CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-037187
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 26S proteasome non-ATPase regulatory subunit 2 
Protein Synonyms/Alias
  
Gene Name
 PSMD2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
38HLAGEVAKEWQELDDubiquitination[1, 2, 3, 4]
48QELDDAEKVQREPLLubiquitination[1, 3, 4, 5, 6]
98IDENAYAKVCLYLTSubiquitination[1]
156EDIFTSCKDVVVQKQubiquitination[1, 2]
162CKDVVVQKQMAFMLGubiquitination[1, 2, 3, 4, 6, 7]
213ELDIMEPKVPDDIYKubiquitination[1, 3]
220KVPDDIYKTHLENNRacetylation[6, 8]
220KVPDDIYKTHLENNRubiquitination[1, 2, 3, 4, 6]
267LLTDDGNKWLYKNKDacetylation[8]
267LLTDDGNKWLYKNKDubiquitination[1, 3, 4, 5, 6, 7]
311YSSEDYIKSGALLACubiquitination[1, 2, 3, 4, 6, 7]
421EKSETELKDTYARWLubiquitination[1, 2, 3, 4, 6]
624QLAQYHAKDPNNLFMubiquitination[1, 2, 3, 4, 6, 7]
643QGLTHLGKGTLTLCPubiquitination[3, 6]
728DVVGQAGKPKTITGFubiquitination[1, 2, 3, 4, 5, 6, 9]
730VGQAGKPKTITGFQTubiquitination[1, 2, 3, 4, 6, 7, 10]
772EGFVILRKNPNYDL*ubiquitination[3, 6]
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] 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]
 [3] 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]
 [4] 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]
 [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] 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]
 [7] 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]
 [8] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [9] A data set of human endogenous protein ubiquitination sites.
 Shi Y, Chan DW, Jung SY, Malovannaya A, Wang Y, Qin J.
 Mol Cell Proteomics. 2011 May;10(5):M110.002089. [PMID: 20972266]
 [10] 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] 
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 778 AA 
Protein Sequence
MTMSGERECL KYRLVGSQEE LASWGHEYVR HLAGEVAKEW QELDDAEKVQ REPLLTLVKE 60
IVPYNMAHNA EHEACDLLME IEQVDMLEKD IDENAYAKVC LYLTSCVNYV PEPENSALLR 120
CALGVFRKFS RFPEALRLAL MLNDMELVED IFTSCKDVVV QKQMAFMLGR HGVFLELSED 180
VEEYEDLTEI MSNVQLNSNF LALARELDIM EPKVPDDIYK THLENNRFGG SGSQVDSARM 240
NLASSFVNGF VNAAFGQDKL LTDDGNKWLY KNKDHGMLSA AASLGMILLW DVDGGLTQID 300
KYLYSSEDYI KSGALLACGI VNSGVRNECD PALALLSDYV LHNSNTMRLG SIFGLGLAYA 360
GSNREDVLTL LLPVMGDSKS SMEVAGVTAL ACGMIAVGSC NGDVTSTILQ TIMEKSETEL 420
KDTYARWLPL GLGLNHLGKG EAIEAILAAL EVVSEPFRSF ANTLVDVCAY AGSGNVLKVQ 480
QLLHICSEHF DSKEKEEDKD KKEKKDKDKK EAPADMGAHQ GVAVLGIALI AMGEEIGAEM 540
ALRTFGHLLR YGEPTLRRAV PLALALISVS NPRLNILDTL SKFSHDADPE VSYNSIFAMG 600
MVGSGTNNAR LAAMLRQLAQ YHAKDPNNLF MVRLAQGLTH LGKGTLTLCP YHSDRQLMSQ 660
VAVAGLLTVL VSFLDVRNII LGKSHYVLYG LVAAMQPRML VTFDEELRPL PVSVRVGQAV 720
DVVGQAGKPK TITGFQTHTT PVLLAHGERA ELATEEFLPV TPILEGFVIL RKNPNYDL 778 
Gene Ontology
 GO:0022624; C:proteasome accessory complex; IEA:Compara.
 GO:0030234; F:enzyme regulator activity; IEA:InterPro.
 GO:0050790; P:regulation of catalytic activity; IEA:GOC.
 GO:0042176; P:regulation of protein catabolic process; IEA:InterPro. 
Interpro
 IPR016643; 26S_Psome_Rpn1.
 IPR002015; APC_proteasome.
 IPR016024; ARM-type_fold. 
Pfam
 PF01851; PC_rep 
SMART
  
PROSITE
  
PRINTS