CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009491
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 26S protease regulatory subunit 10B 
Protein Synonyms/Alias
 26S proteasome AAA-ATPase subunit RPT4; Proteasome 26S subunit ATPase 6; Proteasome subunit p42 
Gene Name
 PSMC6 
Gene Synonyms/Alias
 SUG2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
7*MADPRDKALQDYRKubiquitination[1, 2]
15ALQDYRKKLLEHKEIubiquitination[1]
20RKKLLEHKEIDGRLKacetylation[3]
20RKKLLEHKEIDGRLKubiquitination[1, 2, 4]
34KELREQLKELTKQYEubiquitination[1, 5]
48EKSENDLKALQSVGQubiquitination[1, 2, 4, 5, 6]
62QIVGEVLKQLTEEKFubiquitination[5]
72TEEKFIVKATNGPRYacetylation[3]
93QLDKSKLKPGTRVALsumoylation[7]
168RVGIIPPKGCLLYGPubiquitination[1, 4, 5]
180YGPPGTGKTLLARAVubiquitination[1, 4, 5]
197QLDCNFLKVVSSSIVubiquitination[1, 2, 4, 5, 6, 8, 9]
206VSSSIVDKYIGESARacetylation[3]
206VSSSIVDKYIGESARubiquitination[1, 2, 4, 5, 8]
274FDTLHRVKMIMATNRubiquitination[5, 10, 11]
298RPGRLDRKIHIDLPNsumoylation[7]
298RPGRLDRKIHIDLPNubiquitination[1, 2, 10]
314QARLDILKIHAGPITubiquitination[1, 4, 9, 12]
322IHAGPITKHGEIDYEubiquitination[1, 2, 5, 9, 10, 11]
369VVQEDFMKAVRKVADubiquitination[1, 12]
383DSKKLESKLDYKPV*ubiquitination[9, 10]
Reference
 [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] 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] 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]
 [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] 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] 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]
 [7] Ebp1 sumoylation, regulated by TLS/FUS E3 ligase, is required for its anti-proliferative activity.
 Oh SM, Liu Z, Okada M, Jang SW, Liu X, Chan CB, Luo H, Ye K.
 Oncogene. 2010 Feb 18;29(7):1017-30. [PMID: 19946338]
 [8] 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]
 [9] 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]
 [10] 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]
 [11] 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]
 [12] 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] 
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. 
Sequence Annotation
 NP_BIND 174 181 ATP (Potential).
 MOD_RES 72 72 N6-acetyllysine.
 MOD_RES 206 206 N6-acetyllysine.  
Keyword
 Acetylation; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Nucleotide-binding; Nucleus; Proteasome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 389 AA 
Protein Sequence
MADPRDKALQ DYRKKLLEHK EIDGRLKELR EQLKELTKQY EKSENDLKAL QSVGQIVGEV 60
LKQLTEEKFI VKATNGPRYV VGCRRQLDKS KLKPGTRVAL DMTTLTIMRY LPREVDPLVY 120
NMSHEDPGNV SYSEIGGLSE QIRELREVIE LPLTNPELFQ RVGIIPPKGC LLYGPPGTGK 180
TLLARAVASQ LDCNFLKVVS SSIVDKYIGE SARLIREMFN YARDHQPCII FMDEIDAIGG 240
RRFSEGTSAD REIQRTLMEL LNQMDGFDTL HRVKMIMATN RPDTLDPALL RPGRLDRKIH 300
IDLPNEQARL DILKIHAGPI TKHGEIDYEA IVKLSDGFNG ADLRNVCTEA GMFAIRADHD 360
FVVQEDFMKA VRKVADSKKL ESKLDYKPV 389 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0005886; C:plasma membrane; IDA:HPA.
 GO:0022624; C:proteasome accessory complex; ISS:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0016887; F:ATPase activity; TAS:UniProtKB.
 GO:0030674; F:protein binding, bridging; NAS: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. 
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