CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007102
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 T-complex protein 1 subunit gamma 
Protein Synonyms/Alias
 TCP-1-gamma; CCT-gamma 
Gene Name
 CCT3 
Gene Synonyms/Alias
 BIN2; TCP3; YJL014W; J1336 
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
208KRYVRVEKIPGGDVLubiquitination[1]
227LKGVLLNKDVVHPKMacetylation[2]
311LAQHYLLKGGCSVLRacetylation[2]
311LAQHYLLKGGCSVLRubiquitination[1]
386IMLRGGSKDILNEIDubiquitination[1]
511VIKQQSVKTAIESACubiquitination[1]
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
 MOD_RES 257 257 Phosphoserine.
 DISULFID 371 377 By similarity.  
Keyword
 3D-structure; ATP-binding; Chaperone; Complete proteome; Cytoplasm; Disulfide bond; Nucleotide-binding; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 534 AA 
Protein Sequence
MQAPVVFMNA SQERTTGRQA QISNITAAKA VADVIRTCLG PKAMLKMLLD PMGGLVLTND 60
GHAILREIDV AHPAAKSMLE LSRTQDEEVG DGTTTVIILA GEILAQCAPY LIEKNIHPVI 120
IIQALKKALT DALEVIKQVS KPVDVENDAA MKKLIQASIG TKYVIHWSEK MCELALDAVK 180
TVRKDLGQTV EGEPNFEIDI KRYVRVEKIP GGDVLDSRVL KGVLLNKDVV HPKMSRHIEN 240
PRVVLLDCPL EYKKGESQTN IEIEKEEDWN RILQIEEEQV QLMCEQILAV RPTLVITEKG 300
VSDLAQHYLL KGGCSVLRRV KKSDNNRIAR VTGATIVNRV EDLKESDVGT NCGLFKVEMI 360
GDEYFSFLDN CKEPKACTIM LRGGSKDILN EIDRNLQDAM AVARNVMLSP SLSPGGGATE 420
MAVSVKLAEK AKQLEGIQQW PYQAVADAME CIPRTLIQNA GGDPIRLLSQ LRAKHAQGNF 480
TTGIDGDKGK IVDMVSYGIW EPEVIKQQSV KTAIESACLL LRVDDIVSGV RKQE 534 
Gene Ontology
 GO:0005832; C:chaperonin-containing T-complex; 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
 IPR012719; 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. 
Pfam
 PF00118; Cpn60_TCP1 
SMART
  
PROSITE
 PS00750; TCP1_1
 PS00751; TCP1_2
 PS00995; TCP1_3 
PRINTS
 PR00304; TCOMPLEXTCP1.