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Q6V1X1

- DPP8_HUMAN

UniProt

Q6V1X1 - DPP8_HUMAN

Protein

Dipeptidyl peptidase 8

Gene

DPP8

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    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

    1. dipeptidyl-peptidase activity Source: UniProtKB
    2. serine-type peptidase activity Source: UniProtKB-KW

    GO - Biological processi

    1. immune response Source: UniProtKB
    2. proteolysis Source: UniProtKB

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Protease, Serine protease

    Enzyme and pathway databases

    SABIO-RKQ6V1X1.

    Protein family/group databases

    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: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:16490. DPP8.

    Subcellular locationi

    Cytoplasm 3 Publications

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. membrane Source: InterPro
    3. nucleus Source: HPA

    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.

    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

    ArrayExpressiQ6V1X1.
    BgeeiQ6V1X1.
    GenevestigatoriQ6V1X1.

    Organism-specific databases

    HPAiHPA008706.

    Interactioni

    Protein-protein interaction databases

    BioGridi120226. 14 interactions.
    IntActiQ6V1X1. 3 interactions.
    MINTiMINT-4539721.

    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.
    HOVERGENiHBG061620.
    InParanoidiQ6V1X1.
    KOiK08655.
    OMAiSRHCDFF.
    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. Align

    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

    MWKRSEQMKI KSGKCNMAAA METEQLGVEI FETADCEENI ESQDRPKLEP    50
    FYVERYSWSQ LKKLLADTRK YHGYMMAKAP HDFMFVKRND PDGPHSDRIY 100
    YLAMSGENRE NTLFYSEIPK TINRAAVLML SWKPLLDLFQ ATLDYGMYSR 150
    EEELLRERKR IGTVGIASYD YHQGSGTFLF QAGSGIYHVK DGGPQGFTQQ 200
    PLRPNLVETS CPNIRMDPKL CPADPDWIAF IHSNDIWISN IVTREERRLT 250
    YVHNELANME EDARSAGVAT FVLQEEFDRY SGYWWCPKAE TTPSGGKILR 300
    ILYEENDESE VEIIHVTSPM LETRRADSFR YPKTGTANPK VTFKMSEIMI 350
    DAEGRIIDVI DKELIQPFEI LFEGVEYIAR AGWTPEGKYA WSILLDRSQT 400
    RLQIVLISPE LFIPVEDDVM ERQRLIESVP DSVTPLIIYE ETTDIWINIH 450
    DIFHVFPQSH EEEIEFIFAS ECKTGFRHLY KITSILKESK YKRSSGGLPA 500
    PSDFKCPIKE EIAITSGEWE VLGRHGSNIQ VDEVRRLVYF EGTKDSPLEH 550
    HLYVVSYVNP GEVTRLTDRG YSHSCCISQH CDFFISKYSN QKNPHCVSLY 600
    KLSSPEDDPT CKTKEFWATI LDSAGPLPDY TPPEIFSFES TTGFTLYGML 650
    YKPHDLQPGK KYPTVLFIYG GPQVQLVNNR FKGVKYFRLN TLASLGYVVV 700
    VIDNRGSCHR GLKFEGAFKY KMGQIEIDDQ VEGLQYLASR YDFIDLDRVG 750
    IHGWSYGGYL SLMALMQRSD IFRVAIAGAP VTLWIFYDTG YTERYMGHPD 800
    QNEQGYYLGS VAMQAEKFPS EPNRLLLLHG FLDENVHFAH TSILLSFLVR 850
    AGKPYDLQIY PQERHSIRVP ESGEHYELHL LHYLQENLGS RIAALKVI 898
    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.
    The sequence AAQ13650.1 differs from that shown. Reason: Frameshift at several positions.
    The sequence BAA91059.1 differs from that shown. Reason: Frameshift at position 486.
    The sequence AAQ13657.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAB55395.1 differs from that shown. Reason: Erroneous initiation.

    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. 1 PublicationCurated
    Sequence conflicti686 – 6861Y → F in AAQ13650. 1 PublicationCurated
    Sequence conflicti693 – 6942AS → PF in AAQ13650. 1 PublicationCurated
    Sequence conflicti701 – 7011V → G in AAQ13650. 1 PublicationCurated
    Sequence conflicti709 – 7091H → P in AAQ13650. 1 PublicationCurated
    Sequence conflicti720 – 7201Y → F in AAQ13650. 1 PublicationCurated
    Sequence conflicti799 – 8035PDQNE → LTRMN in AAQ13623. 1 PublicationCurated
    Sequence conflicti820 – 8201S → F in AAQ13623. 1 PublicationCurated

    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:
    EMBL
    GenBank
    DDBJ
    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]
    UniGeneiHs.591106.

    Genome annotation databases

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

    Polymorphism databases

    DMDMi67460301.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    CCDSi CCDS10207.1. [Q6V1X1-1 ]
    CCDS10208.1. [Q6V1X1-2 ]
    CCDS10209.1. [Q6V1X1-4 ]
    CCDS10210.1. [Q6V1X1-3 ]
    RefSeqi NP_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 ]
    UniGenei Hs.591106.

    3D structure databases

    ProteinModelPortali Q6V1X1.
    SMRi Q6V1X1. Positions 136-886.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120226. 14 interactions.
    IntActi Q6V1X1. 3 interactions.
    MINTi MINT-4539721.

    Chemistry

    BindingDBi Q6V1X1.
    ChEMBLi CHEMBL4657.
    GuidetoPHARMACOLOGYi 2356.

    Protein family/group databases

    MEROPSi S09.018.

    PTM databases

    PhosphoSitei Q6V1X1.

    Polymorphism databases

    DMDMi 67460301.

    Proteomic databases

    MaxQBi Q6V1X1.
    PaxDbi Q6V1X1.
    PRIDEi Q6V1X1.

    Protocols and materials databases

    DNASUi 54878.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000300141 ; ENSP00000300141 ; ENSG00000074603 . [Q6V1X1-3 ]
    ENST00000321147 ; ENSP00000318111 ; ENSG00000074603 . [Q6V1X1-2 ]
    ENST00000341861 ; ENSP00000339208 ; ENSG00000074603 . [Q6V1X1-1 ]
    ENST00000358939 ; ENSP00000351817 ; ENSG00000074603 . [Q6V1X1-4 ]
    ENST00000559233 ; ENSP00000453954 ; ENSG00000074603 . [Q6V1X1-1 ]
    GeneIDi 54878.
    KEGGi hsa:54878.
    UCSCi uc002aov.3. human. [Q6V1X1-1 ]
    uc002aoy.3. human. [Q6V1X1-2 ]
    uc002aoz.3. human. [Q6V1X1-4 ]

    Organism-specific databases

    CTDi 54878.
    GeneCardsi GC15M065734.
    HGNCi HGNC:16490. DPP8.
    HPAi HPA008706.
    MIMi 606819. gene.
    neXtProti NX_Q6V1X1.
    PharmGKBi PA27470.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1506.
    HOVERGENi HBG061620.
    InParanoidi Q6V1X1.
    KOi K08655.
    OMAi SRHCDFF.
    OrthoDBi EOG7XWPN8.
    PhylomeDBi Q6V1X1.
    TreeFami TF313309.

    Enzyme and pathway databases

    SABIO-RK Q6V1X1.

    Miscellaneous databases

    GeneWikii DPP8.
    GenomeRNAii 54878.
    NextBioi 57817.
    PROi Q6V1X1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q6V1X1.
    Bgeei Q6V1X1.
    Genevestigatori Q6V1X1.

    Family and domain databases

    Gene3Di 2.140.10.30. 1 hit.
    3.40.50.1820. 1 hit.
    InterProi IPR029058. AB_hydrolase.
    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.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 97 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