ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P78371


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name TCPB_HUMAN
Primary accession number P78371
Secondary accession numbers Q14D36 Q6IAT3
Integrated into Swiss-Prot on July 15, 1998
Sequence was last modified on January 23, 2007 (Sequence version 4)
Annotations were last modified on    June 16, 2009 (Entry version 86)
Name and origin of the protein
Protein name T-complex protein 1 subunit beta
Synonyms TCP-1-beta
CCT-beta
Gene name
Name: CCT2
Synonyms: 99D8.1, CCTB
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9819444 [NCBI, ExPASy, EBI, Israel, Japan]
Won K.-A., Schumacher R.J., Farr G.W., Horwich A.L., Reed S.I.;
"Maturation of human cyclin E requires the function of eukaryotic chaperonin CCT.";
Mol. Cell. Biol. 18:7584-7589(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Xin Y., Yu L., Bi A., Fan Y., Dai F., Zhang M., Zhang Q., Zhao S.;
"Isolation and expression of a human novel cDNA homologous to the beta subunit of mouse CCT (chaperonin-containing TCP-1).";
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE OF 1-217.
Adams M.D., Loftus B.J., Zhou L., Phillips C., Brandon R., Fuhrmann J., Kim U.J., Kerlavage A.R., Venter J.C.;
Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
[7]
PROTEIN SEQUENCE OF 2-20.
TISSUE=Platelet;
DOI=10.1038/nbt810; PubMed=12665801 [NCBI, ExPASy, EBI, Israel, Japan]
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[8]
PROTEIN SEQUENCE OF 2-13, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
TISSUE=B-cell lymphoma;
Bienvenut W.V., Potts A., Quadroni M.;
Submitted (MAY-2004) to UniProtKB.
[9]
PROTEIN SEQUENCE OF 26-40; 58-72; 83-131; 139-154; 157-170; 182-189; 192-203; 205-222; 237-250; 285-342; 348-354; 359-402; 406-427; 432-441; 445-466; 482-500 AND 502-516, AND MASS SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[10]
INTERACTION WITH PACRG.
DOI=10.1074/jbc.M309655200; PubMed=14532270 [NCBI, ExPASy, EBI, Israel, Japan]
Imai Y., Soda M., Murakami T., Shoji M., Abe K., Takahashi R.;
"A product of the human gene adjacent to parkin is a component of Lewy bodies and suppresses Pael receptor-induced cell death.";
J. Biol. Chem. 278:51901-51910(2003).
[11]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
Comments
  • FUNCTION: Molecular chaperone; assist the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin.
  • SUBUNIT: Heterooligomeric complex of about 850 to 900 kDa that forms two stacked rings, 12 to 16 nm in diameter. Interacts with PACRG.
  • SUBCELLULAR LOCATION: Cytoplasm.
  • SIMILARITY: Belongs to the TCP-1 chaperonin family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF026293; AAC96012.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF026166; AAC98906.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT019966; AAV38769.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR457071; CAG33352.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC113514; AAI13515.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC113516; AAI13517.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U91327; AAB67249.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00297779; -.
RefSeq NP_006422.1; -.
UniGene Hs.189772
3D structure databases
HSSP P48424; 1A6D. [HSSP ENTRY / PDB]
ModBase P78371.
Protein-protein interaction databases
IntAct P78371; 13.
PTM databases
PhosphoSite P78371; -.
2D gel databases
SWISS-2DPAGE P78371; -.
OGP P78371; -.
REPRODUCTION-2DPAGE IPI00297779; -.
Organism-specific databases
GeneCards GC12P068265; -.
H-InvDB HIX0036680; -.
HGNC HGNC:1615; CCT2.
GenAtlas CCT2.
HPA CAB009850; -.
HPA003197; -.
HPA003198; -.
MIM 605139; gene. [NCBI / EBI]
PharmGKB PA26179; -.
Gene expression databases
ArrayExpress P78371; -.
Bgee P78371; -.
CleanEx HS_CCT2; -.
GermOnline ENSG00000166226; Homo sapiens.
Ontologies
GO
GO:0005634; Cellular component: nucleus (inferred from direct assay from HPA).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0051082; Molecular function: unfolded protein binding (non-traceable author statement from UniProtKB).
GO:0006457; Biological process: protein folding (non-traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR012716; Chap_CCT_beta.
IPR017998; Chaperone_TCP-1.
IPR002194; Chaperonin_TCP-1_CS.
IPR002423; Cpn60/TCP-1.
Graphical view of domain structure.
PANTHER PTHR11353:SF23; Chap_CCT_beta; 1.
PTHR11353; Cpn60/TCP-1; 1.
Pfam PF00118; Cpn60_TCP1; 1.
Pfam graphical view of domain structure.
PRINTS PR00304; TCOMPLEXTCP1.
TIGRFAMs TIGR02341; chap_CCT_beta; 1.
PROSITE PS00750; TCP1_1; 1.
PS00751; TCP1_2; 1.
PS00995; TCP1_3; 1.
Proteomic databases
PeptideAtlas P78371; -.
PRIDE P78371; -.
Genome annotation databases
Ensembl ENSG00000166226; Homo sapiens. [Contig view]
GeneID 10576; -.
KEGG hsa:10576; -.
Phylogenomic databases
HOGENOM P78371; -.
HOVERGEN P78371; -.
OMA P78371; MKEGTIG.
Other
NextBio 40141; -.
SOURCE CCT2; Homo sapiens.
ProtoNet P78371.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; ATP-binding; Chaperone; Cytoplasm; Direct protein sequencing; Nucleotide-binding.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   535  534     T-complex protein 1 subunit beta. PRO_0000128316
MOD_RES   2     2        N-acetylalanine. 
CONFLICT   126   126        I -> T (in Ref. 4; CAG33352). 
CONFLICT   504   504        L -> P (in Ref. 4; CAG33352). 
Sequence information
Length: 535 AA [This is the length of the unprocessed precursor] Molecular weight: 57488 Da [This is the MW of the unprocessed precursor] CRC64: 57F9E1720D84A31F [This is a checksum on the sequence]
        10         20         30         40         50         60 
MASLSLAPVN IFKAGADEER AETARLTSFI GAIAIGDLVK STLGPKGMDK ILLSSGRDAS 

        70         80         90        100        110        120 
LMVTNDGATI LKNIGVDNPA AKVLVDMSRV QDDEVGDGTT SVTVLAAELL REAESLIAKK 

       130        140        150        160        170        180 
IHPQTIIAGW REATKAAREA LLSSAVDHGS DEVKFRQDLM NIAGTTLSSK LLTHHKDHFT 

       190        200        210        220        230        240 
KLAVEAVLRL KGSGNLEAIH IIKKLGGSLA DSYLDEGFLL DKKIGVNQPK RIENAKILIA 

       250        260        270        280        290        300 
NTGMDTDKIK IFGSRVRVDS TAKVAEIEHA EKEKMKEKVE RILKHGINCF INRQLIYNYP 

       310        320        330        340        350        360 
EQLFGAAGVM AIEHADFAGV ERLALVTGGE IASTFDHPEL VKLGSCKLIE EVMIGEDKLI 

       370        380        390        400        410        420 
HFSGVALGEA CTIVLRGATQ QILDEAERSL HDALCVLAQT VKDSRTVYGG GCSEMLMAHA 

       430        440        450        460        470        480 
VTQLANRTPG KEAVAMESYA KALRMLPTII ADNAGYDSAD LVAQLRAAHS EGNTTAGLDM 

       490        500        510        520        530 
REGTIGDMAI LGITESFQVK RQVLLSAAEA AEVILRVDNI IKAAPRKRVP DHHPC 

P78371 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!