UniProt Accession

 PSA2_HUMAN; P25787; Q6ICS6; Q9BU45 

Genbank Protein ID

 D00760; AK290654; CR450317; CH236951; CH471073; BC002900; BC047697 

Genbank Nucleotide ID

 BAA00657.1; BAF83343.1; CAG29313.1; EAL24005.1; EAW94152.1; AAH02900.2; AAH47697.1 

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

 HC3; PSC3 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
39	GAPSVGIKAANGVVL	ubiquitination	[1]
50	GVVLATEKKQKSILY	acetylation	[2]
50	GVVLATEKKQKSILY	ubiquitination	[1, 2, 3, 4, 5, 6]
51	VVLATEKKQKSILYD	ubiquitination	[2, 5]
53	LATEKKQKSILYDER	acetylation	[2]
53	LATEKKQKSILYDER	ubiquitination	[2, 3, 5, 7, 8]
64	YDERSVHKVEPITKH	ubiquitination	[1, 2, 3, 4, 5, 6]
70	HKVEPITKHIGLVYS	acetylation	[9]
70	HKVEPITKHIGLVYS	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 8, 10, 11, 12]
92	VLVHRARKLAQQYYL	acetylation	[13]
92	VLVHRARKLAQQYYL	ubiquitination	[3, 5, 6, 7, 8, 10]
165	WKATAMGKNYVNGKT	ubiquitination	[3, 4, 5, 6, 7, 8]
171	GKNYVNGKTFLEKRY	acetylation	[9]
171	GKNYVNGKTFLEKRY	ubiquitination	[3, 5, 6, 7, 8]
176	NGKTFLEKRYNEDLE	ubiquitination	[3, 5]
227	RLTPTEVKDYLAAIA	ubiquitination	[3, 4, 5, 6]

Reference

 [1] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [2] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [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] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [5] 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]
 [6] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [7] 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]
 [8] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [9] 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]
 [10] 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]
 [11] 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]
 [12] 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]
 [13] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786] 

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 (By similarity).
 MOD_RES 70 70 N6-acetyllysine.
 MOD_RES 76 76 Phosphotyrosine (By similarity).
 MOD_RES 171 171 N6-acetyllysine.
 MOD_RES 229 229 Nitrated tyrosine.  

Keyword

 Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; Hydrolase; Nitration; Nucleus; Phosphoprotein; Polymorphism; Protease; Proteasome; Reference proteome; Threonine protease. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 234 AA 

Protein Sequence

Gene Ontology

 GO:0000932; C:cytoplasmic mRNA processing body; ISS:UniProtKB.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0005839; C:proteasome core complex; ISS:UniProtKB.
 GO:0019773; C:proteasome core complex, alpha-subunit complex; IEA:InterPro.
 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:0009615; P:response to virus; IEP:UniProtKB.
 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