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Protein

T-complex protein 1 subunit delta

Gene

CCT4

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-29540-MONOMER.
ReactomeiR-SCE-390471. Association of TriC/CCT with target proteins during biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
T-complex protein 1 subunit delta
Short name:
TCP-1-delta
Alternative name(s):
CCT-delta
Gene namesi
Name:CCT4
Synonyms:ANC2, TCP4
Ordered Locus Names:YDL143W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDL143W.
SGDiS000002302. CCT4.

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 – 528528T-complex protein 1 subunit deltaPRO_0000128345Add
BLAST

Proteomic databases

MaxQBiP39078.
PeptideAtlasiP39078.

PTM databases

iPTMnetiP39078.

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

BioGridi31918. 75 interactions.
DIPiDIP-6753N.
IntActiP39078. 31 interactions.
MINTiMINT-628250.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V81X-ray3.80D/L/d/l1-528[»]
4V8RX-ray3.80AD/Ad/BD/Bd1-528[»]
4V94X-ray3.80D/L/d/l1-528[»]
ProteinModelPortaliP39078.
SMRiP39078. Positions 9-528.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TCP-1 chaperonin family.Curated

Phylogenomic databases

GeneTreeiENSGT00550000074956.
HOGENOMiHOG000226735.
InParanoidiP39078.
KOiK09496.
OMAiAYCVRAY.
OrthoDBiEOG773XR5.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR012717. Chap_CCT_delta.
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.
TIGRFAMsiTIGR02342. chap_CCT_delta. 1 hit.
PROSITEiPS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
PS00995. TCP1_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P39078-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAKVPSNAT FKNKEKPQEV RKANIIAARS VADAIRTSLG PKGMDKMIKT
60 70 80 90 100
SRGEIIISND GHTILKQMAI LHPVARMLVE VSAAQDSEAG DGTTSVVILT
110 120 130 140 150
GALLGAAERL LNKGIHPTII ADSFQSAAKR SVDILLEMCH KVSLSDREQL
160 170 180 190 200
VRAASTSLSS KIVSQYSSFL APLAVDSVLK ISDENSKNVD LNDIRLVKKV
210 220 230 240 250
GGTIDDTEMI DGVVLTQTAI KSAGGPTRKE KAKIGLIQFQ ISPPKPDTEN
260 270 280 290 300
NIIVNDYRQM DKILKEERAY LLNICKKIKK AKCNVLLIQK SILRDAVNDL
310 320 330 340 350
ALHFLSKLNI MVVKDIEREE IEFLSKGLGC KPIADIELFT EDRLGSADLV
360 370 380 390 400
EEIDSDGSKI VRVTGIRNNN ARPTVSVVIR GANNMIIDET ERSLHDALCV
410 420 430 440 450
IRCLVKERGL IAGGGAPEIE ISRRLSKEAR SMEGVQAFIW QEFASALEVI
460 470 480 490 500
PTTLAENAGL NSIKVVTELR SKHENGELND GISVRRSGTT NTYEEHILQP
510 520
VLVSTSAITL ASECVKSILR IDDIAFSR
Length:528
Mass (Da):57,604
Last modified:November 1, 1997 - v2
Checksum:iF01146D76F4E850C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti254 – 2541V → A in CAA83912 (PubMed:7916461).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z33504 Genomic DNA. Translation: CAA83912.1.
Z74191 Genomic DNA. Translation: CAA98716.1.
BK006938 Genomic DNA. Translation: DAA11715.1.
PIRiS67690.
RefSeqiNP_010138.1. NM_001180203.1.

Genome annotation databases

EnsemblFungiiYDL143W; YDL143W; YDL143W.
GeneIDi851412.
KEGGisce:YDL143W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z33504 Genomic DNA. Translation: CAA83912.1.
Z74191 Genomic DNA. Translation: CAA98716.1.
BK006938 Genomic DNA. Translation: DAA11715.1.
PIRiS67690.
RefSeqiNP_010138.1. NM_001180203.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V81X-ray3.80D/L/d/l1-528[»]
4V8RX-ray3.80AD/Ad/BD/Bd1-528[»]
4V94X-ray3.80D/L/d/l1-528[»]
ProteinModelPortaliP39078.
SMRiP39078. Positions 9-528.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31918. 75 interactions.
DIPiDIP-6753N.
IntActiP39078. 31 interactions.
MINTiMINT-628250.

PTM databases

iPTMnetiP39078.

Proteomic databases

MaxQBiP39078.
PeptideAtlasiP39078.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDL143W; YDL143W; YDL143W.
GeneIDi851412.
KEGGisce:YDL143W.

Organism-specific databases

EuPathDBiFungiDB:YDL143W.
SGDiS000002302. CCT4.

Phylogenomic databases

GeneTreeiENSGT00550000074956.
HOGENOMiHOG000226735.
InParanoidiP39078.
KOiK09496.
OMAiAYCVRAY.
OrthoDBiEOG773XR5.

Enzyme and pathway databases

BioCyciYEAST:G3O-29540-MONOMER.
ReactomeiR-SCE-390471. Association of TriC/CCT with target proteins during biosynthesis.

Miscellaneous databases

NextBioi968597.
PROiP39078.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR012717. Chap_CCT_delta.
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.
TIGRFAMsiTIGR02342. chap_CCT_delta. 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. "A yeast TCP-1-like protein is required for actin function in vivo."
    Vinh D., Drubin D.G.
    Proc. Natl. Acad. Sci. U.S.A. 91:9116-9120(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [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. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTCPD_YEAST
AccessioniPrimary (citable) accession number: P39078
Secondary accession number(s): D6VRK5, Q07561
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: November 1, 1997
Last modified: May 11, 2016
This is version 140 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 5530 molecules/cell in log phase SD medium.1 Publication

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 IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: 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.