CPLM-004884

Genbank Nucleotide ID

Proteasome subunit beta type-1

Protein Synonyms/Alias

Macropain subunit C5; Multicatalytic endopeptidase complex subunit C5; Proteasome component C5; Proteasome gamma chain

Homo sapiens (Human)

Position	Peptide	Type	References
73	RDSPKCYKLTDKTVI	ubiquitination	[1, 2]
77	KCYKLTDKTVIGCSG	ubiquitination	[1, 2, 3, 4, 5, 6]
94	GDCLTLTKIIEARLK	ubiquitination	[1, 2, 3, 4, 6, 7]
104	EARLKMYKHSNNKAM	ubiquitination	[7]
164	SYQRDSFKAGGSASA	ubiquitination	[1, 4, 5, 7, 8, 9]
184	LDNQVGFKNMQNVEH	ubiquitination	[1, 2, 4, 7, 8, 9]
204	DRAMRLVKDVFISAA	acetylation	[2, 10, 11, 12]
204	DRAMRLVKDVFISAA	ubiquitination	[1, 2, 4, 7, 9, 13]
228	LRICIVTKEGIREET	ubiquitination	[1, 2, 3, 4, 6, 7]
240	EETVSLRKD******	ubiquitination	[9]

[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] 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] 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]
[4] 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]
[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] 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]
[7] 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]
[8] 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]
[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] 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]
[11] 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]
[12] 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]
[13] 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]

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 150 150 Phosphotyrosine (By similarity).
MOD_RES 204 204 N6-acetyllysine.
CARBOHYD 58 58 O-linked (GlcNAc...) (By similarity).
CARBOHYD 209 209 O-linked (GlcNAc...) (By similarity).

Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; Glycoprotein; Host-virus interaction; Hydrolase; Nucleus; Phosphoprotein; Polymorphism; 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: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.

IPR016050; Proteasome_bsu_CS.
IPR001353; Proteasome_sua/b.
IPR023333; Proteasome_suB-type.

PS00854; PROTEASOME_B_1
PS51476; PROTEASOME_B_2