CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015176
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
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
138DDMVSTLKKISTPVDacetylation[1]
196GRKEIDIKKYARVEKacetylation[1]
222LRGVMINKDVTHPRMacetylation[1]
234PRMRRYIKNPRIVLLacetylation[1]
248LDSSLEYKKGESQTDacetylation[1]
381ILLRGASKEILSEVEacetylation[1]
381ILLRGASKEILSEVEubiquitination[2]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405]
 [2] Synaptic protein ubiquitination in rat brain revealed by antibody-based ubiquitome analysis.
 Na CH, Jones DR, Yang Y, Wang X, Xu Y, Peng J.
 J Proteome Res. 2012 Sep 7;11(9):4722-32. [PMID: 22871113] 
Functional Description
 Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin. Plays a role in the assembly of the von Hippel-Lindau ubiquitination complex (By similarity). 
Sequence Annotation
 MOD_RES 1 1 N-acetylmethionine (By similarity).
 MOD_RES 222 222 N6-acetyllysine (By similarity).
 MOD_RES 244 244 Phosphoserine (By similarity).
 MOD_RES 252 252 Phosphoserine (By similarity).
 DISULFID 366 372 By similarity.  
Keyword
 Acetylation; ATP-binding; Chaperone; Complete proteome; Cytoplasm; Direct protein sequencing; Disulfide bond; Nucleotide-binding; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 545 AA 
Protein Sequence
MMGHRPVLVL SQNTKRESGR KVQSGNINAA KTIADIIRTC LGPKSMMKML LDPMGGIVMT 60
NDGNAILREI QVQHPAAKSM IEISRTQDEE VGDGTTSVII LAGEMLSVAE HFLEQQMHPT 120
VVISAYRMAL DDMVSTLKKI STPVDVNNRD MMLNIINSSI TTKVISRWSS LACNIALDAV 180
KTVQFEENGR KEIDIKKYAR VEKIPGGIIE DSCVLRGVMI NKDVTHPRMR RYIKNPRIVL 240
LDSSLEYKKG ESQTDIEITR EEDFTRILQM EEEYIQQLCE DIIQLKPDVV ITEKGISDLA 300
QHYLMRANVT AIRRVRKTDN NRIARACGAR IVSRPEELRE DDVGTGAGLL EIKKIGDEYF 360
TFITDCKDPK ACTILLRGAS KEILSEVERN LQDAMQVCRN VLLDPQLVPG GGASEMAVAH 420
ALTEKSKAMT GVEQWPYRAV AQALEVIPRT LIQNCGASTI RLLTSLRAKH TQENCETWGV 480
NGETGTLVDM KELGIWEPLA VKLQTYKTAV ETAVLLLRID DIVSGHKKKG DDQNRQTGAP 540
DAGQE 545 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0006457; P:protein folding; IEA:InterPro. 
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.