CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009340
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Proteasome activator complex subunit 3 
Protein Synonyms/Alias
 11S regulator complex subunit gamma; REG-gamma; Activator of multicatalytic protease subunit 3; Ki nuclear autoantigen; Proteasome activator 28 subunit gamma; PA28g; PA28gamma 
Gene Name
 PSME3 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
6**MASLLKVDQEVKLsumoylation[1]
6**MASLLKVDQEVKLubiquitination[2]
12LKVDQEVKLKVDSFRsumoylation[1]
14VDQEVKLKVDSFRERsumoylation[1]
14VDQEVKLKVDSFRERubiquitination[2, 3, 4]
36LVANFFPKKLLELDSubiquitination[3, 4, 5]
37VANFFPKKLLELDSFubiquitination[2, 5]
110VMPNGMLKSNQQLVDubiquitination[2, 5]
121QLVDIIEKVKPEIRLubiquitination[2, 4, 5]
132EIRLLIEKCNTVKMWubiquitination[2]
195KLVSKIAKYPHVEDYacetylation[6]
195KLVSKIAKYPHVEDYubiquitination[5]
Reference
 [1] Regulation of REGγ cellular distribution and function by SUMO modification.
 Wu Y, Wang L, Zhou P, Wang G, Zeng Y, Wang Y, Liu J, Zhang B, Liu S, Luo H, Li X.
 Cell Res. 2011 May;21(5):807-16. [PMID: 21445096]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [5] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [6] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861] 
Functional Description
 Subunit of the 11S REG-gamma (also called PA28-gamma) proteasome regulator, a doughnut-shaped homoheptamer which associates with the proteasome. 11S REG-gamma activates the trypsin-like catalytic subunit of the proteasome but inhibits the chymotrypsin-like and postglutamyl-preferring (PGPH) subunits. Facilitates the MDM2-p53/TP53 interaction which promotes ubiquitination- and MDM2-dependent proteasomal degradation of p53/TP53, limiting its accumulation and resulting in inhibited apoptosis after DNA damage. May also be involved in cell cycle regulation. 
Sequence Annotation
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 24 24 Phosphoserine.
 MOD_RES 205 205 Phosphothreonine (By similarity).
 MOD_RES 207 207 Phosphothreonine (By similarity).  
Keyword
 Acetylation; Alternative splicing; Apoptosis; Cell cycle; Complete proteome; Cytoplasm; Direct protein sequencing; Nucleus; Phosphoprotein; Proteasome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 254 AA 
Protein Sequence
MASLLKVDQE VKLKVDSFRE RITSEAEDLV ANFFPKKLLE LDSFLKEPIL NIHDLTQIHS 60
DMNLPVPDPI LLTNSHDGLD GPTYKKRRLD ECEEAFQGTK VFVMPNGMLK SNQQLVDIIE 120
KVKPEIRLLI EKCNTVKMWV QLLIPRIEDG NNFGVSIQEE TVAELRTVES EAASYLDQIS 180
RYYITRAKLV SKIAKYPHVE DYRRTVTEID EKEYISLRLI ISELRNQYVT LHDMILKNIE 240
KIKRPRSSNA ETLY 254 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0008537; C:proteasome activator complex; IEA:InterPro.
 GO:0000502; C:proteasome complex; TAS:ProtInc.
 GO:0061133; F:endopeptidase activator activity; IDA:UniProtKB.
 GO:0097371; F:MDM2/MDM4 family protein binding; IDA:UniProtKB.
 GO:0002039; F:p53 binding; IDA:UniProtKB.
 GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
 GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
 GO:0006915; P:apoptotic process; TAS:Reactome.
 GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
 GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
 GO:0010467; P:gene expression; TAS:Reactome.
 GO:0016071; P:mRNA metabolic process; TAS:Reactome.
 GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
 GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
 GO:0000209; P:protein polyubiquitination; TAS:Reactome.
 GO:0042981; P:regulation of apoptotic process; IDA:UniProtKB.
 GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome.
 GO:0061136; P:regulation of proteasomal protein catabolic process; IDA:UniProtKB.
 GO:0044281; P:small molecule metabolic process; TAS:Reactome.
 GO:0016032; P:viral reproduction; TAS:Reactome. 
Interpro
 IPR003185; Proteasome_activ_REG_asu.
 IPR009077; Proteasome_activ_REG_asu/bsu.
 IPR003186; Proteasome_activ_REG_bsu. 
Pfam
 PF02251; PA28_alpha
 PF02252; PA28_beta 
SMART
  
PROSITE
  
PRINTS