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Protein

Dipeptidyl peptidase 4

Gene

DPP4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

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

Enzyme 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

  • dipeptidyl-peptidase activity Source: UniProtKB
  • identical protein binding Source: IntAct
  • protease binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • receptor binding Source: UniProtKB
  • serine-type endopeptidase activity Source: InterPro
  • serine-type peptidase activity Source: UniProtKB
  • virus receptor activity Source: CACAO

GO - Biological processi

  • behavioral fear response Source: Ensembl
  • endothelial cell migration Source: UniProtKB
  • locomotory exploration behavior Source: Ensembl
  • negative regulation of extracellular matrix disassembly Source: UniProtKB
  • positive regulation of cell proliferation Source: UniProtKB
  • psychomotor behavior Source: Ensembl
  • regulation of cell-cell adhesion mediated by integrin Source: UniProtKB
  • response to hypoxia Source: UniProtKB
  • T cell activation Source: UniProtKB
  • T cell costimulation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease, Receptor, Serine protease

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

BioCyciZFISH:HS09964-MONOMER.
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-RKP27487.
SIGNORiP27487.

Protein family/group databases

ESTHERihuman-DPP4. DPP4N_Peptidase_S9.
MEROPSiS09.003.

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

HGNCiHGNC:3009. DPP4.

Subcellular locationi

Dipeptidyl peptidase 4 soluble form :

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

GO - Cellular componenti

  • apical plasma membrane Source: UniProtKB
  • cell surface Source: UniProtKB
  • endocytic vesicle Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • intercellular canaliculus Source: Ensembl
  • invadopodium membrane Source: UniProtKB
  • lamellipodium Source: UniProtKB
  • lamellipodium membrane Source: UniProtKB-SubCell
  • lysosomal membrane Source: UniProtKB
  • membrane Source: UniProtKB
  • membrane raft Source: UniProtKB-SubCell
  • plasma membrane Source: UniProtKB
Complete GO annotation...

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.
DrugBankiDB06203. Alogliptin.
DB01076. Atorvastatin.
DB08882. Linagliptin.
DB06655. Liraglutide.
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...)4 Publications1
Glycosylationi92N-linked (GlcNAc...)2 Publications1
Glycosylationi150N-linked (GlcNAc...)4 Publications1
Glycosylationi219N-linked (GlcNAc...)3 Publications1
Glycosylationi229N-linked (GlcNAc...)4 Publications1
Glycosylationi281N-linked (GlcNAc...)3 Publications1
Glycosylationi321N-linked (GlcNAc...)2 Publications1
Disulfide bondi328 ↔ 339
Disulfide bondi385 ↔ 394
Disulfide bondi444 ↔ 447
Disulfide bondi454 ↔ 472
Glycosylationi520N-linked (GlcNAc...)4 Publications1
Disulfide bondi649 ↔ 762
Glycosylationi685N-linked (GlcNAc...)2 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

EPDiP27487.
MaxQBiP27487.
PaxDbiP27487.
PeptideAtlasiP27487.
PRIDEiP27487.

PTM databases

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.
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

WithEntry#Exp.IntActNotes
itself12EBI-2871277,EBI-2871277
ADAP566585EBI-2871277,EBI-7475530From a different organism.
CCL11P516712EBI-2871277,EBI-727357
CXCL10P027782EBI-2871277,EBI-7815386
CXCL11O146252EBI-2871277,EBI-2871971
CXCL2P198752EBI-2871277,EBI-2114901
CXCL9Q073252EBI-2871277,EBI-3911467
GCGP012754EBI-2871277,EBI-7629173
VIPP012822EBI-2871277,EBI-751454

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protease binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi108137. 7 interactors.
DIPiDIP-351N.
IntActiP27487. 21 interactors.
MINTiMINT-4998658.
STRINGi9606.ENSP00000353731.

Chemistry databases

BindingDBiP27487.

Structurei

Secondary structure

1766
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi40 – 42Combined sources3
Helixi45 – 50Combined sources6
Beta strandi60 – 62Combined sources3
Beta strandi64 – 72Combined sources9
Beta strandi75 – 80Combined sources6
Turni81 – 83Combined sources3
Beta strandi86 – 90Combined sources5
Turni92 – 97Combined sources6
Beta strandi98 – 100Combined sources3
Beta strandi104 – 107Combined sources4
Beta strandi111 – 122Combined sources12
Beta strandi124 – 126Combined sources3
Beta strandi128 – 136Combined sources9
Turni137 – 140Combined sources4
Beta strandi141 – 143Combined sources3
Beta strandi152 – 157Combined sources6
Beta strandi159 – 162Combined sources4
Beta strandi164 – 168Combined sources5
Beta strandi171 – 177Combined sources7
Turni191 – 193Combined sources3
Beta strandi194 – 198Combined sources5
Helixi201 – 206Combined sources6
Beta strandi208 – 212Combined sources5
Beta strandi214 – 216Combined sources3
Beta strandi220 – 229Combined sources10
Beta strandi235 – 240Combined sources6
Beta strandi250 – 255Combined sources6
Beta strandi265 – 272Combined sources8
Helixi273 – 275Combined sources3
Beta strandi278 – 280Combined sources3
Beta strandi284 – 287Combined sources4
Helixi291 – 294Combined sources4
Beta strandi298 – 307Combined sources10
Beta strandi310 – 319Combined sources10
Beta strandi322 – 330Combined sources9
Turni332 – 334Combined sources3
Beta strandi337 – 339Combined sources3
Helixi341 – 343Combined sources3
Beta strandi345 – 348Combined sources4
Beta strandi350 – 352Combined sources3
Beta strandi354 – 358Combined sources5
Beta strandi362 – 364Combined sources3
Beta strandi368 – 376Combined sources9
Beta strandi378 – 380Combined sources3
Beta strandi382 – 388Combined sources7
Beta strandi391 – 393Combined sources3
Beta strandi395 – 397Combined sources3
Beta strandi400 – 402Combined sources3
Beta strandi404 – 410Combined sources7
Beta strandi412 – 420Combined sources9
Helixi422 – 424Combined sources3
Beta strandi429 – 435Combined sources7
Beta strandi438 – 446Combined sources9
Turni447 – 449Combined sources3
Turni451 – 453Combined sources3
Beta strandi456 – 461Combined sources6
Beta strandi465 – 472Combined sources8
Beta strandi474 – 477Combined sources4
Beta strandi479 – 484Combined sources6
Turni485 – 488Combined sources4
Beta strandi489 – 495Combined sources7
Helixi498 – 504Combined sources7
Beta strandi506 – 508Combined sources3
Beta strandi511 – 519Combined sources9
Beta strandi522 – 530Combined sources9
Beta strandi536 – 538Combined sources3
Beta strandi540 – 545Combined sources6
Helixi563 – 569Combined sources7
Beta strandi574 – 578Combined sources5
Beta strandi584 – 586Combined sources3
Helixi588 – 591Combined sources4
Helixi592 – 594Combined sources3
Turni598 – 600Combined sources3
Helixi601 – 614Combined sources14
Turni615 – 617Combined sources3
Beta strandi619 – 629Combined sources11
Helixi631 – 640Combined sources10
Turni641 – 643Combined sources3
Beta strandi648 – 654Combined sources7
Helixi659 – 661Combined sources3
Helixi664 – 671Combined sources8
Turni676 – 679Combined sources4
Helixi680 – 685Combined sources6
Helixi689 – 697Combined sources9
Beta strandi698 – 705Combined sources8
Beta strandi709 – 711Combined sources3
Helixi714 – 725Combined sources12
Beta strandi731 – 735Combined sources5
Helixi745 – 762Combined sources18

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[»]
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[»]
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.
OMAiWWSPNGT.
OrthoDBiEOG091G0BU5.
PhylomeDBiP27487.
TreeFamiTF313309.

Family and domain databases

Gene3Di2.140.10.30. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002471. Pept_S9_AS.
IPR001375. Peptidase_S9.
IPR002469. Peptidase_S9B_N.
[Graphical view]
PfamiPF00930. DPPIV_N. 1 hit.
PF00326. Peptidase_S9. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00708. PRO_ENDOPEP_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

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

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.

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[»]
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[»]
ProteinModelPortaliP27487.
SMRiP27487.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108137. 7 interactors.
DIPiDIP-351N.
IntActiP27487. 21 interactors.
MINTiMINT-4998658.
STRINGi9606.ENSP00000353731.

Chemistry databases

BindingDBiP27487.
ChEMBLiCHEMBL284.
DrugBankiDB06203. Alogliptin.
DB01076. Atorvastatin.
DB08882. Linagliptin.
DB06655. Liraglutide.
DB06335. Saxagliptin.
DB01261. Sitagliptin.
DB04876. Vildagliptin.
GuidetoPHARMACOLOGYi1612.

Protein family/group databases

ESTHERihuman-DPP4. DPP4N_Peptidase_S9.
MEROPSiS09.003.

PTM databases

iPTMnetiP27487.
PhosphoSitePlusiP27487.

Polymorphism and mutation databases

BioMutaiDPP4.
DMDMi1352311.

Proteomic databases

EPDiP27487.
MaxQBiP27487.
PaxDbiP27487.
PeptideAtlasiP27487.
PRIDEiP27487.

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.
GeneCardsiDPP4.
HGNCiHGNC:3009. DPP4.
HPAiCAB045970.
MIMi102720. gene.
neXtProtiNX_P27487.
OpenTargetsiENSG00000197635.
PharmGKBiPA27467.
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciZFISH:HS09964-MONOMER.
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-RKP27487.
SIGNORiP27487.

Miscellaneous databases

ChiTaRSiDPP4. human.
EvolutionaryTraceiP27487.
GeneWikiiDipeptidyl_peptidase-4.
GenomeRNAii1803.
PROiP27487.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000197635.
CleanExiHS_DPP4.
ExpressionAtlasiP27487. baseline and differential.
GenevisibleiP27487. HS.

Family and domain databases

Gene3Di2.140.10.30. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002471. Pept_S9_AS.
IPR001375. Peptidase_S9.
IPR002469. Peptidase_S9B_N.
[Graphical view]
PfamiPF00930. DPPIV_N. 1 hit.
PF00326. Peptidase_S9. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00708. PRO_ENDOPEP_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDPP4_HUMAN
AccessioniPrimary (citable) accession number: P27487
Secondary accession number(s): Q53TN1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: February 1, 1996
Last modified: November 30, 2016
This is version 191 of the entry and version 2 of the sequence. [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

Miscellaneous

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

Keywords - Technical termi

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

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.