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P27487

- DPP4_HUMAN

UniProt

P27487 - DPP4_HUMAN

Protein

Dipeptidyl peptidase 4

Gene

DPP4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 172 (01 Oct 2014)
      Sequence version 2 (01 Feb 1996)
      Previous versions | rss
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    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.PROSITE-ProRule annotation

    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

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

    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.
    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.

    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 Source: UniProtKB
    12. membrane raft Source: UniProtKB-SubCell
    13. plasma membrane Source: UniProtKB

    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 ↔ 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

    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.4 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.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

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP27487.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 66CytoplasmicSequence Analysis
    Topological domaini29 – 766738ExtracellularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei7 – 2822Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    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

    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

    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:
    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

    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: October 1, 2014
    This is version 172 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