CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009308
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ubiquitin-conjugating enzyme E2 N 
Protein Synonyms/Alias
 Bendless-like ubiquitin-conjugating enzyme; Ubc13; Ubiquitin carrier protein N; Ubiquitin-protein ligase N 
Gene Name
 Ube2n 
Gene Synonyms/Alias
 Blu 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
10GLPRRIIKETQRLLAacetylation[1]
10GLPRRIIKETQRLLAubiquitination[2]
24AEPVPGIKAEPDESNacetylation[1, 3]
24AEPVPGIKAEPDESNubiquitination[2]
68EYPMAAPKVRFMTKIubiquitination[2]
74PKVRFMTKIYHPNVDacetylation[1, 3]
74PKVRFMTKIYHPNVDubiquitination[2]
82IYHPNVDKLGRICLDacetylation[1, 3]
82IYHPNVDKLGRICLDubiquitination[2]
92RICLDILKDKWSPALubiquitination[2]
94CLDILKDKWSPALQIacetylation[1, 4]
94CLDILKDKWSPALQIsuccinylation[4]
94CLDILKDKWSPALQIubiquitination[2]
Reference
 [1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [2] 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]
 [3] 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]
 [4] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337
Functional Description
 The UBE2V1-UBE2N and UBE2V2-UBE2N heterodimers catalyze the synthesis of non-canonical 'Lys-63'-linked polyubiquitin chains. This type of polyubiquitination does not lead to protein degradation by the proteasome. Mediates transcriptional activation of target genes. Plays a role in the control of progress through the cell cycle and differentiation. Plays a role in the error-free DNA repair pathway and contributes to the survival of cells after DNA damage. Acts together with the E3 ligases, HLTF and SHPRH, in the 'Lys-63'-linked poly-ubiquitination of PCNA upon genotoxic stress, which is required for DNA repair. Appears to act together with E3 ligase RNF5 in the 'Lys-63'-linked polyubiquitination of JKAMP thereby regulating JKAMP function by decreasing its association with components of the proteasome and ERAD (By similarity). Promotes TRIM5 capsid-specific restriction activity and the UBE2V1-UBE2N heterodimer acts in concert with TRIM5 to generate 'Lys-63'-linked polyubiquitin chains which activate the MAP3K7/TAK1 complex which in turn results in the induction and expression of NF-kappa-B and MAPK-responsive inflammatory genes (By similarity). 
Sequence Annotation
 ACT_SITE 87 87 Glycyl thioester intermediate.
 MOD_RES 82 82 N6-acetyllysine (By similarity).
 CROSSLNK 92 92 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 Acetylation; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; DNA damage; DNA repair; Isopeptide bond; Ligase; Nucleotide-binding; Nucleus; Reference proteome; Ubl conjugation; Ubl conjugation pathway. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 152 AA 
Protein Sequence
MAGLPRRIIK ETQRLLAEPV PGIKAEPDES NARYFHVVIA GPQDSPFEGG TFKLELFLPE 60
EYPMAAPKVR FMTKIYHPNV DKLGRICLDI LKDKWSPALQ IRTVLLSIQA LLSAPNPDDP 120
LANDVAEQWK TNEAQAIETA RAWTRLYAMN NI 152 
Gene Ontology
 GO:0005737; C:cytoplasm; ISS:UniProtKB.
 GO:0005634; C:nucleus; ISS:UniProtKB.
 GO:0031372; C:UBC13-MMS2 complex; ISS:HGNC.
 GO:0035370; C:UBC13-UEV1A complex; ISS:UniProtKB.
 GO:0000151; C:ubiquitin ligase complex; ISS:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0043130; F:ubiquitin binding; ISS:HGNC.
 GO:0004842; F:ubiquitin-protein ligase activity; ISS:UniProtKB.
 GO:0000729; P:DNA double-strand break processing; ISS:HGNC.
 GO:0000724; P:double-strand break repair via homologous recombination; ISS:HGNC.
 GO:0016574; P:histone ubiquitination; ISS:HGNC.
 GO:0045739; P:positive regulation of DNA repair; ISS:HGNC.
 GO:0031058; P:positive regulation of histone modification; ISS:HGNC.
 GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB cascade; ISS:HGNC.
 GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:HGNC.
 GO:0051443; P:positive regulation of ubiquitin-protein ligase activity; ISS:HGNC.
 GO:0006301; P:postreplication repair; ISS:HGNC.
 GO:0070534; P:protein K63-linked ubiquitination; ISS:UniProtKB.
 GO:0033182; P:regulation of histone ubiquitination; ISS:HGNC.
 GO:0050852; P:T cell receptor signaling pathway; ISS:HGNC.
 GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:MGI. 
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