CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004027
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 T-complex protein 1 subunit alpha 
Protein Synonyms/Alias
 TCP-1-alpha; CCT-alpha 
Gene Name
 TCP1 
Gene Synonyms/Alias
 CCT1; YDR212W; YD8142.13; YD8142B.04 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
19TLFLGGEKISGDDIRubiquitination[1]
201GEIKYPVKAVNVLKAacetylation[2]
410HDSLSVVKRTLESGNacetylation[2]
468TLAVNAAKDSSELVAubiquitination[1]
476DSSELVAKLRSYHAAacetylation[2]
488HAASQMAKPEDVKRRacetylation[2]
508GLDLIRGKIVDEIHAacetylation[2]
Reference
 [1] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301]
 [2] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919] 
Functional Description
 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. 
Sequence Annotation
  
Keyword
 3D-structure; ATP-binding; Chaperone; Complete proteome; Cytoplasm; Nucleotide-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 559 AA 
Protein Sequence
MSQLFNNSRS DTLFLGGEKI SGDDIRNQNV LATMAVANVV KSSLGPVGLD KMLVDDIGDF 60
TVTNDGATIL SLLDVQHPAG KILVELAQQQ DREIGDGTTS VVIIASELLK RANELVKNKI 120
HPTTIITGFR VALREAIRFI NEVLSTSVDT LGKETLINIA KTSMSSKIIG ADSDFFSNMV 180
VDALLAVKTQ NSKGEIKYPV KAVNVLKAHG KSATESLLVP GYALNCTVAS QAMPKRIAGG 240
NVKIACLDLN LQKARMAMGV QINIDDPEQL EQIRKREAGI VLERVKKIID AGAQVVLTTK 300
GIDDLCLKEF VEAKIMGVRR CKKEDLRRIA RATGATLVSS MSNLEGEETF ESSYLGLCDE 360
VVQAKFSDDE CILIKGTSKH SSSSIILRGA NDYSLDEMER SLHDSLSVVK RTLESGNVVP 420
GGGCVEAALN IYLDNFATTV GSREQLAIAE FAAALLIIPK TLAVNAAKDS SELVAKLRSY 480
HAASQMAKPE DVKRRSYRNY GLDLIRGKIV DEIHAGVLEP TISKVKSLKS ALEACVAILR 540
IDTMITVDPE PPKEDPHDH 559 
Gene Ontology
 GO:0005832; C:chaperonin-containing T-complex; IDA:SGD.
 GO:0005886; C:plasma membrane; IDA:SGD.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0051082; F:unfolded protein binding; IDA:SGD.
 GO:0006457; P:protein folding; IDA:SGD. 
Interpro
 IPR012715; 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. 
Pfam
 PF00118; Cpn60_TCP1 
SMART
  
PROSITE
 PS00750; TCP1_1
 PS00751; TCP1_2
 PS00995; TCP1_3 
PRINTS
 PR00304; TCOMPLEXTCP1.