CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015628
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ubiquitin-conjugating enzyme E2 R2 
Protein Synonyms/Alias
 Ubiquitin carrier protein R2; Ubiquitin-conjugating enzyme E2-CDC34B; Ubiquitin-protein ligase R2 
Gene Name
 UBE2R2 
Gene Synonyms/Alias
 CDC34B; UBC3B 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
11QQMTSSQKALMLELKubiquitination[1, 2, 3, 4]
18KALMLELKSLQEEPVubiquitination[5, 6]
63GYFKAHIKFPIDYPYubiquitination[1, 2, 3, 4, 6, 7]
80PTFRFLTKMWHPNIYubiquitination[7]
157KWRDSKGKDKEYAEIubiquitination[3]
167EYAEIIRKQVSATKAubiquitination[5]
173RKQVSATKAEAEKDGubiquitination[5]
182EAEKDGVKVPTTLAEubiquitination[6]
193TLAEYCIKTKVPSNDubiquitination[2]
Reference
 [1] 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]
 [2] 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]
 [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] 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]
 [5] 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]
 [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] 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
Functional Description
 Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes monoubiquitination and 'Lys-48'-linked polyubiquitination. May be involved in degradation of katenin. 
Sequence Annotation
 ACT_SITE 93 93 Glycyl thioester intermediate.
 MOD_RES 233 233 Phosphoserine; by CK2.  
Keyword
 ATP-binding; Complete proteome; Ligase; Nucleotide-binding; Phosphoprotein; Reference proteome; Ubl conjugation pathway. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 238 AA 
Protein Sequence
MAQQQMTSSQ KALMLELKSL QEEPVEGFRI TLVDESDLYN WEVAIFGPPN TLYEGGYFKA 60
HIKFPIDYPY SPPTFRFLTK MWHPNIYENG DVCISILHPP VDDPQSGELP SERWNPTQNV 120
RTILLSVISL LNEPNTFSPA NVDASVMFRK WRDSKGKDKE YAEIIRKQVS ATKAEAEKDG 180
VKVPTTLAEY CIKTKVPSND NSSDLLYDDL YDDDIDDEDE EEEDADCYDD DDSGNEES 238 
Gene Ontology
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB.
 GO:0070936; P:protein K48-linked ubiquitination; IDA:UniProtKB.
 GO:0006513; P:protein monoubiquitination; IDA:UniProtKB. 
Interpro
 IPR000608; UBQ-conjugat_E2.
 IPR023313; UBQ-conjugating_AS.
 IPR016135; UBQ-conjugating_enzyme/RWD. 
Pfam
 PF00179; UQ_con 
SMART
  
PROSITE
 PS00183; UBIQUITIN_CONJUGAT_1
 PS50127; UBIQUITIN_CONJUGAT_2 
PRINTS