DPP8
entrez
54878
canonical
uniprot
Q6V1X1
canonical
ensembl
ENSG00000074603
resolver
ensp
ENSP00000300141
resolver
ensp
ENSP00000318111
resolver
ensp
ENSP00000339208
resolver
ensp
ENSP00000351817
resolver
ensp
ENSP00000542803
resolver
ensp
ENSP00000542812
resolver
ensp
ENSP00000615962
resolver
ensp
ENSP00000677831
resolver
ensp
ENSP00000700401
resolver
ensp
ENSP00000782068
resolver
genesymbol
DPP8
resolver
genesymbol_syn
DPRP1
resolver
hgnc
HGNC:16490
resolver
uniprot
A8K4U2
resolver
uniprot
B4DLA8
resolver
uniprot
Q7Z4C8
resolver
uniprot
Q7Z4D3
resolver
uniprot
Q7Z4E1
resolver
uniprot
Q8IWG7
resolver
uniprot
Q8NEM5
resolver
uniprot
Q96JX1
resolver
uniprot
Q9HBM2
resolver
uniprot
Q9HBM3
resolver
uniprot
Q9HBM4
resolver
uniprot
Q9HBM5
resolver
uniprot
Q9NXF4
resolver
uniprot_entry
A8K4U2_HUMAN
resolver
uniprot_entry
B4DLA8_HUMAN
resolver
uniprot_entry
DPP8_HUMAN
resolver
uniprot_sec
Q7Z4C8
resolver
uniprot_sec
Q7Z4D3
resolver
uniprot_sec
Q7Z4E1
resolver
uniprot_sec
Q8IWG7
resolver
uniprot_sec
Q8NEM5
resolver
uniprot_sec
Q96JX1
resolver
uniprot_sec
Q9HBM2
resolver
uniprot_sec
Q9HBM3
resolver
uniprot_sec
Q9HBM4
resolver
uniprot_sec
Q9HBM5
resolver
uniprot_sec
Q9NXF4
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by zinc. Inhibited by the serine proteinase inhibitor 4-(2-aminoethyl)benzenesulphonyl fluoride (AEBSF), and by di-isopropylfluorophosphate. Specifically inhibited by isoindoline derivatives (PubMed:11012666, PubMed:12662155, PubMed:15664838). Inhibited by Val-boroPro (Talabostat, PT-100), a non-selective inhibitor, which triggers pyroptosis in monocytes and macrophages (PubMed:27820798, PubMed:29967349, PubMed:32796818). {ECO:0000250|UniProtKB:Q86TI2, ECO:0000269|PubMed:11012666, ECO:0000269|PubMed:12662155, ECO:0000269|PubMed:15664838, ECO:0000269|PubMed:27820798, ECO:0000269|PubMed:29967349, ECO:0000269|PubMed:32796818}.
uniprot
proteins
amino_acid_sequence
MWKRSEQMKIKSGKCNMAAAMETEQLGVEIFETADCEENIESQDRPKLEPFYVERYSWSQLKKLLADTRKYHGYMMAKAPHDFMFVKRNDPDGPHSDRIYYLAMSGENRENTLFYSEIPKTINRAAVLMLSWKPLLDLFQATLDYGMYSREEELLRERKRIGTVGIASYDYHQGSGTFLFQAGSGIYHVKDGGPQGFTQQPLRPNLVETSCPNIRMDPKLCPADPDWIAFIHSNDIWISNIVTREERRLTYVHNELANMEEDARSAGVATFVLQEEFDRYSGYWWCPKAETTPSGGKILRILYEENDESEVEIIHVTSPMLETRRADSFRYPKTGTANPKVTFKMSEIMIDAEGRIIDVIDKELIQPFEILFEGVEYIARAGWTPEGKYAWSILLDRSQTRLQIVLISPELFIPVEDDVMERQRLIESVPDSVTPLIIYEETTDIWINIHDIFHVFPQSHEEEIEFIFASECKTGFRHLYKITSILKESKYKRSSGGLPAPSDFKCPIKEEIAITSGEWEVLGRHGSNIQVDEVRRLVYFEGTKDSPLEHHLYVVSYVNPGEVTRLTDRGYSHSCCISQHCDFFISKYSNQKNPHCVSLYKLSSPEDDPTCKTKEFWATILDSAGPLPDYTPPEIFSFESTTGFTLYGMLYKPHDLQPGKKYPTVLFIYGGPQVQLVNNRFKGVKYFRLNTLASLGYVVVVIDNRGSCHRGLKFEGAFKYKMGQIEIDDQVEGLQYLASRYDFIDLDRVGIHGWSYGGYLSLMALMQRSDIFRVAIAGAPVTLWIFYDTGYTERYMGHPDQNEQGYYLGSVAMQAEKFPSEPNRLLLLHGFLDENVHFAHTSILLSFLVRAGKPYDLQIYPQERHSIRVPESGEHYELHLLHYLQENLGSRIAALKVI
uniprot
proteins
ec_number
3.4.14.5
uniprot
proteins
function
FUNCTION: Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2 (PubMed:11012666, PubMed:12534281, PubMed:12662155, PubMed:15039077, PubMed:15664838, PubMed:20536396, PubMed:29382749). 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:32796818). 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 DPP8, suggesting the existence of substrate(s) required for NLRP1 and CARD8 inhibition (By similarity). {ECO:0000250|UniProtKB:Q86TI2, ECO:0000269|PubMed:11012666, ECO:0000269|PubMed:12534281, ECO:0000269|PubMed:12662155, ECO:0000269|PubMed:15039077, ECO:0000269|PubMed:15664838, ECO:0000269|PubMed:20536396, ECO:0000269|PubMed:27820798, ECO:0000269|PubMed:29967349, ECO:0000269|PubMed:32796818, ECO:0000269|PubMed:33731929, ECO:0000269|PubMed:33731932, ECO:0000269|PubMed:34019797, ECO:0000305|PubMed:29382749}.
uniprot
proteins
mass_dalton
103358
uniprot
proteins
mutagenesis
MUTAGEN 275; /note="E->K: 13-fold reduction in affinity for Ala-Pro-AFC; no effect on subcellular location."; /evidence="ECO:0000269|PubMed:12534281"; MUTAGEN 451; /note="D->F: Reduced dimerization and reduced enzyme activity."; /evidence="ECO:0000269|PubMed:20536396"; MUTAGEN 755; /note="S->A: Abolishes activity; no effect on subcellular location."; /evidence="ECO:0000269|PubMed:12534281"; MUTAGEN 788; /note="D->A,S,V: Strongly reduced enzyme activity."; /evidence="ECO:0000269|PubMed:20536396"; MUTAGEN 788; /note="D->E: Loss of enzyme activity. Loss of dimerization."; /evidence="ECO:0000269|PubMed:20536396"; MUTAGEN 833; /note="D->A: Abolishes activity; no effect on subcellular location."; /evidence="ECO:0000269|PubMed:12534281"; MUTAGEN 865; /note="H->A: Abolishes activity; no effect on subcellular location."; /evidence="ECO:0000269|PubMed:12534281
uniprot
proteins
protein_family
DPPIV subfamily
uniprot
proteins
protein_family
Peptidase S9B family
uniprot
proteins
pubmed
11012666
uniprot
proteins
pubmed
12534281
uniprot
proteins
pubmed
12662155
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15039077
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15664838
uniprot
proteins
pubmed
20536396
uniprot
proteins
pubmed
27820798
uniprot
proteins
pubmed
29382749
uniprot
proteins
pubmed
29967349
uniprot
proteins
pubmed
32796818
uniprot
proteins
pubmed
33731929
uniprot
proteins
pubmed
33731932
uniprot
proteins
pubmed
34019797
uniprot
proteins
sequence_length
898
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11012666, ECO:0000269|PubMed:12534281, ECO:0000269|PubMed:12662155}.
uniprot
proteins