CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000091
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 26S proteasome non-ATPase regulatory subunit 14 
Protein Synonyms/Alias
 26S proteasome regulatory subunit RPN11; 26S proteasome-associated PAD1 homolog 1 
Gene Name
 PSMD14 
Gene Synonyms/Alias
 POH1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
43LALLKMLKHGRAGVPubiquitination[1]
94VDPVFQAKMLDMLKQubiquitination[1, 2]
152VDPIQSVKGKVVIDAubiquitination[1, 2, 3, 4, 5, 6]
154PIQSVKGKVVIDAFRubiquitination[1, 2, 3, 5, 7, 8, 9]
186SNLGHLNKPSIQALIubiquitination[1, 3, 8, 9]
209SITINYRKNELEQKMubiquitination[1]
215RKNELEQKMLLNLHKubiquitination[1, 3]
222KMLLNLHKKSWMEGLubiquitination[1, 8]
223MLLNLHKKSWMEGLTubiquitination[3, 8, 9]
239QDYSEHCKHNESVVKacetylation[10]
239QDYSEHCKHNESVVKubiquitination[3, 8]
246KHNESVVKEMLELAKacetylation[10]
246KHNESVVKEMLELAKubiquitination[1, 2, 3, 6, 8, 9]
253KEMLELAKNYNKAVEubiquitination[1, 2, 3, 7, 8]
257ELAKNYNKAVEEEDKubiquitination[1, 2, 3, 5, 6, 7, 8, 9]
264KAVEEEDKMTPEQLAubiquitination[1, 8, 9]
273TPEQLAIKNVGKQDPubiquitination[1, 2, 3, 6, 8, 9, 11]
277LAIKNVGKQDPKRHLubiquitination[1, 2, 8]
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] 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] 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] 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]
 [5] 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]
 [6] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] Monoclonal antibody cocktail as an enrichment tool for acetylome analysis.
 Shaw PG, Chaerkady R, Zhang Z, Davidson NE, Pandey A.
 Anal Chem. 2011 May 15;83(10):3623-6. [PMID: 21466224]
 [11] 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] 
Functional Description
 Metalloprotease component of the 26S proteasome that specifically cleaves 'Lys-63'-linked polyubiquitin chains. The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. Plays a role in response to double-strand breaks (DSBs): acts as a regulator of non-homologous end joining (NHEJ) by cleaving 'Lys-63'-linked polyubiquitin, thereby promoting retention of JMJD2A/KDM4A on chromatin and restricting TP53BP1 accumulation. Also involved in homologous recombination repair by promoting RAD51 loading. 
Sequence Annotation
 DOMAIN 26 139 MPN.
 MOTIF 113 126 JAMM motif.
 METAL 113 113 Zinc; catalytic (Probable).
 METAL 115 115 Zinc; catalytic (Probable).
 METAL 126 126 Zinc; catalytic (By similarity).
 MOD_RES 150 150 Phosphoserine.
 MOD_RES 224 224 Phosphoserine.  
Keyword
 Complete proteome; Direct protein sequencing; DNA damage; DNA repair; Hydrolase; Metal-binding; Metalloprotease; Phosphoprotein; Protease; Proteasome; Reference proteome; Ubl conjugation pathway; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 310 AA 
Protein Sequence
MDRLLRLGGG MPGLGQGPPT DAPAVDTAEQ VYISSLALLK MLKHGRAGVP MEVMGLMLGE 60
FVDDYTVRVI DVFAMPQSGT GVSVEAVDPV FQAKMLDMLK QTGRPEMVVG WYHSHPGFGC 120
WLSGVDINTQ QSFEALSERA VAVVVDPIQS VKGKVVIDAF RLINANMMVL GHEPRQTTSN 180
LGHLNKPSIQ ALIHGLNRHY YSITINYRKN ELEQKMLLNL HKKSWMEGLT LQDYSEHCKH 240
NESVVKEMLE LAKNYNKAVE EEDKMTPEQL AIKNVGKQDP KRHLEEHVDV LMTSNIVQCL 300
AAMLDTVVFK 310 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0008541; C:proteasome regulatory particle, lid subcomplex; IMP:UniProtKB.
 GO:0061133; F:endopeptidase activator activity; IMP:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0008237; F:metallopeptidase activity; TAS:UniProtKB.
 GO:0070628; F:proteasome binding; IDA:UniProtKB.
 GO:0004221; F:ubiquitin thiolesterase activity; IMP: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:0000724; P:double-strand break repair via homologous recombination; IMP:UniProtKB.
 GO:0006303; P:double-strand break repair via nonhomologous end joining; IMP:UniProtKB.
 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:0070536; P:protein K63-linked deubiquitination; IMP:UniProtKB.
 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:0061136; P:regulation of proteasomal protein catabolic process; IMP:UniProtKB.
 GO:0044281; P:small molecule metabolic process; TAS:Reactome.
 GO:0016032; P:viral reproduction; TAS:Reactome. 
Interpro
 IPR000555; JAB1_Mov34_MPN_PAD1.
 IPR024969; Rpn11/EIF3F_C. 
Pfam
 PF01398; JAB
 PF13012; MitMem_reg 
SMART
 SM00232; JAB_MPN 
PROSITE
  
PRINTS