CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010459
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 T-complex protein 1 subunit gamma 
Protein Synonyms/Alias
 TCP-1-gamma; CCT-gamma; Matricin; mTRiC-P5 
Gene Name
 Cct3 
Gene Synonyms/Alias
 Cctg 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
31SGNINAAKTIADIIRubiquitination[1]
44IRTCLGPKSMMKMLLubiquitination[1]
138DDMISTLKKISTPVDubiquitination[1]
139DMISTLKKISTPVDVubiquitination[1]
248LDSSLEYKKGESQTDubiquitination[1]
249DSSLEYKKGESQTDIubiquitination[1]
381ILLRGASKEILSEVEubiquitination[1]
425VAHALTEKSKAMTGVubiquitination[1]
507AVKLQTYKTAVETAVubiquitination[1]
527DDIVSGHKKKGDDQNubiquitination[1]
529IVSGHKKKGDDQNRQubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 
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  
Keyword
 3D-structure; 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 DDMISTLKKI STPVDVNNRE MMLSIINSSI TTKVISRWSS LACNIALDAV 180
KTVQFEENGR KEIDIKKYAR VEKIPGGIIE DSCVLRGVMI NKDVTHPRMR RYIKNPRIVL 240
LDSSLEYKKG ESQTDIEITR EEDFTRILQM EEEYIHQLCE DIIQLKPDVV ITEKGISDLA 300
QHYLMRANVT AIRRVRKTDN NRIARACGAR IVSRPEELRE DDVGTGAGLL EIKKIGDEYF 360
TFITDCKDPK ACTILLRGAS KEILSEVERN LQDAMQVCRN VLLDPQLVPG GGASEMAVAH 420
ALTEKSKAMT GVEQWPYRAV AQALEVIPRT LIQNCGASTI RLLTSLRAKH TQESCETWGV 480
NGETGTLVDM KELGIWEPLA VKLQTYKTAV ETAVLLLRID DIVSGHKKKG DDQNRQTGAP 540
DAGQE 545 
Gene Ontology
 GO:0044297; C:cell body; IDA:MGI.
 GO:0005832; C:chaperonin-containing T-complex; IDA:MGI.
 GO:0005874; C:microtubule; IEA:Compara.
 GO:0005886; C:plasma membrane; IEA:Compara.
 GO:0002199; C:zona pellucida receptor complex; IDA:MGI.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0007339; P:binding of sperm to zona pellucida; IDA:MGI.
 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.