CPLM-008186

Genbank Nucleotide ID

Proteasome subunit beta type-2

Protein Synonyms/Alias

Macropain subunit C7-I; Multicatalytic endopeptidase complex subunit C7-I; Proteasome component C7-I

Homo sapiens (Human)

Position	Peptide	Type	References
29	ASNIVQMKDDHDKMF	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 8]
34	QMKDDHDKMFKMSEK	ubiquitination	[1, 2, 5, 7, 8]
37	DDHDKMFKMSEKILL	ubiquitination	[1, 2, 5, 7, 8]
62	QFAEYIQKNVQLYKM	ubiquitination	[2, 9]
68	QKNVQLYKMRNGYEL	acetylation	[10]
68	QKNVQLYKMRNGYEL	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 9, 11]
162	RAVELLRKCLEELQK	ubiquitination	[1, 2, 3, 5, 7, 8]
169	KCLEELQKRFILNLP	ubiquitination	[2, 3, 5, 8, 9]
185	FSVRIIDKNGIHDLD	acetylation	[8, 10]
185	FSVRIIDKNGIHDLD	ubiquitination	[1, 2, 3, 5, 6, 7, 8, 9, 11]
198	LDNISFPKQGS****	ubiquitination	[1, 2, 3, 5, 6, 7, 8, 9, 11]

[1] 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]
[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] 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] 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] 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]
[8] 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]
[9] 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]
[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] 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. This subunit has a trypsin-like activity.

MOD_RES 1 1 N-acetylmethionine.

Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; Host-virus interaction; Hydrolase; Nucleus; 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:0014070; P:response to organic cyclic compound; IEA:Compara.
GO:0010243; P:response to organic nitrogen; IEA:Compara.
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