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Protein

T-complex protein 1 subunit gamma

Gene

CCT3

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-31489-MONOMER.
ReactomeiR-SCE-390471. Association of TriC/CCT with target proteins during biosynthesis.
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 gamma
Short name:
TCP-1-gamma
Alternative name(s):
CCT-gamma
Gene namesi
Name:CCT3
Synonyms:BIN2, TCP3
Ordered Locus Names:YJL014W
ORF Names:J1336
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome X

Organism-specific databases

EuPathDBiFungiDB:YJL014W.
SGDiS000003551. CCT3.

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 534534T-complex protein 1 subunit gammaPRO_0000128331Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources
Modified residuei257 – 2571PhosphoserineCombined sources
Disulfide bondi371 ↔ 377By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

MaxQBiP39077.
PeptideAtlasiP39077.
PRIDEiP39077.

PTM databases

iPTMnetiP39077.

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

BioGridi33741. 111 interactions.
DIPiDIP-6400N.
IntActiP39077. 19 interactions.
MINTiMINT-682205.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V81X-ray3.80C/K/c/k1-534[»]
4V8RX-ray3.80AG/Ag/BG/Bg1-534[»]
4V94X-ray3.80C/K/c/k1-534[»]
ProteinModelPortaliP39077.
SMRiP39077. Positions 5-529.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TCP-1 chaperonin family.Curated

Phylogenomic databases

GeneTreeiENSGT00570000079224.
HOGENOMiHOG000226732.
InParanoidiP39077.
KOiK09495.
OMAiTQCGLFE.
OrthoDBiEOG773XR5.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR012719. Chap_CCT_gamma.
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]
PANTHERiPTHR11353:SF63. PTHR11353:SF63. 1 hit.
PfamiPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSiPR00304. TCOMPLEXTCP1.
SUPFAMiSSF52029. SSF52029. 1 hit.
TIGRFAMsiTIGR02344. chap_CCT_gamma. 1 hit.
PROSITEiPS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
PS00995. TCP1_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P39077-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQAPVVFMNA SQERTTGRQA QISNITAAKA VADVIRTCLG PKAMLKMLLD
60 70 80 90 100
PMGGLVLTND GHAILREIDV AHPAAKSMLE LSRTQDEEVG DGTTTVIILA
110 120 130 140 150
GEILAQCAPY LIEKNIHPVI IIQALKKALT DALEVIKQVS KPVDVENDAA
160 170 180 190 200
MKKLIQASIG TKYVIHWSEK MCELALDAVK TVRKDLGQTV EGEPNFEIDI
210 220 230 240 250
KRYVRVEKIP GGDVLDSRVL KGVLLNKDVV HPKMSRHIEN PRVVLLDCPL
260 270 280 290 300
EYKKGESQTN IEIEKEEDWN RILQIEEEQV QLMCEQILAV RPTLVITEKG
310 320 330 340 350
VSDLAQHYLL KGGCSVLRRV KKSDNNRIAR VTGATIVNRV EDLKESDVGT
360 370 380 390 400
NCGLFKVEMI GDEYFSFLDN CKEPKACTIM LRGGSKDILN EIDRNLQDAM
410 420 430 440 450
AVARNVMLSP SLSPGGGATE MAVSVKLAEK AKQLEGIQQW PYQAVADAME
460 470 480 490 500
CIPRTLIQNA GGDPIRLLSQ LRAKHAQGNF TTGIDGDKGK IVDMVSYGIW
510 520 530
EPEVIKQQSV KTAIESACLL LRVDDIVSGV RKQE
Length:534
Mass (Da):58,814
Last modified:November 1, 1995 - v2
Checksum:i5C5AFF3D67D9A3B6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 262IT → HA in AAA21658 (PubMed:7916460).Curated
Sequence conflicti86 – 894DEEV → ERRG in AAA21658 (PubMed:7916460).Curated
Sequence conflicti111 – 1111L → F in AAA21658 (PubMed:7916460).Curated
Sequence conflicti265 – 2651K → M in AAA21658 (PubMed:7916460).Curated
Sequence conflicti274 – 2741Q → L in AAA21658 (PubMed:7916460).Curated
Sequence conflicti292 – 2921Missing in AAA21658 (PubMed:7916460).Curated
Sequence conflicti478 – 4781G → A in AAA21658 (PubMed:7916460).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09480 Genomic DNA. Translation: AAA21658.1.
Z49289 Genomic DNA. Translation: CAA89305.1.
BK006943 Genomic DNA. Translation: DAA08779.1.
PIRiS56785.
RefSeqiNP_012520.1. NM_001181448.1.

Genome annotation databases

EnsemblFungiiYJL014W; YJL014W; YJL014W.
GeneIDi853438.
KEGGisce:YJL014W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09480 Genomic DNA. Translation: AAA21658.1.
Z49289 Genomic DNA. Translation: CAA89305.1.
BK006943 Genomic DNA. Translation: DAA08779.1.
PIRiS56785.
RefSeqiNP_012520.1. NM_001181448.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V81X-ray3.80C/K/c/k1-534[»]
4V8RX-ray3.80AG/Ag/BG/Bg1-534[»]
4V94X-ray3.80C/K/c/k1-534[»]
ProteinModelPortaliP39077.
SMRiP39077. Positions 5-529.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33741. 111 interactions.
DIPiDIP-6400N.
IntActiP39077. 19 interactions.
MINTiMINT-682205.

PTM databases

iPTMnetiP39077.

Proteomic databases

MaxQBiP39077.
PeptideAtlasiP39077.
PRIDEiP39077.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYJL014W; YJL014W; YJL014W.
GeneIDi853438.
KEGGisce:YJL014W.

Organism-specific databases

EuPathDBiFungiDB:YJL014W.
SGDiS000003551. CCT3.

Phylogenomic databases

GeneTreeiENSGT00570000079224.
HOGENOMiHOG000226732.
InParanoidiP39077.
KOiK09495.
OMAiTQCGLFE.
OrthoDBiEOG773XR5.

Enzyme and pathway databases

BioCyciYEAST:G3O-31489-MONOMER.
ReactomeiR-SCE-390471. Association of TriC/CCT with target proteins during biosynthesis.
R-SCE-6814122. Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.

Miscellaneous databases

PROiP39077.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR012719. Chap_CCT_gamma.
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]
PANTHERiPTHR11353:SF63. PTHR11353:SF63. 1 hit.
PfamiPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSiPR00304. TCOMPLEXTCP1.
SUPFAMiSSF52029. SSF52029. 1 hit.
TIGRFAMsiTIGR02344. chap_CCT_gamma. 1 hit.
PROSITEiPS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
PS00995. TCP1_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Two yeast genes with similarity to TCP-1 are required for microtubule and actin function in vivo."
    Chen X., Sullivan D.S., Huffaker T.C.
    Proc. Natl. Acad. Sci. U.S.A. 91:9111-9115(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
    Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K.
    , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
    EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  5. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTCPG_YEAST
AccessioniPrimary (citable) accession number: P39077
Secondary accession number(s): D6VWG3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: November 1, 1995
Last modified: June 8, 2016
This is version 136 of the entry and version 2 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 X
    Yeast (Saccharomyces cerevisiae) chromosome X: 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.