UniProt Accession

 PRS7_HUMAN; P35998; A4D0Q1; Q3LIA5; Q9UDI3 

Genbank Protein ID

 D11094; AB075520; CH236947; CH471070; BC002589 

Genbank Nucleotide ID

 BAA01868.1; BAE45763.1; EAL24412.1; EAW83332.1; AAH02589.1 

Protein Name

 26S protease regulatory subunit 7 

Protein Synonyms/Alias

 26S proteasome AAA-ATPase subunit RPT1; Proteasome 26S subunit ATPase 2; Protein MSS1 

Gene Name

 PSMC2 

Gene Synonyms/Alias

 MSS1 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
11	YLGADQRKTKEDEKD	ubiquitination	[1]
13	GADQRKTKEDEKDDK	ubiquitination	[1, 2, 3]
17	RKTKEDEKDDKPIRA	ubiquitination	[1, 2, 3]
20	KEDEKDDKPIRALDE	ubiquitination	[1, 3]
34	EGDIALLKTYGQSTY	ubiquitination	[1, 2, 3, 4, 5, 6, 7]
46	STYSRQIKQVEDDIQ	ubiquitination	[1, 2, 3, 4, 5, 6, 7]
57	DDIQQLLKKINELTG	ubiquitination	[1, 2, 3, 4, 6, 7]
58	DIQQLLKKINELTGI	ubiquitination	[1, 3, 5, 6]
66	INELTGIKESDTGLA	ubiquitination	[1, 3, 6]
84	LWDLAADKQTLQSEQ	ubiquitination	[1, 3, 4, 6, 7]
100	LQVARCTKIINADSE	ubiquitination	[1, 2, 3, 5, 6]
110	NADSEDPKYIINVKQ	ubiquitination	[1, 3, 4, 5, 6, 7]
116	PKYIINVKQFAKFVV	acetylation	[8]
116	PKYIINVKQFAKFVV	ubiquitination	[1, 2, 3, 4, 5, 6, 7]
120	INVKQFAKFVVDLSD	ubiquitination	[1, 3, 6, 9]
146	RVGVDRNKYQIHIPL	ubiquitination	[1, 3, 4, 5, 6, 7]
181	YSDVGGCKEQIEKLR	ubiquitination	[6]
186	GCKEQIEKLREVVET	ubiquitination	[3, 6]
210	NLGIEPPKGVLLFGP	ubiquitination	[1, 2, 3, 4, 6, 7, 10, 11]
222	FGPPGTGKTLCARAV	ubiquitination	[2, 5, 6, 10, 11]
248	IGSELVQKYVGEGAR	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 10, 11]
267	LFEMARTKKACLIFF	ubiquitination	[6, 12]
268	FEMARTKKACLIFFD	ubiquitination	[2, 6]
316	FDPRGNIKVLMATNR	ubiquitination	[1, 3, 5, 6]
340	RPGRLDRKIEFSLPD	ubiquitination	[1, 2, 3, 6]
356	EGRTHIFKIHARSMS	ubiquitination	[1, 3, 4, 6, 7, 11]
402	FAIRARRKIATEKDF	ubiquitination	[1, 2, 6]
407	RRKIATEKDFLEAVN	ubiquitination	[1, 2, 3, 4, 5, 6, 7]
415	DFLEAVNKVIKSYAK	ubiquitination	[1, 2, 3, 4, 5, 6, 7]
418	EAVNKVIKSYAKFSA	ubiquitination	[6]
422	KVIKSYAKFSATPRY	acetylation	[8]
422	KVIKSYAKFSATPRY	ubiquitination	[1, 2, 3, 4, 5, 6, 7]

Reference

 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [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] 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]
 [9] 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]
 [10] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
 [11] 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]
 [12] 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 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. In case of HIV-1 infection, positive modulator of Tat-mediated transactivation. 

Sequence Annotation

 NP_BIND 216 223 ATP (Potential).
 MOD_RES 116 116 N6-acetyllysine.
 MOD_RES 422 422 N6-acetyllysine.  

Keyword

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

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 433 AA 

Protein Sequence

Gene Ontology

 GO:0000932; C:cytoplasmic mRNA processing body; ISS:UniProtKB.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005739; C:mitochondrion; IDA:HPA.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0022624; C:proteasome accessory complex; ISS:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0016887; F:ATPase activity; IDA:UniProtKB.
 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:0016032; P:viral reproduction; TAS:Reactome.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 

Interpro

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

Pfam

 PF00004; AAA 

SMART

 SM00382; AAA 

PROSITE

 PS00674; AAA 

PRINTS