TCPZ_HUMAN
ID TCPZ_HUMAN Reviewed; 531 AA.
AC P40227; A6NCD2; Q3KP28; Q75LP4; Q96S46;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=T-complex protein 1 subunit zeta;
DE Short=TCP-1-zeta;
DE AltName: Full=Acute morphine dependence-related protein 2;
DE AltName: Full=CCT-zeta-1;
DE AltName: Full=HTR3;
DE AltName: Full=Tcp20 {ECO:0000303|PubMed:8034610};
GN Name=CCT6A; Synonyms=CCT6, CCTZ;
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), PROTEIN SEQUENCE OF 324-339, AND
RP SUBCELLULAR LOCATION.
RX PubMed=8034610; DOI=10.1016/s0021-9258(17)32354-2;
RA Li W.-Z., Lin P., Frydman J., Boal T.R., Cardillo T.S., Richard L.M.,
RA Toth D., Lichtman M.A., Hartl F.-U., Sherman F., Segel G.B.;
RT "Tcp20, a subunit of the eukaryotic TRiC chaperonin from humans and
RT yeast.";
RL J. Biol. Chem. 269:18616-18622(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Lee Y.-K., Yoo Y.-D.;
RT "Homo sapiens chaperonin mRNA sequence.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Wang H., Gao X., Li L., Wang B., Huang Y., Han J.;
RT "Homo sapiens chaperonin (MoDP) mRNA expressed in SH-SY5Y neuroblastoma
RT cells.";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-233 (ISOFORM 2).
RC TISSUE=Lung carcinoma;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 98-531 (ISOFORM 1).
RC TISSUE=B-cell;
RX PubMed=1352881; DOI=10.1073/pnas.89.13.6060;
RA Segel G.B., Boal T.R., Cardillo T.S., Murant F.G., Lichtman M.A.,
RA Sherman F.;
RT "Isolation of a gene encoding a chaperonin-like protein by complementation
RT of yeast amino acid transport mutants with human cDNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:6060-6064(1992).
RN [7]
RP PROTEIN SEQUENCE OF 2-15.
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 [8]
RP PROTEIN SEQUENCE OF 105-117 AND 160-180, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Vishwanath V.;
RL Submitted (MAR-2007) to UniProtKB.
RN [9]
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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-199; LYS-365; LYS-377 AND
RP LYS-388, AND 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 [11]
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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [14]
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 [15]
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 [16]
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 [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-251, 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).
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). {ECO:0000269|PubMed:14532270,
CC ECO:0000269|PubMed:25467444}.
CC -!- INTERACTION:
CC P40227; P05067: APP; NbExp=3; IntAct=EBI-356687, EBI-77613;
CC P40227; P42331-2: ARHGAP25; NbExp=3; IntAct=EBI-356687, EBI-21499901;
CC P40227; P54253: ATXN1; NbExp=3; IntAct=EBI-356687, EBI-930964;
CC P40227; P54252: ATXN3; NbExp=3; IntAct=EBI-356687, EBI-946046;
CC P40227; Q8WUW1: BRK1; NbExp=3; IntAct=EBI-356687, EBI-2837444;
CC P40227; P50990: CCT8; NbExp=4; IntAct=EBI-356687, EBI-356507;
CC P40227; P42858: HTT; NbExp=10; IntAct=EBI-356687, EBI-466029;
CC P40227; P17612: PRKACA; NbExp=3; IntAct=EBI-356687, EBI-476586;
CC P40227; Q16560-2: SNRNP35; NbExp=3; IntAct=EBI-356687, EBI-12938570;
CC P40227; P37173: TGFBR2; NbExp=3; IntAct=EBI-356687, EBI-296151;
CC P40227; Q9BZY9: TRIM31; NbExp=3; IntAct=EBI-356687, EBI-747544;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8034610}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P40227-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P40227-2; Sequence=VSP_044918;
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA58676.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BU540578; Type=Miscellaneous discrepancy; Note=Several sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; L27706; AAA61061.1; -; mRNA.
DR EMBL; AF385084; AAK61354.1; -; mRNA.
DR EMBL; AB063318; BAB61032.1; -; mRNA.
DR EMBL; AC092101; AAS07451.1; -; Genomic_DNA.
DR EMBL; AC092579; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC106942; AAI06943.1; -; mRNA.
DR EMBL; BU540578; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; M94083; AAA58676.1; ALT_INIT; mRNA.
DR CCDS; CCDS34640.1; -. [P40227-2]
DR CCDS; CCDS5523.1; -. [P40227-1]
DR PIR; S48087; S48087.
DR RefSeq; NP_001009186.1; NM_001009186.1. [P40227-2]
DR RefSeq; NP_001753.1; NM_001762.3. [P40227-1]
DR PDB; 6NR8; EM; 7.80 A; F/N=11-525.
DR PDB; 6NR9; EM; 8.50 A; F/N=11-525.
DR PDB; 6NRA; EM; 7.70 A; F/N=11-525.
DR PDB; 6NRB; EM; 8.70 A; F/N=11-525.
DR PDB; 6NRC; EM; 8.30 A; F/N=11-525.
DR PDB; 6NRD; EM; 8.20 A; F/N=11-525.
DR PDB; 6QB8; EM; 3.97 A; Z/z=1-531.
DR PDB; 7LUM; EM; 4.50 A; A/I=1-531.
DR PDB; 7LUP; EM; 6.20 A; A/I=1-531.
DR PDB; 7NVL; EM; 2.50 A; Z/z=1-531.
DR PDB; 7NVM; EM; 3.10 A; Z/z=1-531.
DR PDB; 7NVN; EM; 3.00 A; Z/z=1-531.
DR PDB; 7NVO; EM; 3.50 A; Z/z=1-531.
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; P40227; -.
DR SMR; P40227; -.
DR BioGRID; 107346; 478.
DR ComplexPortal; CPX-6030; Chaperonin-containing T-complex.
DR CORUM; P40227; -.
DR DIP; DIP-33558N; -.
DR IntAct; P40227; 266.
DR MINT; P40227; -.
DR STRING; 9606.ENSP00000275603; -.
DR GlyGen; P40227; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P40227; -.
DR MetOSite; P40227; -.
DR PhosphoSitePlus; P40227; -.
DR SwissPalm; P40227; -.
DR BioMuta; CCT6A; -.
DR DMDM; 730922; -.
DR DOSAC-COBS-2DPAGE; P40227; -.
DR REPRODUCTION-2DPAGE; IPI00027626; -.
DR REPRODUCTION-2DPAGE; P40227; -.
DR SWISS-2DPAGE; P40227; -.
DR UCD-2DPAGE; P40227; -.
DR CPTAC; CPTAC-1643; -.
DR CPTAC; CPTAC-41; -.
DR CPTAC; CPTAC-42; -.
DR EPD; P40227; -.
DR jPOST; P40227; -.
DR MassIVE; P40227; -.
DR MaxQB; P40227; -.
DR PaxDb; P40227; -.
DR PeptideAtlas; P40227; -.
DR PRIDE; P40227; -.
DR ProteomicsDB; 55353; -. [P40227-1]
DR ProteomicsDB; 824; -.
DR Antibodypedia; 44791; 160 antibodies from 26 providers.
DR DNASU; 908; -.
DR Ensembl; ENST00000275603.9; ENSP00000275603.4; ENSG00000146731.11. [P40227-1]
DR Ensembl; ENST00000335503.3; ENSP00000352019.2; ENSG00000146731.11. [P40227-2]
DR GeneID; 908; -.
DR KEGG; hsa:908; -.
DR MANE-Select; ENST00000275603.9; ENSP00000275603.4; NM_001762.4; NP_001753.1.
DR UCSC; uc003trl.2; human. [P40227-1]
DR CTD; 908; -.
DR DisGeNET; 908; -.
DR GeneCards; CCT6A; -.
DR HGNC; HGNC:1620; CCT6A.
DR HPA; ENSG00000146731; Low tissue specificity.
DR MIM; 104613; gene.
DR neXtProt; NX_P40227; -.
DR OpenTargets; ENSG00000146731; -.
DR PharmGKB; PA26183; -.
DR VEuPathDB; HostDB:ENSG00000146731; -.
DR eggNOG; KOG0359; Eukaryota.
DR GeneTree; ENSGT00940000154631; -.
DR HOGENOM; CLU_008891_3_1_1; -.
DR InParanoid; P40227; -.
DR OMA; LHPRIMT; -.
DR PhylomeDB; P40227; -.
DR TreeFam; TF106333; -.
DR BRENDA; 3.6.4.B10; 2681.
DR PathwayCommons; P40227; -.
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 SignaLink; P40227; -.
DR BioGRID-ORCS; 908; 753 hits in 1064 CRISPR screens.
DR ChiTaRS; CCT6A; human.
DR GeneWiki; CCT6A; -.
DR GenomeRNAi; 908; -.
DR Pharos; P40227; Tbio.
DR PRO; PR:P40227; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P40227; protein.
DR Bgee; ENSG00000146731; Expressed in cortical plate and 206 other tissues.
DR ExpressionAtlas; P40227; baseline and differential.
DR Genevisible; P40227; HS.
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; IDA:HPA.
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:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0071987; F:WD40-repeat domain binding; IPI:BHF-UCL.
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; cd03342; TCP1_zeta; 1.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR InterPro; IPR012722; Chap_CCT_zeta.
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; TIGR02347; chap_CCT_zeta; 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; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..531
FT /note="T-complex protein 1 subunit zeta"
FT /id="PRO_0000128355"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 5
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P80317"
FT MOD_RES 199
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 287
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P80317"
FT MOD_RES 365
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 377
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 388
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CROSSLNK 251
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 68..112
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_044918"
FT VARIANT 229
FT /note="Y -> C (in dbSNP:rs33922584)"
FT /id="VAR_052268"
FT CONFLICT 301..303
FT /note="SLD -> PLS (in Ref. 3; BAB61032)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 531 AA; 58024 MW; 43ABCF548CC82B81 CRC64;
MAAVKTLNPK AEVARAQAAL AVNISAARGL QDVLRTNLGP KGTMKMLVSG AGDIKLTKDG
NVLLHEMQIQ HPTASLIAKV ATAQDDITGD GTTSNVLIIG ELLKQADLYI SEGLHPRIIT
EGFEAAKEKA LQFLEEVKVS REMDRETLID VARTSLRTKV HAELADVLTE AVVDSILAIK
KQDEPIDLFM IEIMEMKHKS ETDTSLIRGL VLDHGARHPD MKKRVEDAYI LTCNVSLEYE
KTEVNSGFFY KSAEEREKLV KAERKFIEDR VKKIIELKRK VCGDSDKGFV VINQKGIDPF
SLDALSKEGI VALRRAKRRN MERLTLACGG VALNSFDDLS PDCLGHAGLV YEYTLGEEKF
TFIEKCNNPR SVTLLIKGPN KHTLTQIKDA VRDGLRAVKN AIDDGCVVPG AGAVEVAMAE
ALIKHKPSVK GRAQLGVQAF ADALLIIPKV LAQNSGFDLQ ETLVKIQAEH SESGQLVGVD
LNTGEPMVAA EVGVWDNYCV KKQLLHSCTV IATNILLVDE IMRAGMSSLK G
