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Overview

Uniprot IDP63279
Protein NameSUMO-conjugating enzyme UBC9
Gene NameUBE2I
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
146 QNRVEYEKRVRAQAK
18 QERKAWRKDHPFGFV

Function

Accepts the ubiquitin-like proteins SUMO1, SUMO2, SUMO3, SUMO4 and SUMO1P1/SUMO5 from the UBLE1A-UBLE1B E1 complex and catalyzes their covalent attachment to other proteins with the help of an E3 ligase such as RANBP2, CBX4 and ZNF451. Can catalyze the formation of poly-SUMO chains. Necessary for sumoylation of FOXL2 and KAT5. Essential for nuclear architecture and chromosome segregation. Sumoylates p53/TP53 at 'Lys-386'. Mediates sumoylation of ERCC6 which is essential for its transcription-coupled nucleotide excision repair activity (PubMed:26620705). Sumoylates SHMT1 at 'Lys-38' or 'Lys-39' leading to RAN-dependent nuclear import of SHMT1 (PubMed:17446168). Also sumoylates TYMS and DHFR (PubMed:18067453)

Protein Sequence

10 MSGIALSRLA 20 QERKAWRKDH 30 PFGFVAVPTK 40 NPDGTMNLMN 50 WECAIPGKKG 60 TPWEGGLFKL 70 RMLFKDDYPS 80 SPPKCKFEPP 90 LFHPNVYPSG 100 TVCLSILEED 110 KDWRPAITIK 120 QILLGIQELL 130 NEPNIQDPAQ 140 AEAYTIYCQN 150 RVEYEKRVRA QAKKFAPS

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0098978 glutamatergic synapse
Cellular Component GO:0005635 nuclear envelope
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0048471 perinuclear region of cytoplasm
Cellular Component GO:0016605 PML body
Cellular Component GO:0099524 postsynaptic cytosol
Cellular Component GO:0099523 presynaptic cytosol
Cellular Component GO:0098685 Schaffer collateral - CA1 synapse
Cellular Component GO:0106068 SUMO ligase complex
Cellular Component GO:0000795 synaptonemal complex
Cellular Component GO:1990234 transferase complex
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0019899 enzyme binding
Molecular Function GO:0043398 HLH domain binding
Molecular Function GO:0071535 RING-like zinc finger domain binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0044388 small protein activating enzyme binding
Molecular Function GO:0061656 SUMO conjugating enzyme activity
Molecular Function GO:0019789 SUMO transferase activity
Molecular Function GO:0001221 transcription coregulator binding
Molecular Function GO:0008134 transcription factor binding
Biological Process GO:0051301 cell division
Biological Process GO:0007059 chromosome segregation
Biological Process GO:0051170 import into nucleus
Biological Process GO:0007084 mitotic nuclear membrane reassembly
Biological Process GO:0050804 modulation of chemical synaptic transmission
Biological Process GO:0045892 negative regulation of DNA-templated transcription
Biological Process GO:0000122 negative regulation of transcription by RNA polymerase II
Biological Process GO:0051168 nuclear export
Biological Process GO:0030335 positive regulation of cell migration
Biological Process GO:0036211 protein modification process
Biological Process GO:0016925 protein sumoylation
Biological Process GO:0006511 ubiquitin-dependent protein catabolic process

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] 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.

[3] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[4] 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.