CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008187
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Proteasome subunit alpha type-2 
Protein Synonyms/Alias
 Macropain subunit C3; Multicatalytic endopeptidase complex subunit C3; Proteasome component C3 
Gene Name
 Psma2 
Gene Synonyms/Alias
 Lmpc3 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
50GVVLATEKKQKSILYubiquitination[1]
53LATEKKQKSILYDERubiquitination[1]
70HKVEPITKHIGLVYSubiquitination[1]
92VLVHRARKLAQQYYLacetylation[2, 3, 4]
92VLVHRARKLAQQYYLphosphoglycerylation[5]
92VLVHRARKLAQQYYLubiquitination[1]
165WKATAMGKNYVNGKTubiquitination[1]
171GKNYVNGKTFLEKRYacetylation[3, 4]
171GKNYVNGKTFLEKRYubiquitination[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]
 [2] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [3] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [4] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [5] Functional lysine modification by an intrinsically reactive primary glycolytic metabolite.
 Moellering RE, Cravatt BF.
 Science. 2013 Aug 2;341(6145):549-53. [PMID: 23908237
Functional Description
 The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. PSMA2 may have a potential regulatory effect on another component(s) of the proteasome complex through tyrosine phosphorylation. 
Sequence Annotation
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 70 70 N6-acetyllysine (By similarity).
 MOD_RES 76 76 Phosphotyrosine.
 MOD_RES 171 171 N6-acetyllysine (By similarity).
 MOD_RES 229 229 Nitrated tyrosine (By similarity).  
Keyword
 3D-structure; Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; Hydrolase; Nitration; Nucleus; Phosphoprotein; Protease; Proteasome; Reference proteome; Threonine protease. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 234 AA 
Protein Sequence
MAERGYSFSL TTFSPSGKLV QIEYALAAVA GGAPSVGIKA ANGVVLATEK KQKSILYDER 60
SVHKVEPITK HIGLVYSGMG PDYRVLVHRA RKLAQQYYLV YQEPIPTAQL VQRVASVMQE 120
YTQSGGVRPF GVSLLICGWN EGRPYLFQSD PSGAYFAWKA TAMGKNYVNG KTFLEKRYNE 180
DLELEDAIHT AILTLKESFE GQMTEDNIEV GICNEAGFRR LTPTEVRDYL AAIA 234 
Gene Ontology
 GO:0000932; C:cytoplasmic mRNA processing body; IDA:UniProtKB.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0005839; C:proteasome core complex; IDA:UniProtKB.
 GO:0019773; C:proteasome core complex, alpha-subunit complex; IEA:InterPro.
 GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
 GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro. 
Interpro
 IPR000426; Proteasome_asu_N.
 IPR023332; Proteasome_suA-type.
 IPR001353; Proteasome_sua/b. 
Pfam
 PF00227; Proteasome
 PF10584; Proteasome_A_N 
SMART
 SM00948; Proteasome_A_N 
PROSITE
 PS00388; PROTEASOME_A_1
 PS51475; PROTEASOME_A_2 
PRINTS