UniProt Accession

 PSA3_HUMAN; P25788; B2RCK6; Q86U83; Q8N1D8; Q9BS70 

Genbank Protein ID

 D00762; BT006711; BT019715; AK315158; CH471061; BC005265; BC029402; BC038990 

Genbank Nucleotide ID

 BAA00659.1; AAP35357.1; AAV38520.1; BAG37603.1; EAW80719.1; AAH05265.1; AAH29402.1; AAH38990.1 

Protein Name

 Proteasome subunit alpha type-3 

Protein Synonyms/Alias

 Macropain subunit C8; Multicatalytic endopeptidase complex subunit C8; Proteasome component C8 

Gene Name

 PSMA3 

Gene Synonyms/Alias

 HC8; PSC8 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
29	FQVEYAMKAVENSST	ubiquitination	[1, 2, 3]
43	TAIGIRCKDGVVFGV	ubiquitination	[1, 2, 3, 4, 5]
52	GVVFGVEKLVLSKLY	ubiquitination	[1, 2]
57	VEKLVLSKLYEEGSN	acetylation	[3, 6, 7, 8]
57	VEKLVLSKLYEEGSN	ubiquitination	[1, 2, 3, 4, 5, 9, 10, 11, 12, 13]
65	LYEEGSNKRLFNVDR	acetylation	[3]
65	LYEEGSNKRLFNVDR	ubiquitination	[1, 2, 3, 12]
110	FGYNIPLKHLADRVA	acetylation	[6]
110	FGYNIPLKHLADRVA	ubiquitination	[1, 2, 4, 10]
174	GKARQAAKTEIEKLQ	ubiquitination	[2]
179	AAKTEIEKLQMKEMT	ubiquitination	[1, 2]
183	EIEKLQMKEMTCRDI	ubiquitination	[1, 2, 4, 13]
192	MTCRDIVKEVAKIIY	ubiquitination	[2]
206	YIVHDEVKDKAFELE	acetylation	[6]
206	YIVHDEVKDKAFELE	ubiquitination	[1, 2]
208	VHDEVKDKAFELELS	ubiquitination	[2]
230	GRHEIVPKDIREEAE	acetylation	[6]
230	GRHEIVPKDIREEAE	ubiquitination	[1, 2, 4, 10]
238	DIREEAEKYAKESLK	acetylation	[6]
238	DIREEAEKYAKESLK	ubiquitination	[1, 2, 10]

Reference

 [1] 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]
 [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] 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]
 [4] 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]
 [5] 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]
 [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]
 [7] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [8] 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]
 [9] 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]
 [10] 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]
 [11] 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]
 [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] 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] 

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. Binds to the C-terminus of CDKN1A and thereby mediates its degradation. Negatively regulates the membrane trafficking of the cell-surface thromboxane A2 receptor (TBXA2R) isoform 2. 

Sequence Annotation

 MOD_RES 2 2 N-acetylserine.
 MOD_RES 57 57 N6-acetyllysine.
 MOD_RES 206 206 N6-acetyllysine.
 MOD_RES 230 230 N6-acetyllysine.
 MOD_RES 243 243 Phosphoserine.
 MOD_RES 250 250 Phosphoserine.  

Keyword

 Acetylation; Alternative splicing; Complete proteome; Cytoplasm; Direct protein sequencing; Host-virus interaction; Hydrolase; Nucleus; Phosphoprotein; Protease; Proteasome; Reference proteome; Threonine protease. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 255 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0005839; C:proteasome core complex; IDA:BHF-UCL.
 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:0044281; P:small molecule metabolic process; TAS:Reactome.
 GO:0016032; P:viral reproduction; TAS:Reactome.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 

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