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Protein

Dipeptidyl peptidase 9

Gene

DPP9

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.

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 the serine proteinase inhibitor 4-(2-aminoethyl)benzenesulphonyl fluoride (AEBSF), and by di-isopropylfuorophosphate.1 Publication

Kineticsi

  1. KM=161 µM for Ala-Pro-AMC2 Publications
  2. KM=180 µM for Ala-Pro-AFC2 Publications

    pH dependencei

    Optimum pH is 7.5-8.5. Little activity below pH 6.5.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei730 – 7301Charge relay systemBy similarity
    Active sitei808 – 8081Charge relay systemBy similarity
    Active sitei840 – 8401Charge relay systemBy similarity

    GO - Molecular functioni

    • aminopeptidase activity Source: UniProtKB-KW
    • identical protein binding Source: IntAct
    • serine-type peptidase activity Source: UniProtKB-KW
    Complete GO annotation...

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Protease, Serine protease

    Enzyme and pathway databases

    SABIO-RKQ86TI2.

    Protein family/group databases

    ESTHERihuman-DPP9. DPP4N_Peptidase_S9.
    MEROPSiS09.019.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dipeptidyl peptidase 9 (EC:3.4.14.5)
    Short name:
    DP9
    Alternative name(s):
    Dipeptidyl peptidase IV-related protein 2
    Short name:
    DPRP-2
    Dipeptidyl peptidase IX
    Short name:
    DPP IX
    Dipeptidyl peptidase-like protein 9
    Short name:
    DPLP9
    Gene namesi
    Name:DPP9
    Synonyms:DPRP2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:18648. DPP9.

    Subcellular locationi

    Isoform 1 :
    Isoform 2 :
    • Nucleus 1 Publication

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    Orphaneti2032. Idiopathic pulmonary fibrosis.
    PharmGKBiPA38620.

    Polymorphism and mutation databases

    DMDMi67460390.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 863862Dipeptidyl peptidase 9PRO_0000122415Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ86TI2.
    PaxDbiQ86TI2.
    PRIDEiQ86TI2.

    PTM databases

    PhosphoSiteiQ86TI2.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed, with highest levels in liver, heart and muscle, and lowest levels in brain.3 Publications

    Gene expression databases

    BgeeiQ86TI2.
    ExpressionAtlasiQ86TI2. baseline and differential.
    GenevisibleiQ86TI2. HS.

    Organism-specific databases

    HPAiHPA036059.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-7475352,EBI-7475352

    Protein-protein interaction databases

    BioGridi124789. 31 interactions.
    MINTiMINT-4535936.
    STRINGi9606.ENSP00000262960.

    Structurei

    3D structure databases

    ProteinModelPortaliQ86TI2.
    SMRiQ86TI2. Positions 489-861.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase S9B family. DPPIV subfamily.Curated

    Phylogenomic databases

    eggNOGiCOG1506.
    GeneTreeiENSGT00760000119233.
    HOGENOMiHOG000006870.
    HOVERGENiHBG061620.
    InParanoidiQ86TI2.
    KOiK08656.
    OMAiDGRARCY.
    OrthoDBiEOG7XWPN8.
    PhylomeDBiQ86TI2.
    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 (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q86TI2-1) [UniParc]FASTAAdd to basket

    Also known as: DPP9-S, Short

    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
    MATTGTPTAD RGDAAATDDP AARFQVQKHS WDGLRSIIHG SRKYSGLIVN
    60 70 80 90 100
    KAPHDFQFVQ KTDESGPHSH RLYYLGMPYG SRENSLLYSE IPKKVRKEAL
    110 120 130 140 150
    LLLSWKQMLD HFQATPHHGV YSREEELLRE RKRLGVFGIT SYDFHSESGL
    160 170 180 190 200
    FLFQASNSLF HCRDGGKNGF MVSPMKPLEI KTQCSGPRMD PKICPADPAF
    210 220 230 240 250
    FSFINNSDLW VANIETGEER RLTFCHQGLS NVLDDPKSAG VATFVIQEEF
    260 270 280 290 300
    DRFTGYWWCP TASWEGSEGL KTLRILYEEV DESEVEVIHV PSPALEERKT
    310 320 330 340 350
    DSYRYPRTGS KNPKIALKLA EFQTDSQGKI VSTQEKELVQ PFSSLFPKVE
    360 370 380 390 400
    YIARAGWTRD GKYAWAMFLD RPQQWLQLVL LPPALFIPST ENEEQRLASA
    410 420 430 440 450
    RAVPRNVQPY VVYEEVTNVW INVHDIFYPF PQSEGEDELC FLRANECKTG
    460 470 480 490 500
    FCHLYKVTAV LKSQGYDWSE PFSPGEDEFK CPIKEEIALT SGEWEVLARH
    510 520 530 540 550
    GSKIWVNEET KLVYFQGTKD TPLEHHLYVV SYEAAGEIVR LTTPGFSHSC
    560 570 580 590 600
    SMSQNFDMFV SHYSSVSTPP CVHVYKLSGP DDDPLHKQPR FWASMMEAAS
    610 620 630 640 650
    CPPDYVPPEI FHFHTRSDVR LYGMIYKPHA LQPGKKHPTV LFVYGGPQVQ
    660 670 680 690 700
    LVNNSFKGIK YLRLNTLASL GYAVVVIDGR GSCQRGLRFE GALKNQMGQV
    710 720 730 740 750
    EIEDQVEGLQ FVAEKYGFID LSRVAIHGWS YGGFLSLMGL IHKPQVFKVA
    760 770 780 790 800
    IAGAPVTVWM AYDTGYTERY MDVPENNQHG YEAGSVALHV EKLPNEPNRL
    810 820 830 840 850
    LILHGFLDEN VHFFHTNFLV SQLIRAGKPY QLQIYPNERH SIRCPESGEH
    860
    YEVTLLHFLQ EYL
    Length:863
    Mass (Da):98,263
    Last modified:June 7, 2005 - v3
    Checksum:i40FE0B78E26CDED5
    GO
    Isoform 2 (identifier: Q86TI2-2) [UniParc]FASTAAdd to basket

    Also known as: DPP9-L, Long

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MRKVKKLRLDKENTGSWRSFSLNSEGAERM

    Note: Active peptidase. Contains a nuclear localization signal at positions 2-9.1 Publication
    Show »
    Length:892
    Mass (Da):101,669
    Checksum:i2CDB8E40E428AE73
    GO
    Isoform 3 (identifier: Q86TI2-4) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         832-858: Missing.

    Show »
    Length:836
    Mass (Da):95,013
    Checksum:iEF3B224CF112B857
    GO

    Sequence cautioni

    The sequence AAC33801.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
    The sequence AAC62840.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
    The sequence AAH37948.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence AAL47179.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence AAO73880.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
    The sequence BAB70784.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence BAC11362.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence BAC85150.1 differs from that shown.Probable cloning artifact.Curated
    The sequence BAD18643.1 differs from that shown.Aberrant splicing.Curated
    The sequence CAD39039.3 differs from that shown. Reason: Frameshift at positions 432 and 460. Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti204 – 2041I → N in AAO73880 (PubMed:15245913).Curated
    Sequence conflicti204 – 2041I → N in AAQ83119 (PubMed:15245913).Curated
    Sequence conflicti461 – 4611L → F in CAD39039 (PubMed:17974005).Curated
    Sequence conflicti571 – 5711C → W in BAC85150 (PubMed:14702039).Curated
    Sequence conflicti709 – 7091L → P in BAD18643 (PubMed:14702039).Curated
    Sequence conflicti753 – 7531G → C in BAB70784 (PubMed:14702039).Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MRKVKKLRLDKENTGSWRSF SLNSEGAERM in isoform 2. 4 PublicationsVSP_013865
    Alternative sequencei832 – 85827Missing in isoform 3. 1 PublicationVSP_013869Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF452102 mRNA. Translation: AAL47179.1. Different initiation.
    AY172660 mRNA. Translation: AAO17262.1.
    AF542510 mRNA. Translation: AAO73880.2. Different initiation.
    AY374518 mRNA. Translation: AAQ83119.1.
    DQ417928 mRNA. Translation: ABD83624.1.
    AK054656 mRNA. Translation: BAB70784.1. Different initiation.
    AK075030 mRNA. Translation: BAC11362.1. Different initiation.
    AK122654 mRNA. Translation: BAG53644.1.
    AK131100 mRNA. Translation: BAC85150.1. Sequence problems.
    AK131499 mRNA. Translation: BAD18643.1. Sequence problems.
    AC005594 Genomic DNA. Translation: AAC33801.1. Sequence problems.
    AC005783 Genomic DNA. Translation: AAC62840.1. Sequence problems.
    CH471139 Genomic DNA. Translation: EAW69199.1.
    CH471139 Genomic DNA. Translation: EAW69201.1.
    BC000970 mRNA. Translation: AAH00970.1.
    BC037948 mRNA. Translation: AAH37948.1. Different initiation.
    AL834376 mRNA. Translation: CAD39039.3. Frameshift.
    CR627380 mRNA. Translation: CAH10477.1.
    CCDSiCCDS45928.1. [Q86TI2-2]
    RefSeqiNP_631898.3. NM_139159.4. [Q86TI2-2]
    XP_005259730.1. XM_005259673.2. [Q86TI2-2]
    XP_011526710.1. XM_011528408.1. [Q86TI2-2]
    XP_011526712.1. XM_011528410.1. [Q86TI2-1]
    XP_011526713.1. XM_011528411.1. [Q86TI2-1]
    UniGeneiHs.515081.

    Genome annotation databases

    EnsembliENST00000262960; ENSP00000262960; ENSG00000142002. [Q86TI2-2]
    ENST00000594671; ENSP00000472224; ENSG00000142002. [Q86TI2-4]
    ENST00000598800; ENSP00000469603; ENSG00000142002.
    GeneIDi91039.
    KEGGihsa:91039.
    UCSCiuc002mba.3. human. [Q86TI2-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF452102 mRNA. Translation: AAL47179.1. Different initiation.
    AY172660 mRNA. Translation: AAO17262.1.
    AF542510 mRNA. Translation: AAO73880.2. Different initiation.
    AY374518 mRNA. Translation: AAQ83119.1.
    DQ417928 mRNA. Translation: ABD83624.1.
    AK054656 mRNA. Translation: BAB70784.1. Different initiation.
    AK075030 mRNA. Translation: BAC11362.1. Different initiation.
    AK122654 mRNA. Translation: BAG53644.1.
    AK131100 mRNA. Translation: BAC85150.1. Sequence problems.
    AK131499 mRNA. Translation: BAD18643.1. Sequence problems.
    AC005594 Genomic DNA. Translation: AAC33801.1. Sequence problems.
    AC005783 Genomic DNA. Translation: AAC62840.1. Sequence problems.
    CH471139 Genomic DNA. Translation: EAW69199.1.
    CH471139 Genomic DNA. Translation: EAW69201.1.
    BC000970 mRNA. Translation: AAH00970.1.
    BC037948 mRNA. Translation: AAH37948.1. Different initiation.
    AL834376 mRNA. Translation: CAD39039.3. Frameshift.
    CR627380 mRNA. Translation: CAH10477.1.
    CCDSiCCDS45928.1. [Q86TI2-2]
    RefSeqiNP_631898.3. NM_139159.4. [Q86TI2-2]
    XP_005259730.1. XM_005259673.2. [Q86TI2-2]
    XP_011526710.1. XM_011528408.1. [Q86TI2-2]
    XP_011526712.1. XM_011528410.1. [Q86TI2-1]
    XP_011526713.1. XM_011528411.1. [Q86TI2-1]
    UniGeneiHs.515081.

    3D structure databases

    ProteinModelPortaliQ86TI2.
    SMRiQ86TI2. Positions 489-861.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi124789. 31 interactions.
    MINTiMINT-4535936.
    STRINGi9606.ENSP00000262960.

    Chemistry

    BindingDBiQ86TI2.
    ChEMBLiCHEMBL4793.

    Protein family/group databases

    ESTHERihuman-DPP9. DPP4N_Peptidase_S9.
    MEROPSiS09.019.

    PTM databases

    PhosphoSiteiQ86TI2.

    Polymorphism and mutation databases

    DMDMi67460390.

    Proteomic databases

    MaxQBiQ86TI2.
    PaxDbiQ86TI2.
    PRIDEiQ86TI2.

    Protocols and materials databases

    DNASUi91039.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000262960; ENSP00000262960; ENSG00000142002. [Q86TI2-2]
    ENST00000594671; ENSP00000472224; ENSG00000142002. [Q86TI2-4]
    ENST00000598800; ENSP00000469603; ENSG00000142002.
    GeneIDi91039.
    KEGGihsa:91039.
    UCSCiuc002mba.3. human. [Q86TI2-2]

    Organism-specific databases

    CTDi91039.
    GeneCardsiGC19M004675.
    H-InvDBHIX0027578.
    HGNCiHGNC:18648. DPP9.
    HPAiHPA036059.
    MIMi608258. gene.
    neXtProtiNX_Q86TI2.
    Orphaneti2032. Idiopathic pulmonary fibrosis.
    PharmGKBiPA38620.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG1506.
    GeneTreeiENSGT00760000119233.
    HOGENOMiHOG000006870.
    HOVERGENiHBG061620.
    InParanoidiQ86TI2.
    KOiK08656.
    OMAiDGRARCY.
    OrthoDBiEOG7XWPN8.
    PhylomeDBiQ86TI2.
    TreeFamiTF313309.

    Enzyme and pathway databases

    SABIO-RKQ86TI2.

    Miscellaneous databases

    ChiTaRSiDPP9. human.
    GeneWikiiDPP9.
    GenomeRNAii91039.
    NextBioi77078.
    PROiQ86TI2.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ86TI2.
    ExpressionAtlasiQ86TI2. baseline and differential.
    GenevisibleiQ86TI2. 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. "Identification and characterization of human DPP9, a novel homologue of dipeptidyl peptidase IV."
      Olsen C., Wagtmann N.
      Gene 299:185-193(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
    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 1), CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
      Tissue: Colon.
    3. "Dipeptidyl peptidase 9 has two forms, a broad tissue distribution, cytoplasmic localization and DPIV-like peptidase activity."
      Ajami K., Abbott C.A., McCaughan G.W., Gorrell M.D.
      Biochim. Biophys. Acta 1679:18-28(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    4. "Dipeptidyl peptidases 8 and 9: specificity and molecular characterization compared with dipeptidyl peptidase IV."
      Bjelke J.R., Christensen J., Nielsen P.F., Branner S., Kanstrup A.B., Wagtmann N., Rasmussen H.B.
      Biochem. J. 396:391-399(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, SUBUNIT.
    5. "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 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 30-649 (ISOFORMS 1/3).
      Tissue: Glial tumor, Ovary, Spleen and Trachea.
    6. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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] (ISOFORM 2).
      Tissue: Placenta and Skin.
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 209-863 (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 298-863 (ISOFORMS 1/2).
      Tissue: Melanoma.
    10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "The amino terminus extension in the long dipeptidyl peptidase 9 isoform contains a nuclear localization signal targeting the active peptidase to the nucleus."
      Justa-Schuch D., Moller U., Geiss-Friedlander R.
      Cell. Mol. Life Sci. 71:3611-3626(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION (ISOFORM 2), NUCLEAR LOCALIZATION SIGNAL (ISOFORM 2).

    Entry informationi

    Entry nameiDPP9_HUMAN
    AccessioniPrimary (citable) accession number: Q86TI2
    Secondary accession number(s): O75273
    , O75868, Q1ZZB8, Q6AI37, Q6UAL0, Q6ZMT2, Q6ZNJ5, Q8N2J7, Q8N3F5, Q8WXD8, Q96NT8, Q9BVR3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2005
    Last sequence update: June 7, 2005
    Last modified: July 22, 2015
    This is version 119 of the entry and version 3 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 19
      Human chromosome 19: 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.