Search Results

Overview

Uniprot IDQ86TI2
Protein NameDipeptidyl peptidase 9
Gene NameDPP9
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
97 EIPKKVRKEALLLLS

Function

Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2 (PubMed:12662155, PubMed:16475979, PubMed:19667070, PubMed:29382749, PubMed:30291141, PubMed:33731929, PubMed:36112693). Acts as a key inhibitor of caspase-1-dependent monocyte and macrophage pyroptosis in resting cells by preventing activation of NLRP1 and CARD8 (PubMed:27820798, PubMed:29967349, PubMed:30291141, PubMed:31525884, PubMed:32796818, PubMed:36112693, PubMed:36357533). Sequesters the cleaved C-terminal part of NLRP1 and CARD8, which respectively constitute the active part of the NLRP1 and CARD8 inflammasomes, in a ternary complex, thereby preventing their oligomerization and activation (PubMed:33731929, PubMed:33731932, PubMed:34019797). The dipeptidyl peptidase activity is required to suppress NLRP1 and CARD8; however, neither NLRP1 nor CARD8 are bona fide substrates of DPP9, suggesting the existence of substrate(s) required for NLRP1 and CARD8 inhibition (PubMed:33731929)

Protein Sequence

10 MATTGTPTAD 20 RGDAAATDDP 30 AARFQVQKHS 40 WDGLRSIIHG 50 SRKYSGLIVN 60 KAPHDFQFVQ 70 KTDESGPHSH 80 RLYYLGMPYG 90 SRENSLLYSE 100 IPKKVRKEAL 110 LLLSWKQMLD 120 HFQATPHHGV 130 YSREEELLRE 140 RKRLGVFGIT 150 SYDFHSESGL 160 FLFQASNSLF 170 HCRDGGKNGF 180 MVSPMKPLEI 190 KTQCSGPRMD 200 PKICPADPAF 210 FSFINNSDLW 220 VANIETGEER 230 RLTFCHQGLS 240 NVLDDPKSAG 250 VATFVIQEEF 260 DRFTGYWWCP 270 TASWEGSEGL 280 KTLRILYEEV 290 DESEVEVIHV 300 PSPALEERKT 310 DSYRYPRTGS 320 KNPKIALKLA 330 EFQTDSQGKI 340 VSTQEKELVQ 350 PFSSLFPKVE 360 YIARAGWTRD 370 GKYAWAMFLD 380 RPQQWLQLVL 390 LPPALFIPST 400 ENEEQRLASA 410 RAVPRNVQPY 420 VVYEEVTNVW 430 INVHDIFYPF 440 PQSEGEDELC 450 FLRANECKTG 460 FCHLYKVTAV 470 LKSQGYDWSE 480 PFSPGEDEFK 490 CPIKEEIALT 500 SGEWEVLARH 510 GSKIWVNEET 520 KLVYFQGTKD 530 TPLEHHLYVV 540 SYEAAGEIVR 550 LTTPGFSHSC 560 SMSQNFDMFV 570 SHYSSVSTPP 580 CVHVYKLSGP 590 DDDPLHKQPR 600 FWASMMEAAS 610 CPPDYVPPEI 620 FHFHTRSDVR 630 LYGMIYKPHA 640 LQPGKKHPTV 650 LFVYGGPQVQ 660 LVNNSFKGIK 670 YLRLNTLASL 680 GYAVVVIDGR 690 GSCQRGLRFE 700 GALKNQMGQV 710 EIEDQVEGLQ 720 FVAEKYGFID 730 LSRVAIHGWS 740 YGGFLSLMGL 750 IHKPQVFKVA 760 IAGAPVTVWM 770 AYDTGYTERY 780 MDVPENNQHG 790 YEAGSVALHV 800 EKLPNEPNRL 810 LILHGFLDEN 820 VHFFHTNFLV 830 SQLIRAGKPY 840 QLQIYPNERH 850 SIRCPESGEH 860 YEVTLLHFLQ EYL

Gene Ontology

Classification GO ID Description
Molecular Function GO:0008239 dipeptidyl-peptidase activity
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0008236 serine-type peptidase activity
Biological Process GO:0043069 negative regulation of programmed cell death
Biological Process GO:0006508 proteolysis
Biological Process GO:0070269 pyroptotic inflammatory response
Cellular Component GO:0031252 cell leading edge
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005874 microtubule
Cellular Component GO:0005634 nucleus
Molecular Function GO:0004177 aminopeptidase activity

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] 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] 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.

[4] 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.