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Overview

Uniprot IDQ9GZR1
Protein NameSentrin-specific protease 6
Gene NameSENP6
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
311 KVILPGAKIPKITNL
314 LPGAKIPKITNLKER
863 SVKYSVKKINHTASE
910 HHTDGLSKIRLNYSD

Function

Protease that deconjugates SUMO1, SUMO2 and SUMO3 from targeted proteins. Processes preferentially poly-SUMO2 and poly-SUMO3 chains, but does not efficiently process SUMO1, SUMO2 and SUMO3 precursors. Deconjugates SUMO1 from RXRA, leading to transcriptional activation. Involved in chromosome alignment and spindle assembly, by regulating the kinetochore CENPH-CENPI-CENPK complex. Desumoylates PML and CENPI, protecting them from degradation by the ubiquitin ligase RNF4, which targets polysumoylated proteins for proteasomal degradation. Also desumoylates RPA1, thus preventing recruitment of RAD51 to the DNA damage foci to initiate DNA repair through homologous recombination

Protein Sequence

10 MAAGKSGGSA 20 GEITFLEALA 30 RSESKRDGGF 40 KNNWSFDHEE 50 ESEGDTDKDG 60 TNLLSVDEDE 70 DSETSKGKKL 80 NRRSEIVANS 90 SGEFILKTYV 100 RRNKSESFKT 110 LKGNPIGLNM 120 LSNNKKLSEN 130 TQNTSLCSGT 140 VVHGRRFHHA 150 HAQIPVVKTA 160 AQSSLDRKER 170 KEYPPHVQKV 180 EINPVRLSRL 190 QGVERIMKKT 200 EESESQVEPE 210 IKRKVQQKRH 220 CSTYQPTPPL 230 SPASKKCLTH 240 LEDLQRNCRQ 250 AITLNESTGP 260 LLRTSIHQNS 270 GGQKSQNTGL 280 TTKKFYGNNV 290 EKVPIDIIVN 300 CDDSKHTYLQ 310 TNGKVILPGA 320 KIPKITNLKE 330 RKTSLSDLND 340 PIILSSDDDD 350 DNDRTNRRES 360 ISPQPADSAC 370 SSPAPSTGKV 380 EAALNENTCR 390 AERELRSIPE 400 DSELNTVTLP 410 RKARMKDQFG 420 NSIINTPLKR 430 RKVFSQEPPD 440 ALALSCQSSF 450 DSVILNCRSI 460 RVGTLFRLLI 470 EPVIFCLDFI 480 KIQLDEPDHD 490 PVEIILNTSD 500 LTKCEWCNVR 510 KLPVVFLQAI 520 PAVYQKLSIQ 530 LQMNKEDKVW 540 NDCKGVNKLT 550 NLEEQYIILI 560 FQNGLDPPAN 570 MVFESIINEI 580 GIKNNISNFF 590 AKIPFEEANG 600 RLVACTRTYE 610 ESIKGSCGQK 620 ENKIKTVSFE 630 SKIQLRSKQE 640 FQFFDEEEET 650 GENHTIFIGP 660 VEKLIVYPPP 670 PAKGGISVTN 680 EDLHCLNEGE 690 FLNDVIIDFY 700 LKYLVLEKLK 710 KEDADRIHIF 720 SSFFYKRLNQ 730 RERRNHETTN 740 LSIQQKRHGR 750 VKTWTRHVDI 760 FEKDFIFVPL 770 NEAAHWFLAV 780 VCFPGLEKPK 790 YEPNPHYHEN 800 AVIQKCSTVE 810 DSCISSSASE 820 MESCSQNSSA 830 KPVIKKMLNK 840 KHCIAVIDSN 850 PGQEESDPRY 860 KRNICSVKYS 870 VKKINHTASE 880 NEEFNKGEST 890 SQKVADRTKS 900 ENGLQNESLS 910 STHHTDGLSK 920 IRLNYSDESP 930 EAGKMLEDEL 940 VDFSEDQDNQ 950 DDSSDDGFLA 960 DDNCSSEIGQ 970 WHLKPTICKQ 980 PCILLMDSLR 990 GPSRSNVVKI 1000 LREYLEVEWE 1010 VKKGSKRSFS 1020 KDVMKGSNPK 1030 VPQQNNFSDC 1040 GVYVLQYVES 1050 FFENPILSFE 1060 LPMNLANWFP 1070 PPRMRTKREE 1080 IRNIILKLQE 1090 DQSKEKRKHK 1100 DTYSTEAPLG 1110 EGTEQYVNSI SD

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
Molecular Function GO:0070139 SUMO-specific endopeptidase activity
Biological Process GO:0016926 protein desumoylation
Biological Process GO:0070646 protein modification by small protein removal
Biological Process GO:0016925 protein sumoylation
Biological Process GO:0006508 proteolysis
Biological Process GO:0090234 regulation of kinetochore assembly
Biological Process GO:0090169 regulation of spindle assembly

Reference

[1] 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.

[2] 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.