ID TCPB_HUMAN Reviewed; 535 AA. AC P78371; A8K402; B5BTY7; B7Z243; B7Z7K4; B7ZAT2; Q14D36; Q6IAT3; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 27-MAR-2024, entry version 216. DE RecName: Full=T-complex protein 1 subunit beta; DE Short=TCP-1-beta; DE AltName: Full=CCT-beta; GN Name=CCT2; Synonyms=99D8.1, CCTB; 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). 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 [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Xin Y., Yu L., Bi A., Fan Y., Dai F., Zhang M., Zhang Q., Zhao S.; RT "Isolation and expression of a human novel cDNA homologous to the beta RT subunit of mouse CCT (chaperonin-containing TCP-1)."; RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Amygdala, and Testis; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=19054851; DOI=10.1038/nmeth.1273; RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B., RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., RA Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., RA Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., RA Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., RA Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., RA Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., RA Nomura N.; RT "Human protein factory for converting the transcriptome into an in vitro- RT expressed proteome."; RL Nat. Methods 5:1011-1017(2008). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., RA Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [9] 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 [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-217. RA Adams M.D., Loftus B.J., Zhou L., Phillips C., Brandon R., Fuhrmann J., RA Kim U.J., Kerlavage A.R., Venter J.C.; RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases. RN [11] RP PROTEIN SEQUENCE OF 2-20. 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 [12] RP PROTEIN SEQUENCE OF 2-13, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=B-cell lymphoma; RA Bienvenut W.V., Potts A., Quadroni M.; RL Submitted (MAY-2004) to UniProtKB. RN [13] RP PROTEIN SEQUENCE OF 26-40; 58-72; 83-131; 139-154; 157-170; 182-189; RP 192-203; 205-222; 237-250; 285-342; 348-354; 359-402; 406-427; 432-441; RP 445-466; 482-500 AND 502-516, AND 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 [14] 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 [15] RP IDENTIFICATION BY MASS SPECTROMETRY. 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 [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=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 [17] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-13; LYS-154 AND LYS-181, 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 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-3, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE RP ANALYSIS], AND 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 [20] 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 [21] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-3; SER-260 AND THR-261, CLEAVAGE OF INITIATOR METHIONINE RP [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE RP 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 [22] 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 [23] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, ACETYLATION [LARGE SCALE RP ANALYSIS] AT MET-1 (ISOFORM 2), CLEAVAGE OF INITIATOR METHIONINE [LARGE RP SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [24] 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 [25] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3 AND SER-60, 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 [26] 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 [27] 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 [28] RP INTERACTION WITH FLCN. RX PubMed=27353360; DOI=10.1038/ncomms12037; RA Woodford M.R., Dunn D.M., Blanden A.R., Capriotti D., Loiselle D., RA Prodromou C., Panaretou B., Hughes P.F., Smith A., Ackerman W., RA Haystead T.A., Loh S.N., Bourboulia D., Schmidt L.S., Marston Linehan W., RA Bratslavsky G., Mollapour M.; RT "The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance RT drug binding."; RL Nat. Commun. 7:12037-12037(2016). RN [29] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-248, 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). RN [30] 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). 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 FLCN CC (PubMed:27353360). Interacts with DLEC1 (PubMed:33144677). Interacts CC with SVEP1 (By similarity). {ECO:0000250|UniProtKB:P80314, CC ECO:0000269|PubMed:14532270, ECO:0000269|PubMed:20080638, CC ECO:0000269|PubMed:25467444, ECO:0000269|PubMed:27353360, CC ECO:0000269|PubMed:33144677}. CC -!- INTERACTION: CC P78371; Q8IWZ6: BBS7; NbExp=3; IntAct=EBI-357407, EBI-1806001; CC P78371; A0A024R9H7: CCDC26; NbExp=3; IntAct=EBI-357407, EBI-10271580; CC P78371; P50991: CCT4; NbExp=4; IntAct=EBI-357407, EBI-356876; CC P78371; Q99832: CCT7; NbExp=2; IntAct=EBI-357407, EBI-357046; CC P78371; P42858: HTT; NbExp=6; IntAct=EBI-357407, EBI-466029; CC P78371; C9J082: NPHP1; NbExp=3; IntAct=EBI-357407, EBI-25830675; CC P78371; O14744: PRMT5; NbExp=3; IntAct=EBI-357407, EBI-351098; CC P78371; Q8TAS3: PRRG2; NbExp=3; IntAct=EBI-357407, EBI-10272071; CC P78371; Q9UMY4: SNX12; NbExp=3; IntAct=EBI-357407, EBI-1752602; CC P78371; P17987: TCP1; NbExp=3; IntAct=EBI-357407, EBI-356553; CC P78371; O43493-5: TGOLN2; NbExp=3; IntAct=EBI-357407, EBI-25830716; CC P78371; Q8N0U8: VKORC1L1; NbExp=3; IntAct=EBI-357407, EBI-11337915; CC P78371; O76024: WFS1; NbExp=3; IntAct=EBI-357407, EBI-720609; CC P78371; O60232: ZNRD2; NbExp=6; IntAct=EBI-357407, EBI-741415; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20080638}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P78371-1; Sequence=Displayed; CC Name=2; CC IsoId=P78371-2; Sequence=VSP_042648; 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; AF026293; AAC96012.1; -; mRNA. DR EMBL; AF026166; AAC98906.1; -; mRNA. DR EMBL; BT019966; AAV38769.1; -; mRNA. DR EMBL; AK290767; BAF83456.1; -; mRNA. DR EMBL; AK294307; BAH11729.1; -; mRNA. DR EMBL; AK302157; BAH13640.1; -; mRNA. DR EMBL; AK316397; BAH14768.1; -; mRNA. DR EMBL; AK316408; BAH14779.1; -; mRNA. DR EMBL; CR457071; CAG33352.1; -; mRNA. DR EMBL; AB451223; BAG70037.1; -; mRNA. DR EMBL; AB451346; BAG70160.1; -; mRNA. DR EMBL; AC018921; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471054; EAW97230.1; -; Genomic_DNA. DR EMBL; BC113514; AAI13515.1; -; mRNA. DR EMBL; BC113516; AAI13517.1; -; mRNA. DR EMBL; U91327; AAB67249.1; -; Genomic_DNA. DR CCDS; CCDS55843.1; -. [P78371-2] DR CCDS; CCDS8991.1; -. [P78371-1] DR RefSeq; NP_001185771.1; NM_001198842.1. [P78371-2] DR RefSeq; NP_006422.1; NM_006431.2. [P78371-1] DR PDB; 6NR8; EM; 7.80 A; B/J=16-524. DR PDB; 6NR9; EM; 8.50 A; B/J=16-524. DR PDB; 6NRA; EM; 7.70 A; B/J=16-524. DR PDB; 6NRB; EM; 8.70 A; B/J=16-524. DR PDB; 6NRC; EM; 8.30 A; B/J=16-524. DR PDB; 6NRD; EM; 8.20 A; B/J=16-524. DR PDB; 6QB8; EM; 3.97 A; B/b=1-535. DR PDB; 7LUM; EM; 4.50 A; E/M=1-535. DR PDB; 7LUP; EM; 6.20 A; E/M=1-535. DR PDB; 7NVL; EM; 2.50 A; B/b=1-535. DR PDB; 7NVM; EM; 3.10 A; B/b=1-535. DR PDB; 7NVN; EM; 3.00 A; B/b=1-535. DR PDB; 7NVO; EM; 3.50 A; B/b=1-535. DR PDB; 7TRG; EM; 3.00 A; E=1-535. DR PDB; 7TTN; EM; 3.30 A; E=1-535. DR PDB; 7TTT; EM; 2.90 A; E=1-535. DR PDB; 7TUB; EM; 3.60 A; E=1-535. DR PDB; 7WU7; EM; 3.85 A; B/J=1-535. DR PDB; 7WZ3; EM; 4.10 A; B/b=1-535. DR PDB; 7X0A; EM; 3.10 A; B/b=1-535. DR PDB; 7X0S; EM; 3.10 A; B/L=1-535. DR PDB; 7X0V; EM; 3.20 A; B/L=1-535. DR PDB; 7X3J; EM; 4.20 A; B/b=1-535. DR PDB; 7X3U; EM; 3.30 A; B/b=1-535. DR PDB; 7X6Q; EM; 4.50 A; B/L=1-535. DR PDB; 7X7Y; EM; 3.80 A; B/b=1-535. DR PDB; 8SFE; EM; 3.36 A; B/b=2-527. DR PDB; 8SFF; EM; 3.20 A; B/b=2-527. DR PDB; 8SG8; EM; 3.00 A; B/b=2-527. DR PDB; 8SG9; EM; 2.90 A; B/b=2-527. DR PDB; 8SGC; EM; 2.90 A; B/b=2-527. DR PDB; 8SGL; EM; 2.90 A; B/b=2-527. DR PDB; 8SGQ; EM; 3.70 A; B/b=2-527. DR PDB; 8SH9; EM; 2.70 A; B/b=2-527. DR PDB; 8SHA; EM; 3.00 A; B/b=2-527. DR PDB; 8SHD; EM; 2.90 A; B/b=2-527. DR PDB; 8SHE; EM; 2.80 A; B/b=2-527. DR PDB; 8SHF; EM; 3.00 A; B/b=2-527. DR PDB; 8SHG; EM; 2.80 A; B/b=2-527. DR PDB; 8SHL; EM; 3.00 A; B/b=2-527. DR PDB; 8SHN; EM; 2.80 A; B/b=2-527. DR PDB; 8SHO; EM; 3.00 A; B/b=2-527. DR PDB; 8SHP; EM; 3.00 A; B/b=2-527. DR PDB; 8SHQ; EM; 2.90 A; B/b=2-527. DR PDB; 8SHT; EM; 3.00 A; B/b=2-527. DR PDBsum; 6NR8; -. DR PDBsum; 6NR9; -. DR PDBsum; 6NRA; -. DR PDBsum; 6NRB; -. DR PDBsum; 6NRC; -. DR PDBsum; 6NRD; -. DR PDBsum; 6QB8; -. DR PDBsum; 7LUM; -. DR PDBsum; 7LUP; -. DR PDBsum; 7NVL; -. DR PDBsum; 7NVM; -. DR PDBsum; 7NVN; -. DR PDBsum; 7NVO; -. DR PDBsum; 7TRG; -. DR PDBsum; 7TTN; -. DR PDBsum; 7TTT; -. DR PDBsum; 7TUB; -. DR PDBsum; 7WU7; -. DR PDBsum; 7WZ3; -. DR PDBsum; 7X0A; -. DR PDBsum; 7X0S; -. DR PDBsum; 7X0V; -. DR PDBsum; 7X3J; -. DR PDBsum; 7X3U; -. DR PDBsum; 7X6Q; -. DR PDBsum; 7X7Y; -. DR PDBsum; 8SFE; -. DR PDBsum; 8SFF; -. DR PDBsum; 8SG8; -. DR PDBsum; 8SG9; -. DR PDBsum; 8SGC; -. DR PDBsum; 8SGL; -. DR PDBsum; 8SGQ; -. DR PDBsum; 8SH9; -. DR PDBsum; 8SHA; -. DR PDBsum; 8SHD; -. DR PDBsum; 8SHE; -. DR PDBsum; 8SHF; -. DR PDBsum; 8SHG; -. DR PDBsum; 8SHL; -. DR PDBsum; 8SHN; -. DR PDBsum; 8SHO; -. DR PDBsum; 8SHP; -. DR PDBsum; 8SHQ; -. DR PDBsum; 8SHT; -. DR AlphaFoldDB; P78371; -. DR EMDB; EMD-0490; -. DR EMDB; EMD-0491; -. DR EMDB; EMD-0492; -. DR EMDB; EMD-0493; -. DR EMDB; EMD-0494; -. DR EMDB; EMD-0495; -. DR EMDB; EMD-12605; -. DR EMDB; EMD-12606; -. DR EMDB; EMD-12607; -. DR EMDB; EMD-12608; -. DR EMDB; EMD-13754; -. DR EMDB; EMD-23522; -. DR EMDB; EMD-23526; -. DR EMDB; EMD-26089; -. DR EMDB; EMD-26120; -. DR EMDB; EMD-26123; -. DR EMDB; EMD-26131; -. DR EMDB; EMD-32823; -. DR EMDB; EMD-32903; -. DR EMDB; EMD-32922; -. DR EMDB; EMD-32923; -. DR EMDB; EMD-32926; -. DR EMDB; EMD-32989; -. DR EMDB; EMD-32993; -. DR EMDB; EMD-33025; -. DR EMDB; EMD-33053; -. DR EMDB; EMD-40439; -. DR EMDB; EMD-40440; -. DR EMDB; EMD-40452; -. DR EMDB; EMD-40453; -. DR EMDB; EMD-40454; -. DR EMDB; EMD-40461; -. DR EMDB; EMD-40464; -. DR EMDB; EMD-40481; -. DR EMDB; EMD-40482; -. DR EMDB; EMD-40484; -. DR EMDB; EMD-40485; -. DR EMDB; EMD-40486; -. DR EMDB; EMD-40487; -. DR EMDB; EMD-40488; -. DR EMDB; EMD-40489; -. DR EMDB; EMD-40490; -. DR EMDB; EMD-40491; -. DR EMDB; EMD-40492; -. DR EMDB; EMD-40494; -. DR EMDB; EMD-4489; -. DR SMR; P78371; -. DR BioGRID; 115827; 705. DR ComplexPortal; CPX-6030; Chaperonin-containing T-complex. DR CORUM; P78371; -. DR DIP; DIP-38123N; -. DR IntAct; P78371; 280. DR MINT; P78371; -. DR STRING; 9606.ENSP00000299300; -. DR GlyGen; P78371; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P78371; -. DR MetOSite; P78371; -. DR PhosphoSitePlus; P78371; -. DR SwissPalm; P78371; -. DR BioMuta; CCT2; -. DR DMDM; 6094436; -. DR OGP; P78371; -. DR REPRODUCTION-2DPAGE; IPI00297779; -. DR CPTAC; CPTAC-39; -. DR CPTAC; CPTAC-40; -. DR EPD; P78371; -. DR jPOST; P78371; -. DR MassIVE; P78371; -. DR MaxQB; P78371; -. DR PaxDb; 9606-ENSP00000299300; -. DR PeptideAtlas; P78371; -. DR ProteomicsDB; 57599; -. [P78371-1] DR ProteomicsDB; 57600; -. [P78371-2] DR Pumba; P78371; -. DR TopDownProteomics; P78371-1; -. [P78371-1] DR Antibodypedia; 762; 396 antibodies from 39 providers. DR DNASU; 10576; -. DR Ensembl; ENST00000299300.11; ENSP00000299300.6; ENSG00000166226.13. [P78371-1] DR Ensembl; ENST00000543146.2; ENSP00000445471.2; ENSG00000166226.13. [P78371-2] DR GeneID; 10576; -. DR KEGG; hsa:10576; -. DR MANE-Select; ENST00000299300.11; ENSP00000299300.6; NM_006431.3; NP_006422.1. DR UCSC; uc010stl.2; human. [P78371-1] DR AGR; HGNC:1615; -. DR CTD; 10576; -. DR DisGeNET; 10576; -. DR GeneCards; CCT2; -. DR HGNC; HGNC:1615; CCT2. DR HPA; ENSG00000166226; Low tissue specificity. DR MIM; 605139; gene. DR neXtProt; NX_P78371; -. DR OpenTargets; ENSG00000166226; -. DR PharmGKB; PA26179; -. DR VEuPathDB; HostDB:ENSG00000166226; -. DR eggNOG; KOG0363; Eukaryota. DR GeneTree; ENSGT00550000074930; -. DR InParanoid; P78371; -. DR OMA; CAEMVMS; -. DR OrthoDB; 212971at2759; -. DR PhylomeDB; P78371; -. DR TreeFam; TF105645; -. DR BRENDA; 3.6.4.B10; 2681. DR PathwayCommons; P78371; -. 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-6798695; Neutrophil degranulation. 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 Reactome; R-HSA-9013422; RHOBTB1 GTPase cycle. DR SignaLink; P78371; -. DR SIGNOR; P78371; -. DR BioGRID-ORCS; 10576; 815 hits in 1148 CRISPR screens. DR ChiTaRS; CCT2; human. DR GeneWiki; CCT2_(gene); -. DR GenomeRNAi; 10576; -. DR Pharos; P78371; Tbio. DR PRO; PR:P78371; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; P78371; Protein. DR Bgee; ENSG00000166226; Expressed in sperm and 205 other cell types or tissues. DR ExpressionAtlas; P78371; baseline and differential. DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome. DR GO; GO:0044297; C:cell body; IEA:Ensembl. 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:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005874; C:microtubule; IDA:UniProtKB. 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:BHF-UCL. 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:0051086; P:chaperone mediated protein folding independent of cofactor; IMP:BHF-UCL. DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IMP:MGI. DR GO; GO:0061077; P:chaperone-mediated protein folding; IDA:ComplexPortal. DR GO; GO:1904851; P:positive regulation of establishment of protein localization to telomere; IMP:BHF-UCL. DR GO; GO:1904871; P:positive regulation of protein localization to Cajal body; HMP:BHF-UCL. DR GO; GO:0051973; P:positive regulation of telomerase activity; IMP:BHF-UCL. DR GO; GO:1904874; P:positive regulation of telomerase RNA localization to Cajal body; IMP:BHF-UCL. DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; IMP:BHF-UCL. DR GO; GO:0006457; P:protein folding; IDA:FlyBase. DR GO; GO:0050821; P:protein stabilization; IMP:BHF-UCL. DR GO; GO:0090666; P:scaRNA localization to Cajal body; IMP:BHF-UCL. DR CDD; cd03336; TCP1_beta; 1. DR Gene3D; 3.50.7.10; GroEL; 1. DR Gene3D; 1.10.560.10; GroEL-like equatorial domain; 1. DR Gene3D; 3.30.260.10; TCP-1-like chaperonin intermediate domain; 1. DR InterPro; IPR012716; Chap_CCT_beta. DR InterPro; IPR017998; Chaperone_TCP-1. DR InterPro; IPR002194; Chaperonin_TCP-1_CS. DR InterPro; IPR002423; Cpn60/GroEL/TCP-1. DR InterPro; IPR027409; GroEL-like_apical_dom_sf. DR InterPro; IPR027413; GROEL-like_equatorial_sf. DR InterPro; IPR027410; TCP-1-like_intermed_sf. DR NCBIfam; TIGR02341; chap_CCT_beta; 1. DR NCBIfam; NF041083; thermosome_beta; 1. DR PANTHER; PTHR11353; CHAPERONIN; 1. DR PANTHER; PTHR11353:SF23; T-COMPLEX PROTEIN 1 SUBUNIT BETA; 1. DR Pfam; PF00118; Cpn60_TCP1; 1. DR PRINTS; PR00304; TCOMPLEXTCP1. DR SUPFAM; SSF52029; GroEL apical domain-like; 1. DR SUPFAM; SSF48592; GroEL equatorial domain-like; 1. DR SUPFAM; SSF54849; GroEL-intermediate domain like; 1. DR PROSITE; PS00750; TCP1_1; 1. DR PROSITE; PS00751; TCP1_2; 1. DR PROSITE; PS00995; TCP1_3; 1. DR SWISS-2DPAGE; P78371; -. DR UCD-2DPAGE; P78371; -. DR Genevisible; P78371; HS. 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, ECO:0000269|Ref.12, FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22223895, FT ECO:0007744|PubMed:22814378" FT CHAIN 2..535 FT /note="T-complex protein 1 subunit beta" FT /id="PRO_0000128316" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|Ref.12, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378" FT MOD_RES 3 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 13 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 60 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 154 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 181 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 260 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 261 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21406692" FT CROSSLNK 248 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..47 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_042648" FT CONFLICT 51 FT /note="I -> T (in Ref. 4; BAH11729)" FT /evidence="ECO:0000305" FT CONFLICT 126 FT /note="I -> T (in Ref. 5; CAG33352)" FT /evidence="ECO:0000305" FT CONFLICT 354 FT /note="I -> T (in Ref. 4; BAF83456)" FT /evidence="ECO:0000305" FT CONFLICT 438 FT /note="S -> P (in Ref. 4; BAH13640)" FT /evidence="ECO:0000305" FT CONFLICT 444 FT /note="R -> K (in Ref. 6; BAG70037/BAG70160)" FT /evidence="ECO:0000305" FT CONFLICT 504 FT /note="L -> P (in Ref. 5; CAG33352)" FT /evidence="ECO:0000305" FT STRAND 4..9 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 13..15 FT /evidence="ECO:0007829|PDB:7X0S" FT STRAND 17..19 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 21..39 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 42..44 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 49..51 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 56..58 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 62..64 FT /evidence="ECO:0007829|PDB:7X0A" FT HELIX 67..72 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 79..94 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 95..97 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 99..118 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 125..144 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 149..151 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 152..168 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 171..175 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 176..188 FT /evidence="ECO:0007829|PDB:7NVL" FT TURN 189..192 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 198..207 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 209..211 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 213..215 FT /evidence="ECO:0007829|PDB:7X0A" FT STRAND 216..220 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 226..228 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 232..240 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 245..248 FT /evidence="ECO:0007829|PDB:7X3U" FT STRAND 252..259 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 261..283 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 288..294 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 298..307 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 310..312 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 317..327 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 338..340 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 344..354 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 357..366 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 370..379 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 380..402 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 405..408 FT /evidence="ECO:0007829|PDB:7NVL" FT TURN 409..411 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 412..427 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 431..454 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 458..471 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 476..479 FT /evidence="ECO:0007829|PDB:7NVL" FT TURN 480..483 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 484..487 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 488..491 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 494..496 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 497..515 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 517..522 FT /evidence="ECO:0007829|PDB:7NVL" FT MOD_RES P78371-2:1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22814378" SQ SEQUENCE 535 AA; 57488 MW; 57F9E1720D84A31F CRC64; MASLSLAPVN IFKAGADEER AETARLTSFI GAIAIGDLVK STLGPKGMDK ILLSSGRDAS LMVTNDGATI LKNIGVDNPA AKVLVDMSRV QDDEVGDGTT SVTVLAAELL REAESLIAKK IHPQTIIAGW REATKAAREA LLSSAVDHGS DEVKFRQDLM NIAGTTLSSK LLTHHKDHFT KLAVEAVLRL KGSGNLEAIH IIKKLGGSLA DSYLDEGFLL DKKIGVNQPK RIENAKILIA NTGMDTDKIK IFGSRVRVDS TAKVAEIEHA EKEKMKEKVE RILKHGINCF INRQLIYNYP EQLFGAAGVM AIEHADFAGV ERLALVTGGE IASTFDHPEL VKLGSCKLIE EVMIGEDKLI HFSGVALGEA CTIVLRGATQ QILDEAERSL HDALCVLAQT VKDSRTVYGG GCSEMLMAHA VTQLANRTPG KEAVAMESYA KALRMLPTII ADNAGYDSAD LVAQLRAAHS EGNTTAGLDM REGTIGDMAI LGITESFQVK RQVLLSAAEA AEVILRVDNI IKAAPRKRVP DHHPC //