ID TCPD_HUMAN Reviewed; 539 AA. AC P50991; B2R6I3; B7Z8B1; F5H5W3; O14870; Q53QP9; Q96C51; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 17-JUN-2020, entry version 195. DE RecName: Full=T-complex protein 1 subunit delta; DE Short=TCP-1-delta; DE AltName: Full=CCT-delta; DE AltName: Full=Stimulator of TAR RNA-binding; GN Name=CCT4; Synonyms=CCTD, SRB; 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), AND PARTIAL PROTEIN SEQUENCE. RX PubMed=8626763; DOI=10.1074/jbc.271.8.4201; RA Wu-Baer F., Lane W.S., Gaynor R.B.; RT "Identification of a group of cellular cofactors that stimulate the binding RT of RNA polymerase II and TRP-185 to human immunodeficiency virus 1 TAR RT RNA."; RL J. Biol. Chem. 271:4201-4208(1996). RN [2] 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Brain, and Thymus; 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 MRNA] (ISOFORM 1). RC TISSUE=Brain; 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 2-8. 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 420-435, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=B-cell lymphoma; RA Bienvenut W.V., Barblan J., Quadroni M.; RL Submitted (MAR-2004) to UniProtKB. RN [8] 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 [9] 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 [10] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RC TISSUE=Melanoma; RX PubMed=17081065; DOI=10.1021/pr060363j; RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., RA Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., RA Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.; RT "Proteomic and bioinformatic characterization of the biogenesis and RT function of melanosomes."; RL J. Proteome Res. 5:3135-3144(2006). RN [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-288; LYS-302; LYS-319 AND RP LYS-326, 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 [12] 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 [13] 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 [14] RP IDENTIFICATION 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 [15] 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 [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; SER-184; SER-202 AND RP SER-444, 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 [17] 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 [18] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-19, 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 [19] 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). 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:20080638, PubMed:25467444). CC Interacts with PACRG (PubMed:14532270). Interacts with DNAAF4 (By CC similarity). {ECO:0000250|UniProtKB:P80315, CC ECO:0000269|PubMed:14532270, ECO:0000269|PubMed:20080638, CC ECO:0000269|PubMed:25467444}. CC -!- INTERACTION: CC P50991; P51946: CCNH; NbExp=3; IntAct=EBI-356876, EBI-741406; CC P50991; P78371: CCT2; NbExp=4; IntAct=EBI-356876, EBI-357407; CC P50991; P78380: OLR1; NbExp=3; IntAct=EBI-356876, EBI-7151999; CC P50991; P17987: TCP1; NbExp=2; IntAct=EBI-356876, EBI-356553; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17081065, CC ECO:0000269|PubMed:20080638}. Melanosome {ECO:0000269|PubMed:17081065}. CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome CC {ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:20080638}. Cytoplasm, CC cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:P80315}. CC Note=Identified by mass spectrometry in melanosome fractions from stage CC I to stage IV. {ECO:0000269|PubMed:17081065}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P50991-1; Sequence=Displayed; CC Name=2; CC IsoId=P50991-2; Sequence=VSP_045537; 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; U38846; AAC50384.1; -; mRNA. DR EMBL; AF026291; AAC96010.1; -; mRNA. DR EMBL; AK303082; BAH13897.1; -; mRNA. DR EMBL; AK312586; BAG35480.1; -; mRNA. DR EMBL; AC107081; AAY24140.1; -; Genomic_DNA. DR EMBL; BC014676; AAH14676.1; -; mRNA. DR EMBL; BC106934; AAI06935.1; -; mRNA. DR EMBL; BC106933; AAI06934.1; -; mRNA. DR CCDS; CCDS33206.1; -. [P50991-1] DR CCDS; CCDS58711.1; -. [P50991-2] DR RefSeq; NP_001243650.1; NM_001256721.1. [P50991-2] DR RefSeq; NP_006421.2; NM_006430.3. [P50991-1] DR PDB; 6NR8; EM; 7.80 A; D/L=26-539. DR PDB; 6NR9; EM; 8.50 A; D/L=26-539. DR PDB; 6NRA; EM; 7.70 A; D/L=26-539. DR PDB; 6NRB; EM; 8.70 A; D/L=26-539. DR PDB; 6NRC; EM; 8.30 A; D/L=26-539. DR PDB; 6NRD; EM; 8.20 A; D/L=26-539. DR PDB; 6QB8; EM; 3.97 A; D/d=1-539. DR PDBsum; 6NR8; -. DR PDBsum; 6NR9; -. DR PDBsum; 6NRA; -. DR PDBsum; 6NRB; -. DR PDBsum; 6NRC; -. DR PDBsum; 6NRD; -. DR PDBsum; 6QB8; -. DR SMR; P50991; -. DR BioGRID; 115826; 294. DR CORUM; P50991; -. DR DIP; DIP-32971N; -. DR IntAct; P50991; 184. DR MINT; P50991; -. DR STRING; 9606.ENSP00000377958; -. DR iPTMnet; P50991; -. DR MetOSite; P50991; -. DR PhosphoSitePlus; P50991; -. DR SwissPalm; P50991; -. DR BioMuta; CCT4; -. DR DMDM; 52001478; -. DR REPRODUCTION-2DPAGE; IPI00302927; -. DR UCD-2DPAGE; P50991; -. DR EPD; P50991; -. DR jPOST; P50991; -. DR MassIVE; P50991; -. DR MaxQB; P50991; -. DR PaxDb; P50991; -. DR PeptideAtlas; P50991; -. DR PRIDE; P50991; -. DR ProteomicsDB; 27004; -. DR ProteomicsDB; 56273; -. [P50991-1] DR TopDownProteomics; P50991-1; -. [P50991-1] DR Antibodypedia; 15920; 242 antibodies. DR DNASU; 10575; -. DR Ensembl; ENST00000394440; ENSP00000377958; ENSG00000115484. [P50991-1] DR Ensembl; ENST00000544079; ENSP00000443061; ENSG00000115484. [P50991-2] DR GeneID; 10575; -. DR KEGG; hsa:10575; -. DR UCSC; uc002sbo.5; human. [P50991-1] DR CTD; 10575; -. DR DisGeNET; 10575; -. DR EuPathDB; HostDB:ENSG00000115484.14; -. DR GeneCards; CCT4; -. DR HGNC; HGNC:1617; CCT4. DR HPA; ENSG00000115484; Low tissue specificity. DR MIM; 605142; gene. DR neXtProt; NX_P50991; -. DR OpenTargets; ENSG00000115484; -. DR PharmGKB; PA26181; -. DR eggNOG; KOG0358; Eukaryota. DR eggNOG; COG0459; LUCA. DR GeneTree; ENSGT00550000074956; -. DR HOGENOM; CLU_008891_9_1_1; -. DR InParanoid; P50991; -. DR KO; K09496; -. DR OMA; TGIQNMG; -. DR OrthoDB; 511484at2759; -. DR PhylomeDB; P50991; -. DR TreeFam; TF106332; -. 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 BioGRID-ORCS; 10575; 701 hits in 790 CRISPR screens. DR ChiTaRS; CCT4; human. DR GeneWiki; CCT4; -. DR GenomeRNAi; 10575; -. DR Pharos; P50991; Tbio. DR PRO; PR:P50991; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; P50991; protein. DR Bgee; ENSG00000115484; Expressed in female gonad and 237 other tissues. DR Genevisible; P50991; HS. DR GO; GO:0044297; C:cell body; IEA:Ensembl. DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW. 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; IDA:HPA. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell. DR GO; GO:0005874; C:microtubule; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0002199; C:zona pellucida receptor complex; IEA:Ensembl. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0051082; F:unfolded protein binding; TAS:ProtInc. DR GO; GO:0007339; P:binding of sperm to zona pellucida; IEA:Ensembl. 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; TAS:Reactome. 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:1901998; P:toxin transport; IEA:Ensembl. DR CDD; cd03338; TCP1_delta; 1. DR Gene3D; 1.10.560.10; -; 2. DR Gene3D; 3.50.7.10; -; 1. DR InterPro; IPR012717; Chap_CCT_delta. DR InterPro; IPR017998; Chaperone_TCP-1. DR InterPro; IPR002194; Chaperonin_TCP-1_CS. DR InterPro; IPR002423; Cpn60/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 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; TIGR02342; chap_CCT_delta; 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; KW Cell projection; Chaperone; Cytoplasm; Cytoskeleton; KW Direct protein sequencing; Methylation; Nucleotide-binding; Phosphoprotein; KW Polymorphism; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:12665801" FT CHAIN 2..539 FT /note="T-complex protein 1 subunit delta" FT /id="PRO_0000128332" FT MOD_RES 19 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000244|PubMed:24129315" FT MOD_RES 21 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P80315" FT MOD_RES 36 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:23186163" FT MOD_RES 184 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:23186163" FT MOD_RES 202 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:23186163" FT MOD_RES 288 FT /note="N6-acetyllysine" FT /evidence="ECO:0000244|PubMed:19608861" FT MOD_RES 302 FT /note="N6-acetyllysine" FT /evidence="ECO:0000244|PubMed:19608861" FT MOD_RES 319 FT /note="N6-acetyllysine" FT /evidence="ECO:0000244|PubMed:19608861" FT MOD_RES 326 FT /note="N6-acetyllysine" FT /evidence="ECO:0000244|PubMed:19608861" FT MOD_RES 444 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:23186163" FT VAR_SEQ 60..89 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_045537" FT VARIANT 112 FT /note="I -> V (in dbSNP:rs2272428)" FT /id="VAR_052266" FT CONFLICT 435 FT /note="R -> A (in Ref. 1; AAC50384)" FT /evidence="ECO:0000305" FT CONFLICT 531 FT /note="K -> R (in Ref. 3; BAH13897)" FT /evidence="ECO:0000305" SQ SEQUENCE 539 AA; 57924 MW; 39913C0D0735180D CRC64; MPENVAPRSG ATAGAAGGRG KGAYQDRDKP AQIRFSNISA AKAVADAIRT SLGPKGMDKM IQDGKGDVTI TNDGATILKQ MQVLHPAARM LVELSKAQDI EAGDGTTSVV IIAGSLLDSC TKLLQKGIHP TIISESFQKA LEKGIEILTD MSRPVELSDR ETLLNSATTS LNSKVVSQYS SLLSPMSVNA VMKVIDPATA TSVDLRDIKI VKKLGGTIDD CELVEGLVLT QKVSNSGITR VEKAKIGLIQ FCLSAPKTDM DNQIVVSDYA QMDRVLREER AYILNLVKQI KKTGCNVLLI QKSILRDALS DLALHFLNKM KIMVIKDIER EDIEFICKTI GTKPVAHIDQ FTADMLGSAE LAEEVNLNGS GKLLKITGCA SPGKTVTIVV RGSNKLVIEE AERSIHDALC VIRCLVKKRA LIAGGGAPEI ELALRLTEYS RTLSGMESYC VRAFADAMEV IPSTLAENAG LNPISTVTEL RNRHAQGEKT AGINVRKGGI SNILEELVVQ PLLVSVSALT LATETVRSIL KIDDVVNTR //