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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei630 – 6301Charge relay systemPROSITE-ProRule annotation
Active sitei708 – 7081Charge relay systemPROSITE-ProRule annotation
Active sitei740 – 7401Charge relay systemPROSITE-ProRule annotation

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

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)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66CytoplasmicSequence analysis
Transmembranei7 – 2822Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini29 – 766738ExtracellularSequence analysisAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi85 – 851N → A: Does not inhibit dipeptidyl peptidase activity, interaction with ADA and homodimer formation. 1 Publication
Mutagenesisi92 – 921N → A: Does not inhibit dipeptidyl peptidase activity, interaction with ADA and homodimer formation. 1 Publication
Mutagenesisi150 – 1501N → A: Does not inhibit dipeptidyl peptidase activity, interaction with ADA and homodimer formation. 1 Publication
Mutagenesisi205 – 2051E → K: Inhibits dipeptidyl peptidase activity. 1 Publication
Mutagenesisi206 – 2061E → L: Inhibits dipeptidyl peptidase activity. 1 Publication
Mutagenesisi219 – 2191N → A: Does not inhibit dipeptidyl peptidase activity, interaction with ADA and homodimer formation. 1 Publication
Mutagenesisi229 – 2291N → A: Does not inhibit dipeptidyl peptidase activity, interaction with ADA and homodimer formation. 1 Publication
Mutagenesisi281 – 2811N → A: Does not inhibit dipeptidyl peptidase activity, interaction with ADA and homodimer formation. 1 Publication
Mutagenesisi321 – 3211N → A: Does not inhibit dipeptidyl peptidase activity, interaction with ADA and homodimer formation. 1 Publication
Mutagenesisi520 – 5201N → A: Does not inhibit dipeptidyl peptidase activity, interaction with ADA and homodimer formation. 1 Publication
Mutagenesisi685 – 6851N → A: Does not inhibit dipeptidyl peptidase activity, interaction with ADA and homodimer formation. 1 Publication
Mutagenesisi750 – 7501H → A: Inhibits weakly homodimerization and dipeptidyl peptidase activity. 2 Publications
Mutagenesisi750 – 7501H → E: Inhibits strongly homodimerization, dipeptidyl peptidase activity, interaction with CARD11 and T-cell costimulation activity. 2 Publications

Organism-specific databases

PharmGKBiPA27467.

Chemistry

ChEMBLiCHEMBL2111469.
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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 766766Dipeptidyl peptidase 4 membrane formPRO_0000027213Add
BLAST
Chaini39 – 766728Dipeptidyl peptidase 4 soluble formPRO_0000027214Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi85 – 851N-linked (GlcNAc...)4 Publications
Glycosylationi92 – 921N-linked (GlcNAc...)2 Publications
Glycosylationi150 – 1501N-linked (GlcNAc...)4 Publications
Glycosylationi219 – 2191N-linked (GlcNAc...)3 Publications
Glycosylationi229 – 2291N-linked (GlcNAc...)4 Publications
Glycosylationi281 – 2811N-linked (GlcNAc...)3 Publications
Glycosylationi321 – 3211N-linked (GlcNAc...)2 Publications
Disulfide bondi328 ↔ 339
Disulfide bondi385 ↔ 394
Disulfide bondi444 ↔ 447
Disulfide bondi454 ↔ 472
Glycosylationi520 – 5201N-linked (GlcNAc...)4 Publications
Disulfide bondi649 ↔ 762
Glycosylationi685 – 6851N-linked (GlcNAc...)2 Publications

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.
PhosphoSiteiP27487.

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.4 Publications

Gene expression databases

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

Organism-specific databases

HPAiCAB045970.

Interactioni

Subunit structurei

Monomer. Homodimer or heterodimer with Seprase (FAP). 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. Associates with collagen. Interacts with PTPRC; the interaction is enhanced in a interleukin-12-dependent manner in activated lymphocytes. Interacts (extracellular domain) with ADA; does not inhibit its dipeptidyl peptidase activity. Interacts with CAV1 (via the N-terminus); the interaction is direct. Interacts (via cytoplasmic tail) with CARD11 (via PDZ domain); its homodimerization is necessary for interaction with CARD11. Interacts with IGF2R; the interaction is direct. Interacts with GPC3. Interacts with human coronavirus-EMC spike protein and acts as a receptor for this virus.10 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 interactions.
DIPiDIP-351N.
IntActiP27487. 21 interactions.
MINTiMINT-4998658.
STRINGi9606.ENSP00000353731.

Chemistry

BindingDBiP27487.

Structurei

Secondary structure

1
766
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi40 – 423Combined sources
Helixi45 – 506Combined sources
Beta strandi60 – 623Combined sources
Beta strandi64 – 729Combined sources
Beta strandi75 – 806Combined sources
Turni81 – 833Combined sources
Beta strandi86 – 905Combined sources
Turni92 – 976Combined sources
Beta strandi98 – 1003Combined sources
Beta strandi104 – 1074Combined sources
Beta strandi111 – 12212Combined sources
Beta strandi124 – 1263Combined sources
Beta strandi128 – 1369Combined sources
Turni137 – 1404Combined sources
Beta strandi141 – 1433Combined sources
Beta strandi152 – 1576Combined sources
Beta strandi159 – 1624Combined sources
Beta strandi164 – 1685Combined sources
Beta strandi171 – 1777Combined sources
Turni191 – 1933Combined sources
Beta strandi194 – 1985Combined sources
Helixi201 – 2066Combined sources
Beta strandi208 – 2125Combined sources
Beta strandi214 – 2163Combined sources
Beta strandi220 – 22910Combined sources
Beta strandi235 – 2406Combined sources
Beta strandi250 – 2556Combined sources
Beta strandi265 – 2728Combined sources
Helixi273 – 2753Combined sources
Beta strandi278 – 2803Combined sources
Beta strandi284 – 2874Combined sources
Helixi291 – 2944Combined sources
Beta strandi298 – 30710Combined sources
Beta strandi310 – 31910Combined sources
Beta strandi322 – 3309Combined sources
Turni332 – 3343Combined sources
Beta strandi337 – 3393Combined sources
Helixi341 – 3433Combined sources
Beta strandi345 – 3484Combined sources
Beta strandi350 – 3523Combined sources
Beta strandi354 – 3585Combined sources
Beta strandi362 – 3643Combined sources
Beta strandi368 – 3769Combined sources
Beta strandi378 – 3803Combined sources
Beta strandi382 – 3887Combined sources
Beta strandi391 – 3933Combined sources
Beta strandi395 – 3973Combined sources
Beta strandi400 – 4023Combined sources
Beta strandi404 – 4107Combined sources
Beta strandi412 – 4209Combined sources
Helixi422 – 4243Combined sources
Beta strandi429 – 4357Combined sources
Beta strandi438 – 4469Combined sources
Turni447 – 4493Combined sources
Turni451 – 4533Combined sources
Beta strandi456 – 4616Combined sources
Beta strandi465 – 4728Combined sources
Beta strandi474 – 4774Combined sources
Beta strandi479 – 4846Combined sources
Turni485 – 4884Combined sources
Beta strandi489 – 4957Combined sources
Helixi498 – 5047Combined sources
Beta strandi506 – 5083Combined sources
Beta strandi511 – 5199Combined sources
Beta strandi522 – 5309Combined sources
Beta strandi536 – 5383Combined sources
Beta strandi540 – 5456Combined sources
Helixi563 – 5697Combined sources
Beta strandi574 – 5785Combined sources
Beta strandi584 – 5863Combined sources
Helixi588 – 5914Combined sources
Helixi592 – 5943Combined sources
Turni598 – 6003Combined sources
Helixi601 – 61414Combined sources
Turni615 – 6173Combined sources
Beta strandi619 – 62911Combined sources
Helixi631 – 64010Combined sources
Turni641 – 6433Combined sources
Beta strandi648 – 6547Combined sources
Helixi659 – 6613Combined sources
Helixi664 – 6718Combined sources
Turni676 – 6794Combined sources
Helixi680 – 6856Combined sources
Helixi689 – 6979Combined sources
Beta strandi698 – 7058Combined sources
Beta strandi709 – 7113Combined sources
Helixi714 – 72512Combined sources
Beta strandi731 – 7355Combined sources
Helixi745 – 76218Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP27487.
SMRiP27487. Positions 39-766.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61K → R in AAA52308 (PubMed:1347043).Curated
Sequence conflicti7 – 71V → I in CAA43118 (PubMed:1352704).Curated
Sequence conflicti437 – 4371S → I in CAA43118 (PubMed:1352704).Curated
Sequence conflicti557 – 5571T → I in AAA52308 (PubMed:1347043).Curated
Sequence conflicti663 – 6631D → E in AAA52308 (PubMed:1347043).Curated

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
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[»]
ProteinModelPortaliP27487.
SMRiP27487. Positions 39-766.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry

BindingDBiP27487.
ChEMBLiCHEMBL2111469.
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.
PhosphoSiteiP27487.

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

Phylogenomic databases

eggNOGiKOG2100. Eukaryota.
COG1506. LUCA.
GeneTreeiENSGT00760000119233.
HOGENOMiHOG000231875.
HOVERGENiHBG005527.
InParanoidiP27487.
KOiK01278.
OMAiWWSPNGT.
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-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: September 7, 2016
This is version 188 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.