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Protein

T-complex protein 1 subunit beta

Gene

CCT2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • protein binding involved in protein folding Source: BHF-UCL
  • ubiquitin protein ligase binding Source: ParkinsonsUK-UCL
  • unfolded protein binding Source: GO_Central

GO - Biological processi

  • binding of sperm to zona pellucida Source: Ensembl
  • chaperone-mediated protein complex assembly Source: MGI
  • chaperone mediated protein folding independent of cofactor Source: BHF-UCL
  • neutrophil degranulation Source: Reactome
  • positive regulation of establishment of protein localization to telomere Source: BHF-UCL
  • positive regulation of protein localization to Cajal body Source: BHF-UCL
  • positive regulation of telomerase activity Source: BHF-UCL
  • positive regulation of telomerase RNA localization to Cajal body Source: BHF-UCL
  • positive regulation of telomere maintenance via telomerase Source: BHF-UCL
  • protein folding Source: Reactome
  • protein stabilization Source: BHF-UCL
  • scaRNA localization to Cajal body Source: BHF-UCL
  • toxin transport Source: Ensembl

Keywordsi

Molecular functionChaperone
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-389957. Prefoldin mediated transfer of substrate to CCT/TriC.
R-HSA-389960. Formation of tubulin folding intermediates by CCT/TriC.
R-HSA-390450. Folding of actin by CCT/TriC.
R-HSA-390471. Association of TriC/CCT with target proteins during biosynthesis.
R-HSA-5620922. BBSome-mediated cargo-targeting to cilium.
R-HSA-6798695. Neutrophil degranulation.
R-HSA-6814122. Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
SIGNORiP78371.

Names & Taxonomyi

Protein namesi
Recommended name:
T-complex protein 1 subunit beta
Short name:
TCP-1-beta
Alternative name(s):
CCT-beta
Gene namesi
Name:CCT2
Synonyms:99D8.1, CCTB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:1615. CCT2.

Subcellular locationi

GO - Cellular componenti

  • azurophil granule lumen Source: Reactome
  • cell body Source: Ensembl
  • chaperonin-containing T-complex Source: UniProtKB
  • cytosol Source: HPA
  • extracellular exosome Source: UniProtKB
  • extracellular matrix Source: BHF-UCL
  • extracellular region Source: Reactome
  • microtubule Source: UniProtKB
  • myelin sheath Source: Ensembl
  • zona pellucida receptor complex Source: Ensembl

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

DisGeNETi10576.
OpenTargetsiENSG00000166226.
PharmGKBiPA26179.

Polymorphism and mutation databases

BioMutaiCCT2.
DMDMi6094436.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources2 Publications
ChainiPRO_00001283162 – 535T-complex protein 1 subunit betaAdd BLAST534

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1 Publication1
Modified residuei3PhosphoserineCombined sources1
Modified residuei13N6-acetyllysineCombined sources1
Modified residuei60PhosphoserineCombined sources1
Modified residuei154N6-acetyllysineCombined sources1
Modified residuei181N6-acetyllysineCombined sources1
Cross-linki248Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei260PhosphoserineCombined sources1
Modified residuei261PhosphothreonineCombined sources1
Isoform 2 (identifier: P78371-2)
Modified residuei1N-acetylmethionineCombined sources1

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP78371.
PaxDbiP78371.
PeptideAtlasiP78371.
PRIDEiP78371.
TopDownProteomicsiP78371-1. [P78371-1]

2D gel databases

OGPiP78371.
REPRODUCTION-2DPAGEiIPI00297779.
SWISS-2DPAGEiP78371.
UCD-2DPAGEiP78371.

PTM databases

iPTMnetiP78371.
PhosphoSitePlusiP78371.
SwissPalmiP78371.

Expressioni

Gene expression databases

BgeeiENSG00000166226.
CleanExiHS_CCT2.
ExpressionAtlasiP78371. baseline and differential.
GenevisibleiP78371. HS.

Organism-specific databases

HPAiHPA003197.
HPA003198.

Interactioni

Subunit structurei

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. Interacts with FLCN (PubMed:27353360).3 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • protein binding involved in protein folding Source: BHF-UCL
  • ubiquitin protein ligase binding Source: ParkinsonsUK-UCL
  • unfolded protein binding Source: GO_Central

Protein-protein interaction databases

BioGridi115827. 324 interactors.
DIPiDIP-38123N.
IntActiP78371. 127 interactors.
MINTiMINT-8213815.
STRINGi9606.ENSP00000299300.

Structurei

3D structure databases

ProteinModelPortaliP78371.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TCP-1 chaperonin family.Curated

Phylogenomic databases

eggNOGiKOG0363. Eukaryota.
COG0459. LUCA.
GeneTreeiENSGT00550000074930.
HOGENOMiHOG000226736.
HOVERGENiHBG001052.
InParanoidiP78371.
KOiK09494.
OMAiPGVHQPQ.
OrthoDBiEOG091G07BP.
PhylomeDBiP78371.
TreeFamiTF105645.

Family and domain databases

CDDicd03336. TCP1_beta. 1 hit.
Gene3Di1.10.560.10. 2 hits.
3.50.7.10. 1 hit.
InterProiView protein in InterPro
IPR012716. Chap_CCT_beta.
IPR017998. Chaperone_TCP-1.
IPR002194. Chaperonin_TCP-1_CS.
IPR002423. Cpn60/TCP-1.
IPR027409. GroEL-like_apical_dom.
IPR027413. GROEL-like_equatorial.
PANTHERiPTHR11353:SF119. PTHR11353:SF119. 1 hit.
PfamiView protein in Pfam
PF00118. Cpn60_TCP1. 1 hit.
PRINTSiPR00304. TCOMPLEXTCP1.
SUPFAMiSSF52029. SSF52029. 1 hit.
TIGRFAMsiTIGR02341. chap_CCT_beta. 1 hit.
PROSITEiView protein in PROSITE
PS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
PS00995. TCP1_3. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P78371-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MASLSLAPVN IFKAGADEER AETARLTSFI GAIAIGDLVK STLGPKGMDK
60 70 80 90 100
ILLSSGRDAS LMVTNDGATI LKNIGVDNPA AKVLVDMSRV QDDEVGDGTT
110 120 130 140 150
SVTVLAAELL REAESLIAKK IHPQTIIAGW REATKAAREA LLSSAVDHGS
160 170 180 190 200
DEVKFRQDLM NIAGTTLSSK LLTHHKDHFT KLAVEAVLRL KGSGNLEAIH
210 220 230 240 250
IIKKLGGSLA DSYLDEGFLL DKKIGVNQPK RIENAKILIA NTGMDTDKIK
260 270 280 290 300
IFGSRVRVDS TAKVAEIEHA EKEKMKEKVE RILKHGINCF INRQLIYNYP
310 320 330 340 350
EQLFGAAGVM AIEHADFAGV ERLALVTGGE IASTFDHPEL VKLGSCKLIE
360 370 380 390 400
EVMIGEDKLI HFSGVALGEA CTIVLRGATQ QILDEAERSL HDALCVLAQT
410 420 430 440 450
VKDSRTVYGG GCSEMLMAHA VTQLANRTPG KEAVAMESYA KALRMLPTII
460 470 480 490 500
ADNAGYDSAD LVAQLRAAHS EGNTTAGLDM REGTIGDMAI LGITESFQVK
510 520 530
RQVLLSAAEA AEVILRVDNI IKAAPRKRVP DHHPC
Length:535
Mass (Da):57,488
Last modified:January 23, 2007 - v4
Checksum:i57F9E1720D84A31F
GO
Isoform 2 (identifier: P78371-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-47: Missing.

Note: No experimental confirmation available.Combined sources
Show »
Length:488
Mass (Da):52,718
Checksum:i5947D87827A365E3
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti51I → T in BAH11729 (PubMed:14702039).Curated1
Sequence conflicti126I → T in CAG33352 (Ref. 5) Curated1
Sequence conflicti354I → T in BAF83456 (PubMed:14702039).Curated1
Sequence conflicti438S → P in BAH13640 (PubMed:14702039).Curated1
Sequence conflicti444R → K in BAG70037 (PubMed:19054851).Curated1
Sequence conflicti444R → K in BAG70160 (PubMed:19054851).Curated1
Sequence conflicti504L → P in CAG33352 (Ref. 5) Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0426481 – 47Missing in isoform 2. 1 PublicationAdd BLAST47

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF026293 mRNA. Translation: AAC96012.1.
AF026166 mRNA. Translation: AAC98906.1.
BT019966 mRNA. Translation: AAV38769.1.
AK290767 mRNA. Translation: BAF83456.1.
AK294307 mRNA. Translation: BAH11729.1.
AK302157 mRNA. Translation: BAH13640.1.
AK316397 mRNA. Translation: BAH14768.1.
AK316408 mRNA. Translation: BAH14779.1.
CR457071 mRNA. Translation: CAG33352.1.
AB451223 mRNA. Translation: BAG70037.1.
AB451346 mRNA. Translation: BAG70160.1.
AC018921 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW97230.1.
BC113514 mRNA. Translation: AAI13515.1.
BC113516 mRNA. Translation: AAI13517.1.
U91327 Genomic DNA. Translation: AAB67249.1.
CCDSiCCDS55843.1. [P78371-2]
CCDS8991.1. [P78371-1]
RefSeqiNP_001185771.1. NM_001198842.1. [P78371-2]
NP_006422.1. NM_006431.2. [P78371-1]
UniGeneiHs.189772.

Genome annotation databases

EnsembliENST00000299300; ENSP00000299300; ENSG00000166226. [P78371-1]
ENST00000543146; ENSP00000445471; ENSG00000166226. [P78371-2]
GeneIDi10576.
KEGGihsa:10576.
UCSCiuc010stl.2. human. [P78371-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiTCPB_HUMAN
AccessioniPrimary (citable) accession number: P78371
Secondary accession number(s): A8K402
, B5BTY7, B7Z243, B7Z7K4, B7ZAT2, Q14D36, Q6IAT3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: August 30, 2017
This is version 173 of the entry and version 4 of the sequence. See complete history.
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families