CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007336
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 T-complex protein 1 subunit epsilon 
Protein Synonyms/Alias
 TCP-1-epsilon; CCT-epsilon 
Gene Name
 CCT5 
Gene Synonyms/Alias
 TCP5; YJR064W; J1752 
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
145QKGIHPIKIANGFDEubiquitination[1]
160AAKLAISKLEETCDDubiquitination[1]
286PKPKTKHKLDISSVEacetylation[2]
413CFVRGSNKMIVDEAEubiquitination[1]
559DNVIISGKDEY****ubiquitination[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
  
Keyword
 3D-structure; ATP-binding; Chaperone; Complete proteome; Cytoplasm; Nucleotide-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 562 AA 
Protein Sequence
MAARPQQPPM EMPDLSNAIV AQDEMGRPFI IVKDQGNKKR QHGLEAKKSH ILAARSVASI 60
IKTSLGPRGL DKILISPDGE ITITNDGATI LSQMELDNEI AKLLVQLSKS QDDEIGDGTT 120
GVVVLASALL DQALELIQKG IHPIKIANGF DEAAKLAISK LEETCDDISA SNDELFRDFL 180
LRAAKTSLGS KIVSKDHDRF AEMAVEAVIN VMDKDRKDVD FDLIKMQGRV GGSISDSKLI 240
NGVILDKDFS HPQMPKCVLP KEGSDGVKLA ILTCPFEPPK PKTKHKLDIS SVEEYQKLQT 300
YEQDKFKEMI DDVKKAGADV VICQWGFDDE ANHLLLQNDL PAVRWVGGQE LEHIAISTNG 360
RIVPRFQDLS KDKLGTCSRI YEQEFGTTKD RMLIIEQSKE TKTVTCFVRG SNKMIVDEAE 420
RALHDSLCVV RNLVKDSRVV YGGGAAEVTM SLAVSEEADK QRGIDQYAFR GFAQALDTIP 480
MTLAENSGLD PIGTLSTLKS KQLKEKISNI GVDCLGYGSN DMKELFVVDP FIGKKQQILL 540
ATQLCRMILK IDNVIISGKD EY 562 
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
 IPR012718; Chap_CCT_epsi.
 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.