CPLM-005647

Genbank Nucleotide ID

Proteasome subunit alpha type-5

Protein Synonyms/Alias

Macropain zeta chain; Multicatalytic endopeptidase complex zeta chain; Proteasome zeta chain

Homo sapiens (Human)

Position	Peptide	Type	References
66	MEPSSIEKIVEIDAH	ubiquitination	[1]
86	SGLIADAKTLIDKAR	ubiquitination	[1, 2, 3, 4]
91	DAKTLIDKARVETQN	acetylation	[5]
91	DAKTLIDKARVETQN	ubiquitination	[1, 2]
187	SLQEVYHKSMTLKEA	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 8, 9]
192	YHKSMTLKEAIKSSL	ubiquitination	[1, 2, 3, 5, 6, 7, 9]
196	MTLKEAIKSSLIILK	ubiquitination	[1, 2, 3, 4, 5, 6, 8, 9]
203	KSSLIILKQVMEEKL	ubiquitination	[1, 2, 3, 4, 5, 7, 9]
209	LKQVMEEKLNATNIE	ubiquitination	[1, 2, 3, 5, 7, 9]
231	QNFHMFTKEELEEVI	ubiquitination	[1, 2, 3, 9]
239	EELEEVIKDI*****	ubiquitination	[1, 2, 3, 5, 9, 10]

[1] 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]
[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] 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]
[4] 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]
[5] 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]
[6] 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]
[7] 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]
[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] 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]
[10] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
Xu G, Paige JS, Jaffrey SR.
Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]

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.

MOD_RES 1 1 N-acetylmethionine (By similarity).
MOD_RES 16 16 Phosphoserine.
MOD_RES 55 55 Phosphothreonine.
MOD_RES 56 56 Phosphoserine.
CARBOHYD 198 198 O-linked (GlcNAc...) (By similarity).

Acetylation; Alternative splicing; Complete proteome; Cytoplasm; Direct protein sequencing; Glycoprotein; Hydrolase; Nucleus; Phosphoprotein; Protease; Proteasome; Reference proteome; Threonine protease.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

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:0044281; P:small molecule metabolic process; TAS:Reactome.
GO:0016032; P:viral reproduction; TAS:Reactome.

IPR000426; Proteasome_asu_N.
IPR023332; Proteasome_suA-type.
IPR001353; Proteasome_sua/b.

PF00227; Proteasome
PF10584; Proteasome_A_N

SM00948; Proteasome_A_N

PS00388; PROTEASOME_A_1
PS51475; PROTEASOME_A_2