CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005452
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Proteasome subunit alpha type-1 
Protein Synonyms/Alias
 30 kDa prosomal protein; PROS-30; Macropain subunit C2; Multicatalytic endopeptidase complex subunit C2; Proteasome component C2; Proteasome nu chain 
Gene Name
 PSMA1 
Gene Synonyms/Alias
 HC2; NU; PROS30; PSC2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
30EYAMEAVKQGSATVGubiquitination[1, 2]
39GSATVGLKSKTHAVLubiquitination[2]
41ATVGLKSKTHAVLVAubiquitination[1]
61SELAAHQKKILHVDNubiquitination[2]
115LVSLIGSKTQIPTQRubiquitination[1, 2, 3, 4, 5, 6, 7]
208AEQDLTTKNVSIGIVubiquitination[1, 2, 3, 7]
243LEERPQRKAQPAQPAubiquitination[2]
256PADEPAEKADEPMEHubiquitination[2, 5]
Reference
 [1] 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]
 [2] 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]
 [3] Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry.
 Meierhofer D, Wang X, Huang L, Kaiser P.
 J Proteome Res. 2008 Oct;7(10):4566-76. [PMID: 18781797]
 [4] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [5] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [6] 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]
 [7] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789
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. Mediates the lipopolysaccharide-induced signal transduction in the macrophage proteasome (By similarity). Might be involved in the anti-inflammatory response of macrophages during the interaction with C.albicans heat-inactivated cells (By similarity). 
Sequence Annotation
 MOD_RES 1 1 N-acetylmethionine (By similarity).
 MOD_RES 14 14 Phosphoserine.
 CARBOHYD 110 110 O-linked (GlcNAc...) (By similarity).
 CROSSLNK 115 115 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 208 208 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 Acetylation; Alternative splicing; Complete proteome; Cytoplasm; Direct protein sequencing; Glycoprotein; Hydrolase; Immunity; Isopeptide bond; Nucleus; Phosphoprotein; Polymorphism; Protease; Proteasome; Reference proteome; Threonine protease; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 263 AA 
Protein Sequence
MFRNQYDNDV TVWSPQGRIH QIEYAMEAVK QGSATVGLKS KTHAVLVALK RAQSELAAHQ 60
KKILHVDNHI GISIAGLTAD ARLLCNFMRQ ECLDSRFVFD RPLPVSRLVS LIGSKTQIPT 120
QRYGRRPYGV GLLIAGYDDM GPHIFQTCPS ANYFDCRAMS IGARSQSART YLERHMSEFM 180
ECNLNELVKH GLRALRETLP AEQDLTTKNV SIGIVGKDLE FTIYDDDDVS PFLEGLEERP 240
QRKAQPAQPA DEPAEKADEP MEH 263 
Gene Ontology
 GO:0005813; C:centrosome; IDA:HPA.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0005844; C:polysome; TAS:ProtInc.
 GO:0005839; C:proteasome core complex; ISS:UniProtKB.
 GO:0019773; C:proteasome core complex, alpha-subunit complex; IEA:InterPro.
 GO:0003723; F:RNA binding; TAS:ProtInc.
 GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
 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; TAS:Reactome.
 GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome.
 GO:0044281; P:small molecule metabolic process; TAS:Reactome.
 GO:0016032; P:viral reproduction; TAS:Reactome. 
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