CPLM-009269

Genbank Nucleotide ID

Proteasome subunit alpha type-6

Protein Synonyms/Alias

27 kDa prosomal protein; PROS-27; p27K; Macropain iota chain; Multicatalytic endopeptidase complex iota chain; Proteasome iota chain

Homo sapiens (Human)

Position	Peptide	Type	References
30	YQVEYAFKAINQGGL	ubiquitination	[1, 2]
45	TSVAVRGKDCAVIVT	ubiquitination	[1, 3]
55	AVIVTQKKVPDKLLD	ubiquitination	[1, 2, 3]
59	TQKKVPDKLLDSSTV	ubiquitination	[4, 5]
102	RYEAANWKYKYGYEI	acetylation	[6]
102	RYEAANWKYKYGYEI	ubiquitination	[1, 2, 3, 5, 7, 8, 9]
104	EAANWKYKYGYEIPV	acetylation	[6]
104	EAANWKYKYGYEIPV	ubiquitination	[1, 5]
116	IPVDMLCKRIADISQ	ubiquitination	[1, 8]
164	AGYYCGFKATAAGVK	ubiquitination	[1, 3]
171	KATAAGVKQTESTSF	ubiquitination	[1, 2, 3]
181	ESTSFLEKKVKKKFD	acetylation	[6]
181	ESTSFLEKKVKKKFD	ubiquitination	[1, 2, 3]

[1] 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]
[2] 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]
[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] Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry.
Denis NJ, Vasilescu J, Lambert JP, Smith JC, Figeys D.
Proteomics. 2007 Mar;7(6):868-74. [PMID: 17370265]
[5] 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]
[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] 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]
[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] 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 102 102 N6-acetyllysine.
MOD_RES 104 104 N6-acetyllysine.
MOD_RES 159 159 Phosphotyrosine (By similarity).
CARBOHYD 5 5 O-linked (GlcNAc...) (By similarity).
CROSSLNK 59 59 Glycyl lysine isopeptide (Lys-Gly)

Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; Glycoprotein; Hydrolase; Isopeptide bond; Nucleus; Phosphoprotein; Polymorphism; Protease; Proteasome; Reference proteome; Threonine protease; Ubl conjugation.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0000932; C:cytoplasmic mRNA processing body; ISS:UniProtKB.
GO:0005829; C:cytosol; TAS:Reactome.
GO:0005739; C:mitochondrion; IDA:HPA.
GO:0016363; C:nuclear matrix; ISS:BHF-UCL.
GO:0005654; C:nucleoplasm; TAS:Reactome.
GO:0005844; C:polysome; IDA:BHF-UCL.
GO:0019773; C:proteasome core complex, alpha-subunit complex; IDA:BHF-UCL.
GO:0030017; C:sarcomere; ISS:BHF-UCL.
GO:0004175; F:endopeptidase activity; NAS:UniProtKB.
GO:0035639; F:purine ribonucleoside triphosphate binding; NAS:BHF-UCL.
GO:0003723; F:RNA binding; NAS: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:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:BHF-UCL.
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:0050727; P:regulation of inflammatory response; IC:BHF-UCL.
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