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Protein

T-complex protein 1 subunit alpha

Gene

TCP1

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-29794-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 alpha
Short name:
TCP-1-alpha
Alternative name(s):
CCT-alpha
Gene namesi
Name:TCP1
Synonyms:CCT1
Ordered Locus Names:YDR212W
ORF Names:YD8142.13, YD8142B.04
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR212W.
SGDiS000002620. TCP1.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi48 – 481G → E: Temperature-sensitive. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 559558T-complex protein 1 subunit alphaPRO_0000128315Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP12612.
PeptideAtlasiP12612.
PRIDEiP12612.

PTM databases

iPTMnetiP12612.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
ACT1P600103EBI-19045,EBI-2169

GO - Molecular functioni

  • unfolded protein binding Source: SGD

Protein-protein interaction databases

BioGridi32266. 170 interactions.
DIPiDIP-2965N.
IntActiP12612. 38 interactions.
MINTiMINT-549766.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V81X-ray3.80A/I/a/i1-559[»]
4V8RX-ray3.80AA/Aa/BA/Ba1-559[»]
4V94X-ray3.80A/I/a/i1-559[»]
ProteinModelPortaliP12612.
SMRiP12612. Positions 17-547.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TCP-1 chaperonin family.Curated

Phylogenomic databases

GeneTreeiENSGT00550000074878.
HOGENOMiHOG000226729.
InParanoidiP12612.
KOiK09493.
OMAiRESGMII.
OrthoDBiEOG773XR5.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR012715. Chap_CCT_alpha.
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.
TIGRFAMsiTIGR02340. chap_CCT_alpha. 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.

P12612-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQLFNNSRS DTLFLGGEKI SGDDIRNQNV LATMAVANVV KSSLGPVGLD
60 70 80 90 100
KMLVDDIGDF TVTNDGATIL SLLDVQHPAG KILVELAQQQ DREIGDGTTS
110 120 130 140 150
VVIIASELLK RANELVKNKI HPTTIITGFR VALREAIRFI NEVLSTSVDT
160 170 180 190 200
LGKETLINIA KTSMSSKIIG ADSDFFSNMV VDALLAVKTQ NSKGEIKYPV
210 220 230 240 250
KAVNVLKAHG KSATESLLVP GYALNCTVAS QAMPKRIAGG NVKIACLDLN
260 270 280 290 300
LQKARMAMGV QINIDDPEQL EQIRKREAGI VLERVKKIID AGAQVVLTTK
310 320 330 340 350
GIDDLCLKEF VEAKIMGVRR CKKEDLRRIA RATGATLVSS MSNLEGEETF
360 370 380 390 400
ESSYLGLCDE VVQAKFSDDE CILIKGTSKH SSSSIILRGA NDYSLDEMER
410 420 430 440 450
SLHDSLSVVK RTLESGNVVP GGGCVEAALN IYLDNFATTV GSREQLAIAE
460 470 480 490 500
FAAALLIIPK TLAVNAAKDS SELVAKLRSY HAASQMAKPE DVKRRSYRNY
510 520 530 540 550
GLDLIRGKIV DEIHAGVLEP TISKVKSLKS ALEACVAILR IDTMITVDPE

PPKEDPHDH
Length:559
Mass (Da):60,481
Last modified:October 1, 1996 - v2
Checksum:i02C625D329359E61
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti530 – 5301S → L in AAA35139 (PubMed:1901944).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M21160 Genomic DNA. Translation: AAA35139.1.
Z68194 Genomic DNA. Translation: CAA92355.1.
Z68195 Genomic DNA. Translation: CAA92363.1.
BK006938 Genomic DNA. Translation: DAA12056.1.
PIRiA39793.
RefSeqiNP_010498.1. NM_001180520.1.

Genome annotation databases

EnsemblFungiiYDR212W; YDR212W; YDR212W.
GeneIDi851798.
KEGGisce:YDR212W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M21160 Genomic DNA. Translation: AAA35139.1.
Z68194 Genomic DNA. Translation: CAA92355.1.
Z68195 Genomic DNA. Translation: CAA92363.1.
BK006938 Genomic DNA. Translation: DAA12056.1.
PIRiA39793.
RefSeqiNP_010498.1. NM_001180520.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V81X-ray3.80A/I/a/i1-559[»]
4V8RX-ray3.80AA/Aa/BA/Ba1-559[»]
4V94X-ray3.80A/I/a/i1-559[»]
ProteinModelPortaliP12612.
SMRiP12612. Positions 17-547.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32266. 170 interactions.
DIPiDIP-2965N.
IntActiP12612. 38 interactions.
MINTiMINT-549766.

PTM databases

iPTMnetiP12612.

Proteomic databases

MaxQBiP12612.
PeptideAtlasiP12612.
PRIDEiP12612.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR212W; YDR212W; YDR212W.
GeneIDi851798.
KEGGisce:YDR212W.

Organism-specific databases

EuPathDBiFungiDB:YDR212W.
SGDiS000002620. TCP1.

Phylogenomic databases

GeneTreeiENSGT00550000074878.
HOGENOMiHOG000226729.
InParanoidiP12612.
KOiK09493.
OMAiRESGMII.
OrthoDBiEOG773XR5.

Enzyme and pathway databases

BioCyciYEAST:G3O-29794-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

PROiP12612.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR012715. Chap_CCT_alpha.
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.
TIGRFAMsiTIGR02340. chap_CCT_alpha. 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. "The yeast homolog to mouse Tcp-1 affects microtubule-mediated processes."
    Ursic D., Culbertson M.R.
    Mol. Cell. Biol. 11:2629-2640(1991) [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. "Primary structure and function of a second essential member of the heterooligomeric TCP1 chaperonin complex of yeast, TCP1 beta."
    Miklos D., Caplan S., Mertens D., Hynes G., Pitluk Z., Kashi Y., Harrison-Lavoie K., Stevenson S., Brown C., Barrell B.G., Horwich A.L., Willison K.
    Proc. Natl. Acad. Sci. U.S.A. 91:2743-2747(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  5. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTCPA_YEAST
AccessioniPrimary (citable) accession number: P12612
Secondary accession number(s): D6VSJ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1996
Last modified: June 8, 2016
This is version 155 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 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.