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P78371 (TCPB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
T-complex protein 1 subunit beta

Short name=TCP-1-beta
Alternative name(s):
CCT-beta
Gene names
Name:CCT2
Synonyms:99D8.1, CCTB
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length535 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin. Ref.13

Subunit structure

Heterooligomeric complex of about 850 to 900 kDa that forms two stacked rings, 12 to 16 nm in diameter. Interacts with PACRG. Component of the BBS/CCT complex composed at least of MKKS, BBS10, BBS12, TCP1, CCT2, CCT3, CCT4, CCT5 AND CCT8. Ref.10

Subcellular location

Cytoplasm Ref.13.

Sequence similarities

Belongs to the TCP-1 chaperonin family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionChaperone
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological process'de novo' posttranslational protein folding

Traceable author statement. Source: Reactome

   Cellular componentnucleus

Inferred from direct assay. Source: HPA

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

unfolded protein binding

Non-traceable author statement. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7 Ref.8
Chain2 – 535534T-complex protein 1 subunit beta
PRO_0000128316

Amino acid modifications

Modified residue21N-acetylalanine Ref.8 Ref.11
Modified residue131N6-acetyllysine Ref.12
Modified residue1541N6-acetyllysine Ref.12
Modified residue1811N6-acetyllysine Ref.12

Experimental info

Sequence conflict1261I → T in CAG33352. Ref.4
Sequence conflict5041L → P in CAG33352. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P78371 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 57F9E1720D84A31F

FASTA53557,488
        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 

« Hide

References

« Hide 'large scale' references
[1]"Maturation of human cyclin E requires the function of eukaryotic chaperonin CCT."
Won K.-A., Schumacher R.J., Farr G.W., Horwich A.L., Reed S.I.
Mol. Cell. Biol. 18:7584-7589(1998) [PubMed: 9819444] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Isolation and expression of a human novel cDNA homologous to the beta subunit of mouse CCT (chaperonin-containing TCP-1)."
Xin Y., Yu L., Bi A., Fan Y., Dai F., Zhang M., Zhang Q., Zhao S.
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
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.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[6]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
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-217.
[7]"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
Nat. Biotechnol. 21:566-569(2003) [PubMed: 12665801] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-20.
Tissue: Platelet.
[8]Bienvenut W.V., Potts A., Quadroni M.
Submitted (MAY-2004) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-13, ACETYLATION AT ALA-2, MASS SPECTROMETRY.
Tissue: B-cell lymphoma.
[9]Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: 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, MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[10]"A product of the human gene adjacent to parkin is a component of Lewy bodies and suppresses Pael receptor-induced cell death."
Imai Y., Soda M., Murakami T., Shoji M., Abe K., Takahashi R.
J. Biol. Chem. 278:51901-51910(2003) [PubMed: 14532270] [Abstract]
Cited for: INTERACTION WITH PACRG.
[11]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[12]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-13; LYS-154 AND LYS-181, MASS SPECTROMETRY.
[13]"BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family chaperonins and mediate BBSome assembly."
Seo S., Baye L.M., Schulz N.P., Beck J.S., Zhang Q., Slusarski D.C., Sheffield V.C.
Proc. Natl. Acad. Sci. U.S.A. 107:1488-1493(2010) [PubMed: 20080638] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN BBS/CCT COMPLEX.
[14]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF026293 mRNA. Translation: AAC96012.1.
AF026166 mRNA. Translation: AAC98906.1.
BT019966 mRNA. Translation: AAV38769.1.
CR457071 mRNA. Translation: CAG33352.1.
BC113514 mRNA. Translation: AAI13515.1.
BC113516 mRNA. Translation: AAI13517.1.
U91327 Genomic DNA. Translation: AAB67249.1.
IPIIPI00297779.
RefSeqNP_006422.1. NM_006431.2.
UniGeneHs.189772.

3D structure databases

ProteinModelPortalP78371.
SMRP78371. Positions 14-526.
ModBaseSearch...

Protein-protein interaction databases

IntActP78371. 29 interactions.
MINTMINT-1133770.
STRINGP78371.

PTM databases

PhosphoSiteP78371.

Polymorphism databases

DMDM6094436.

2D gel databases

SWISS-2DPAGEP78371.
OGPP78371.
REPRODUCTION-2DPAGEIPI00297779.
UCD-2DPAGEP78371.

Proteomic databases

PeptideAtlasP78371.
PRIDEP78371.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000299300; ENSP00000299300; ENSG00000166226.
GeneID10576.
KEGGhsa:10576.
UCSCuc001svb.1. human.

Organism-specific databases

CTD10576.
GeneCardsGC12P069979.
H-InvDBHIX0036680.
HGNCHGNC:1615. CCT2.
HPACAB009850.
HPA003197.
HPA003198.
MIM605139. gene.
neXtProtNX_P78371.
PharmGKBPA26179.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG11386.
HOGENOMHBG497503.
HOVERGENHBG001052.
InParanoidP78371.
OMAPRTVYGG.
OrthoDBEOG47WNNK.
PhylomeDBP78371.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressP78371.
BgeeP78371.
CleanExHS_CCT2.
GenevestigatorP78371.
GermOnlineENSG00000166226. Homo sapiens.

Family and domain databases

InterProIPR012716. Chap_CCT_beta.
IPR017998. Chaperone_TCP-1.
IPR002194. Chaperonin_TCP-1_CS.
IPR002423. Cpn60/TCP-1.
[Graphical view]
KOK09494.
PANTHERPTHR11353:SF23. Chap_CCT_beta. 1 hit.
PTHR11353. Cpn60/TCP-1. 1 hit.
PfamPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSPR00304. TCOMPLEXTCP1.
SUPFAMSSF48592. GroEL-ATPase. 1 hit.
TIGRFAMsTIGR02341. Chap_CCT_beta. 1 hit.
PROSITEPS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
PS00995. TCP1_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio40141.
SOURCESearch...

Entry information

Entry nameTCPB_HUMAN
AccessionPrimary (citable) accession number: P78371
Secondary accession number(s): Q14D36, Q6IAT3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 113 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families