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Protein

Dipeptidyl peptidase 8

Gene

DPP8

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2. May play a role in T-cell activation and immune function.1 Publication

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.3 Publications

Enzyme regulationi

Inhibited by zinc. Inhibited by the serine proteinase inhibitor 4-(2-aminoethyl)benzenesulphonyl fluoride (AEBSF), and by di-isopropylfuorophosphate. Specifically inhibited by isoindoline derivatives.3 Publications

Kineticsi

  1. KM=208 µM for Ala-Pro-AMC3 Publications
  2. KM=130 µM for Ala-Pro-AFC3 Publications
  3. KM=120 µM for H-Ala-Pro-pNa3 Publications
  4. KM=1420 µM for H-Ala-Ala-pNa3 Publications
  5. KM=310 µM for H-Arg-Pro-pNa3 Publications
  6. KM=2050 µM for H-Asp-Pro-pNa3 Publications
  7. KM=480 µM for H-Gly-Pro-pNa3 Publications

    pH dependencei

    Optimum pH is 7.4-8.5. Little activity below pH 6.5.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei755 – 7551Charge relay systemCurated
    Active sitei833 – 8331Charge relay systemCurated
    Active sitei865 – 8651Charge relay systemCurated

    GO - Molecular functioni

    • dipeptidyl-peptidase activity Source: UniProtKB
    • serine-type peptidase activity Source: UniProtKB-KW

    GO - Biological processi

    • immune response Source: UniProtKB
    • proteolysis Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Protease, Serine protease

    Enzyme and pathway databases

    SABIO-RKQ6V1X1.

    Protein family/group databases

    ESTHERihuman-DPP8. DPP4N_Peptidase_S9.
    MEROPSiS09.018.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dipeptidyl peptidase 8 (EC:3.4.14.5)
    Short name:
    DP8
    Alternative name(s):
    Dipeptidyl peptidase IV-related protein 1
    Short name:
    DPRP-1
    Dipeptidyl peptidase VIII
    Short name:
    DPP VIII
    Prolyl dipeptidase DPP8
    Gene namesi
    Name:DPP8
    Synonyms:DPRP1
    ORF Names:MSTP097, MSTP135, MSTP141
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:16490. DPP8.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: UniProtKB
    • membrane Source: InterPro
    • nucleoplasm Source: HPA
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi275 – 2751E → K: 13-fold reduction in affinity for Ala-Pro-AFC; no effect on subcellular location. 1 Publication
    Mutagenesisi755 – 7551S → A: Abolishes activity; no effect on subcellular location. 1 Publication
    Mutagenesisi833 – 8331D → A: Abolishes activity; no effect on subcellular location. 1 Publication
    Mutagenesisi865 – 8651H → A: Abolishes activity; no effect on subcellular location. 1 Publication

    Organism-specific databases

    PharmGKBiPA27470.

    Polymorphism and mutation databases

    BioMutaiDPP8.
    DMDMi67460301.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 898898Dipeptidyl peptidase 8PRO_0000122413Add
    BLAST

    Proteomic databases

    MaxQBiQ6V1X1.
    PaxDbiQ6V1X1.
    PRIDEiQ6V1X1.

    PTM databases

    PhosphoSiteiQ6V1X1.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed, with highest levels in testis, placenta, prostate, muscle and brain.2 Publications

    Inductioni

    In activated T-cells.1 Publication

    Gene expression databases

    BgeeiQ6V1X1.
    ExpressionAtlasiQ6V1X1. baseline and differential.
    GenevisibleiQ6V1X1. HS.

    Organism-specific databases

    HPAiHPA008706.

    Interactioni

    Protein-protein interaction databases

    BioGridi120226. 19 interactions.
    IntActiQ6V1X1. 3 interactions.
    MINTiMINT-4539721.
    STRINGi9606.ENSP00000339208.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6V1X1.
    SMRiQ6V1X1. Positions 136-886.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase S9B family. DPPIV subfamily.Curated

    Phylogenomic databases

    eggNOGiCOG1506.
    GeneTreeiENSGT00760000119233.
    HOVERGENiHBG061620.
    InParanoidiQ6V1X1.
    KOiK08655.
    OMAiMDNRGTA.
    OrthoDBiEOG7XWPN8.
    PhylomeDBiQ6V1X1.
    TreeFamiTF313309.

    Family and domain databases

    Gene3Di2.140.10.30. 1 hit.
    3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR001375. Peptidase_S9.
    IPR002469. Peptidase_S9B.
    [Graphical view]
    PfamiPF00930. DPPIV_N. 1 hit.
    PF00326. Peptidase_S9. 1 hit.
    [Graphical view]
    SUPFAMiSSF53474. SSF53474. 1 hit.

    Sequences (6)i

    Sequence statusi: Complete.

    This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q6V1X1-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

            10         20         30         40         50
    MWKRSEQMKI KSGKCNMAAA METEQLGVEI FETADCEENI ESQDRPKLEP
    60 70 80 90 100
    FYVERYSWSQ LKKLLADTRK YHGYMMAKAP HDFMFVKRND PDGPHSDRIY
    110 120 130 140 150
    YLAMSGENRE NTLFYSEIPK TINRAAVLML SWKPLLDLFQ ATLDYGMYSR
    160 170 180 190 200
    EEELLRERKR IGTVGIASYD YHQGSGTFLF QAGSGIYHVK DGGPQGFTQQ
    210 220 230 240 250
    PLRPNLVETS CPNIRMDPKL CPADPDWIAF IHSNDIWISN IVTREERRLT
    260 270 280 290 300
    YVHNELANME EDARSAGVAT FVLQEEFDRY SGYWWCPKAE TTPSGGKILR
    310 320 330 340 350
    ILYEENDESE VEIIHVTSPM LETRRADSFR YPKTGTANPK VTFKMSEIMI
    360 370 380 390 400
    DAEGRIIDVI DKELIQPFEI LFEGVEYIAR AGWTPEGKYA WSILLDRSQT
    410 420 430 440 450
    RLQIVLISPE LFIPVEDDVM ERQRLIESVP DSVTPLIIYE ETTDIWINIH
    460 470 480 490 500
    DIFHVFPQSH EEEIEFIFAS ECKTGFRHLY KITSILKESK YKRSSGGLPA
    510 520 530 540 550
    PSDFKCPIKE EIAITSGEWE VLGRHGSNIQ VDEVRRLVYF EGTKDSPLEH
    560 570 580 590 600
    HLYVVSYVNP GEVTRLTDRG YSHSCCISQH CDFFISKYSN QKNPHCVSLY
    610 620 630 640 650
    KLSSPEDDPT CKTKEFWATI LDSAGPLPDY TPPEIFSFES TTGFTLYGML
    660 670 680 690 700
    YKPHDLQPGK KYPTVLFIYG GPQVQLVNNR FKGVKYFRLN TLASLGYVVV
    710 720 730 740 750
    VIDNRGSCHR GLKFEGAFKY KMGQIEIDDQ VEGLQYLASR YDFIDLDRVG
    760 770 780 790 800
    IHGWSYGGYL SLMALMQRSD IFRVAIAGAP VTLWIFYDTG YTERYMGHPD
    810 820 830 840 850
    QNEQGYYLGS VAMQAEKFPS EPNRLLLLHG FLDENVHFAH TSILLSFLVR
    860 870 880 890
    AGKPYDLQIY PQERHSIRVP ESGEHYELHL LHYLQENLGS RIAALKVI
    Length:898
    Mass (Da):103,358
    Last modified:July 5, 2004 - v1
    Checksum:i60B0D036F026DE2A
    GO
    Isoform 2 (identifier: Q6V1X1-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         723-773: Missing.

    Show »
    Length:847
    Mass (Da):97,464
    Checksum:iAB07EF0087231B56
    GO
    Isoform 3 (identifier: Q6V1X1-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-16: Missing.

    Show »
    Length:882
    Mass (Da):101,422
    Checksum:iAD801C302DB4652B
    GO
    Isoform 4 (identifier: Q6V1X1-4) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-16: Missing.
         674-773: Missing.

    Show »
    Length:782
    Mass (Da):89,908
    Checksum:i784922477DB8F5B5
    GO
    Isoform 5 (identifier: Q6V1X1-5) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         674-722: Missing.

    Show »
    Length:849
    Mass (Da):97,739
    Checksum:i4B6C88F29CA55475
    GO
    Isoform 6 (identifier: Q6V1X1-6) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         358-530: Missing.

    Show »
    Length:725
    Mass (Da):83,398
    Checksum:i0476E0AEBD94131B
    GO

    Sequence cautioni

    The sequence AAQ13623.1 differs from that shown. Reason: Frameshift at several positions. Curated
    The sequence AAQ13650.1 differs from that shown. Reason: Frameshift at several positions. Curated
    The sequence AAQ13657.1 differs from that shown. Reason: Erroneous initiation. Curated
    The sequence BAA91059.1 differs from that shown. Reason: Frameshift at position 486. Curated
    The sequence BAB55395.1 differs from that shown. Reason: Erroneous initiation. Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti233 – 2331S → G in BC040203 (PubMed:15489334).Curated
    Sequence conflicti570 – 5701G → S in BAB55395 (PubMed:14702039).Curated
    Sequence conflicti673 – 6731Q → K in AAQ13650 (Ref. 6) Curated
    Sequence conflicti686 – 6861Y → F in AAQ13650 (Ref. 6) Curated
    Sequence conflicti693 – 6942AS → PF in AAQ13650 (Ref. 6) Curated
    Sequence conflicti701 – 7011V → G in AAQ13650 (Ref. 6) Curated
    Sequence conflicti709 – 7091H → P in AAQ13650 (Ref. 6) Curated
    Sequence conflicti720 – 7201Y → F in AAQ13650 (Ref. 6) Curated
    Sequence conflicti799 – 8035PDQNE → LTRMN in AAQ13623 (Ref. 6) Curated
    Sequence conflicti820 – 8201S → F in AAQ13623 (Ref. 6) Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1616Missing in isoform 3 and isoform 4. 3 PublicationsVSP_013860Add
    BLAST
    Alternative sequencei358 – 530173Missing in isoform 6. 1 PublicationVSP_013861Add
    BLAST
    Alternative sequencei674 – 773100Missing in isoform 4. 2 PublicationsVSP_013862Add
    BLAST
    Alternative sequencei674 – 72249Missing in isoform 5. 1 PublicationVSP_013863Add
    BLAST
    Alternative sequencei723 – 77351Missing in isoform 2. 2 PublicationsVSP_013864Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF221634 mRNA. Translation: AAG29766.1.
    AF221635 mRNA. Translation: AAG29767.1.
    AF221636 mRNA. Translation: AAG29768.1.
    AF221637 mRNA. Translation: AAG29769.1.
    AY172659 mRNA. Translation: AAO17261.1.
    AY354202 mRNA. Translation: AAQ63887.1.
    AK000290 mRNA. Translation: BAA91059.1. Frameshift.
    AK027826 mRNA. Translation: BAB55395.1. Different initiation.
    BC030688 mRNA. Translation: AAH30688.3.
    BC040203 mRNA. No translation available.
    AF176779 mRNA. Translation: AAQ13657.1. Different initiation.
    AF175225 mRNA. Translation: AAQ13650.1. Frameshift.
    AF173382 mRNA. Translation: AAQ13623.1. Frameshift.
    CCDSiCCDS10207.1. [Q6V1X1-1]
    CCDS10208.1. [Q6V1X1-2]
    CCDS10209.1. [Q6V1X1-4]
    CCDS10210.1. [Q6V1X1-3]
    RefSeqiNP_060213.2. NM_017743.4. [Q6V1X1-4]
    NP_569118.1. NM_130434.3. [Q6V1X1-3]
    NP_932064.1. NM_197960.2. [Q6V1X1-1]
    NP_932065.1. NM_197961.2. [Q6V1X1-2]
    XP_005254557.1. XM_005254500.1. [Q6V1X1-1]
    XP_011520031.1. XM_011521729.1. [Q6V1X1-1]
    UniGeneiHs.591106.

    Genome annotation databases

    EnsembliENST00000300141; ENSP00000300141; ENSG00000074603. [Q6V1X1-3]
    ENST00000321147; ENSP00000318111; ENSG00000074603. [Q6V1X1-2]
    ENST00000341861; ENSP00000339208; ENSG00000074603.
    ENST00000358939; ENSP00000351817; ENSG00000074603. [Q6V1X1-4]
    ENST00000559233; ENSP00000453954; ENSG00000074603.
    GeneIDi54878.
    KEGGihsa:54878.
    UCSCiuc002aov.3. human. [Q6V1X1-1]
    uc002aoy.3. human. [Q6V1X1-2]
    uc002aoz.3. human. [Q6V1X1-4]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF221634 mRNA. Translation: AAG29766.1.
    AF221635 mRNA. Translation: AAG29767.1.
    AF221636 mRNA. Translation: AAG29768.1.
    AF221637 mRNA. Translation: AAG29769.1.
    AY172659 mRNA. Translation: AAO17261.1.
    AY354202 mRNA. Translation: AAQ63887.1.
    AK000290 mRNA. Translation: BAA91059.1. Frameshift.
    AK027826 mRNA. Translation: BAB55395.1. Different initiation.
    BC030688 mRNA. Translation: AAH30688.3.
    BC040203 mRNA. No translation available.
    AF176779 mRNA. Translation: AAQ13657.1. Different initiation.
    AF175225 mRNA. Translation: AAQ13650.1. Frameshift.
    AF173382 mRNA. Translation: AAQ13623.1. Frameshift.
    CCDSiCCDS10207.1. [Q6V1X1-1]
    CCDS10208.1. [Q6V1X1-2]
    CCDS10209.1. [Q6V1X1-4]
    CCDS10210.1. [Q6V1X1-3]
    RefSeqiNP_060213.2. NM_017743.4. [Q6V1X1-4]
    NP_569118.1. NM_130434.3. [Q6V1X1-3]
    NP_932064.1. NM_197960.2. [Q6V1X1-1]
    NP_932065.1. NM_197961.2. [Q6V1X1-2]
    XP_005254557.1. XM_005254500.1. [Q6V1X1-1]
    XP_011520031.1. XM_011521729.1. [Q6V1X1-1]
    UniGeneiHs.591106.

    3D structure databases

    ProteinModelPortaliQ6V1X1.
    SMRiQ6V1X1. Positions 136-886.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi120226. 19 interactions.
    IntActiQ6V1X1. 3 interactions.
    MINTiMINT-4539721.
    STRINGi9606.ENSP00000339208.

    Chemistry

    BindingDBiQ6V1X1.
    ChEMBLiCHEMBL4657.
    GuidetoPHARMACOLOGYi2356.

    Protein family/group databases

    ESTHERihuman-DPP8. DPP4N_Peptidase_S9.
    MEROPSiS09.018.

    PTM databases

    PhosphoSiteiQ6V1X1.

    Polymorphism and mutation databases

    BioMutaiDPP8.
    DMDMi67460301.

    Proteomic databases

    MaxQBiQ6V1X1.
    PaxDbiQ6V1X1.
    PRIDEiQ6V1X1.

    Protocols and materials databases

    DNASUi54878.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000300141; ENSP00000300141; ENSG00000074603. [Q6V1X1-3]
    ENST00000321147; ENSP00000318111; ENSG00000074603. [Q6V1X1-2]
    ENST00000341861; ENSP00000339208; ENSG00000074603.
    ENST00000358939; ENSP00000351817; ENSG00000074603. [Q6V1X1-4]
    ENST00000559233; ENSP00000453954; ENSG00000074603.
    GeneIDi54878.
    KEGGihsa:54878.
    UCSCiuc002aov.3. human. [Q6V1X1-1]
    uc002aoy.3. human. [Q6V1X1-2]
    uc002aoz.3. human. [Q6V1X1-4]

    Organism-specific databases

    CTDi54878.
    GeneCardsiGC15M065734.
    HGNCiHGNC:16490. DPP8.
    HPAiHPA008706.
    MIMi606819. gene.
    neXtProtiNX_Q6V1X1.
    PharmGKBiPA27470.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG1506.
    GeneTreeiENSGT00760000119233.
    HOVERGENiHBG061620.
    InParanoidiQ6V1X1.
    KOiK08655.
    OMAiMDNRGTA.
    OrthoDBiEOG7XWPN8.
    PhylomeDBiQ6V1X1.
    TreeFamiTF313309.

    Enzyme and pathway databases

    SABIO-RKQ6V1X1.

    Miscellaneous databases

    ChiTaRSiDPP8. human.
    GeneWikiiDPP8.
    GenomeRNAii54878.
    NextBioi57817.
    PROiQ6V1X1.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ6V1X1.
    ExpressionAtlasiQ6V1X1. baseline and differential.
    GenevisibleiQ6V1X1. HS.

    Family and domain databases

    Gene3Di2.140.10.30. 1 hit.
    3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR001375. Peptidase_S9.
    IPR002469. Peptidase_S9B.
    [Graphical view]
    PfamiPF00930. DPPIV_N. 1 hit.
    PF00326. Peptidase_S9. 1 hit.
    [Graphical view]
    SUPFAMiSSF53474. SSF53474. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Cloning, expression and chromosomal localization of a novel human dipeptidyl peptidase (DPP) IV homolog, DPP8."
      Abbott C.A., Yu D.M.T., Woollatt E., Sutherland G.R., McCaughan G.W., Gorrell M.D.
      Eur. J. Biochem. 267:6140-6150(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [MRNA] OF 334-898 (ISOFORM 4), NUCLEOTIDE SEQUENCE [MRNA] OF 540-898 (ISOFORM 5), NUCLEOTIDE SEQUENCE [MRNA] OF 260-792 (ISOFORM 6), FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, TISSUE SPECIFICITY, INDUCTION, SUBCELLULAR LOCATION.
      Tissue: Placenta.
    2. "Cloning and characterization of dipeptidyl peptidase 10, a new member of an emerging subgroup of serine proteases."
      Qi S.Y., Riviere P.J., Trojnar J., Junien J.-L., Akinsanya K.O.
      Biochem. J. 373:179-189(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Testis.
    3. Sha J.H., Zhou Z.M., Li J.M.
      Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Testis.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 211-898 (ISOFORM 2).
      Tissue: Hepatoma and Placenta.
    5. "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] (ISOFORMS 1 AND 2).
      Tissue: Testis.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 561-898.
      Tissue: Aorta.
    7. "Structural requirements for catalysis, expression, and dimerization in the CD26/DPIV gene family."
      Ajami K., Abbott C.A., Obradovic M., Gysbers V., Kaehne T., McCaughan G.W., Gorrell M.D.
      Biochemistry 42:694-701(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF GLU-275; SER-755; ASP-833 AND HIS-865, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION.
    8. "Purification and characterization of human prolyl dipeptidase DPP8 in Sf9 insect cells."
      Chen Y.-S., Chien C.-H., Goparaju C.M., Hsu J.T.-A., Liang P.-H., Chen X.
      Protein Expr. Purif. 35:142-146(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
    9. "Novel isoindoline compounds for potent and selective inhibition of prolyl dipeptidase DPP8."
      Jiaang W.-T., Chen Y.-S., Hsu T., Wu S.-H., Chien C.-H., Chang C.-N., Chang S.-P., Lee S.-J., Chen X.
      Bioorg. Med. Chem. Lett. 15:687-691(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.

    Entry informationi

    Entry nameiDPP8_HUMAN
    AccessioniPrimary (citable) accession number: Q6V1X1
    Secondary accession number(s): Q7Z4C8
    , Q7Z4D3, Q7Z4E1, Q8IWG7, Q8NEM5, Q96JX1, Q9HBM2, Q9HBM3, Q9HBM4, Q9HBM5, Q9NXF4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2005
    Last sequence update: July 5, 2004
    Last modified: July 22, 2015
    This is version 104 of the entry and version 1 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

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 15
      Human chromosome 15: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. Peptidase families
      Classification of peptidase families and list of entries
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    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 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.