ID TCPH_HUMAN Reviewed; 543 AA. AC Q99832; A8K7E6; A8MWI8; B7WNW9; B7Z4T9; B7Z4Z7; O14871; Q6FI26; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 2. DT 27-MAR-2024, entry version 218. DE RecName: Full=T-complex protein 1 subunit eta; DE Short=TCP-1-eta; DE AltName: Full=CCT-eta; DE AltName: Full=HIV-1 Nef-interacting protein; DE Contains: DE RecName: Full=T-complex protein 1 subunit eta, N-terminally processed; GN Name=CCT7; Synonyms=CCTH, NIP7-1; 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 [MRNA] (ISOFORM 1). RX PubMed=9819444; DOI=10.1128/mcb.18.12.7584; RA Won K.-A., Schumacher R.J., Farr G.W., Horwich A.L., Reed S.I.; RT "Maturation of human cyclin E requires the function of eukaryotic RT chaperonin CCT."; RL Mol. Cell. Biol. 18:7584-7589(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., RA LaBaer J.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4). RC TISSUE=Cerebellum, and Heart; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=PNS, and Skin; 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 1-10; 56-67; 85-123; 127-144; 178-193; 200-217; RP 219-230; 237-247; 293-306; 314-320; 376-397; 402-418; 431-447 AND 500-535, RP ACETYLATION AT MET-1, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Colon carcinoma, Hepatoma, and Osteosarcoma; RA Bienvenut W.V., Glen H., Brunton V.G., Frame M.C., Boldt K., RA von Kriegsheim A.F., Kolch W.; RL Submitted (DEC-2008) to UniProtKB. RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 13-424 (ISOFORM 1). RA Fukushi M., Kimura T., Yamamoto N.; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. RN [9] RP PROTEIN SEQUENCE OF 107-123, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Brain, and Cajal-Retzius cell; RA Lubec G., Afjehi-Sadat L.; RL Submitted (MAR-2007) to UniProtKB. 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. 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 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 [13] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-67 AND LYS-320, 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 [14] 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 [15] RP CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORM 3), AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). 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 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 [19] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-535, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [20] 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 [21] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-430, AND IDENTIFICATION BY MASS RP 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 [22] 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). The TRiC complex plays a role in the folding of CC actin and tubulin (Probable). {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:25467444). Interacts with PACRG CC (PubMed:14532270). Interacts with DLEC1 (PubMed:33144677). CC {ECO:0000269|PubMed:14532270, ECO:0000269|PubMed:25467444, CC ECO:0000269|PubMed:33144677}. CC -!- INTERACTION: CC Q99832; P78371: CCT2; NbExp=2; IntAct=EBI-357046, EBI-357407; CC Q99832; A0A024RCP2: DOM3Z; NbExp=3; IntAct=EBI-357046, EBI-25847826; CC Q99832; Q02575: NHLH1; NbExp=3; IntAct=EBI-357046, EBI-3930567; CC Q99832; Q6PHZ7: NR2C2; NbExp=3; IntAct=EBI-357046, EBI-2802743; CC Q99832; O15534: PER1; NbExp=3; IntAct=EBI-357046, EBI-2557276; CC Q99832; Q969T9: WBP2; NbExp=3; IntAct=EBI-357046, EBI-727055; CC Q99832; Q9BYN7-2: ZNF341; NbExp=3; IntAct=EBI-357046, EBI-16435478; CC Q99832; O60232: ZNRD2; NbExp=7; IntAct=EBI-357046, EBI-741415; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P80313}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q99832-1; Sequence=Displayed; CC Name=2; CC IsoId=Q99832-2; Sequence=VSP_043573, VSP_043574; CC Name=3; CC IsoId=Q99832-3; Sequence=VSP_043572; CC Name=4; CC IsoId=Q99832-4; Sequence=VSP_043573; CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {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; AF026292; AAC96011.1; -; mRNA. DR EMBL; CR536511; CAG38749.1; -; mRNA. DR EMBL; AK291961; BAF84650.1; -; mRNA. DR EMBL; AK293597; BAH11543.1; -; mRNA. DR EMBL; AK297846; BAH12675.1; -; mRNA. DR EMBL; AK298153; BAH12733.1; -; mRNA. DR EMBL; AC010913; AAX88902.1; -; Genomic_DNA. DR EMBL; CH471053; EAW99739.1; -; Genomic_DNA. DR EMBL; CH471053; EAW99740.1; -; Genomic_DNA. DR EMBL; BC019296; AAH19296.1; -; mRNA. DR EMBL; BC088351; AAH88351.1; -; mRNA. DR EMBL; U83843; AAB41437.1; -; mRNA. DR CCDS; CCDS42696.1; -. [Q99832-2] DR CCDS; CCDS46336.1; -. [Q99832-1] DR CCDS; CCDS54366.1; -. [Q99832-4] DR CCDS; CCDS54367.1; -. [Q99832-3] DR RefSeq; NP_001009570.1; NM_001009570.2. [Q99832-2] DR RefSeq; NP_001159756.1; NM_001166284.1. [Q99832-4] DR RefSeq; NP_001159757.1; NM_001166285.1. [Q99832-3] DR RefSeq; NP_006420.1; NM_006429.3. [Q99832-1] DR RefSeq; XP_011530780.1; XM_011532478.2. DR RefSeq; XP_011530781.1; XM_011532479.1. DR PDB; 6NR8; EM; 7.80 A; G/O=12-525. DR PDB; 6NR9; EM; 8.50 A; G/O=12-525. DR PDB; 6NRA; EM; 7.70 A; G/O=12-525. DR PDB; 6NRB; EM; 8.70 A; G/O=12-525. DR PDB; 6NRC; EM; 8.30 A; G/O=12-525. DR PDB; 6NRD; EM; 8.20 A; G/O=12-525. DR PDB; 6QB8; EM; 3.97 A; H/h=1-543. DR PDB; 7LUM; EM; 4.50 A; C/K=1-543. DR PDB; 7LUP; EM; 6.20 A; C/K=1-543. DR PDB; 7NVL; EM; 2.50 A; H/h=1-543. DR PDB; 7NVM; EM; 3.10 A; H/h=1-543. DR PDB; 7NVN; EM; 3.00 A; H/h=1-543. DR PDB; 7NVO; EM; 3.50 A; H/h=1-543. DR PDB; 7TRG; EM; 3.00 A; C=1-542. DR PDB; 7TTN; EM; 3.30 A; C=1-543. DR PDB; 7TTT; EM; 2.90 A; C=1-543. DR PDB; 7TUB; EM; 3.60 A; C=1-543. DR PDB; 7WU7; EM; 3.85 A; G/O=1-543. DR PDB; 7WZ3; EM; 4.10 A; H/h=1-543. DR PDB; 7X0A; EM; 3.10 A; H/h=1-543. DR PDB; 7X0S; EM; 3.10 A; H/O=1-543. DR PDB; 7X0V; EM; 3.20 A; H/O=1-543. DR PDB; 7X3J; EM; 4.20 A; H/h=1-543. DR PDB; 7X3U; EM; 3.30 A; H/h=1-543. DR PDB; 7X6Q; EM; 4.50 A; H/O=1-543. DR PDB; 7X7Y; EM; 3.80 A; H/h=1-543. DR PDB; 8SFE; EM; 3.36 A; H/h=1-528. DR PDB; 8SFF; EM; 3.20 A; H/h=1-528. DR PDB; 8SG8; EM; 3.00 A; H/h=1-528. DR PDB; 8SG9; EM; 2.90 A; H/h=1-528. DR PDB; 8SGC; EM; 2.90 A; H/h=1-528. DR PDB; 8SGL; EM; 2.90 A; H/h=1-528. DR PDB; 8SGQ; EM; 3.70 A; H/h=12-525. DR PDB; 8SH9; EM; 2.70 A; H/h=1-528. DR PDB; 8SHA; EM; 3.00 A; H/h=1-528. DR PDB; 8SHD; EM; 2.90 A; H/h=1-528. DR PDB; 8SHE; EM; 2.80 A; H/h=1-528. DR PDB; 8SHF; EM; 3.00 A; H/h=1-528. DR PDB; 8SHG; EM; 2.80 A; H/h=1-528. DR PDB; 8SHL; EM; 3.00 A; H/h=1-528. DR PDB; 8SHN; EM; 2.80 A; H/h=1-528. DR PDB; 8SHO; EM; 3.00 A; H/h=1-528. DR PDB; 8SHP; EM; 3.00 A; H/h=1-528. DR PDB; 8SHQ; EM; 2.90 A; H/h=1-528. DR PDB; 8SHT; EM; 3.00 A; H/h=1-528. 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; Q99832; -. 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-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; Q99832; -. DR BioGRID; 115825; 585. DR ComplexPortal; CPX-6030; Chaperonin-containing T-complex. DR CORUM; Q99832; -. DR DIP; DIP-51608N; -. DR IntAct; Q99832; 273. DR MINT; Q99832; -. DR STRING; 9606.ENSP00000258091; -. DR GlyGen; Q99832; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q99832; -. DR MetOSite; Q99832; -. DR PhosphoSitePlus; Q99832; -. DR SwissPalm; Q99832; -. DR BioMuta; CCT7; -. DR DMDM; 3041738; -. DR REPRODUCTION-2DPAGE; IPI00018465; -. DR CPTAC; CPTAC-181; -. DR EPD; Q99832; -. DR jPOST; Q99832; -. DR MassIVE; Q99832; -. DR MaxQB; Q99832; -. DR PaxDb; 9606-ENSP00000258091; -. DR PeptideAtlas; Q99832; -. DR PRIDE; Q99832; -. DR ProteomicsDB; 78495; -. [Q99832-1] DR ProteomicsDB; 78496; -. [Q99832-2] DR ProteomicsDB; 78497; -. [Q99832-3] DR ProteomicsDB; 78498; -. [Q99832-4] DR Pumba; Q99832; -. DR Antibodypedia; 1382; 304 antibodies from 31 providers. DR DNASU; 10574; -. DR Ensembl; ENST00000258091.10; ENSP00000258091.5; ENSG00000135624.17. [Q99832-1] DR Ensembl; ENST00000398422.2; ENSP00000381456.2; ENSG00000135624.17. [Q99832-2] DR Ensembl; ENST00000539919.5; ENSP00000437824.1; ENSG00000135624.17. [Q99832-3] DR Ensembl; ENST00000540468.5; ENSP00000442058.1; ENSG00000135624.17. [Q99832-4] DR GeneID; 10574; -. DR KEGG; hsa:10574; -. DR MANE-Select; ENST00000258091.10; ENSP00000258091.5; NM_006429.4; NP_006420.1. DR UCSC; uc002siz.4; human. [Q99832-1] DR AGR; HGNC:1622; -. DR CTD; 10574; -. DR DisGeNET; 10574; -. DR GeneCards; CCT7; -. DR HGNC; HGNC:1622; CCT7. DR HPA; ENSG00000135624; Low tissue specificity. DR MalaCards; CCT7; -. DR MIM; 605140; gene. DR neXtProt; NX_Q99832; -. DR OpenTargets; ENSG00000135624; -. DR PharmGKB; PA26185; -. DR VEuPathDB; HostDB:ENSG00000135624; -. DR eggNOG; KOG0361; Eukaryota. DR GeneTree; ENSGT00550000074832; -. DR HOGENOM; CLU_008891_7_1_1; -. DR InParanoid; Q99832; -. DR OMA; HRKGNTW; -. DR OrthoDB; 212971at2759; -. DR PhylomeDB; Q99832; -. DR TreeFam; TF105641; -. DR BRENDA; 3.6.4.B10; 2681. DR PathwayCommons; Q99832; -. 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-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding. DR Reactome; R-HSA-9013418; RHOBTB2 GTPase cycle. DR Reactome; R-HSA-9013422; RHOBTB1 GTPase cycle. DR SignaLink; Q99832; -. DR SIGNOR; Q99832; -. DR BioGRID-ORCS; 10574; 646 hits in 1153 CRISPR screens. DR ChiTaRS; CCT7; human. DR GeneWiki; CCT7; -. DR GenomeRNAi; 10574; -. DR Pharos; Q99832; Tbio. DR PRO; PR:Q99832; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q99832; Protein. DR Bgee; ENSG00000135624; Expressed in ganglionic eminence and 210 other cell types or tissues. DR ExpressionAtlas; Q99832; 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:0005737; C:cytoplasm; 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: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: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; cd03340; TCP1_eta; 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; IPR012720; Chap_CCT_eta. 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; TIGR02345; chap_CCT_eta; 1. DR NCBIfam; NF041082; thermosome_alpha; 1. DR NCBIfam; NF041083; thermosome_beta; 1. DR PANTHER; PTHR11353; CHAPERONIN; 1. DR PANTHER; PTHR11353:SF22; T-COMPLEX PROTEIN 1 SUBUNIT ETA; 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; Q99832; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; Chaperone; KW Cytoplasm; Direct protein sequencing; Isopeptide bond; Methylation; KW Nucleotide-binding; Reference proteome; Ubl conjugation. FT CHAIN 1..543 FT /note="T-complex protein 1 subunit eta" FT /id="PRO_0000128365" FT INIT_MET 1 FT /note="Removed; alternate" FT /evidence="ECO:0007744|PubMed:22223895" FT CHAIN 2..543 FT /note="T-complex protein 1 subunit eta, N-terminally FT processed" FT /id="PRO_0000434391" FT REGION 524..543 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330" FT MOD_RES 67 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 250 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P80313" FT MOD_RES 320 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 535 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT CROSSLNK 430 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..44 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_043572" FT VAR_SEQ 3..89 FT /note="Missing (in isoform 2 and isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_043573" FT VAR_SEQ 90..206 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_043574" FT VARIANT 259 FT /note="T -> A (in dbSNP:rs2231427)" FT /id="VAR_052269" FT CONFLICT 282..283 FT /note="HH -> RQ (in Ref. 8; AAB41437)" FT /evidence="ECO:0000305" FT CONFLICT 293 FT /note="L -> P (in Ref. 8; AAB41437)" FT /evidence="ECO:0000305" FT CONFLICT 336 FT /note="A -> P (in Ref. 8; AAB41437)" FT /evidence="ECO:0000305" FT CONFLICT 364 FT /note="C -> L (in Ref. 8; AAB41437)" FT /evidence="ECO:0000305" FT CONFLICT 374..376 FT /note="LRG -> SPC (in Ref. 8; AAB41437)" FT /evidence="ECO:0000305" FT CONFLICT 407 FT /note="A -> P (in Ref. 8; AAB41437)" FT /evidence="ECO:0000305" FT CONFLICT 411 FT /note="A -> P (in Ref. 8; AAB41437)" FT /evidence="ECO:0000305" FT STRAND 9..12 FT /evidence="ECO:0007829|PDB:7X0A" FT STRAND 14..18 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 19..37 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 41..43 FT /evidence="ECO:0007829|PDB:7NVO" FT STRAND 46..50 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 56..59 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 62..68 FT /evidence="ECO:0007829|PDB:7NVL" FT TURN 74..76 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 77..89 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 94..113 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 118..139 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 148..163 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 169..171 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 172..184 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 192..194 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 195..203 FT /evidence="ECO:0007829|PDB:7NVL" FT TURN 205..207 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 209..217 FT /evidence="ECO:0007829|PDB:7NVL" FT TURN 223..227 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 231..234 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 236..240 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 244..246 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 253..259 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 260..283 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 287..293 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 297..305 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 309..311 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 316..326 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 330..332 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 334..336 FT /evidence="ECO:0007829|PDB:7X0S" FT TURN 339..341 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 342..344 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 346..353 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 356..362 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 370..378 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 379..401 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 405..407 FT /evidence="ECO:0007829|PDB:7NVL" FT TURN 408..410 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 411..424 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 430..442 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 444..453 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 457..469 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 473..478 FT /evidence="ECO:0007829|PDB:7NVL" FT TURN 479..482 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 483..486 FT /evidence="ECO:0007829|PDB:7NVL" FT TURN 487..491 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 493..495 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 496..515 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 516..521 FT /evidence="ECO:0007829|PDB:7NVL" FT MOD_RES Q99832-3:1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22814378" SQ SEQUENCE 543 AA; 59367 MW; 9F1E33FA80E6238E CRC64; MMPTPVILLK EGTDSSQGIP QLVSNISACQ VIAEAVRTTL GPRGMDKLIV DGRGKATISN DGATILKLLD VVHPAAKTLV DIAKSQDAEV GDGTTSVTLL AAEFLKQVKP YVEEGLHPQI IIRAFRTATQ LAVNKIKEIA VTVKKADKVE QRKLLEKCAM TALSSKLISQ QKAFFAKMVV DAVMMLDDLL QLKMIGIKKV QGGALEDSQL VAGVAFKKTF SYAGFEMQPK KYHNPKIALL NVELELKAEK DNAEIRVHTV EDYQAIVDAE WNILYDKLEK IHHSGAKVVL SKLPIGDVAT QYFADRDMFC AGRVPEEDLK RTMMACGGSI QTSVNALSAD VLGRCQVFEE TQIGGERYNF FTGCPKAKTC TFILRGGAEQ FMEETERSLH DAIMIVRRAI KNDSVVAGGG AIEMELSKYL RDYSRTIPGK QQLLIGAYAK ALEIIPRQLC DNAGFDATNI LNKLRARHAQ GGTWYGVDIN NEDIADNFEA FVWEPAMVRI NALTAASEAA CLIVSVDETI KNPRSTVDAP TAAGRGRGRG RPH //