CPLM-005457

Genbank Nucleotide ID

Proteasome subunit alpha type-4

Protein Synonyms/Alias

Macropain subunit C9; Multicatalytic endopeptidase complex subunit C9; Proteasome component C9; Proteasome subunit L

Homo sapiens (Human)

Position	Peptide	Type	References
54	AERRNIHKLLDEVFF	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 8]
64	DEVFFSEKIYKLNED	ubiquitination	[2, 3, 5, 7, 8]
67	FFSEKIYKLNEDMAC	ubiquitination	[4, 7]
127	AYTQFGGKRPFGVSL	acetylation	[9]
127	AYTQFGGKRPFGVSL	ubiquitination	[8]
176	AAAVSMLKQDYKEGE	acetylation	[9]
176	AAAVSMLKQDYKEGE	ubiquitination	[2, 4, 5, 6, 7, 10]
180	SMLKQDYKEGEMTLK	ubiquitination	[3, 7, 10]
187	KEGEMTLKSALALAI	ubiquitination	[3, 7]
195	SALALAIKVLNKTMD	ubiquitination	[7, 8]
199	LAIKVLNKTMDVSKL	ubiquitination	[2, 3, 5, 6, 7, 8]
205	NKTMDVSKLSAEKVE	ubiquitination	[2, 3, 7, 8]
210	VSKLSAEKVEIATLT	ubiquitination	[2, 3, 7]
222	TLTRENGKTVIRVLK	ubiquitination	[7, 8]
229	KTVIRVLKQKEVEQL	ubiquitination	[7]
231	VIRVLKQKEVEQLIK	ubiquitination	[2, 3, 6, 7]
238	KEVEQLIKKHEEEEA	acetylation	[9]
238	KEVEQLIKKHEEEEA	ubiquitination	[2, 3, 7]
246	KHEEEEAKAEREKKE	ubiquitination	[3, 8]

[1] 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]
[2] 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]
[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] 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]
[5] 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]
[6] 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]
[7] 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]
[8] 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]
[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] 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]

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 13 13 Phosphoserine.
MOD_RES 75 75 Phosphoserine.
MOD_RES 127 127 N6-acetyllysine.
MOD_RES 176 176 N6-acetyllysine.

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

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

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:0044281; P:small molecule metabolic process; TAS:Reactome.
GO:0016032; P:viral reproduction; TAS:Reactome.
GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW.

IPR000426; Proteasome_asu_N.
IPR016050; Proteasome_bsu_CS.
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