TCPH_HUMAN
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 03-AUG-2022, entry version 209.
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}.
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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. [Q99832-3]
DR RefSeq; XP_011530781.1; XM_011532479.1. [Q99832-3]
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 PDBsum; 6NR8; -.
DR PDBsum; 6NR9; -.
DR PDBsum; 6NRA; -.
DR PDBsum; 6NRB; -.
DR PDBsum; 6NRC; -.
DR PDBsum; 6NRD; -.
DR PDBsum; 6QB8; -.
DR PDBsum; 7LUM; -.
DR PDBsum; 7LUP; -.
DR PDBsum; 7NVL; -.
DR PDBsum; 7NVM; -.
DR PDBsum; 7NVN; -.
DR PDBsum; 7NVO; -.
DR AlphaFoldDB; Q99832; -.
DR SMR; Q99832; -.
DR BioGRID; 115825; 483.
DR ComplexPortal; CPX-6030; Chaperonin-containing T-complex.
DR CORUM; Q99832; -.
DR DIP; DIP-51608N; -.
DR IntAct; Q99832; 270.
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; Q99832; -.
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 Antibodypedia; 1382; 282 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 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; 335406at2759; -.
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 BioGRID-ORCS; 10574; 614 hits in 1074 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 208 other tissues.
DR ExpressionAtlas; Q99832; baseline and differential.
DR Genevisible; Q99832; HS.
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 GO; GO:1901998; P:toxin transport; IEA:Ensembl.
DR CDD; cd03340; TCP1_eta; 1.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 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 PANTHER; PTHR11353; PTHR11353; 1.
DR PANTHER; PTHR11353:SF22; PTHR11353:SF22; 1.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR PRINTS; PR00304; TCOMPLEXTCP1.
DR SUPFAM; SSF48592; SSF48592; 1.
DR SUPFAM; SSF52029; SSF52029; 1.
DR SUPFAM; SSF54849; SSF54849; 1.
DR TIGRFAMs; TIGR02345; chap_CCT_eta; 1.
DR PROSITE; PS00750; TCP1_1; 1.
DR PROSITE; PS00751; TCP1_2; 1.
DR PROSITE; PS00995; TCP1_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; Chaperone;
KW Cytoplasm; Direct protein sequencing; 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 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
