CPLM-004634

Genbank Nucleotide ID

26S protease regulatory subunit 6A

Protein Synonyms/Alias

26S proteasome AAA-ATPase subunit RPT5; Proteasome 26S subunit ATPase 3; Proteasome subunit P50; Tat-binding protein 1; TBP-1

Homo sapiens (Human)

Position	Peptide	Type	References
16	SPVTRQEKMATVWDE	ubiquitination	[1, 2, 3, 4, 5, 6]
35	GIGEEVLKMSTEEII	ubiquitination	[2, 5]
53	RLLDSEIKIMKSEVL	ubiquitination	[1, 2, 4, 5, 6, 7]
56	DSEIKIMKSEVLRVT	ubiquitination	[1, 2, 3, 4, 5, 6, 7]
70	THELQAMKDKIKENS	ubiquitination	[2, 3, 4, 5]
72	ELQAMKDKIKENSEK	ubiquitination	[4]
74	QAMKDKIKENSEKIK	ubiquitination	[4]
125	KGKCAVIKTSTRQTY	ubiquitination	[4, 5, 7]
144	IGLVDAEKLKPGDLV	ubiquitination	[2, 4]
146	LVDAEKLKPGDLVGV	ubiquitination	[1, 2, 4, 5, 6, 7]
155	GDLVGVNKDSYLILE	ubiquitination	[1, 2, 3, 4, 5, 6]
173	TEYDSRVKAMEVDER	ubiquitination	[1, 2, 4, 5, 6, 7]
209	IVLPMNHKEKFENLG	ubiquitination	[1, 2, 5, 6]
211	LPMNHKEKFENLGIQ	ubiquitination	[1, 2, 4, 5, 6, 7]
221	NLGIQPPKGVLMYGP	ubiquitination	[2, 3, 4]
233	YGPPGTGKTLLARAC	ubiquitination	[1, 4, 5, 6, 7]
245	RACAAQTKATFLKLA	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 8]
250	QTKATFLKLAGPQLV	ubiquitination	[1, 2, 4, 5, 6, 8]
266	MFIGDGAKLVRDAFA	ubiquitination	[2, 4, 5]
276	RDAFALAKEKAPSII	ubiquitination	[2, 3, 4, 5]
278	AFALAKEKAPSIIFI	ubiquitination	[2, 4, 5]
294	ELDAIGTKRFDSEKA	ubiquitination	[2, 4, 5, 8]
300	TKRFDSEKAGDREVQ	ubiquitination	[2, 3, 4, 5]
327	FQPNTQVKVIAATNR	ubiquitination	[2]
351	RSGRLDRKIEFPMPN	ubiquitination	[4]
372	IMQIHSRKMNVSPDV	ubiquitination	[2, 3, 4, 5, 7]
397	DFNGAQCKAVCVEAG	ubiquitination	[4]
431	ILEVQAKKKANLQYY	ubiquitination	[4]
432	LEVQAKKKANLQYYA	ubiquitination	[4]

[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] 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]
[4] 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]
[5] 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]
[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] 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]
[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]

Functional Description

The 26S protease is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex (By similarity). In case of HIV-1 infection, suppresses Tat-mediated transactivation.

NP_BIND 227 234 ATP (Potential).
MOD_RES 1 1 N-acetylmethionine.
MOD_RES 9 9 Phosphoserine.

Acetylation; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Host-virus interaction; Nucleotide-binding; Nucleus; Phosphoprotein; Proteasome; Reference proteome; Ubl conjugation.

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:0048471; C:perinuclear region of cytoplasm; IEA:Compara.
GO:0022624; C:proteasome accessory complex; ISS:UniProtKB.
GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO:0016887; F:ATPase activity; ISS:UniProtKB.
GO:0003713; F:transcription coactivator activity; TAS:ProtInc.
GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
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:0001824; P:blastocyst development; IEA:Compara.
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:0016032; P:viral reproduction; TAS:Reactome.
GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW.

IPR005937; 26S_Psome_P45.
IPR003593; AAA+_ATPase.
IPR003959; ATPase_AAA_core.
IPR003960; ATPase_AAA_CS.
IPR027417; P-loop_NTPase.