ID   TCPB_HUMAN              Reviewed;         535 AA.
AC   P78371; Q14D36; Q6IAT3;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   25-JAN-2012, entry version 113.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=99038262; PubMed=9819444;
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].
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].
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
RT   vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-217.
RA   Adams M.D., Loftus B.J., Zhou L., Phillips C., Brandon R.,
RA   Fuhrmann J., Kim U.J., Kerlavage A.R., Venter J.C.;
RL   Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   PROTEIN SEQUENCE OF 2-20.
RC   TISSUE=Platelet;
RX   MEDLINE=22608298; PubMed=12665801; DOI=10.1038/nbt810;
RA   Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA   Thomas G.R., Vandekerckhove J.;
RT   "Exploring proteomes and analyzing protein processing by mass
RT   spectrometric identification of sorted N-terminal peptides.";
RL   Nat. Biotechnol. 21:566-569(2003).
RN   [8]
RP   PROTEIN SEQUENCE OF 2-13, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RA   Bienvenut W.V., Potts A., Quadroni M.;
RL   Submitted (MAY-2004) to UniProtKB.
RN   [9]
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;
RP   432-441; 445-466; 482-500 AND 502-516, AND 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   [10]
RP   INTERACTION WITH PACRG.
RX   PubMed=14532270; DOI=10.1074/jbc.M309655200;
RA   Imai Y., Soda M., Murakami T., Shoji M., Abe K., Takahashi R.;
RT   "A product of the human gene adjacent to parkin is a component of Lewy
RT   bodies and suppresses Pael receptor-induced cell death.";
RL   J. Biol. Chem. 278:51901-51910(2003).
RN   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [12]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-13; LYS-154 AND LYS-181, AND
RP   MASS SPECTROMETRY.
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,
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   [13]
RP   FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN BBS/CCT 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
RT   chaperonins and 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.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
CC   -!- FUNCTION: Molecular chaperone; assists the folding of proteins
CC       upon ATP hydrolysis. As part of the BBS/CCT complex may play a
CC       role in the assembly of BBSome, a complex involved in ciliogenesis
CC       regulating transports vesicles to the cilia. Known to play a role,
CC       in vitro, in the folding of actin and tubulin.
CC   -!- SUBUNIT: Heterooligomeric complex of about 850 to 900 kDa that
CC       forms two stacked rings, 12 to 16 nm in diameter. Interacts with
CC       PACRG. Component of the BBS/CCT complex composed at least of MKKS,
CC       BBS10, BBS12, TCP1, CCT2, CCT3, CCT4, CCT5 AND CCT8.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the TCP-1 chaperonin family.
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DR   EMBL; AF026293; AAC96012.1; -; mRNA.
DR   EMBL; AF026166; AAC98906.1; -; mRNA.
DR   EMBL; BT019966; AAV38769.1; -; mRNA.
DR   EMBL; CR457071; CAG33352.1; -; mRNA.
DR   EMBL; BC113514; AAI13515.1; -; mRNA.
DR   EMBL; BC113516; AAI13517.1; -; mRNA.
DR   EMBL; U91327; AAB67249.1; -; Genomic_DNA.
DR   IPI; IPI00297779; -.
DR   RefSeq; NP_006422.1; NM_006431.2.
DR   UniGene; Hs.189772; -.
DR   ProteinModelPortal; P78371; -.
DR   SMR; P78371; 14-526.
DR   IntAct; P78371; 29.
DR   MINT; MINT-1133770; -.
DR   STRING; P78371; -.
DR   PhosphoSite; P78371; -.
DR   DMDM; 6094436; -.
DR   SWISS-2DPAGE; P78371; -.
DR   OGP; P78371; -.
DR   REPRODUCTION-2DPAGE; IPI00297779; -.
DR   UCD-2DPAGE; P78371; -.
DR   PeptideAtlas; P78371; -.
DR   PRIDE; P78371; -.
DR   Ensembl; ENST00000299300; ENSP00000299300; ENSG00000166226.
DR   GeneID; 10576; -.
DR   KEGG; hsa:10576; -.
DR   UCSC; uc001svb.1; human.
DR   CTD; 10576; -.
DR   GeneCards; GC12P069979; -.
DR   H-InvDB; HIX0036680; -.
DR   HGNC; HGNC:1615; CCT2.
DR   HPA; CAB009850; -.
DR   HPA; HPA003197; -.
DR   HPA; HPA003198; -.
DR   MIM; 605139; gene.
DR   neXtProt; NX_P78371; -.
DR   PharmGKB; PA26179; -.
DR   eggNOG; prNOG11386; -.
DR   HOGENOM; HBG497503; -.
DR   HOVERGEN; HBG001052; -.
DR   InParanoid; P78371; -.
DR   OMA; PRTVYGG; -.
DR   OrthoDB; EOG47WNNK; -.
DR   PhylomeDB; P78371; -.
DR   Reactome; REACT_17015; Metabolism of proteins.
DR   NextBio; 40141; -.
DR   ArrayExpress; P78371; -.
DR   Bgee; P78371; -.
DR   CleanEx; HS_CCT2; -.
DR   Genevestigator; P78371; -.
DR   GermOnline; ENSG00000166226; Homo sapiens.
DR   GO; GO:0005634; C:nucleus; IDA:HPA.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0051082; F:unfolded protein binding; NAS:UniProtKB.
DR   GO; GO:0051084; P:'de novo' posttranslational protein folding; TAS:Reactome.
DR   InterPro; IPR012716; Chap_CCT_beta.
DR   InterPro; IPR017998; Chaperone_TCP-1.
DR   InterPro; IPR002194; Chaperonin_TCP-1_CS.
DR   InterPro; IPR002423; Cpn60/TCP-1.
DR   KO; K09494; -.
DR   PANTHER; PTHR11353:SF23; Chap_CCT_beta; 1.
DR   PANTHER; PTHR11353; Cpn60/TCP-1; 1.
DR   Pfam; PF00118; Cpn60_TCP1; 1.
DR   PRINTS; PR00304; TCOMPLEXTCP1.
DR   SUPFAM; SSF48592; GroEL-ATPase; 1.
DR   TIGRFAMs; TIGR02341; Chap_CCT_beta; 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   Acetylation; ATP-binding; Chaperone; Complete proteome; Cytoplasm;
KW   Direct protein sequencing; Nucleotide-binding; Reference proteome.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    535       T-complex protein 1 subunit beta.
FT                                /FTId=PRO_0000128316.
FT   MOD_RES       2      2       N-acetylalanine.
FT   MOD_RES      13     13       N6-acetyllysine.
FT   MOD_RES     154    154       N6-acetyllysine.
FT   MOD_RES     181    181       N6-acetyllysine.
FT   CONFLICT    126    126       I -> T (in Ref. 4; CAG33352).
FT   CONFLICT    504    504       L -> P (in Ref. 4; CAG33352).
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
//