Search Results

Overview

Uniprot IDQ9UBE0
Protein NameSUMO-activating enzyme subunit 1
Gene NameSAE1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
109 LNPMVDVKVDTEDIE
183 EEKTKVAKVSQGVED
195 VEDGPDTKRAKLDSS
198 GPDTKRAKLDSSETT

Function

The heterodimer acts as an E1 ligase for SUMO1, SUMO2, SUMO3, and probably SUMO4. It mediates ATP-dependent activation of SUMO proteins followed by formation of a thioester bond between a SUMO protein and a conserved active site cysteine residue on UBA2/SAE2

Protein Sequence

10 MVEKEEAGGG 20 ISEEEAAQYD 30 RQIRLWGLEA 40 QKRLRASRVL 50 LVGLKGLGAE 60 IAKNLILAGV 70 KGLTMLDHEQ 80 VTPEDPGAQF 90 LIRTGSVGRN 100 RAEASLERAQ 110 NLNPMVDVKV 120 DTEDIEKKPE 130 SFFTQFDAVC 140 LTCCSRDVIV 150 KVDQICHKNS 160 IKFFTGDVFG 170 YHGYTFANLG 180 EHEFVEEKTK 190 VAKVSQGVED 200 GPDTKRAKLD 210 SSETTMVKKK 220 VVFCPVKEAL 230 EVDWSSEKAK 240 AALKRTTSDY 250 FLLQVLLKFR 260 TDKGRDPSSD 270 TYEEDSELLL 280 QIRNDVLDSL 290 GISPDLLPED 300 FVRYCFSEMA 310 PVCAVVGGIL 320 AQEIVKALSQ 330 RDPPHNNFFF 340 FDGMKGNGIV ECLGPK

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0031510 SUMO activating enzyme complex
Molecular Function GO:0043008 ATP-dependent protein binding
Molecular Function GO:0008047 enzyme activator activity
Molecular Function GO:0046982 protein heterodimerization activity
Molecular Function GO:0044388 small protein activating enzyme binding
Molecular Function GO:0019948 SUMO activating enzyme activity
Molecular Function GO:0004839 ubiquitin activating enzyme activity
Biological Process GO:0033235 positive regulation of protein sumoylation
Biological Process GO:1903955 positive regulation of protein targeting to mitochondrion
Biological Process GO:0016925 protein sumoylation

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] 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.

[3] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[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] 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.

[6] Chao L, Xu Y, Yang Y, Ao X, Liang J. Identification of lactylation-related biomarkers for diagnosis, prognosis, and treatment responsiveness in triple-negative breast cancer.. World J Surg Oncol 24(1):77. 2026 Jan 22. PMID: 41566505.

[7] 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.