CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012030
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 26S proteasome non-ATPase regulatory subunit 2 
Protein Synonyms/Alias
 26S proteasome regulatory subunit RPN1; 26S proteasome regulatory subunit S2; 26S proteasome subunit p97; Protein 55.11; Tumor necrosis factor type 1 receptor-associated protein 2 
Gene Name
 PSMD2 
Gene Synonyms/Alias
 TRAP2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
8MEEGGRDKAPVQPQQubiquitination[1, 2]
27APGGTDEKPSGKERRubiquitination[1, 2, 3, 4]
31TDEKPSGKERRDAGDubiquitination[1, 2, 3, 4]
39ERRDAGDKDKEQELSubiquitination[1, 2]
41RDAGDKDKEQELSEEubiquitination[1, 2]
50QELSEEDKQLQDELEubiquitination[1]
66LVERLGEKDTSLYRPubiquitination[2, 4, 5, 6, 7]
105FLRPHYGKLKEIYENubiquitination[5, 7]
107RPHYGKLKEIYENMAubiquitination[1, 2, 4]
119NMAPGENKRFAADIIubiquitination[1, 4]
141SGERECLKYRLVGSQubiquitination[4]
168HLAGEVAKEWQELDDubiquitination[1, 2, 4]
178QELDDAEKVQREPLLubiquitination[1, 2, 3, 4]
228IDENAYAKVCLYLTSubiquitination[1]
286EDIFTSCKDVVVQKQubiquitination[1, 8]
292CKDVVVQKQMAFMLGubiquitination[1, 2, 4, 6, 7]
343ELDIMEPKVPDDIYKubiquitination[1, 4]
350KVPDDIYKTHLENNRubiquitination[1, 2, 4]
397LLTDDGNKWLYKNKDubiquitination[1, 2, 3, 4, 6, 7]
441YSSEDYIKSGALLACubiquitination[1, 2, 4, 6, 7]
551EKSETELKDTYARWLubiquitination[1, 2, 4]
754QLAQYHAKDPNNLFMubiquitination[1, 2, 4, 6, 7]
773QGLTHLGKGTLTLCPubiquitination[4]
858DVVGQAGKPKTITGFubiquitination[1, 2, 3, 4]
860VGQAGKPKTITGFQTubiquitination[1, 2, 4, 5, 6, 7]
902EGFVILRKNPNYDL*ubiquitination[4]
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] 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] 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]
 [6] 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]
 [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] 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
 Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. 
Sequence Annotation
 REPEAT 409 442 PC 1.
 REPEAT 443 479 PC 2.
 REPEAT 480 514 PC 3.
 REPEAT 517 551 PC 4.
 REPEAT 560 589 PC 5.
 REPEAT 692 723 PC 6.
 REPEAT 742 757 PC 7.
 MOD_RES 1 1 N-acetylmethionine (By similarity).
 MOD_RES 16 16 Phosphoserine.
 MOD_RES 24 24 Phosphothreonine.
 MOD_RES 29 29 Phosphoserine.
 MOD_RES 194 194 Phosphotyrosine.
 MOD_RES 361 361 Phosphoserine.  
Keyword
 Acetylation; Complete proteome; Direct protein sequencing; Phosphoprotein; Polymorphism; Proteasome; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 908 AA 
Protein Sequence
MEEGGRDKAP VQPQQSPAAA PGGTDEKPSG KERRDAGDKD KEQELSEEDK QLQDELEMLV 60
ERLGEKDTSL YRPALEELRR QIRSSTTSMT SVPKPLKFLR PHYGKLKEIY ENMAPGENKR 120
FAADIISVLA MTMSGERECL KYRLVGSQEE LASWGHEYVR HLAGEVAKEW QELDDAEKVQ 180
REPLLTLVKE IVPYNMAHNA EHEACDLLME IEQVDMLEKD IDENAYAKVC LYLTSCVNYV 240
PEPENSALLR CALGVFRKFS RFPEALRLAL MLNDMELVED IFTSCKDVVV QKQMAFMLGR 300
HGVFLELSED VEEYEDLTEI MSNVQLNSNF LALARELDIM EPKVPDDIYK THLENNRFGG 360
SGSQVDSARM NLASSFVNGF VNAAFGQDKL LTDDGNKWLY KNKDHGMLSA AASLGMILLW 420
DVDGGLTQID KYLYSSEDYI KSGALLACGI VNSGVRNECD PALALLSDYV LHNSNTMRLG 480
SIFGLGLAYA GSNREDVLTL LLPVMGDSKS SMEVAGVTAL ACGMIAVGSC NGDVTSTILQ 540
TIMEKSETEL KDTYARWLPL GLGLNHLGKG EAIEAILAAL EVVSEPFRSF ANTLVDVCAY 600
AGSGNVLKVQ QLLHICSEHF DSKEKEEDKD KKEKKDKDKK EAPADMGAHQ GVAVLGIALI 660
AMGEEIGAEM ALRTFGHLLR YGEPTLRRAV PLALALISVS NPRLNILDTL SKFSHDADPE 720
VSYNSIFAMG MVGSGTNNAR LAAMLRQLAQ YHAKDPNNLF MVRLAQGLTH LGKGTLTLCP 780
YHSDRQLMSQ VAVAGLLTVL VSFLDVRNII LGKSHYVLYG LVAAMQPRML VTFDEELRPL 840
PVSVRVGQAV DVVGQAGKPK TITGFQTHTT PVLLAHGERA ELATEEFLPV TPILEGFVIL 900
RKNPNYDL 908 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0005838; C:proteasome regulatory particle; TAS:ProtInc.
 GO:0030234; F:enzyme regulator activity; IEA:InterPro.
 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:0042176; P:regulation of protein catabolic process; IEA:InterPro.
 GO:0044281; P:small molecule metabolic process; TAS:Reactome.
 GO:0016032; P:viral reproduction; TAS:Reactome. 
Interpro
 IPR016643; 26S_Psome_Rpn1.
 IPR002015; APC_proteasome.
 IPR016024; ARM-type_fold. 
Pfam
 PF01851; PC_rep 
SMART
  
PROSITE
  
PRINTS