Search Results

Overview

Uniprot IDQ9H4L4
Protein NameSentrin-specific protease 3
Gene NameSENP3
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
43 PPPKPRLKSGGGFGP

Function

Protease that releases SUMO2 and SUMO3 monomers from sumoylated substrates, but has only weak activity against SUMO1 conjugates (PubMed:16608850, PubMed:32832608, PubMed:36050397). Deconjugates SUMO2 from MEF2D, which increases its transcriptional activation capability (PubMed:15743823). Deconjugates SUMO2 and SUMO3 from CDCA8 (PubMed:18946085). Redox sensor that, when redistributed into nucleoplasm, can act as an effector to enhance HIF1A transcriptional activity by desumoylating EP300 (PubMed:19680224). Required for rRNA processing through deconjugation of SUMO2 and SUMO3 from nucleophosmin, NPM1 (PubMed:19015314). Plays a role in the regulation of sumoylation status of ZNF148 (PubMed:18259216). Functions as a component of the Five Friends of Methylated CHTOP (5FMC) complex; the 5FMC complex is recruited to ZNF148 by methylated CHTOP, leading to desumoylation of ZNF148 and subsequent transactivation of ZNF148 target genes (PubMed:22872859). Deconjugates SUMO2 from KAT5 (PubMed:32832608). Catalyzes desumoylation of MRE11 (PubMed:36050397)

Protein Sequence

10 MKETIQGTGS 20 WGPEPPGPGI 30 PPAYSSPRRE 40 RLRWPPPPKP 50 RLKSGGGFGP 60 DPGSGTTVPA 70 RRLPVPRPSF 80 DASASEEEEE 90 EEEEEDEDEE 100 EEVAAWRLPP 110 RWSQLGTSQR 120 PRPSRPTHRK 130 TCSQRRRRAM 140 RAFRMLLYSK 150 STSLTFHWKL 160 WGRHRGRRRG 170 LAHPKNHLSP 180 QQGGATPQVP 190 SPCCRFDSPR 200 GPPPPRLGLL 210 GALMAEDGVR 220 GSPPVPSGPP 230 MEEDGLRWTP 240 KSPLDPDSGL 250 LSCTLPNGFG 260 GQSGPEGERS 270 LAPPDASILI 280 SNVCSIGDHV 290 AQELFQGSDL 300 GMAEEAERPG 310 EKAGQHSPLR 320 EEHVTCVQSI 330 LDEFLQTYGS 340 LIPLSTDEVV 350 EKLEDIFQQE 360 FSTPSRKGLV 370 LQLIQSYQRM 380 PGNAMVRGFR 390 VAYKRHVLTM 400 DDLGTLYGQN 410 WLNDQVMNMY 420 GDLVMDTVPE 430 KVHFFNSFFY 440 DKLRTKGYDG 450 VKRWTKNVDI 460 FNKELLLIPI 470 HLEVHWSLIS 480 VDVRRRTITY 490 FDSQRTLNRR 500 CPKHIAKYLQ 510 AEAVKKDRLD 520 FHQGWKGYFK 530 MNVARQNNDS 540 DCGAFVLQYC 550 KHLALSQPFS 560 FTQQDMPKLR 570 RQIYKELCHC KLTV

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0071339 MLL1 complex
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Molecular Function GO:0004843 cysteine-type deubiquitinase activity
Molecular Function GO:0008234 cysteine-type peptidase activity
Molecular Function GO:0016929 deSUMOylase activity
Biological Process GO:0000448 cleavage in ITS2 between 5.8S rRNA and LSU-rRNA of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
Biological Process GO:2000042 negative regulation of double-strand break repair via homologous recombination
Biological Process GO:0016926 protein desumoylation
Biological Process GO:0006508 proteolysis

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] 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.

[3] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.

[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.