TCPE_HUMAN
ID TCPE_HUMAN Reviewed; 541 AA.
AC P48643; A8JZY8; A8K2X8; B4DYD8;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=T-complex protein 1 subunit epsilon;
DE Short=TCP-1-epsilon;
DE AltName: Full=CCT-epsilon;
GN Name=CCT5; Synonyms=CCTE, KIAA0098 {ECO:0000303|PubMed:7788527};
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=7788527; DOI=10.1093/dnares/2.1.37;
RA Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S.,
RA Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. III. The
RT coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 2:37-43(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Testis, and Umbilical cord blood;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
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] (ISOFORM 1).
RC TISSUE=Lung, and Uterus;
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 2-24; 28-35; 50-59; 90-96; 133-170; 184-201; 203-214;
RP 248-261; 264-275; 283-293; 324-340; 345-368; 382-388; 393-399; 401-410;
RP 484-496; 514-525 AND 530-541, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION
RP AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lung carcinoma;
RA Bienvenut W.V., Vousden K.H., Lukashchuk N.;
RL Submitted (MAR-2008) to UniProtKB.
RN [7]
RP PROTEIN SEQUENCE OF 2-20; 97-126; 133-170; 184-201; 203-214; 266-275;
RP 294-340; 345-368; 382-388 AND 401-410, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [8]
RP PROTEIN SEQUENCE OF 203-210; 248-261; 324-340; 353-368 AND 515-525, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) 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 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 [11]
RP INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16548883; DOI=10.1111/j.1462-5822.2005.00644.x;
RA Leong W.F., Chow V.T.;
RT "Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal
RT differential cellular gene expression in response to enterovirus 71
RT infection.";
RL Cell. Microbiol. 8:565-580(2006).
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=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN CHAPERONIN-CONTAINING
RP 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 [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND IDENTIFICATION BY
RP 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 [16]
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=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 [17]
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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-346 AND SER-539, AND
RP IDENTIFICATION BY 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 [19]
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 [20]
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 [21]
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=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 [22]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-20; LYS-210; LYS-214; LYS-265;
RP LYS-275; LYS-279 AND LYS-392, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [23]
RP UBIQUITINATION.
RX PubMed=29779948; DOI=10.1016/j.cell.2018.04.028;
RA Koren I., Timms R.T., Kula T., Xu Q., Li M.Z., Elledge S.J.;
RT "The eukaryotic proteome is shaped by E3 ubiquitin ligases targeting C-
RT terminal degrons.";
RL Cell 173:1622-1635(2018).
RN [24]
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 [25]
RP VARIANT HSNSP ARG-147.
RX PubMed=16399879; DOI=10.1136/jmg.2005.039230;
RA Bouhouche A., Benomar A., Bouslam N., Chkili T., Yahyaoui M.;
RT "Mutation in the epsilon subunit of the cytosolic chaperonin-containing T-
RT complex peptide-1 (Cct5) gene causes autosomal recessive mutilating sensory
RT neuropathy with spastic paraplegia.";
RL J. Med. Genet. 43:441-443(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:20080638, PubMed:25467444).
CC Interacts with PACRG (PubMed:14532270). Interacts with DNAAF4 (By
CC similarity). Interacts with DLEC1 (PubMed:33144677).
CC {ECO:0000250|UniProtKB:P80316, ECO:0000269|PubMed:14532270,
CC ECO:0000269|PubMed:20080638, ECO:0000269|PubMed:25467444,
CC ECO:0000269|PubMed:33144677}.
CC -!- INTERACTION:
CC P48643; Q9NP61: ARFGAP3; NbExp=3; IntAct=EBI-355710, EBI-2875816;
CC P48643; P54253: ATXN1; NbExp=3; IntAct=EBI-355710, EBI-930964;
CC P48643; O95817: BAG3; NbExp=3; IntAct=EBI-355710, EBI-747185;
CC P48643; Q14457: BECN1; NbExp=3; IntAct=EBI-355710, EBI-949378;
CC P48643; Q9UNS2: COPS3; NbExp=3; IntAct=EBI-355710, EBI-350590;
CC P48643; Q9H9Q2: COPS7B; NbExp=3; IntAct=EBI-355710, EBI-2510162;
CC P48643; Q6NXG1: ESRP1; NbExp=3; IntAct=EBI-355710, EBI-10213520;
CC P48643; Q9UKC9: FBXL2; NbExp=3; IntAct=EBI-355710, EBI-724253;
CC P48643; Q9NXC2: GFOD1; NbExp=3; IntAct=EBI-355710, EBI-8799578;
CC P48643; O75409: H2AP; NbExp=3; IntAct=EBI-355710, EBI-6447217;
CC P48643; P52790: HK3; NbExp=3; IntAct=EBI-355710, EBI-2965780;
CC P48643; P49639: HOXA1; NbExp=3; IntAct=EBI-355710, EBI-740785;
CC P48643; P42858: HTT; NbExp=3; IntAct=EBI-355710, EBI-466029;
CC P48643; Q14525: KRT33B; NbExp=3; IntAct=EBI-355710, EBI-1049638;
CC P48643; Q68G74: LHX8; NbExp=3; IntAct=EBI-355710, EBI-8474075;
CC P48643; A2RU56: LOC401296; NbExp=3; IntAct=EBI-355710, EBI-9088215;
CC P48643; Q1L5Z9: LONRF2; NbExp=3; IntAct=EBI-355710, EBI-2510853;
CC P48643; O15130-2: NPFF; NbExp=3; IntAct=EBI-355710, EBI-25840002;
CC P48643; Q96LB9: PGLYRP3; NbExp=3; IntAct=EBI-355710, EBI-12339509;
CC P48643; O75925: PIAS1; NbExp=3; IntAct=EBI-355710, EBI-629434;
CC P48643; Q6ZR37: PLEKHG7; NbExp=3; IntAct=EBI-355710, EBI-12891828;
CC P48643; Q9H0F5-2: RNF38; NbExp=3; IntAct=EBI-355710, EBI-25866807;
CC P48643; Q9NTN9-3: SEMA4G; NbExp=3; IntAct=EBI-355710, EBI-9089805;
CC P48643; O60902-3: SHOX2; NbExp=3; IntAct=EBI-355710, EBI-9092164;
CC P48643; Q99932-2: SPAG8; NbExp=3; IntAct=EBI-355710, EBI-11959123;
CC P48643; O75886: STAM2; NbExp=3; IntAct=EBI-355710, EBI-373258;
CC P48643; O95630: STAMBP; NbExp=3; IntAct=EBI-355710, EBI-396676;
CC P48643; A1L378: STRC; NbExp=3; IntAct=EBI-355710, EBI-22013242;
CC P48643; O60220: TIMM8A; NbExp=3; IntAct=EBI-355710, EBI-1049822;
CC P48643; P04637: TP53; NbExp=3; IntAct=EBI-355710, EBI-366083;
CC P48643; Q9UGJ1-2: TUBGCP4; NbExp=3; IntAct=EBI-355710, EBI-10964469;
CC P48643; Q96B02: UBE2W; NbExp=3; IntAct=EBI-355710, EBI-716589;
CC P48643; P45880: VDAC2; NbExp=3; IntAct=EBI-355710, EBI-354022;
CC P48643; O00308: WWP2; NbExp=6; IntAct=EBI-355710, EBI-743923;
CC P48643; Q96N77-2: ZNF641; NbExp=3; IntAct=EBI-355710, EBI-12939666;
CC P48643; O60232: ZNRD2; NbExp=4; IntAct=EBI-355710, EBI-741415;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20080638}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:20080638}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P48643-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P48643-2; Sequence=VSP_054005, VSP_054006;
CC -!- INDUCTION: Down-regulated in response to enterovirus 71 (EV71)
CC infection (at protein level). {ECO:0000269|PubMed:16548883}.
CC -!- PTM: Ubiquitinated by the DCX(DCAF12) complex specifically recognizes
CC the diglutamate (Glu-Glu) at the C-terminus, leading to its
CC degradation. {ECO:0000269|PubMed:29779948}.
CC -!- DISEASE: Neuropathy, hereditary sensory, with spastic paraplegia,
CC autosomal recessive (HSNSP) [MIM:256840]: A disease characterized by
CC spastic paraplegia and progressive distal sensory neuropathy leading to
CC mutilating ulcerations of the upper and lower limbs.
CC {ECO:0000269|PubMed:16399879}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA07894.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D43950; BAA07894.2; ALT_INIT; mRNA.
DR EMBL; AK289353; BAF82042.1; -; mRNA.
DR EMBL; AK290393; BAF83082.1; -; mRNA.
DR EMBL; AK302383; BAG63700.1; -; mRNA.
DR EMBL; AC012640; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471102; EAX08072.1; -; Genomic_DNA.
DR EMBL; BC006543; AAH06543.1; -; mRNA.
DR EMBL; BC035499; AAH35499.1; -; mRNA.
DR CCDS; CCDS3877.1; -. [P48643-1]
DR CCDS; CCDS82990.1; -. [P48643-2]
DR RefSeq; NP_001293084.1; NM_001306155.1. [P48643-2]
DR RefSeq; NP_036205.1; NM_012073.4. [P48643-1]
DR PDB; 5UYX; X-ray; 3.50 A; A/B/C/D=1-541.
DR PDB; 5UYZ; X-ray; 3.60 A; A/B/C/D=1-541.
DR PDB; 6NR8; EM; 7.80 A; E/M=25-541.
DR PDB; 6NR9; EM; 8.50 A; E/M=25-541.
DR PDB; 6NRA; EM; 7.70 A; E/M=25-541.
DR PDB; 6NRB; EM; 8.70 A; E/M=25-541.
DR PDB; 6NRC; EM; 8.30 A; E/M=25-541.
DR PDB; 6NRD; EM; 8.20 A; E/M=25-541.
DR PDB; 6QB8; EM; 3.97 A; E/e=1-541.
DR PDB; 7LUM; EM; 4.50 A; D/L=1-541.
DR PDB; 7LUP; EM; 6.20 A; D/L=1-541.
DR PDB; 7NVL; EM; 2.50 A; E/e=1-541.
DR PDB; 7NVM; EM; 3.10 A; E/e=1-541.
DR PDB; 7NVN; EM; 3.00 A; E/e=1-541.
DR PDB; 7NVO; EM; 3.50 A; E/e=1-541.
DR PDBsum; 5UYX; -.
DR PDBsum; 5UYZ; -.
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; P48643; -.
DR SMR; P48643; -.
DR BioGRID; 116603; 422.
DR ComplexPortal; CPX-6030; Chaperonin-containing T-complex.
DR CORUM; P48643; -.
DR DIP; DIP-31181N; -.
DR IntAct; P48643; 246.
DR MINT; P48643; -.
DR STRING; 9606.ENSP00000280326; -.
DR ChEMBL; CHEMBL4295766; -.
DR GlyGen; P48643; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P48643; -.
DR MetOSite; P48643; -.
DR PhosphoSitePlus; P48643; -.
DR SwissPalm; P48643; -.
DR BioMuta; CCT5; -.
DR DMDM; 1351211; -.
DR OGP; P48643; -.
DR REPRODUCTION-2DPAGE; IPI00010720; -.
DR SWISS-2DPAGE; P48643; -.
DR EPD; P48643; -.
DR jPOST; P48643; -.
DR MassIVE; P48643; -.
DR MaxQB; P48643; -.
DR PaxDb; P48643; -.
DR PeptideAtlas; P48643; -.
DR PRIDE; P48643; -.
DR ProteomicsDB; 5518; -.
DR ProteomicsDB; 55918; -. [P48643-1]
DR ABCD; P48643; 1 sequenced antibody.
DR Antibodypedia; 1210; 340 antibodies from 34 providers.
DR DNASU; 22948; -.
DR Ensembl; ENST00000280326.9; ENSP00000280326.4; ENSG00000150753.12. [P48643-1]
DR Ensembl; ENST00000506600.1; ENSP00000423052.1; ENSG00000150753.12. [P48643-2]
DR GeneID; 22948; -.
DR KEGG; hsa:22948; -.
DR MANE-Select; ENST00000280326.9; ENSP00000280326.4; NM_012073.5; NP_036205.1.
DR UCSC; uc011cmt.3; human. [P48643-1]
DR CTD; 22948; -.
DR DisGeNET; 22948; -.
DR GeneCards; CCT5; -.
DR HGNC; HGNC:1618; CCT5.
DR HPA; ENSG00000150753; Low tissue specificity.
DR MalaCards; CCT5; -.
DR MIM; 256840; phenotype.
DR MIM; 610150; gene.
DR neXtProt; NX_P48643; -.
DR OpenTargets; ENSG00000150753; -.
DR Orphanet; 139578; Mutilating hereditary sensory neuropathy with spastic paraplegia.
DR PharmGKB; PA26182; -.
DR VEuPathDB; HostDB:ENSG00000150753; -.
DR eggNOG; KOG0357; Eukaryota.
DR GeneTree; ENSGT00550000074988; -.
DR InParanoid; P48643; -.
DR OMA; QTGSNDM; -.
DR PhylomeDB; P48643; -.
DR TreeFam; TF105638; -.
DR BRENDA; 3.6.4.B10; 2681.
DR PathwayCommons; P48643; -.
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 SignaLink; P48643; -.
DR BioGRID-ORCS; 22948; 756 hits in 1073 CRISPR screens.
DR ChiTaRS; CCT5; human.
DR GeneWiki; CCT5_(gene); -.
DR GenomeRNAi; 22948; -.
DR Pharos; P48643; Tbio.
DR PRO; PR:P48643; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P48643; protein.
DR Bgee; ENSG00000150753; Expressed in endometrium epithelium and 209 other tissues.
DR ExpressionAtlas; P48643; baseline and differential.
DR Genevisible; P48643; HS.
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: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:0048487; F:beta-tubulin binding; IPI:UniProtKB.
DR GO; GO:0031681; F:G-protein beta-subunit binding; IPI:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:CAFA.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; IDA:CAFA.
DR GO; GO:0044183; F:protein folding chaperone; IDA:FlyBase.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IEA:Ensembl.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IDA:ComplexPortal.
DR GO; GO:1904851; P:positive regulation of establishment of protein localization to telomere; IMP:BHF-UCL.
DR GO; GO:1904871; P:positive regulation of protein localization to Cajal body; HMP:BHF-UCL.
DR GO; GO:1904874; P:positive regulation of telomerase RNA localization to Cajal body; HMP:BHF-UCL.
DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; IMP:BHF-UCL.
DR GO; GO:0006457; P:protein folding; IDA:FlyBase.
DR GO; GO:0050821; P:protein stabilization; IMP:BHF-UCL.
DR GO; GO:0009615; P:response to virus; IEP:UniProtKB.
DR GO; GO:1901998; P:toxin transport; IEA:Ensembl.
DR CDD; cd03339; TCP1_epsilon; 1.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR InterPro; IPR012718; Chap_CCT_epsi.
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; TIGR02343; chap_CCT_epsi; 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; Cytoskeleton; Direct protein sequencing; Disease variant;
KW Isopeptide bond; Neuropathy; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.6, ECO:0000269|Ref.7,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"
FT CHAIN 2..541
FT /note="T-complex protein 1 subunit epsilon"
FT /id="PRO_0000128346"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.6, ECO:0000269|Ref.7,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 539
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 20
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 210
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 214
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 265
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 275
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 279
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 392
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..38
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054005"
FT VAR_SEQ 56..110
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054006"
FT VARIANT 146
FT /note="E -> V (in dbSNP:rs11557652)"
FT /id="VAR_052267"
FT VARIANT 147
FT /note="H -> R (in HSNSP; dbSNP:rs118203986)"
FT /evidence="ECO:0000269|PubMed:16399879"
FT /id="VAR_030658"
FT CONFLICT 55
FT /note="N -> D (in Ref. 2; BAF83082)"
FT /evidence="ECO:0000305"
FT CONFLICT 512
FT /note="G -> D (in Ref. 2; BAF83082)"
FT /evidence="ECO:0000305"
FT HELIX 32..49
FT /evidence="ECO:0007829|PDB:5UYX"
FT HELIX 74..80
FT /evidence="ECO:0007829|PDB:5UYX"
FT HELIX 86..102
FT /evidence="ECO:0007829|PDB:5UYX"
FT HELIX 107..125
FT /evidence="ECO:0007829|PDB:5UYX"
FT HELIX 130..151
FT /evidence="ECO:0007829|PDB:5UYX"
FT STRAND 158..161
FT /evidence="ECO:0007829|PDB:5UYX"
FT HELIX 164..169
FT /evidence="ECO:0007829|PDB:5UYX"
FT HELIX 183..195
FT /evidence="ECO:0007829|PDB:5UYX"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:5UYX"
FT STRAND 208..213
FT /evidence="ECO:0007829|PDB:5UYX"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:5UYX"
FT STRAND 226..230
FT /evidence="ECO:0007829|PDB:5UYX"
FT STRAND 241..246
FT /evidence="ECO:0007829|PDB:5UYX"
FT STRAND 248..251
FT /evidence="ECO:0007829|PDB:5UYX"
FT HELIX 271..293
FT /evidence="ECO:0007829|PDB:5UYX"
FT STRAND 298..301
FT /evidence="ECO:0007829|PDB:5UYX"
FT HELIX 308..315
FT /evidence="ECO:0007829|PDB:5UYX"
FT TURN 316..318
FT /evidence="ECO:0007829|PDB:5UYX"
FT TURN 328..330
FT /evidence="ECO:0007829|PDB:5UYX"
FT HELIX 331..336
FT /evidence="ECO:0007829|PDB:5UYX"
FT HELIX 350..352
FT /evidence="ECO:0007829|PDB:5UYX"
FT STRAND 356..364
FT /evidence="ECO:0007829|PDB:5UYX"
FT STRAND 367..374
FT /evidence="ECO:0007829|PDB:5UYX"
FT STRAND 383..387
FT /evidence="ECO:0007829|PDB:5UYX"
FT TURN 391..393
FT /evidence="ECO:0007829|PDB:5UYX"
FT HELIX 394..414
FT /evidence="ECO:0007829|PDB:5UYX"
FT TURN 421..423
FT /evidence="ECO:0007829|PDB:5UYX"
FT HELIX 424..438
FT /evidence="ECO:0007829|PDB:5UYX"
FT HELIX 444..455
FT /evidence="ECO:0007829|PDB:5UYX"
FT HELIX 457..464
FT /evidence="ECO:0007829|PDB:5UYX"
FT TURN 465..467
FT /evidence="ECO:0007829|PDB:5UYX"
FT HELIX 470..484
FT /evidence="ECO:0007829|PDB:5UYX"
FT HELIX 503..505
FT /evidence="ECO:0007829|PDB:5UYX"
FT HELIX 510..528
FT /evidence="ECO:0007829|PDB:5UYX"
SQ SEQUENCE 541 AA; 59671 MW; 164168BB80EF022A CRC64;
MASMGTLAFD EYGRPFLIIK DQDRKSRLMG LEALKSHIMA AKAVANTMRT SLGPNGLDKM
MVDKDGDVTV TNDGATILSM MDVDHQIAKL MVELSKSQDD EIGDGTTGVV VLAGALLEEA
EQLLDRGIHP IRIADGYEQA ARVAIEHLDK ISDSVLVDIK DTEPLIQTAK TTLGSKVVNS
CHRQMAEIAV NAVLTVADME RRDVDFELIK VEGKVGGRLE DTKLIKGVIV DKDFSHPQMP
KKVEDAKIAI LTCPFEPPKP KTKHKLDVTS VEDYKALQKY EKEKFEEMIQ QIKETGANLA
ICQWGFDDEA NHLLLQNNLP AVRWVGGPEI ELIAIATGGR IVPRFSELTA EKLGFAGLVQ
EISFGTTKDK MLVIEQCKNS RAVTIFIRGG NKMIIEEAKR SLHDALCVIR NLIRDNRVVY
GGGAAEISCA LAVSQEADKC PTLEQYAMRA FADALEVIPM ALSENSGMNP IQTMTEVRAR
QVKEMNPALG IDCLHKGTND MKQQHVIETL IGKKQQISLA TQMVRMILKI DDIRKPGESE
E
