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Overview

Uniprot IDQ13404
Protein NameUbiquitin-conjugating enzyme E2 variant 1
Gene NameUBE2V1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
10 ATTGSGVKVPRNFRL
131 LRRLMMSKENMKLPQ
68 ENRIYSLKIECGPKY
74 LKIECGPKYPEAPPF

Function

Has no ubiquitin ligase activity on its own. The UBE2V1-UBE2N heterodimer catalyzes the synthesis of non-canonical poly-ubiquitin chains that are linked through Lys-63. This type of poly-ubiquitination activates IKK and does not seem to involve protein degradation by the proteasome. Plays a role in the activation of NF-kappa-B mediated by IL1B, TNF, TRAF6 and TRAF2. 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. 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. Together with RNF135 and UBE2N, catalyzes the viral RNA-dependent 'Lys-63'-linked polyubiquitination of RIGI to activate the downstream signaling pathway that leads to interferon beta production (PubMed:31006531). UBE2V1-UBE2N together with TRAF3IP2 E3 ubiquitin ligase mediate 'Lys-63'-linked polyubiquitination of TRAF6, a component of IL17A-mediated signaling pathway

Protein Sequence

10 MAATTGSGVK 20 VPRNFRLLEE 30 LEEGQKGVGD 40 GTVSWGLEDD 50 EDMTLTRWTG 60 MIIGPPRTIY 70 ENRIYSLKIE 80 CGPKYPEAPP 90 FVRFVTKINM 100 NGVNSSNGVV 110 DPRAISVLAK 120 WQNSYSIKVV 130 LQELRRLMMS 140 KENMKLPQPP EGQCYSN

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0032991 protein-containing complex
Cellular Component GO:0031372 UBC13-MMS2 complex
Cellular Component GO:0031371 ubiquitin conjugating enzyme complex
Cellular Component GO:0000151 ubiquitin ligase complex
Molecular Function GO:0061631 ubiquitin conjugating enzyme activity
Molecular Function GO:0031624 ubiquitin conjugating enzyme binding
Biological Process GO:0030154 cell differentiation
Biological Process GO:0006301 DNA damage tolerance
Biological Process GO:0043123 positive regulation of canonical NF-kappaB signal transduction
Biological Process GO:0045893 positive regulation of DNA-templated transcription
Biological Process GO:1902533 positive regulation of intracellular signal transduction
Biological Process GO:1902523 positive regulation of protein K63-linked ubiquitination
Biological Process GO:0070534 protein K63-linked ubiquitination
Biological Process GO:0000209 protein polyubiquitination
Biological Process GO:0006282 regulation of DNA repair
Biological Process GO:0006355 regulation of DNA-templated transcription

Reference

[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[2] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[3] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.

[4] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.

[5] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.