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Protein

T-complex protein 1 subunit beta

Gene

CCT2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation.

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • unfolded protein binding Source: SGD

GO - Biological processi

  • protein folding Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-31392-MONOMER.
ReactomeiR-SCE-390471. Association of TriC/CCT with target proteins during biosynthesis.
R-SCE-6798695. Neutrophil degranulation.
R-SCE-6814122. Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.

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:BIN3, TCP2
Ordered Locus Names:YIL142W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IX

Organism-specific databases

EuPathDBiFungiDB:YIL142W.
SGDiS000001404. CCT2.

Subcellular locationi

GO - Cellular componenti

  • chaperonin-containing T-complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001283202 – 527T-complex protein 1 subunit betaAdd BLAST526

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP39076.
PRIDEiP39076.

PTM databases

iPTMnetiP39076.

Interactioni

Subunit structurei

Heterooligomeric complex of about 850 to 900 kDa that forms two stacked rings, 12 to 16 nm in diameter.

GO - Molecular functioni

  • unfolded protein binding Source: SGD

Protein-protein interaction databases

BioGridi34850. 82 interactors.
DIPiDIP-4451N.
IntActiP39076. 20 interactors.
MINTiMINT-568696.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4V81X-ray3.80B/J/b/j1-527[»]
4V8RX-ray3.80AB/Ab/BB/Bb1-527[»]
4V94X-ray3.80B/J/b/j1-527[»]
ProteinModelPortaliP39076.
SMRiP39076.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TCP-1 chaperonin family.Curated

Phylogenomic databases

GeneTreeiENSGT00550000074930.
HOGENOMiHOG000226736.
InParanoidiP39076.
KOiK09494.
OMAiAAHYEGH.
OrthoDBiEOG092C1WYZ.

Family and domain databases

CDDicd03336. TCP1_beta. 1 hit.
Gene3Di1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR012716. 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.
IPR027410. TCP-1-like_intermed.
[Graphical view]
PfamiPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSiPR00304. TCOMPLEXTCP1.
SUPFAMiSSF52029. SSF52029. 1 hit.
TIGRFAMsiTIGR02341. chap_CCT_beta. 1 hit.
PROSITEiPS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
PS00995. TCP1_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P39076-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVQIFGDQV TEERAENARL SAFVGAIAVG DLVKSTLGPK GMDKLLQSAS
60 70 80 90 100
SNTCMVTNDG ATILKSIPLD NPAAKVLVNI SKVQDDEVGD GTTSVTVLSA
110 120 130 140 150
ELLREAEKLI DQSKIHPQTI IEGYRLASAA ALDALTKAAV DNSHDKTMFR
160 170 180 190 200
EDLIHIAKTT LSSKILSQDK DHFAELATNA ILRLKGSTNL EHIQIIKILG
210 220 230 240 250
GKLSDSFLDE GFILAKKFGN NQPKRIENAK ILIANTTLDT DKVKIFGTKF
260 270 280 290 300
KVDSTAKLAQ LEKAEREKMK NKIAKISKFG INTFINRQLI YDYPEQLFTD
310 320 330 340 350
LGINSIEHAD FEGVERLALV TGGEVVSTFD EPSKCKLGEC DVIEEIMLGE
360 370 380 390 400
QPFLKFSGCK AGEACTIVLR GATDQTLDEA ERSLHDALSV LSQTTKETRT
410 420 430 440 450
VLGGGCAEMV MSKAVDTEAQ NIDGKKSLAV EAFARALRQL PTILADNAGF
460 470 480 490 500
DSSELVSKLR SSIYNGISTS GLDLNNGTIA DMRQLGIVES YKLKRAVVSS
510 520
ASEAAEVLLR VDNIIRARPR TANRQHM
Length:527
Mass (Da):57,203
Last modified:February 1, 1995 - v1
Checksum:iC5DB2BC3660EC7E6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X77675 Genomic DNA. Translation: CAA54745.1.
U16761 Genomic DNA. Translation: AAA53433.1.
Z38059 Genomic DNA. Translation: CAA86136.1.
AY723831 Genomic DNA. Translation: AAU09748.1.
U49845 Genomic DNA. Translation: AAA98665.1.
BK006942 Genomic DNA. Translation: DAA08411.1.
PIRiS48232.
RefSeqiNP_012124.1. NM_001179490.1.

Genome annotation databases

EnsemblFungiiYIL142W; YIL142W; YIL142W.
GeneIDi854664.
KEGGisce:YIL142W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X77675 Genomic DNA. Translation: CAA54745.1.
U16761 Genomic DNA. Translation: AAA53433.1.
Z38059 Genomic DNA. Translation: CAA86136.1.
AY723831 Genomic DNA. Translation: AAU09748.1.
U49845 Genomic DNA. Translation: AAA98665.1.
BK006942 Genomic DNA. Translation: DAA08411.1.
PIRiS48232.
RefSeqiNP_012124.1. NM_001179490.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4V81X-ray3.80B/J/b/j1-527[»]
4V8RX-ray3.80AB/Ab/BB/Bb1-527[»]
4V94X-ray3.80B/J/b/j1-527[»]
ProteinModelPortaliP39076.
SMRiP39076.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34850. 82 interactors.
DIPiDIP-4451N.
IntActiP39076. 20 interactors.
MINTiMINT-568696.

PTM databases

iPTMnetiP39076.

Proteomic databases

MaxQBiP39076.
PRIDEiP39076.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYIL142W; YIL142W; YIL142W.
GeneIDi854664.
KEGGisce:YIL142W.

Organism-specific databases

EuPathDBiFungiDB:YIL142W.
SGDiS000001404. CCT2.

Phylogenomic databases

GeneTreeiENSGT00550000074930.
HOGENOMiHOG000226736.
InParanoidiP39076.
KOiK09494.
OMAiAAHYEGH.
OrthoDBiEOG092C1WYZ.

Enzyme and pathway databases

BioCyciYEAST:G3O-31392-MONOMER.
ReactomeiR-SCE-390471. Association of TriC/CCT with target proteins during biosynthesis.
R-SCE-6798695. Neutrophil degranulation.
R-SCE-6814122. Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.

Miscellaneous databases

PROiP39076.

Family and domain databases

CDDicd03336. TCP1_beta. 1 hit.
Gene3Di1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR012716. 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.
IPR027410. TCP-1-like_intermed.
[Graphical view]
PfamiPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSiPR00304. TCOMPLEXTCP1.
SUPFAMiSSF52029. SSF52029. 1 hit.
TIGRFAMsiTIGR02341. chap_CCT_beta. 1 hit.
PROSITEiPS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
PS00995. TCP1_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTCPB_YEAST
AccessioniPrimary (citable) accession number: P39076
Secondary accession number(s): D6VVE5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 30, 2016
This is version 149 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome IX
    Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.