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Protein

Dipeptidyl peptidase 4

Gene

DPP4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Cell surface glycoprotein receptor involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Acts as a positive regulator of T-cell coactivation, by binding at least ADA, CAV1, IGF2R, and PTPRC. Its binding to CAV1 and CARD11 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. Its interaction with ADA also regulates lymphocyte-epithelial cell adhesion. In association with FAP is involved in the pericellular proteolysis of the extracellular matrix (ECM), the migration and invasion of endothelial cells into the ECM. May be involved in the promotion of lymphatic endothelial cells adhesion, migration and tube formation. When overexpressed, enhanced cell proliferation, a process inhibited by GPC3. Acts also as a serine exopeptidase with a dipeptidyl peptidase activity that regulates various physiological processes by cleaving peptides in the circulation, including many chemokines, mitogenic growth factors, neuropeptides and peptide hormones. Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline.10 Publications

Miscellaneous

Level of plasma concentrations of the soluble form (SDPP) can be managed as a colon carcinoma diagnostic and prognostic marker.

Catalytic activityi

Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline.PROSITE-ProRule annotation1 Publication

Activity regulationi

Inhibited by GPC3 and diprotin A.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei630Charge relay systemPROSITE-ProRule annotation1
Active sitei708Charge relay systemPROSITE-ProRule annotation1
Active sitei740Charge relay systemPROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAminopeptidase, Hydrolase, Protease, Receptor, Serine protease
Biological processCell adhesion

Enzyme and pathway databases

BRENDAi3.4.14.5 2681
ReactomeiR-HSA-381771 Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1)
R-HSA-400511 Synthesis, secretion, and inactivation of Glucose-dependent Insulinotropic Polypeptide (GIP)
SABIO-RKiP27487
SIGNORiP27487

Protein family/group databases

ESTHERihuman-DPP4 DPP4N_Peptidase_S9
MEROPSiS09.003
MoonProtiP27487

Names & Taxonomyi

Protein namesi
Recommended name:
Dipeptidyl peptidase 4 (EC:3.4.14.51 Publication)
Alternative name(s):
ADABP
Adenosine deaminase complexing protein 2
Short name:
ADCP-2
Dipeptidyl peptidase IV
Short name:
DPP IV
T-cell activation antigen CD26
TP103
CD_antigen: CD26
Cleaved into the following 2 chains:
Alternative name(s):
Dipeptidyl peptidase IV membrane form
Alternative name(s):
Dipeptidyl peptidase IV soluble form
Gene namesi
Name:DPP4
Synonyms:ADCP2, CD26
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

EuPathDBiHostDB:ENSG00000197635.9
HGNCiHGNC:3009 DPP4
MIMi102720 gene
neXtProtiNX_P27487

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 6CytoplasmicSequence analysis6
Transmembranei7 – 28Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST22
Topological domaini29 – 766ExtracellularSequence analysisAdd BLAST738

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Membrane, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi85N → A: Does not inhibit dipeptidyl peptidase activity, interaction with ADA and homodimer formation. 1 Publication1
Mutagenesisi92N → A: Does not inhibit dipeptidyl peptidase activity, interaction with ADA and homodimer formation. 1 Publication1
Mutagenesisi150N → A: Does not inhibit dipeptidyl peptidase activity, interaction with ADA and homodimer formation. 1 Publication1
Mutagenesisi205E → K: Inhibits dipeptidyl peptidase activity. 1 Publication1
Mutagenesisi206E → L: Inhibits dipeptidyl peptidase activity. 1 Publication1
Mutagenesisi219N → A: Does not inhibit dipeptidyl peptidase activity, interaction with ADA and homodimer formation. 1 Publication1
Mutagenesisi229N → A: Does not inhibit dipeptidyl peptidase activity, interaction with ADA and homodimer formation. 1 Publication1
Mutagenesisi281N → A: Does not inhibit dipeptidyl peptidase activity, interaction with ADA and homodimer formation. 1 Publication1
Mutagenesisi321N → A: Does not inhibit dipeptidyl peptidase activity, interaction with ADA and homodimer formation. 1 Publication1
Mutagenesisi520N → A: Does not inhibit dipeptidyl peptidase activity, interaction with ADA and homodimer formation. 1 Publication1
Mutagenesisi685N → A: Does not inhibit dipeptidyl peptidase activity, interaction with ADA and homodimer formation. 1 Publication1
Mutagenesisi750H → A: Inhibits weakly homodimerization and dipeptidyl peptidase activity. 2 Publications1
Mutagenesisi750H → E: Inhibits strongly homodimerization, dipeptidyl peptidase activity, interaction with CARD11 and T-cell costimulation activity. 2 Publications1

Organism-specific databases

DisGeNETi1803
OpenTargetsiENSG00000197635
PharmGKBiPA27467

Chemistry databases

ChEMBLiCHEMBL284
DrugBankiDB07482 (2R)-N-[(2R)-2-(DIHYDROXYBORYL)-1-L-PROLYLPYRROLIDIN-2-YL]-N-[(5R)-5-(DIHYDROXYBORYL)-1-L-PROLYLPYRROLIDIN-2-YL]-L-PROLINAMIDE
DB03253 (2s)-Pyrrolidin-2-Ylmethylamine
DB04577 1-(1-phenylcyclopentyl)methylamine
DB08024 1-[2-(S)-AMINO-3-BIPHENYL-4-YL-PROPIONYL]-PYRROLIDINE-2-(S)-CARBONITRILE
DB07412 1-biphenyl-2-ylmethanamine
DB08588 2-({2-[(3R)-3-AMINOPIPERIDIN-1-YL]-4-OXOQUINAZOLIN-3(4H)-YL}METHYL)BENZONITRILE
DB01884 2-Amino-3-Methyl-1-Pyrrolidin-1-Yl-Butan-1-One
DB08672 4-[(3R)-3-{[2-(4-FLUOROPHENYL)-2-OXOETHYL]AMINO}BUTYL]BENZAMIDE
DB03660 4-Iodo-L-phenylalanine
DB07239 7-(aminomethyl)-6-(2-chlorophenyl)-1-methyl-1H-benzimidazole-5-carbonitrile
DB06203 Alogliptin
DB01076 Atorvastatin
DB04491 Diisopropylphosphono Group
DB06127 KRP-104
DB08882 Linagliptin
DB06655 Liraglutide
DB07779 N-({(2S)-1-[(3R)-3-AMINO-4-(2-FLUOROPHENYL)BUTANOYL]PYRROLIDIN-2-YL}METHYL)BENZAMIDE
DB08429 N-({(2S)-1-[(3R)-3-amino-4-(3-chlorophenyl)butanoyl]pyrrolidin-2-yl}methyl)-3-(methylsulfonyl)benzamide
DB05065 PHX1149
DB05001 PSN9301
DB06335 Saxagliptin
DB01261 Sitagliptin
DB04876 Vildagliptin
GuidetoPHARMACOLOGYi1612

Polymorphism and mutation databases

BioMutaiDPP4
DMDMi1352311

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000272131 – 766Dipeptidyl peptidase 4 membrane formAdd BLAST766
ChainiPRO_000002721439 – 766Dipeptidyl peptidase 4 soluble formAdd BLAST728

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi85N-linked (GlcNAc...) asparagine4 Publications1
Glycosylationi92N-linked (GlcNAc...) asparagine2 Publications1
Glycosylationi150N-linked (GlcNAc...) asparagine4 Publications1
Glycosylationi219N-linked (GlcNAc...) asparagine3 Publications1
Glycosylationi229N-linked (GlcNAc...) asparagine4 Publications1
Glycosylationi281N-linked (GlcNAc...) asparagine3 Publications1
Glycosylationi321N-linked (GlcNAc...) asparagine2 Publications1
Disulfide bondi328 ↔ 339
Disulfide bondi385 ↔ 394
Disulfide bondi444 ↔ 447
Disulfide bondi454 ↔ 472
Glycosylationi520N-linked (GlcNAc...) asparagine4 Publications1
Disulfide bondi649 ↔ 762
Glycosylationi685N-linked (GlcNAc...) asparagine2 Publications1

Post-translational modificationi

The soluble form (Dipeptidyl peptidase 4 soluble form also named SDPP) derives from the membrane form (Dipeptidyl peptidase 4 membrane form also named MDPP) by proteolytic processing.
N- and O-Glycosylated.8 Publications
Phosphorylated. Mannose 6-phosphate residues in the carbohydrate moiety are necessary for interaction with IGF2R in activated T-cells. Mannose 6-phosphorylation is induced during T-cell activation.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP27487
PaxDbiP27487
PeptideAtlasiP27487
PRIDEiP27487
ProteomicsDBi54396

PTM databases

GlyConnecti1177
iPTMnetiP27487
PhosphoSitePlusiP27487

Expressioni

Tissue specificityi

Expressed specifically in lymphatic vessels but not in blood vessels in the skin, small intestine, esophagus, ovary, breast and prostate glands. Not detected in lymphatic vessels in the lung, kidney, uterus, liver and stomach (at protein level). Expressed in the poorly differentiated crypt cells of the small intestine as well as in the mature villous cells. Expressed at very low levels in the colon.2 Publications

Inductioni

Up-regulated by IL12/interleukin-12 on activated T-cells. IL12-activated cells expressed enhanced levels of DPP4 but not mRNAs. Down-regulated by TNF. Up-regulated in migratory endothelial cells and in the invasive endothelial cells in tumors. Induced by hypoxia (PubMed:16670267).5 Publications

Gene expression databases

BgeeiENSG00000197635 Expressed in 171 organ(s), highest expression level in tendon of biceps brachii
CleanExiHS_DPP4
ExpressionAtlasiP27487 baseline and differential
GenevisibleiP27487 HS

Organism-specific databases

HPAiCAB045970

Interactioni

Subunit structurei

Monomer. Homodimer (PubMed:12832764, PubMed:15448155, PubMed:17287217, PubMed:12646248, PubMed:12483204, PubMed:12906826). Heterodimer with Seprase (FAP) (PubMed:16651416). Requires homodimerization for optimal dipeptidyl peptidase activity and T-cell costimulation. Found in a membrane raft complex, at least composed of BCL10, CARD11, DPP4 and IKBKB (PubMed:17287217). Associates with collagen (PubMed:8526932). Interacts with PTPRC; the interaction is enhanced in a interleukin-12-dependent manner in activated lymphocytes (PubMed:12676959). Interacts (via extracellular domain) with ADA; does not inhibit its dipeptidyl peptidase activity (PubMed:15016824, PubMed:10951221, PubMed:14691230, PubMed:7907293, PubMed:8101391). Interacts with CAV1 (via the N-terminus); the interaction is direct (PubMed:17287217). Interacts (via cytoplasmic tail) with CARD11 (via PDZ domain); its homodimerization is necessary for interaction with CARD11 (PubMed:17287217). Interacts with IGF2R; the interaction is direct (PubMed:10900005). Interacts with GPC3 (PubMed:17549790). Interacts with human coronavirus-EMC spike protein and acts as a receptor for this virus (PubMed:23486063).17 Publications

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi108137, 8 interactors
DIPiDIP-351N
IntActiP27487, 23 interactors
MINTiP27487
STRINGi9606.ENSP00000353731

Chemistry databases

BindingDBiP27487

Structurei

Secondary structure

1766
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP27487
SMRiP27487
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27487

Family & Domainsi

Domaini

The extracellular cysteine-rich region is necessary for association with collagen, dimer formation and optimal dipeptidyl peptidase activity.

Sequence similaritiesi

Belongs to the peptidase S9B family. DPPIV subfamily.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2100 Eukaryota
COG1506 LUCA
GeneTreeiENSGT00760000119233
HOGENOMiHOG000231875
HOVERGENiHBG005527
InParanoidiP27487
KOiK01278
OMAiQFILLEY
OrthoDBiEOG091G0BU5
PhylomeDBiP27487
TreeFamiTF313309

Family and domain databases

Gene3Di2.140.10.30, 1 hit
3.40.50.1820, 1 hit
InterProiView protein in InterPro
IPR029058 AB_hydrolase
IPR002471 Pept_S9_AS
IPR001375 Peptidase_S9
IPR002469 Peptidase_S9B_N
IPR038554 Peptidase_S9B_N_sf
PfamiView protein in Pfam
PF00930 DPPIV_N, 1 hit
PF00326 Peptidase_S9, 1 hit
SUPFAMiSSF53474 SSF53474, 1 hit
PROSITEiView protein in PROSITE
PS00708 PRO_ENDOPEP_SER, 1 hit

Sequence (1+)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All

P27487-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKTPWKVLLG LLGAAALVTI ITVPVVLLNK GTDDATADSR KTYTLTDYLK
60 70 80 90 100
NTYRLKLYSL RWISDHEYLY KQENNILVFN AEYGNSSVFL ENSTFDEFGH
110 120 130 140 150
SINDYSISPD GQFILLEYNY VKQWRHSYTA SYDIYDLNKR QLITEERIPN
160 170 180 190 200
NTQWVTWSPV GHKLAYVWNN DIYVKIEPNL PSYRITWTGK EDIIYNGITD
210 220 230 240 250
WVYEEEVFSA YSALWWSPNG TFLAYAQFND TEVPLIEYSF YSDESLQYPK
260 270 280 290 300
TVRVPYPKAG AVNPTVKFFV VNTDSLSSVT NATSIQITAP ASMLIGDHYL
310 320 330 340 350
CDVTWATQER ISLQWLRRIQ NYSVMDICDY DESSGRWNCL VARQHIEMST
360 370 380 390 400
TGWVGRFRPS EPHFTLDGNS FYKIISNEEG YRHICYFQID KKDCTFITKG
410 420 430 440 450
TWEVIGIEAL TSDYLYYISN EYKGMPGGRN LYKIQLSDYT KVTCLSCELN
460 470 480 490 500
PERCQYYSVS FSKEAKYYQL RCSGPGLPLY TLHSSVNDKG LRVLEDNSAL
510 520 530 540 550
DKMLQNVQMP SKKLDFIILN ETKFWYQMIL PPHFDKSKKY PLLLDVYAGP
560 570 580 590 600
CSQKADTVFR LNWATYLAST ENIIVASFDG RGSGYQGDKI MHAINRRLGT
610 620 630 640 650
FEVEDQIEAA RQFSKMGFVD NKRIAIWGWS YGGYVTSMVL GSGSGVFKCG
660 670 680 690 700
IAVAPVSRWE YYDSVYTERY MGLPTPEDNL DHYRNSTVMS RAENFKQVEY
710 720 730 740 750
LLIHGTADDN VHFQQSAQIS KALVDVGVDF QAMWYTDEDH GIASSTAHQH
760
IYTHMSHFIK QCFSLP
Length:766
Mass (Da):88,279
Last modified:February 1, 1996 - v2
Checksum:i5FB4A2C6662D6117
GO

Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F8WBB6F8WBB6_HUMAN
Dipeptidyl peptidase 4
DPP4
118Annotation score:
F8WE17F8WE17_HUMAN
Dipeptidyl peptidase 4
DPP4
170Annotation score:
H7C1N5H7C1N5_HUMAN
Dipeptidyl peptidase 4
DPP4
86Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti6K → R in AAA52308 (PubMed:1347043).Curated1
Sequence conflicti7V → I in CAA43118 (PubMed:1352704).Curated1
Sequence conflicti437S → I in CAA43118 (PubMed:1352704).Curated1
Sequence conflicti557T → I in AAA52308 (PubMed:1347043).Curated1
Sequence conflicti663D → E in AAA52308 (PubMed:1347043).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60708 mRNA Translation: CAA43118.1
M80536 mRNA Translation: AAA52308.1
M74777 mRNA Translation: AAA51943.1
U13735
, U13710, U13711, U13712, U13713, U13714, U13715, U13716, U13717, U13718, U13719, U13720, U13721, U13722, U13723, U13724, U13725, U13726, U13727, U13728, U13729, U13730, U13731, U13732, U13733, U13734 Genomic DNA Translation: AAB60646.1
AB451339 mRNA Translation: BAG70153.1
AB451488 mRNA Translation: BAG70302.1
AC008063 Genomic DNA Translation: AAX93179.1
CH471058 Genomic DNA Translation: EAX11361.1
BC013329 mRNA Translation: AAH13329.2
BC065265 mRNA Translation: AAH65265.1
S79876 Genomic DNA Translation: AAB35614.1
CCDSiCCDS2216.1
PIRiS24313 CDHU26
RefSeqiNP_001926.2, NM_001935.3
UniGeneiHs.368912

Genome annotation databases

EnsembliENST00000360534; ENSP00000353731; ENSG00000197635
GeneIDi1803
KEGGihsa:1803
UCSCiuc002ubz.4 human

Similar proteinsi

Cross-referencesi

Web resourcesi

Wikipedia

Dipeptidyl peptidase-4 entry

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60708 mRNA Translation: CAA43118.1
M80536 mRNA Translation: AAA52308.1
M74777 mRNA Translation: AAA51943.1
U13735
, U13710, U13711, U13712, U13713, U13714, U13715, U13716, U13717, U13718, U13719, U13720, U13721, U13722, U13723, U13724, U13725, U13726, U13727, U13728, U13729, U13730, U13731, U13732, U13733, U13734 Genomic DNA Translation: AAB60646.1
AB451339 mRNA Translation: BAG70153.1
AB451488 mRNA Translation: BAG70302.1
AC008063 Genomic DNA Translation: AAX93179.1
CH471058 Genomic DNA Translation: EAX11361.1
BC013329 mRNA Translation: AAH13329.2
BC065265 mRNA Translation: AAH65265.1
S79876 Genomic DNA Translation: AAB35614.1
CCDSiCCDS2216.1
PIRiS24313 CDHU26
RefSeqiNP_001926.2, NM_001935.3
UniGeneiHs.368912

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1J2EX-ray2.60A/B33-766[»]
1N1MX-ray2.50A/B39-766[»]
1NU6X-ray2.10A/B39-766[»]
1NU8X-ray2.50A/B39-766[»]
1PFQX-ray1.90A/B36-766[»]
1R9MX-ray2.10A/B/C/D39-766[»]
1R9NX-ray2.30A/B/C/D39-766[»]
1RWQX-ray2.20A/B39-766[»]
1TK3X-ray2.00A/B39-766[»]
1TKRX-ray2.70A/B39-766[»]
1U8EX-ray2.20A/B39-766[»]
1W1IX-ray3.03A/B/C/D39-766[»]
1WCYX-ray2.20A/B33-766[»]
1X70X-ray2.10A/B39-766[»]
2AJLX-ray2.50I/J39-766[»]
2BGNX-ray3.15A/B/C/D39-766[»]
2BGRX-ray2.00A/B29-766[»]
2BUBX-ray2.66A/B39-766[»]
2FJPX-ray2.40A/B39-766[»]
2G5PX-ray2.40A/B39-764[»]
2G5TX-ray2.30A/B39-764[»]
2G63X-ray2.00A/B/C/D39-764[»]
2HHAX-ray2.35A/B40-766[»]
2I03X-ray2.40A/B/C/D39-764[»]
2I78X-ray2.50A/B/C/D39-764[»]
2IITX-ray2.35A/B39-766[»]
2IIVX-ray2.15A/B39-766[»]
2JIDX-ray2.80A/B31-766[»]
2OAGX-ray2.30A/B/C/D39-764[»]
2OGZX-ray2.10A/B39-766[»]
2OLEX-ray2.40A/B39-766[»]
2ONCX-ray2.55A/B/C/D41-766[»]
2OPHX-ray2.40A/B39-766[»]
2OQIX-ray2.80A/B/C/D39-766[»]
2OQVX-ray2.80A/B39-764[»]
2P8SX-ray2.20A/B40-766[»]
2QJRX-ray2.20A/B31-766[»]
2QKYX-ray3.10A/B/C/D40-766[»]
2QOEX-ray2.30A/B39-766[»]
2QT9X-ray2.10A/B1-766[»]
2QTBX-ray2.25A/B1-766[»]
2RGUX-ray2.60A/B39-766[»]
2RIPX-ray2.90A38-766[»]
3BJMX-ray2.35A/B39-766[»]
3C43X-ray2.30A/B39-766[»]
3C45X-ray2.05A/B39-766[»]
3CCBX-ray2.49A/B/C/D39-766[»]
3CCCX-ray2.71A/B/C/D39-766[»]
3D4LX-ray2.00A/B39-766[»]
3EIOX-ray2.00A/B39-766[»]
3F8SX-ray2.43A/B31-766[»]
3G0BX-ray2.25A/B/C/D39-766[»]
3G0CX-ray2.69A/B/C/D39-766[»]
3G0DX-ray2.39A/B/C/D39-766[»]
3G0GX-ray2.45A/B/C/D39-766[»]
3H0CX-ray2.66A/B39-766[»]
3HABX-ray2.10A/B39-766[»]
3HACX-ray2.00A/B39-766[»]
3KWFX-ray2.40A/B39-766[»]
3KWJX-ray2.80A/B39-766[»]
3NOXX-ray2.34A/B39-766[»]
3O95X-ray2.85A/B/C/D39-766[»]
3O9VX-ray2.75A/B/C/D39-766[»]
3OC0X-ray2.70A/B39-766[»]
3OPMX-ray2.72A/B/C/D39-766[»]
3Q0TX-ray2.40A/B39-766[»]
3Q8WX-ray3.64A/B39-764[»]
3QBJX-ray2.21A/B31-766[»]
3SWWX-ray2.00A/B39-766[»]
3SX4X-ray2.60A/B39-766[»]
3VJKX-ray2.49A/B33-766[»]
3VJLX-ray2.39A/B33-766[»]
3VJMX-ray2.10A/B33-766[»]
3W2TX-ray2.36A/B33-766[»]
3WQHX-ray2.85A/B39-766[»]
4A5SX-ray1.62A/B39-766[»]
4DSAX-ray3.25A/B39-766[»]
4DSZX-ray3.20A/B39-766[»]
4DTCX-ray3.00A/B39-766[»]
4G1FX-ray2.90A/B/C/D39-766[»]
4J3JX-ray3.20A/B39-766[»]
4JH0X-ray2.35A/B39-766[»]
4KR0X-ray2.70A39-766[»]
4L72X-ray3.00A39-766[»]
4LKOX-ray2.43A/B39-766[»]
4N8DX-ray1.65A/B39-766[»]
4N8EX-ray2.30A/B39-766[»]
4PNZX-ray1.90A/B39-766[»]
4PV7X-ray3.24A/B39-766[»]
4QZVX-ray2.59A/C39-766[»]
5I7UX-ray1.95A/B39-766[»]
5ISMX-ray2.00A/B39-766[»]
5J3JX-ray2.75A/B40-766[»]
5KBYX-ray2.24A/B/C/D39-766[»]
5T4BX-ray1.76A/B40-766[»]
5T4EX-ray1.77A/B40-766[»]
5T4FX-ray1.90A/B40-766[»]
5T4HX-ray2.61A/B40-766[»]
6B1EX-ray1.77A/B39-766[»]
6B1OX-ray1.91A/B39-766[»]
ProteinModelPortaliP27487
SMRiP27487
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108137, 8 interactors
DIPiDIP-351N
IntActiP27487, 23 interactors
MINTiP27487
STRINGi9606.ENSP00000353731

Chemistry databases

BindingDBiP27487
ChEMBLiCHEMBL284
DrugBankiDB07482 (2R)-N-[(2R)-2-(DIHYDROXYBORYL)-1-L-PROLYLPYRROLIDIN-2-YL]-N-[(5R)-5-(DIHYDROXYBORYL)-1-L-PROLYLPYRROLIDIN-2-YL]-L-PROLINAMIDE
DB03253 (2s)-Pyrrolidin-2-Ylmethylamine
DB04577 1-(1-phenylcyclopentyl)methylamine
DB08024 1-[2-(S)-AMINO-3-BIPHENYL-4-YL-PROPIONYL]-PYRROLIDINE-2-(S)-CARBONITRILE
DB07412 1-biphenyl-2-ylmethanamine
DB08588 2-({2-[(3R)-3-AMINOPIPERIDIN-1-YL]-4-OXOQUINAZOLIN-3(4H)-YL}METHYL)BENZONITRILE
DB01884 2-Amino-3-Methyl-1-Pyrrolidin-1-Yl-Butan-1-One
DB08672 4-[(3R)-3-{[2-(4-FLUOROPHENYL)-2-OXOETHYL]AMINO}BUTYL]BENZAMIDE
DB03660 4-Iodo-L-phenylalanine
DB07239 7-(aminomethyl)-6-(2-chlorophenyl)-1-methyl-1H-benzimidazole-5-carbonitrile
DB06203 Alogliptin
DB01076 Atorvastatin
DB04491 Diisopropylphosphono Group
DB06127 KRP-104
DB08882 Linagliptin
DB06655 Liraglutide
DB07779 N-({(2S)-1-[(3R)-3-AMINO-4-(2-FLUOROPHENYL)BUTANOYL]PYRROLIDIN-2-YL}METHYL)BENZAMIDE
DB08429 N-({(2S)-1-[(3R)-3-amino-4-(3-chlorophenyl)butanoyl]pyrrolidin-2-yl}methyl)-3-(methylsulfonyl)benzamide
DB05065 PHX1149
DB05001 PSN9301
DB06335 Saxagliptin
DB01261 Sitagliptin
DB04876 Vildagliptin
GuidetoPHARMACOLOGYi1612

Protein family/group databases

ESTHERihuman-DPP4 DPP4N_Peptidase_S9
MEROPSiS09.003
MoonProtiP27487

PTM databases

GlyConnecti1177
iPTMnetiP27487
PhosphoSitePlusiP27487

Polymorphism and mutation databases

BioMutaiDPP4
DMDMi1352311

Proteomic databases

MaxQBiP27487
PaxDbiP27487
PeptideAtlasiP27487
PRIDEiP27487
ProteomicsDBi54396

Protocols and materials databases

DNASUi1803
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000360534; ENSP00000353731; ENSG00000197635
GeneIDi1803
KEGGihsa:1803
UCSCiuc002ubz.4 human

Organism-specific databases

CTDi1803
DisGeNETi1803
EuPathDBiHostDB:ENSG00000197635.9
GeneCardsiDPP4
HGNCiHGNC:3009 DPP4
HPAiCAB045970
MIMi102720 gene
neXtProtiNX_P27487
OpenTargetsiENSG00000197635
PharmGKBiPA27467
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2100 Eukaryota
COG1506 LUCA
GeneTreeiENSGT00760000119233
HOGENOMiHOG000231875
HOVERGENiHBG005527
InParanoidiP27487
KOiK01278
OMAiQFILLEY
OrthoDBiEOG091G0BU5
PhylomeDBiP27487
TreeFamiTF313309

Enzyme and pathway databases

BRENDAi3.4.14.5 2681
ReactomeiR-HSA-381771 Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1)
R-HSA-400511 Synthesis, secretion, and inactivation of Glucose-dependent Insulinotropic Polypeptide (GIP)
SABIO-RKiP27487
SIGNORiP27487

Miscellaneous databases

ChiTaRSiDPP4 human
EvolutionaryTraceiP27487
GeneWikiiDipeptidyl_peptidase-4
GenomeRNAii1803
PROiPR:P27487
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000197635 Expressed in 171 organ(s), highest expression level in tendon of biceps brachii
CleanExiHS_DPP4
ExpressionAtlasiP27487 baseline and differential
GenevisibleiP27487 HS

Family and domain databases

Gene3Di2.140.10.30, 1 hit
3.40.50.1820, 1 hit
InterProiView protein in InterPro
IPR029058 AB_hydrolase
IPR002471 Pept_S9_AS
IPR001375 Peptidase_S9
IPR002469 Peptidase_S9B_N
IPR038554 Peptidase_S9B_N_sf
PfamiView protein in Pfam
PF00930 DPPIV_N, 1 hit
PF00326 Peptidase_S9, 1 hit
SUPFAMiSSF53474 SSF53474, 1 hit
PROSITEiView protein in PROSITE
PS00708 PRO_ENDOPEP_SER, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiDPP4_HUMAN
AccessioniPrimary (citable) accession number: P27487
Secondary accession number(s): Q53TN1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: February 1, 1996
Last modified: October 10, 2018
This is version 208 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  5. Peptidase families
    Classification of peptidase families and list of entries
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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