ID TCPA_HUMAN Reviewed; 556 AA. AC P17987; E1P5B2; Q15556; Q5TCM3; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1990, sequence version 1. DT 27-MAR-2024, entry version 230. DE RecName: Full=T-complex protein 1 subunit alpha; DE Short=TCP-1-alpha; DE AltName: Full=CCT-alpha; GN Name=TCP1; Synonyms=CCT1, CCTA; 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]. RC TISSUE=Testis; RX PubMed=2377466; DOI=10.1093/nar/18.14.4247; RA Kirchhoff C., Willison K.R.; RT "Nucleotide and amino-acid sequence of human testis-derived TCP1."; RL Nucleic Acids Res. 18:4247-4247(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [4] 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Colon; 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 [6] RP PROTEIN SEQUENCE OF 1-11, AND ACETYLATION AT MET-1. RC TISSUE=Platelet; RX PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., RA Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass spectrometric RT identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [7] RP PROTEIN SEQUENCE OF 112-122; 131-145; 248-264; 469-480 AND 516-526, AND RP IDENTIFICATION BY 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 [GENOMIC DNA] OF 308-365 AND 462-516. RX PubMed=3653076; DOI=10.1002/j.1460-2075.1987.tb02459.x; RA Willison K., Kelly A., Dudley K., Goodfellow P., Spurr N., Groves V., RA Gorman P., Sheer D., Trowsdale J.; RT "The human homologue of the mouse T-complex gene, TCP1, is located on RT chromosome 6 but is not near the HLA region."; RL EMBO J. 6:1967-1974(1987). RN [9] RP SUBCELLULAR LOCATION, AND SUBUNIT. RX PubMed=1630492; DOI=10.1038/358249a0; RA Lewis V.A., Hynes G.M., Zheng D., Saibil H., Willison K.R.; RT "T-complex polypeptide-1 is a subunit of a heteromeric particle in the RT eukaryotic cytosol."; RL Nature 358:249-252(1992). 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544, 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 [15] 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 [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-181 AND SER-544, 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 [17] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-199 AND LYS-400, 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 [18] 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 [19] RP INTERACTION WITH GBA1. RX PubMed=21098288; DOI=10.1073/pnas.1014376107; RA Lu J., Chiang J., Iyer R.R., Thompson E., Kaneski C.R., Xu D.S., Yang C., RA Chen M., Hodes R.J., Lonser R.R., Brady R.O., Zhuang Z.; RT "Decreased glucocerebrosidase activity in Gaucher disease parallels RT quantitative enzyme loss due to abnormal interaction with TCP1 and c-Cbl."; RL Proc. Natl. Acad. Sci. U.S.A. 107:21665-21670(2010). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544 AND SER-551, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [21] 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 [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544 AND SER-551, AND RP IDENTIFICATION BY 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 [23] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP 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 [24] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP 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 [25] 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 [26] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-491; SER-544 AND RP SER-551, AND IDENTIFICATION BY MASS SPECTROMETRY [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 [27] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544, 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 [28] 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 [29] 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). RN [30] RP VARIANT [LARGE SCALE ANALYSIS] LEU-7. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). 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:1630492, PubMed:20080638, CC PubMed:25467444). Interacts with PACRG (PubMed:14532270). Interacts CC with GBA1 (PubMed:21098288). Interacts with DLEC1 (PubMed:33144677). CC {ECO:0000269|PubMed:14532270, ECO:0000269|PubMed:1630492, CC ECO:0000269|PubMed:20080638, ECO:0000269|PubMed:21098288, CC ECO:0000269|PubMed:25467444, ECO:0000269|PubMed:33144677}. CC -!- INTERACTION: CC P17987; Q9Y2Y0: ARL2BP; NbExp=3; IntAct=EBI-356553, EBI-3449344; CC P17987; Q9ULD4-2: BRPF3; NbExp=3; IntAct=EBI-356553, EBI-23662416; CC P17987; O43439: CBFA2T2; NbExp=3; IntAct=EBI-356553, EBI-748628; CC P17987; P78371: CCT2; NbExp=3; IntAct=EBI-356553, EBI-357407; CC P17987; P50991: CCT4; NbExp=2; IntAct=EBI-356553, EBI-356876; CC P17987; P50990: CCT8; NbExp=2; IntAct=EBI-356553, EBI-356507; CC P17987; P04062: GBA1; NbExp=2; IntAct=EBI-356553, EBI-1564609; CC P17987; P83110: HTRA3; NbExp=5; IntAct=EBI-356553, EBI-2867394; CC P17987; P83110-1: HTRA3; NbExp=6; IntAct=EBI-356553, EBI-25469082; CC P17987; P83110-2: HTRA3; NbExp=7; IntAct=EBI-356553, EBI-22017714; CC P17987; P83105: HTRA4; NbExp=7; IntAct=EBI-356553, EBI-21776319; CC P17987; P42858: HTT; NbExp=3; IntAct=EBI-356553, EBI-466029; CC P17987; P78380: OLR1; NbExp=5; IntAct=EBI-356553, EBI-7151999; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:1630492}. CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome CC {ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:20080638}. 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; X52882; CAA37064.1; -; mRNA. DR EMBL; BT006969; AAP35615.1; -; mRNA. DR EMBL; AL135914; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471051; EAW47616.1; -; Genomic_DNA. DR EMBL; CH471051; EAW47618.1; -; Genomic_DNA. DR EMBL; BC000665; AAH00665.1; -; mRNA. DR EMBL; M26885; AAA61059.1; -; Genomic_DNA. DR EMBL; M27272; AAA61060.1; -; Genomic_DNA. DR EMBL; M26889; AAA61060.1; JOINED; Genomic_DNA. DR CCDS; CCDS5269.1; -. DR PIR; S10486; S10486. DR RefSeq; NP_110379.2; NM_030752.2. DR PDB; 6NR8; EM; 7.80 A; A/I=1-534. DR PDB; 6NR9; EM; 8.50 A; A/I=1-534. DR PDB; 6NRA; EM; 7.70 A; A/I=1-534. DR PDB; 6NRB; EM; 8.70 A; A/I=1-534. DR PDB; 6NRC; EM; 8.30 A; A/I=1-534. DR PDB; 6NRD; EM; 8.20 A; A/I=1-534. DR PDB; 6QB8; EM; 3.97 A; A/a=1-556. DR PDB; 7LUM; EM; 4.50 A; G/O=1-556. DR PDB; 7LUP; EM; 6.20 A; G/O=1-556. DR PDB; 7NVL; EM; 2.50 A; A/a=1-556. DR PDB; 7NVM; EM; 3.10 A; A/a=1-556. DR PDB; 7NVN; EM; 3.00 A; A/a=1-556. DR PDB; 7NVO; EM; 3.50 A; A/a=1-556. DR PDB; 7TRG; EM; 3.00 A; G=1-556. DR PDB; 7TTN; EM; 3.30 A; G=1-556. DR PDB; 7TTT; EM; 2.90 A; G=1-556. DR PDB; 7TUB; EM; 3.60 A; G=1-556. DR PDB; 7WU7; EM; 3.85 A; A/I=1-556. DR PDB; 7WZ3; EM; 4.10 A; A/a=1-556. DR PDB; 7X0A; EM; 3.10 A; A/a=1-556. DR PDB; 7X0S; EM; 3.10 A; A/a=1-556. DR PDB; 7X0V; EM; 3.20 A; A/a=1-556. DR PDB; 7X3J; EM; 4.20 A; A/a=1-556. DR PDB; 7X3U; EM; 3.30 A; A/a=1-556. DR PDB; 7X6Q; EM; 4.50 A; A/a=1-556. DR PDB; 7X7Y; EM; 3.80 A; A/a=1-556. DR PDB; 8SFE; EM; 3.36 A; A/a=2-537. DR PDB; 8SFF; EM; 3.20 A; A/a=2-537. DR PDB; 8SG8; EM; 3.00 A; A/a=2-537. DR PDB; 8SG9; EM; 2.90 A; A/a=2-537. DR PDB; 8SGC; EM; 2.90 A; A/a=2-537. DR PDB; 8SGL; EM; 2.90 A; A/a=2-537. DR PDB; 8SGQ; EM; 3.70 A; A/a=2-537. DR PDB; 8SH9; EM; 2.70 A; A/a=2-537. DR PDB; 8SHA; EM; 3.00 A; A/a=2-537. DR PDB; 8SHD; EM; 2.90 A; A/a=2-537. DR PDB; 8SHE; EM; 2.80 A; A/a=2-537. DR PDB; 8SHF; EM; 3.00 A; A/a=2-537. DR PDB; 8SHG; EM; 2.80 A; A/a=2-537. DR PDB; 8SHL; EM; 3.00 A; A/a=2-537. DR PDB; 8SHN; EM; 2.80 A; A/a=2-537. DR PDB; 8SHO; EM; 3.00 A; A/a=2-537. DR PDB; 8SHP; EM; 3.00 A; A/a=2-537. DR PDB; 8SHQ; EM; 2.90 A; A/a=2-537. DR PDB; 8SHT; EM; 3.00 A; A/a=2-537. 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; P17987; -. 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; P17987; -. DR BioGRID; 112810; 593. DR ComplexPortal; CPX-6030; Chaperonin-containing T-complex. DR CORUM; P17987; -. DR DIP; DIP-33676N; -. DR IntAct; P17987; 249. DR MINT; P17987; -. DR STRING; 9606.ENSP00000317334; -. DR GlyGen; P17987; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P17987; -. DR MetOSite; P17987; -. DR PhosphoSitePlus; P17987; -. DR SwissPalm; P17987; -. DR BioMuta; TCP1; -. DR DMDM; 135538; -. DR OGP; P17987; -. DR REPRODUCTION-2DPAGE; IPI00290566; -. DR REPRODUCTION-2DPAGE; P17987; -. DR EPD; P17987; -. DR jPOST; P17987; -. DR MassIVE; P17987; -. DR MaxQB; P17987; -. DR PaxDb; 9606-ENSP00000317334; -. DR PeptideAtlas; P17987; -. DR PRIDE; P17987; -. DR ProteomicsDB; 53538; -. DR Pumba; P17987; -. DR Antibodypedia; 20023; 738 antibodies from 39 providers. DR DNASU; 6950; -. DR Ensembl; ENST00000321394.12; ENSP00000317334.7; ENSG00000120438.12. DR GeneID; 6950; -. DR KEGG; hsa:6950; -. DR MANE-Select; ENST00000321394.12; ENSP00000317334.7; NM_030752.3; NP_110379.2. DR UCSC; uc003qsr.4; human. DR AGR; HGNC:11655; -. DR CTD; 6950; -. DR DisGeNET; 6950; -. DR GeneCards; TCP1; -. DR HGNC; HGNC:11655; TCP1. DR HPA; ENSG00000120438; Low tissue specificity. DR MIM; 186980; gene. DR neXtProt; NX_P17987; -. DR OpenTargets; ENSG00000120438; -. DR PharmGKB; PA36406; -. DR VEuPathDB; HostDB:ENSG00000120438; -. DR eggNOG; KOG0360; Eukaryota. DR GeneTree; ENSGT00550000074878; -. DR InParanoid; P17987; -. DR OMA; RGPNDYQ; -. DR OrthoDB; 212971at2759; -. DR PhylomeDB; P17987; -. DR TreeFam; TF106331; -. DR BRENDA; 3.6.4.B10; 2681. DR PathwayCommons; P17987; -. 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 Reactome; R-HSA-8950505; Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation. DR SignaLink; P17987; -. DR SIGNOR; P17987; -. DR BioGRID-ORCS; 6950; 820 hits in 1161 CRISPR screens. DR ChiTaRS; TCP1; human. DR GeneWiki; T-complex_1; -. DR GenomeRNAi; 6950; -. DR Pharos; P17987; Tbio. DR PRO; PR:P17987; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; P17987; Protein. DR Bgee; ENSG00000120438; Expressed in primordial germ cell in gonad and 200 other cell types or tissues. DR ExpressionAtlas; P17987; baseline and differential. DR GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl. 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:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl. DR GO; GO:0000792; C:heterochromatin; IEA:Ensembl. DR GO; GO:0005874; C:microtubule; IDA:UniProtKB. DR GO; GO:0000242; C:pericentriolar material; IEA:Ensembl. 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:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL. 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:0051973; P:positive regulation of telomerase activity; IMP:BHF-UCL. DR GO; GO:1904874; P:positive regulation of telomerase RNA localization to Cajal body; IMP: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:0090666; P:scaRNA localization to Cajal body; IMP:BHF-UCL. DR GO; GO:0007021; P:tubulin complex assembly; NAS:UniProtKB. DR CDD; cd03335; TCP1_alpha; 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; IPR012715; Chap_CCT_alpha. 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; TIGR02340; chap_CCT_alpha; 1. DR NCBIfam; NF041082; thermosome_alpha; 1. DR NCBIfam; NF041083; thermosome_beta; 1. DR PANTHER; PTHR11353; CHAPERONIN; 1. DR PANTHER; PTHR11353:SF84; T-COMPLEX PROTEIN 1 SUBUNIT ALPHA; 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 UCD-2DPAGE; P17987; -. DR Genevisible; P17987; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; ATP-binding; Chaperone; Cytoplasm; Cytoskeleton; KW Direct protein sequencing; Nucleotide-binding; Phosphoprotein; KW Reference proteome. FT CHAIN 1..556 FT /note="T-complex protein 1 subunit alpha" FT /id="PRO_0000128302" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000269|PubMed:12665801, FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, FT ECO:0007744|PubMed:22814378" FT MOD_RES 6 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 181 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 199 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 491 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 494 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P11983" FT MOD_RES 544 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 551 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT VARIANT 7 FT /note="V -> L (in a breast cancer sample; somatic mutation; FT dbSNP:rs537218073)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036258" FT CONFLICT 480 FT /note="R -> S (in Ref. 8; AAA61060)" FT /evidence="ECO:0000305" FT CONFLICT 537..540 FT /note="SKDD -> ILRI (in Ref. 1; CAA37064)" FT /evidence="ECO:0000305" FT STRAND 8..13 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 15..32 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 33..35 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 37..39 FT /evidence="ECO:0007829|PDB:7NVO" FT STRAND 42..46 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 48..50 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 52..55 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 58..64 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 70..85 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 86..88 FT /evidence="ECO:0007829|PDB:7NVO" FT HELIX 90..109 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 114..135 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 137..139 FT /evidence="ECO:0007829|PDB:7X0A" FT HELIX 140..143 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 146..156 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 160..164 FT /evidence="ECO:0007829|PDB:7X0A" FT HELIX 165..178 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 181..183 FT /evidence="ECO:0007829|PDB:7X0S" FT HELIX 184..186 FT /evidence="ECO:0007829|PDB:7NVM" FT STRAND 187..189 FT /evidence="ECO:0007829|PDB:7X0S" FT STRAND 194..199 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 205..207 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 209..217 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 227..239 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 250..252 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 254..256 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 257..259 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 260..280 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 285..290 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 294..303 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 306..308 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 313..323 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 328..331 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 334..336 FT /evidence="ECO:0007829|PDB:7X0A" FT HELIX 342..344 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 346..356 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 359..370 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 373..377 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..426 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 427..429 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 433..445 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 447..456 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 460..476 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 478..485 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 486..489 FT /evidence="ECO:0007829|PDB:7NVL" FT TURN 490..493 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 494..497 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 498..501 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 504..506 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 507..525 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 527..533 FT /evidence="ECO:0007829|PDB:7NVL" SQ SEQUENCE 556 AA; 60344 MW; 486ECA836EA258A1 CRC64; MEGPLSVFGD RSTGETIRSQ NVMAAASIAN IVKSSLGPVG LDKMLVDDIG DVTITNDGAT ILKLLEVEHP AAKVLCELAD LQDKEVGDGT TSVVIIAAEL LKNADELVKQ KIHPTSVISG YRLACKEAVR YINENLIVNT DELGRDCLIN AAKTSMSSKI IGINGDFFAN MVVDAVLAIK YTDIRGQPRY PVNSVNILKA HGRSQMESML ISGYALNCVV GSQGMPKRIV NAKIACLDFS LQKTKMKLGV QVVITDPEKL DQIRQRESDI TKERIQKILA TGANVILTTG GIDDMCLKYF VEAGAMAVRR VLKRDLKRIA KASGATILST LANLEGEETF EAAMLGQAEE VVQERICDDE LILIKNTKAR TSASIILRGA NDFMCDEMER SLHDALCVVK RVLESKSVVP GGGAVEAALS IYLENYATSM GSREQLAIAE FARSLLVIPN TLAVNAAQDS TDLVAKLRAF HNEAQVNPER KNLKWIGLDL SNGKPRDNKQ AGVFEPTIVK VKSLKFATEA AITILRIDDL IKLHPESKDD KHGSYEDAVH SGALND //