of the cytosolic RT chaperonin containing TCP-1."; RL Gene 154:231-236(1995). RN [9] RP IDENTIFICATION AS A RENAL CANCER ANTIGEN. RC TISSUE=Renal cell carcinoma; RX PubMed=10508479; RX DOI=10.1002/(sici)1097-0215(19991112)83:4<456::aid-ijc4>3.0.co;2-5; RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H., RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T., RA Old L.J.; RT "Antigens recognized by autologous antibody in patients with renal-cell RT carcinoma."; RL Int. J. Cancer 83:456-464(1999). RN [10] 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 [11] RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE RP ANALYSIS]. 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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-505, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.-M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23 AND TYR-30, AND RP IDENTIFICATION BY 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 [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-318; LYS-400 AND LYS-466, AND RP IDENTIFICATION BY MASS 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 [16] RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE RP 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 [17] 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 [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; TYR-30; SER-162; SER-213; RP SER-269; SER-317 AND SER-537, 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 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 [20] RP IDENTIFICATION BY 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 [21] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-534, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; DOI=10.1038/nsmb.2890; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [22] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-459, 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 [23] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-534 AND LYS-539, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25755297; DOI=10.1074/mcp.o114.044792; RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., RA Vertegaal A.C.; RT "System-wide analysis of SUMOylation dynamics in response to replication RT stress reveals novel small ubiquitin-like modified target proteins and RT acceptor lysines relevant for genome stability."; RL Mol. Cell. Proteomics 14:1419-1434(2015). RN [24] 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 [25] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-224; LYS-254; LYS-260; LYS-534 RP AND LYS-539, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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). 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 synaptic plasticity regulator PANTS (By CC similarity). {ECO:0000250|UniProtKB:P42932, CC ECO:0000269|PubMed:14532270, ECO:0000269|PubMed:20080638, CC ECO:0000269|PubMed:25467444}. CC -!- INTERACTION: CC P50990; P46379-2: BAG6; NbExp=3; IntAct=EBI-356507, EBI-10988864; CC P50990; Q0VDD7: BRME1; NbExp=3; IntAct=EBI-356507, EBI-741210; CC P50990; P40227: CCT6A; NbExp=4; IntAct=EBI-356507, EBI-356687; CC P50990; Q6ZTQ4: CDHR3; NbExp=3; IntAct=EBI-356507, EBI-12143631; CC P50990; P42858: HTT; NbExp=4; IntAct=EBI-356507, EBI-466029; CC P50990; Q8N7X4: MAGEB6; NbExp=3; IntAct=EBI-356507, EBI-6447163; CC P50990; Q9UMY4: SNX12; NbExp=3; IntAct=EBI-356507, EBI-1752602; CC P50990; P17987: TCP1; NbExp=2; IntAct=EBI-356507, EBI-356553; CC P50990; P68363-2: TUBA1B; NbExp=3; IntAct=EBI-356507, EBI-25895616; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20080638}. CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome CC {ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:20080638}. Cytoplasm, CC cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:P42932}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P50990-1; Sequence=Displayed; CC Name=2; CC IsoId=P50990-2; Sequence=VSP_054692; CC Name=3; CC IsoId=P50990-3; Sequence=VSP_054691; CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA02792.2; 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; D13627; BAA02792.2; ALT_INIT; mRNA. DR EMBL; D42052; BAA07652.1; ALT_SEQ; Genomic_DNA. DR EMBL; AF129075; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AK293705; BAG57138.1; -; mRNA. DR EMBL; AK298801; BAG60936.1; -; mRNA. DR EMBL; AL163249; CAB90433.1; -; Genomic_DNA. DR EMBL; BC072001; AAH72001.1; -; mRNA. DR EMBL; BC095470; AAH95470.1; -; mRNA. DR EMBL; Z37163; CAA85520.1; -; mRNA. DR CCDS; CCDS33528.1; -. [P50990-1] DR CCDS; CCDS68180.1; -. [P50990-3] DR CCDS; CCDS68181.1; -. [P50990-2] DR PIR; PC4021; PC4021. DR RefSeq; NP_001269836.1; NM_001282907.1. [P50990-2] DR RefSeq; NP_001269838.1; NM_001282909.1. [P50990-3] DR RefSeq; NP_006576.2; NM_006585.3. [P50990-1] DR PDB; 6NR8; EM; 7.80 A; H/P=14-527. DR PDB; 6NR9; EM; 8.50 A; H/P=14-527. DR PDB; 6NRA; EM; 7.70 A; H/P=14-527. DR PDB; 6NRB; EM; 8.70 A; H/P=14-527. DR PDB; 6NRC; EM; 8.30 A; H/P=14-527. DR PDB; 6NRD; EM; 8.20 A; H/P=14-527. DR PDB; 6QB8; EM; 3.97 A; Q/q=1-548. DR PDB; 7LUM; EM; 4.50 A; B/J=1-548. DR PDB; 7LUP; EM; 6.20 A; B/J=1-548. DR PDB; 7NVL; EM; 2.50 A; Q/q=1-548. DR PDB; 7NVM; EM; 3.10 A; Q/q=1-548. DR PDB; 7NVN; EM; 3.00 A; Q/q=1-548. DR PDB; 7NVO; EM; 3.50 A; Q/q=1-548. DR PDB; 7TRG; EM; 3.00 A; B=1-547. DR PDB; 7TTN; EM; 3.30 A; B=1-547. DR PDB; 7TTT; EM; 2.90 A; B=1-547. DR PDB; 7TUB; EM; 3.60 A; B=1-547. DR PDB; 7WU7; EM; 3.85 A; H/P=1-547. DR PDB; 7WZ3; EM; 4.10 A; Q/q=1-548. DR PDB; 7X0A; EM; 3.10 A; Q/q=1-548. DR PDB; 7X0S; EM; 3.10 A; J/P=1-548. DR PDB; 7X0V; EM; 3.20 A; J/P=1-548. DR PDB; 7X3J; EM; 4.20 A; Q/q=1-548. DR PDB; 7X3U; EM; 3.30 A; Q/q=1-548. DR PDB; 7X6Q; EM; 4.50 A; J/P=1-548. DR PDB; 7X7Y; EM; 3.80 A; Q/q=1-548. DR PDB; 8SFE; EM; 3.36 A; Q/q=2-539. DR PDB; 8SFF; EM; 3.20 A; Q/q=2-539. DR PDB; 8SG8; EM; 3.00 A; Q/q=2-539. DR PDB; 8SG9; EM; 2.90 A; Q/q=2-539. DR PDB; 8SGC; EM; 2.90 A; Q/q=2-539. DR PDB; 8SGL; EM; 2.90 A; Q/q=2-539. DR PDB; 8SGQ; EM; 3.70 A; Q/q=29-526. DR PDB; 8SH9; EM; 2.70 A; Q/q=2-539. DR PDB; 8SHA; EM; 3.00 A; Q/q=2-539. DR PDB; 8SHD; EM; 2.90 A; Q/q=2-539. DR PDB; 8SHE; EM; 2.80 A; Q/q=2-539. DR PDB; 8SHF; EM; 3.00 A; Q/q=2-539. DR PDB; 8SHG; EM; 2.80 A; Q/q=2-539. DR PDB; 8SHL; EM; 3.00 A; Q/q=2-539. DR PDB; 8SHN; EM; 2.80 A; Q/q=2-539. DR PDB; 8SHO; EM; 3.00 A; Q/q=2-539. DR PDB; 8SHP; EM; 3.00 A; Q/q=2-539. DR PDB; 8SHQ; EM; 2.90 A; Q/q=2-539. DR PDB; 8SHT; EM; 3.00 A; Q/q=2-539. 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; P50990; -. 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; P50990; -. DR BioGRID; 115933; 602. DR ComplexPortal; CPX-6030; Chaperonin-containing T-complex. DR CORUM; P50990; -. DR DIP; DIP-38124N; -. DR IntAct; P50990; 211. DR MINT; P50990; -. DR STRING; 9606.ENSP00000286788; -. DR ChEMBL; CHEMBL4295775; -. DR GlyGen; P50990; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; P50990; -. DR MetOSite; P50990; -. DR PhosphoSitePlus; P50990; -. DR SwissPalm; P50990; -. DR BioMuta; CCT8; -. DR DMDM; 9988062; -. DR OGP; P50990; -. DR REPRODUCTION-2DPAGE; IPI00784090; -. DR REPRODUCTION-2DPAGE; P50990; -. DR CPTAC; CPTAC-331; -. DR CPTAC; CPTAC-332; -. DR EPD; P50990; -. DR jPOST; P50990; -. DR MassIVE; P50990; -. DR MaxQB; P50990; -. DR PaxDb; 9606-ENSP00000286788; -. DR PeptideAtlas; P50990; -. DR PRIDE; P50990; -. DR ProteomicsDB; 3972; -. DR ProteomicsDB; 4872; -. DR ProteomicsDB; 56272; -. [P50990-1] DR Pumba; P50990; -. DR TopDownProteomics; P50990-1; -. [P50990-1] DR Antibodypedia; 6409; 325 antibodies from 32 providers. DR DNASU; 10694; -. DR Ensembl; ENST00000286788.9; ENSP00000286788.4; ENSG00000156261.13. [P50990-1] DR Ensembl; ENST00000540844.5; ENSP00000442730.1; ENSG00000156261.13. [P50990-3] DR Ensembl; ENST00000626972.2; ENSP00000486921.1; ENSG00000156261.13. [P50990-2] DR Ensembl; ENST00000707884.1; ENSP00000517017.1; ENSG00000291533.1. [P50990-1] DR Ensembl; ENST00000707885.1; ENSP00000517018.1; ENSG00000291533.1. [P50990-2] DR Ensembl; ENST00000707892.1; ENSP00000517020.1; ENSG00000291533.1. [P50990-3] DR GeneID; 10694; -. DR KEGG; hsa:10694; -. DR MANE-Select; ENST00000286788.9; ENSP00000286788.4; NM_006585.4; NP_006576.2. DR UCSC; uc002ynb.5; human. [P50990-1] DR AGR; HGNC:1623; -. DR CTD; 10694; -. DR DisGeNET; 10694; -. DR GeneCards; CCT8; -. DR HGNC; HGNC:1623; CCT8. DR HPA; ENSG00000156261; Low tissue specificity. DR MIM; 617786; gene. DR neXtProt; NX_P50990; -. DR OpenTargets; ENSG00000156261; -. DR PharmGKB; PA26186; -. DR VEuPathDB; HostDB:ENSG00000156261; -. DR eggNOG; KOG0362; Eukaryota. DR GeneTree; ENSGT00550000074783; -. DR InParanoid; P50990; -. DR OMA; WGLKYAV; -. DR OrthoDB; 1103624at2759; -. DR PhylomeDB; P50990; -. DR TreeFam; TF105699; -. DR BRENDA; 3.6.4.B10; 2681. DR PathwayCommons; P50990; -. 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-6798695; Neutrophil degranulation. DR Reactome; R-HSA-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding. DR SignaLink; P50990; -. DR SIGNOR; P50990; -. DR BioGRID-ORCS; 10694; 807 hits in 1135 CRISPR screens. DR ChiTaRS; CCT8; human. DR GeneWiki; CCT8; -. DR GenomeRNAi; 10694; -. DR Pharos; P50990; Tbio. DR PRO; PR:P50990; -. DR Proteomes; UP000005640; Chromosome 21. DR RNAct; P50990; Protein. DR Bgee; ENSG00000156261; Expressed in oocyte and 217 other cell types or tissues. DR ExpressionAtlas; P50990; baseline and differential. DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome. DR GO; GO:0044297; C:cell body; IEA:Ensembl. DR GO; GO:0005813; C:centrosome; IDA:MGI. DR GO; GO:0005832; C:chaperonin-containing T-complex; IDA:UniProtKB. DR GO; GO:0005929; C:cilium; IEA:UniProtKB-KW. DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome. DR GO; GO:0045111; C:intermediate filament cytoskeleton; IDA:HPA. DR GO; GO:0005874; C:microtubule; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome. 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:0045296; F:cadherin binding; HDA:BHF-UCL. DR GO; GO:0044183; F:protein folding chaperone; IDA:FlyBase. 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; cd03341; TCP1_theta; 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; IPR012721; Chap_CCT_theta. 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; TIGR02346; chap_CCT_theta; 1. DR PANTHER; PTHR11353; CHAPERONIN; 1. DR PANTHER; PTHR11353:SF78; T-COMPLEX PROTEIN 1 SUBUNIT THETA; 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 Genevisible; P50990; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; KW Cell projection; Chaperone; Cilium; Cytoplasm; Cytoskeleton; KW Direct protein sequencing; Isopeptide bond; Nucleotide-binding; KW Phosphoprotein; Reference proteome; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.7" FT CHAIN 2..548 FT /note="T-complex protein 1 subunit theta" FT /id="PRO_0000128373" FT REGION 529..548 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|Ref.7" FT MOD_RES 23 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163" FT MOD_RES 30 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163" FT MOD_RES 162 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 213 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 269 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 317 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 318 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 400 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 466 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 505 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:15592455" FT MOD_RES 537 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CROSSLNK 224 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 254 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 260 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 459 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1)" FT /evidence="ECO:0007744|PubMed:25114211" FT CROSSLNK 534 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733" FT CROSSLNK 539 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25755297, FT ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..78 FT /note="MALHVPKAPGFAQMLKEGAKHFSGLEEAVYRNIQACKELAQTTRTAYGPNGM FT NKMVINHLEKLFVTNDAATILRELEV -> MDQMV (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_054691" FT VAR_SEQ 1..20 FT /note="MALHVPKAPGFAQMLKEGAK -> M (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_054692" FT VARIANT 4 FT /note="H -> Q (in dbSNP:rs16983693)" FT /id="VAR_052270" FT VARIANT 409 FT /note="V -> I (in dbSNP:rs8129954)" FT /id="VAR_052271" FT CONFLICT 50 FT /note="N -> K (in Ref. 1 and 2)" FT /evidence="ECO:0000305" FT CONFLICT 391 FT /note="A -> V (in Ref. 1; BAA02792)" FT /evidence="ECO:0000305" FT HELIX 11..14 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 20..23 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 24..27 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 29..44 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 53..57 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 63..66 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 69..75 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 81..96 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 97..99 FT /evidence="ECO:0007829|PDB:7NVO" FT HELIX 101..121 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 125..146 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 149..151 FT /evidence="ECO:0007829|PDB:7X0S" FT HELIX 158..164 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 167..170 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 177..189 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 193..195 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 199..201 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 202..210 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 212..214 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 216..224 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 228..230 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 233..237 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 240..244 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 255..259 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 262..285 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 290..295 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 299..307 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 311..314 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 318..328 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 333..335 FT /evidence="ECO:0007829|PDB:7NVL" FT TURN 341..343 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 347..355 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 358..364 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 366..368 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 373..380 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 382..404 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 407..410 FT /evidence="ECO:0007829|PDB:7NVL" FT TURN 411..413 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 414..429 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 434..445 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 447..456 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 460..473 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 478..480 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 483..486 FT /evidence="ECO:0007829|PDB:7X0S" FT STRAND 489..491 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 492..495 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 498..500 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 501..520 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 521..526 FT /evidence="ECO:0007829|PDB:7NVL" FT TURN 536..538 FT /evidence="ECO:0007829|PDB:7NVM" SQ SEQUENCE 548 AA; 59621 MW; 566A6622BC2D15E9 CRC64; MALHVPKAPG FAQMLKEGAK HFSGLEEAVY RNIQACKELA QTTRTAYGPN GMNKMVINHL EKLFVTNDAA TILRELEVQH PAAKMIVMAS HMQEQEVGDG TNFVLVFAGA LLELAEELLR IGLSVSEVIE GYEIACRKAH EILPNLVCCS AKNLRDIDEV SSLLRTSIMS KQYGNEVFLA KLIAQACVSI FPDSGHFNVD NIRVCKILGS GISSSSVLHG MVFKKETEGD VTSVKDAKIA VYSCPFDGMI TETKGTVLIK TAEELMNFSK GEENLMDAQV KAIADTGANV VVTGGKVADM ALHYANKYNI MLVRLNSKWD LRRLCKTVGA TALPRLTPPV LEEMGHCDSV YLSEVGDTQV VVFKHEKEDG AISTIVLRGS TDNLMDDIER AVDDGVNTFK VLTRDKRLVP GGGATEIELA KQITSYGETC PGLEQYAIKK FAEAFEAIPR ALAENSGVKA NEVISKLYAV HQEGNKNVGL DIEAEVPAVK DMLEAGILDT YLGKYWAIKL ATNAAVTVLR VDQIIMAKPA GGPKPPSGKK DWDDDQND //