SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P27487

- DPP4_HUMAN

UniProt

P27487 - DPP4_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Dipeptidyl peptidase 4

Gene
DPP4, ADCP2, CD26
Organism
Homo sapiens (Human)
Status
Reviewed - 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.9 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.

Enzyme regulationi

Inhibited by GPC3 and diprotin A.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei630 – 6301Charge relay system By similarity
Active sitei708 – 7081Charge relay system By similarity
Active sitei740 – 7401Charge relay system By similarity

GO - Molecular functioni

  1. aminopeptidase activity Source: UniProtKB-KW
  2. dipeptidyl-peptidase activity Source: UniProtKB
  3. identical protein binding Source: IntAct
  4. protease binding Source: UniProtKB
  5. protein binding Source: UniProtKB
  6. protein homodimerization activity Source: UniProtKB
  7. receptor binding Source: UniProtKB
  8. serine-type endopeptidase activity Source: InterPro
  9. serine-type peptidase activity Source: UniProtKB

GO - Biological processi

  1. cell adhesion Source: UniProtKB-KW
  2. endothelial cell migration Source: UniProtKB
  3. negative regulation of extracellular matrix disassembly Source: UniProtKB
  4. positive regulation of cell proliferation Source: UniProtKB
  5. regulation of cell-cell adhesion mediated by integrin Source: UniProtKB
  6. response to hypoxia Source: UniProtKB
  7. T cell activation Source: UniProtKB
  8. 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.
ReactomeiREACT_23824. Synthesis, secretion, and inactivation of Glucose-dependent Insulinotropic Polypeptide (GIP).
REACT_24019. Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
SABIO-RKP27487.

Protein family/group databases

MEROPSiS09.003.

Names & Taxonomyi

Protein namesi
Recommended name:
Dipeptidyl peptidase 4 (EC:3.4.14.5)
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
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:3009. DPP4.

Subcellular locationi

Chain Dipeptidyl peptidase 4 soluble form : Secreted
Note: Detected in the serum and the seminal fluid.8 Publications
Cell membrane; Single-pass type II membrane protein. Apical cell membrane; Single-pass type II membrane protein. Cell projectioninvadopodium membrane; Single-pass type II membrane protein. Cell projectionlamellipodium membrane; Single-pass type II membrane protein. Cell junction. Membrane raft
Note: Translocated to the apical membrane through the concerted action of N- and O-Glycans and its association with lipid microdomains containing cholesterol and sphingolipids. Redistributed to membrane rafts in T-cell in a interleukin-12-dependent activation. Its interaction with CAV1 is necessary for its translocation to membrane rafts. Colocalized with PTPRC in membrane rafts. Colocalized with FAP in invadopodia and lamellipodia of migratory activated endothelial cells in collagenous matrix. Colocalized with FAP on endothelial cells of capillary-like microvessels but not large vessels within invasive breast ductal carcinoma. Colocalized with ADA at the cell junction in lymphocyte-epithelial cell adhesion. Colocalized with IGF2R in internalized cytoplasmic vesicles adjacent to the cell surface.8 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66Cytoplasmic Reviewed prediction
Transmembranei7 – 2822Helical; Signal-anchor for type II membrane protein; Reviewed predictionAdd
BLAST
Topological domaini29 – 766738Extracellular Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. apical plasma membrane Source: UniProtKB
  2. cell surface Source: UniProtKB
  3. endocytic vesicle Source: UniProtKB
  4. extracellular vesicular exosome Source: UniProtKB
  5. integral component of membrane Source: UniProtKB-KW
  6. intercellular canaliculus Source: Ensembl
  7. invadopodium membrane Source: UniProtKB
  8. lamellipodium Source: UniProtKB
  9. lamellipodium membrane Source: UniProtKB-SubCell
  10. lysosomal membrane Source: UniProtKB
  11. membrane raft Source: UniProtKB-SubCell
  12. 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.

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 ↔ 3393 Publications
Disulfide bondi385 ↔ 3943 Publications
Disulfide bondi444 ↔ 4473 Publications
Disulfide bondi454 ↔ 4723 Publications
Glycosylationi520 – 5201N-linked (GlcNAc...)4 Publications
Disulfide bondi649 ↔ 7623 Publications
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.6 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.

PTM databases

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.6 Publications

Gene expression databases

ArrayExpressiP27487.
BgeeiP27487.
CleanExiHS_DPP4.
GenevestigatoriP27487.

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.15 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

Protein-protein interaction databases

BioGridi108137. 5 interactions.
DIPiDIP-351N.
IntActiP27487. 21 interactions.
MINTiMINT-4998658.
STRINGi9606.ENSP00000353731.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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[»]
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[»]
ProteinModelPortaliP27487.
SMRiP27487. Positions 39-766.

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

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1506.
HOGENOMiHOG000231875.
HOVERGENiHBG005527.
InParanoidiP27487.
KOiK01278.
OMAiETKFWYQ.
OrthoDBiEOG761BT2.
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.
[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

MKTPWKVLLG LLGAAALVTI ITVPVVLLNK GTDDATADSR KTYTLTDYLK    50
NTYRLKLYSL RWISDHEYLY KQENNILVFN AEYGNSSVFL ENSTFDEFGH 100
SINDYSISPD GQFILLEYNY VKQWRHSYTA SYDIYDLNKR QLITEERIPN 150
NTQWVTWSPV GHKLAYVWNN DIYVKIEPNL PSYRITWTGK EDIIYNGITD 200
WVYEEEVFSA YSALWWSPNG TFLAYAQFND TEVPLIEYSF YSDESLQYPK 250
TVRVPYPKAG AVNPTVKFFV VNTDSLSSVT NATSIQITAP ASMLIGDHYL 300
CDVTWATQER ISLQWLRRIQ NYSVMDICDY DESSGRWNCL VARQHIEMST 350
TGWVGRFRPS EPHFTLDGNS FYKIISNEEG YRHICYFQID KKDCTFITKG 400
TWEVIGIEAL TSDYLYYISN EYKGMPGGRN LYKIQLSDYT KVTCLSCELN 450
PERCQYYSVS FSKEAKYYQL RCSGPGLPLY TLHSSVNDKG LRVLEDNSAL 500
DKMLQNVQMP SKKLDFIILN ETKFWYQMIL PPHFDKSKKY PLLLDVYAGP 550
CSQKADTVFR LNWATYLAST ENIIVASFDG RGSGYQGDKI MHAINRRLGT 600
FEVEDQIEAA RQFSKMGFVD NKRIAIWGWS YGGYVTSMVL GSGSGVFKCG 650
IAVAPVSRWE YYDSVYTERY MGLPTPEDNL DHYRNSTVMS RAENFKQVEY 700
LLIHGTADDN VHFQQSAQIS KALVDVGVDF QAMWYTDEDH GIASSTAHQH 750
IYTHMSHFIK QCFSLP 766
Length:766
Mass (Da):88,279
Last modified:February 1, 1996 - v2
Checksum:i5FB4A2C6662D6117
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61K → R in AAA52308. 1 Publication
Sequence conflicti7 – 71V → I in CAA43118. 1 Publication
Sequence conflicti437 – 4371S → I in CAA43118. 1 Publication
Sequence conflicti557 – 5571T → I in AAA52308. 1 Publication
Sequence conflicti663 – 6631D → E in AAA52308. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.3. human.

Polymorphism databases

DMDMi1352311.

Cross-referencesi

Web resourcesi

Wikipedia

Dipeptidyl peptidase-4 entry

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS2216.1.
PIRi S24313. CDHU26.
RefSeqi NP_001926.2. NM_001935.3.
UniGenei Hs.368912.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1J2E X-ray 2.60 A/B 33-766 [» ]
1N1M X-ray 2.50 A/B 39-766 [» ]
1NU6 X-ray 2.10 A/B 39-766 [» ]
1NU8 X-ray 2.50 A/B 39-766 [» ]
1PFQ X-ray 1.90 A/B 36-766 [» ]
1R9M X-ray 2.10 A/B/C/D 39-766 [» ]
1R9N X-ray 2.30 A/B/C/D 39-766 [» ]
1RWQ X-ray 2.20 A/B 39-766 [» ]
1TK3 X-ray 2.00 A/B 39-766 [» ]
1TKR X-ray 2.70 A/B 39-766 [» ]
1U8E X-ray 2.20 A/B 39-766 [» ]
1W1I X-ray 3.03 A/B/C/D 39-766 [» ]
1WCY X-ray 2.20 A/B 33-766 [» ]
1X70 X-ray 2.10 A/B 39-766 [» ]
2AJL X-ray 2.50 I/J 39-766 [» ]
2BGN X-ray 3.15 A/B/C/D 39-766 [» ]
2BGR X-ray 2.00 A/B 29-766 [» ]
2BUB X-ray 2.66 A/B 39-766 [» ]
2FJP X-ray 2.40 A/B 39-766 [» ]
2G5P X-ray 2.40 A/B 39-764 [» ]
2G5T X-ray 2.30 A/B 39-764 [» ]
2G63 X-ray 2.00 A/B/C/D 39-764 [» ]
2HHA X-ray 2.35 A/B 40-766 [» ]
2I03 X-ray 2.40 A/B/C/D 39-764 [» ]
2I78 X-ray 2.50 A/B/C/D 39-764 [» ]
2IIT X-ray 2.35 A/B 39-766 [» ]
2IIV X-ray 2.15 A/B 39-766 [» ]
2JID X-ray 2.80 A/B 31-766 [» ]
2OAG X-ray 2.30 A/B/C/D 39-764 [» ]
2OGZ X-ray 2.10 A/B 39-766 [» ]
2OLE X-ray 2.40 A/B 39-766 [» ]
2ONC X-ray 2.55 A/B/C/D 41-766 [» ]
2OPH X-ray 2.40 A/B 39-766 [» ]
2OQI X-ray 2.80 A/B/C/D 39-766 [» ]
2OQV X-ray 2.80 A/B 39-764 [» ]
2P8S X-ray 2.20 A/B 40-766 [» ]
2QJR X-ray 2.20 A/B 31-766 [» ]
2QKY X-ray 3.10 A/B/C/D 40-766 [» ]
2QOE X-ray 2.30 A/B 39-766 [» ]
2QT9 X-ray 2.10 A/B 1-766 [» ]
2QTB X-ray 2.25 A/B 1-766 [» ]
2RGU X-ray 2.60 A/B 39-766 [» ]
2RIP X-ray 2.90 A 38-766 [» ]
3BJM X-ray 2.35 A/B 39-766 [» ]
3C43 X-ray 2.30 A/B 39-766 [» ]
3C45 X-ray 2.05 A/B 39-766 [» ]
3CCB X-ray 2.49 A/B/C/D 39-766 [» ]
3CCC X-ray 2.71 A/B/C/D 39-766 [» ]
3D4L X-ray 2.00 A/B 39-766 [» ]
3EIO X-ray 2.00 A/B 39-766 [» ]
3F8S X-ray 2.43 A/B 31-766 [» ]
3G0B X-ray 2.25 A/B/C/D 39-766 [» ]
3G0C X-ray 2.69 A/B/C/D 39-766 [» ]
3G0D X-ray 2.39 A/B/C/D 39-766 [» ]
3G0G X-ray 2.45 A/B/C/D 39-766 [» ]
3H0C X-ray 2.66 A/B 39-766 [» ]
3HAB X-ray 2.10 A/B 39-766 [» ]
3HAC X-ray 2.00 A/B 39-766 [» ]
3KWF X-ray 2.40 A/B 39-766 [» ]
3KWJ X-ray 2.80 A/B 39-766 [» ]
3NOX X-ray 2.34 A/B 39-766 [» ]
3O95 X-ray 2.85 A/B/C/D 39-766 [» ]
3O9V X-ray 2.75 A/B/C/D 39-766 [» ]
3OC0 X-ray 2.70 A/B 39-766 [» ]
3OPM X-ray 2.72 A/B/C/D 39-766 [» ]
3Q0T X-ray 2.40 A/B 39-766 [» ]
3Q8W X-ray 3.64 A/B 39-764 [» ]
3QBJ X-ray 2.21 A/B 31-766 [» ]
3SWW X-ray 2.00 A/B 39-766 [» ]
3SX4 X-ray 2.60 A/B 39-766 [» ]
3VJK X-ray 2.49 A/B 33-766 [» ]
3VJL X-ray 2.39 A/B 33-766 [» ]
3VJM X-ray 2.10 A/B 33-766 [» ]
3W2T X-ray 2.36 A/B 33-766 [» ]
4A5S X-ray 1.62 A/B 39-766 [» ]
4DSA X-ray 3.25 A/B 39-766 [» ]
4DSZ X-ray 3.20 A/B 39-766 [» ]
4DTC X-ray 3.00 A/B 39-766 [» ]
4G1F X-ray 2.90 A/B/C/D 39-766 [» ]
4J3J X-ray 3.20 A/B 39-766 [» ]
4JH0 X-ray 2.35 A/B 39-766 [» ]
4KR0 X-ray 2.70 A 39-766 [» ]
4L72 X-ray 3.00 A 39-766 [» ]
4LKO X-ray 2.43 A/B 39-766 [» ]
4N8D X-ray 1.65 A/B 39-766 [» ]
4N8E X-ray 2.30 A/B 39-766 [» ]
4PNZ X-ray 1.90 A/B 39-766 [» ]
ProteinModelPortali P27487.
SMRi P27487. Positions 39-766.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108137. 5 interactions.
DIPi DIP-351N.
IntActi P27487. 21 interactions.
MINTi MINT-4998658.
STRINGi 9606.ENSP00000353731.

Chemistry

BindingDBi P27487.
ChEMBLi CHEMBL284.
DrugBanki DB01261. Sitagliptin.
GuidetoPHARMACOLOGYi 1612.

Protein family/group databases

MEROPSi S09.003.

PTM databases

PhosphoSitei P27487.

Polymorphism databases

DMDMi 1352311.

Proteomic databases

MaxQBi P27487.
PaxDbi P27487.
PeptideAtlasi P27487.
PRIDEi P27487.

Protocols and materials databases

DNASUi 1803.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000360534 ; ENSP00000353731 ; ENSG00000197635 .
GeneIDi 1803.
KEGGi hsa:1803.
UCSCi uc002ubz.3. human.

Organism-specific databases

CTDi 1803.
GeneCardsi GC02M162812.
HGNCi HGNC:3009. DPP4.
HPAi CAB045970.
MIMi 102720. gene.
neXtProti NX_P27487.
PharmGKBi PA27467.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1506.
HOGENOMi HOG000231875.
HOVERGENi HBG005527.
InParanoidi P27487.
KOi K01278.
OMAi ETKFWYQ.
OrthoDBi EOG761BT2.
PhylomeDBi P27487.
TreeFami TF313309.

Enzyme and pathway databases

BRENDAi 3.4.14.5. 2681.
Reactomei REACT_23824. Synthesis, secretion, and inactivation of Glucose-dependent Insulinotropic Polypeptide (GIP).
REACT_24019. Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
SABIO-RK P27487.

Miscellaneous databases

ChiTaRSi DPP4. human.
EvolutionaryTracei P27487.
GeneWikii Dipeptidyl_peptidase-4.
GenomeRNAii 1803.
NextBioi 7345.
PROi P27487.
SOURCEi Search...

Gene expression databases

ArrayExpressi P27487.
Bgeei P27487.
CleanExi HS_DPP4.
Genevestigatori P27487.

Family and domain databases

Gene3Di 2.140.10.30. 1 hit.
3.40.50.1820. 1 hit.
InterProi IPR029058. AB_hydrolase.
IPR002471. Pept_S9_AS.
IPR001375. Peptidase_S9.
IPR002469. Peptidase_S9B.
[Graphical view ]
Pfami PF00930. DPPIV_N. 1 hit.
PF00326. Peptidase_S9. 1 hit.
[Graphical view ]
SUPFAMi SSF53474. SSF53474. 1 hit.
PROSITEi PS00708. PRO_ENDOPEP_SER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and sequence analysis of human dipeptidyl peptidase IV, a serine proteinase on the cell surface."
    Misumi Y., Hayashi Y., Arakawa F., Ikehara Y.
    Biochim. Biophys. Acta 1131:333-336(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. "Dipeptidyl peptidase IV (CD 26) gene expression in enterocyte-like colon cancer cell lines HT-29 and Caco-2. Cloning of the complete human coding sequence and changes of dipeptidyl peptidase IV mRNA levels during cell differentiation."
    Darmoul D., Lacasa M., Baricault L., Marguet D., Sapin C., Trotot P., Barbat A.
    J. Biol. Chem. 267:4824-4833(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Colon.
  3. "Cloning and functional expression of the T cell activation antigen CD26."
    Tanaka T., Camerini D., Seed B., Torimoto Y., Dang N.H., Kameoka J., Dahlberg H.N., Schlossman S.F., Morimoto C.
    J. Immunol. 149:481-486(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Peripheral blood.
  4. Erratum
    Tanaka T.
    J. Immunol. 150:2090-2090(1993) [PubMed] [Europe PMC] [Abstract]
  5. "Genomic organization, exact localization, and tissue expression of the human CD26 (dipeptidyl peptidase IV) gene."
    Abbott C.A., Baker E., Sutherland G.R., McCaughan G.W.
    Immunogenetics 40:331-338(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Placenta.
  6. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
    Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
    , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
    Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  7. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Prostate and Uterus.
  10. "Isolation of a cDNA probe for the human intestinal dipeptidylpeptidase IV and assignment of the gene locus DPP4 to chromosome 2."
    Darmoul D., Lacasa M., Chantret I., Swallow D., Trugnan G.
    Ann. Hum. Genet. 54:191-197(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 545-766.
    Tissue: Colon.
  11. "Human dipeptidyl peptidase IV gene promoter: tissue-specific regulation from a TATA-less GC-rich sequence characteristic of a housekeeping gene promoter."
    Boehm S.K., Gum J.R. Jr., Erickson R.H., Hicks J.W., Kim Y.S.
    Biochem. J. 311:835-843(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31.
  12. "Expression of sucrase-isomaltase and dipeptidylpeptidase IV in human small intestine and colon."
    Gorvel J.P., Ferrero A., Chambraud L., Rigal A., Bonicel J., Maroux S.
    Gastroenterology 101:618-625(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-22, TISSUE SPECIFICITY.
  13. "Molecular characterization of dipeptidyl peptidase activity in serum: soluble CD26/dipeptidyl peptidase IV is responsible for the release of X-Pro dipeptides."
    Durinx C., Lambeir A.M., Bosmans E., Falmagne J.B., Berghmans R., Haemers A., Scharpe S., De Meester I.
    Eur. J. Biochem. 267:5608-5613(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 29-34 AND 39-43, FUNCTION, INTERACTION WITH ADA, SUBCELLULAR LOCATION.
  14. "The Simpson-Golabi-Behmel syndrome causative glypican-3, binds to and inhibits the dipeptidyl peptidase activity of CD26."
    Davoodi J., Kelly J., Gendron N.H., MacKenzie A.E.
    Proteomics 7:2300-2310(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 659-669, FUNCTION, ENZYME REGULATION, INTERACTION WITH GPC3, IDENTIFICATION BY MASS SPECTROMETRY.
  15. "A marker for neoplastic progression of human melanocytes is a cell surface ectopeptidase."
    Morrison M.E., Vijayasaradhi S., Engelstein D., Albino A.P., Houghton A.N.
    J. Exp. Med. 177:1135-1143(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE.
    Tissue: Kidney.
  16. "Direct association of adenosine deaminase with a T cell activation antigen, CD26."
    Kameoka J., Tanaka T., Nojima Y., Schlossman S.F., Morimoto C.
    Science 261:466-469(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ADA, SUBCELLULAR LOCATION.
  17. "Binding of adenosine deaminase to the lymphocyte surface via CD26."
    De Meester I., Vanham G., Kestens L., Vanhoof G., Bosmans E., Gigase P., Scharpe S.
    Eur. J. Immunol. 24:566-570(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ADA.
  18. "The cysteine-rich region of dipeptidyl peptidase IV (CD 26) is the collagen-binding site."
    Loster K., Zeilinger K., Schuppan D., Reutter W.
    Biochem. Biophys. Res. Commun. 217:341-348(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION WITH COLLAGEN.
  19. "Interleukin-12 enhances CD26 expression and dipeptidyl peptidase IV function on human activated lymphocytes."
    Cordero O.J., Salgado F.J., Vinuela J.E., Nogueira M.
    Immunobiology 197:522-533(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  20. "Two highly conserved glutamic acid residues in the predicted beta propeller domain of dipeptidyl peptidase IV are required for its enzyme activity."
    Abbott C.A., McCaughan G.W., Gorrell M.D.
    FEBS Lett. 458:278-284(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF GLU-205 AND GLU-206.
  21. "Preoperative serum CD26 levels: diagnostic efficiency and predictive value for colorectal cancer."
    Cordero O.J., Ayude D., Nogueira M., Rodriguez-Berrocal F.J., de la Cadena M.P.
    Br. J. Cancer 83:1139-1146(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION WITH CANCER.
  22. "Mechanisms of CD26/dipeptidyl peptidase IV cytokine-dependent regulation on human activated lymphocytes."
    Salgado F.J., Vela E., Martin M., Franco R., Nogueira M., Cordero O.J.
    Cytokine 12:1136-1141(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  23. "Internalization of CD26 by mannose 6-phosphate/insulin-like growth factor II receptor contributes to T cell activation."
    Ikushima H., Munakata Y., Ishii T., Iwata S., Terashima M., Tanaka H., Schlossman S.F., Morimoto C.
    Proc. Natl. Acad. Sci. U.S.A. 97:8439-8444(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH IGF2R, GLYCOSYLATION, PHOSPHORYLATION, SUBCELLULAR LOCATION.
  24. "Regulation of epithelial and lymphocyte cell adhesion by adenosine deaminase-CD26 interaction."
    Gines S., Marino M., Mallol J., Canela E.I., Morimoto C., Callebaut C., Hovanessian A., Casado V., Lluis C., Franco R.
    Biochem. J. 361:203-209(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  25. "Intestinal dipeptidyl peptidase IV is efficiently sorted to the apical membrane through the concerted action of N- and O-glycans as well as association with lipid microdomains."
    Alfalah M., Jacob R., Naim H.Y.
    J. Biol. Chem. 277:10683-10690(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION, SUBCELLULAR LOCATION.
  26. "A role for interleukin-12 in the regulation of T cell plasma membrane compartmentation."
    Salgado F.J., Lojo J., Alonso-Lebrero J.L., Lluis C., Franco R., Cordero O.J., Nogueira M.
    J. Biol. Chem. 278:24849-24857(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PTPRC, INDUCTION, SUBCELLULAR LOCATION.
  27. "One site mutation disrupts dimer formation in human DPP-IV proteins."
    Chien C.H., Huang L.H., Chou C.Y., Chen Y.S., Han Y.S., Chang G.G., Liang P.H., Chen X.
    J. Biol. Chem. 279:52338-52345(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: HOMODIMERIZATION, MUTAGENESIS OF HIS-750.
  28. "N-linked glycosylation of dipeptidyl peptidase IV (CD26): effects on enzyme activity, homodimer formation, and adenosine deaminase binding."
    Aertgeerts K., Ye S., Shi L., Prasad S.G., Witmer D., Chi E., Sang B.C., Wijnands R.A., Webb D.R., Swanson R.V.
    Protein Sci. 13:145-154(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ADA, MUTAGENESIS OF ASN-85; ASN-92; ASN-150; ASN-219; ASN-229; ASN-281; ASN-321; ASN-520 AND ASN-685.
  29. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
    Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
    J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-520 AND ASN-685.
    Tissue: Plasma.
  30. "The protease complex consisting of dipeptidyl peptidase IV and seprase plays a role in the migration and invasion of human endothelial cells in collagenous matrices."
    Ghersi G., Zhao Q., Salamone M., Yeh Y., Zucker S., Chen W.T.
    Cancer Res. 66:4652-4661(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, HETERODIMERIZATION, INDUCTION, SUBCELLULAR LOCATION.
  31. Cited for: FUNCTION, IDENTIFICATION IN A MEMBRANE RAFT COMPLEX, HOMODIMERIZATION, INTERACTION WITH CARD11 AND CAV1, SUBCELLULAR LOCATION, MUTAGENESIS OF HIS-750.
  32. "Lymphatic-specific expression of dipeptidyl peptidase IV and its dual role in lymphatic endothelial function."
    Shin J.W., Jurisic G., Detmar M.
    Exp. Cell Res. 314:3048-3056(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, TISSUE SPECIFICITY.
  33. "On the origin of serum CD26 and its altered concentration in cancer patients."
    Cordero O.J., Salgado F.J., Nogueira M.
    Cancer Immunol. Immunother. 58:1723-1747(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  34. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-92; ASN-150; ASN-520 AND ASN-685.
    Tissue: Liver.
  35. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  36. Cited for: INTERACTION WITH HUMAN CORONAVIRUS-EMC SPIKE PROTEIN.
  37. "High-resolution structure of human apo dipeptidyl peptidase IV/CD26 and its complex with 1-[([2-[(5-iodopyridin-2-yl)amino]-ethyl]amino)-acetyl]-2-cyano-(S)-pyrrolidine."
    Oefner C., D'Arcy A., Mac Sweeney A., Pierau S., Gardiner R., Dale G.E.
    Acta Crystallogr. D 59:1206-1212(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 38-766 IN COMPLEX WITH INHIBITOR, HOMODIMERIZATION.
  38. "The structure and function of human dipeptidyl peptidase IV, possessing a unique eight-bladed beta-propeller fold."
    Hiramatsu H., Kyono K., Higashiyama Y., Fukushima C., Shima H., Sugiyama S., Inaka K., Yamamoto A., Shimizu R.
    Biochem. Biophys. Res. Commun. 302:849-854(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 35-771, HOMODIMERIZATION, GLYCOSYLATION AT ASN-85; ASN-219; ASN-229; ASN-281 AND ASN-321, DISULFIDE BONDS.
  39. "Crystal structure of human dipeptidyl peptidase IV/CD26 in complex with a substrate analog."
    Rasmussen H.B., Branner S., Wiberg F.C., Wagtmann N.
    Nat. Struct. Biol. 10:19-25(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 39-766, HOMODIMERIZATION, GLYCOSYLATION AT ASN-85; ASN-150; ASN-219; ASN-229; ASN-281; ASN-321 AND ASN-520, DISULFIDE BONDS.
  40. "Structural basis of proline-specific exopeptidase activity as observed in human dipeptidyl peptidase-IV."
    Thoma R., Loeffler B., Stihle M., Huber W., Ruf A., Hennig M.
    Structure 11:947-959(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 39-766, HOMODIMERIZATION, GLYCOSYLATION AT ASN-85; ASN-150; ASN-229 AND ASN-281, DISULFIDE BONDS.
  41. "Discovery of 6-(aminomethyl)-5-(2,4-dichlorophenyl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamides as potent, selective dipeptidyl peptidase-4 (DPP4) inhibitors."
    Meng W., Brigance R.P., Chao H.J., Fura A., Harrity T., Marcinkeviciene J., O'Connor S.P., Tamura J.K., Xie D., Zhang Y., Klei H.E., Kish K., Weigelt C.A., Turdi H., Wang A., Zahler R., Kirby M.S., Hamann L.G.
    J. Med. Chem. 53:5620-5628(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.34 ANGSTROMS) OF 39-766, GLYCOSYLATION AT ASN-85; ASN-92; ASN-150; ASN-219; ASN-229 AND ASN-520.

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 3, 2014
This is version 171 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

External Data

Dasty 3

Similar proteinsi