TCPA_HUMAN
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 03-AUG-2022, entry version 221.
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 GBA.
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 GBA (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: GBA; 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}.
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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 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; P17987; -.
DR SMR; P17987; -.
DR BioGRID; 112810; 494.
DR ComplexPortal; CPX-6030; Chaperonin-containing T-complex.
DR CORUM; P17987; -.
DR DIP; DIP-33676N; -.
DR IntAct; P17987; 247.
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 UCD-2DPAGE; P17987; -.
DR EPD; P17987; -.
DR jPOST; P17987; -.
DR MassIVE; P17987; -.
DR MaxQB; P17987; -.
DR PaxDb; P17987; -.
DR PeptideAtlas; P17987; -.
DR PRIDE; P17987; -.
DR ProteomicsDB; 53538; -.
DR Antibodypedia; 20023; 699 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 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; KNYKNYG; -.
DR OrthoDB; 335406at2759; -.
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; 784 hits in 1085 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 cortical plate and 198 other tissues.
DR ExpressionAtlas; P17987; baseline and differential.
DR Genevisible; P17987; HS.
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:2000109; P:regulation of macrophage apoptotic process; IEA:Ensembl.
DR GO; GO:0090666; P:scaRNA localization to Cajal body; IMP:BHF-UCL.
DR GO; GO:1901998; P:toxin transport; IEA:Ensembl.
DR GO; GO:0044053; P:translocation of peptides or proteins into host cell cytoplasm; IEA:Ensembl.
DR GO; GO:0007021; P:tubulin complex assembly; NAS:UniProtKB.
DR CDD; cd03335; TCP1_alpha; 1.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 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 PANTHER; PTHR11353; PTHR11353; 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; TIGR02340; chap_CCT_alpha; 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; 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"
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
