Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

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

Q86TI2

- DPP9_HUMAN

UniProt

Q86TI2 - DPP9_HUMAN

Protein

Dipeptidyl peptidase 9

Gene

DPP9

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 3 (07 Jun 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    1. aminopeptidase activity Source: UniProtKB-KW
    2. identical protein binding Source: IntAct
    3. serine-type peptidase activity Source: UniProtKB-KW

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Protease, Serine protease

    Enzyme and pathway databases

    SABIO-RKQ86TI2.

    Protein family/group databases

    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: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:18648. DPP9.

    Subcellular locationi

    Cytoplasmcytosol 2 Publications

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: UniProtKB-SubCell
    3. membrane Source: InterPro

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    Orphaneti2032. Idiopathic pulmonary fibrosis.
    PharmGKBiPA38620.

    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

    ArrayExpressiQ86TI2.
    BgeeiQ86TI2.
    GenevestigatoriQ86TI2.

    Organism-specific databases

    HPAiHPA036059.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Binary interactionsi

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

    Protein-protein interaction databases

    BioGridi124789. 17 interactions.
    MINTiMINT-4535936.

    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.
    HOVERGENiHBG061620.
    InParanoidiQ86TI2.
    KOiK08656.
    OMAiFPRVEYI.
    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. Align

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

    Also known as: 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

    MATTGTPTAD RGDAAATDDP AARFQVQKHS WDGLRSIIHG SRKYSGLIVN    50
    KAPHDFQFVQ KTDESGPHSH RLYYLGMPYG SRENSLLYSE IPKKVRKEAL 100
    LLLSWKQMLD HFQATPHHGV YSREEELLRE RKRLGVFGIT SYDFHSESGL 150
    FLFQASNSLF HCRDGGKNGF MVSPMKPLEI KTQCSGPRMD PKICPADPAF 200
    FSFINNSDLW VANIETGEER RLTFCHQGLS NVLDDPKSAG VATFVIQEEF 250
    DRFTGYWWCP TASWEGSEGL KTLRILYEEV DESEVEVIHV PSPALEERKT 300
    DSYRYPRTGS KNPKIALKLA EFQTDSQGKI VSTQEKELVQ PFSSLFPKVE 350
    YIARAGWTRD GKYAWAMFLD RPQQWLQLVL LPPALFIPST ENEEQRLASA 400
    RAVPRNVQPY VVYEEVTNVW INVHDIFYPF PQSEGEDELC FLRANECKTG 450
    FCHLYKVTAV LKSQGYDWSE PFSPGEDEFK CPIKEEIALT SGEWEVLARH 500
    GSKIWVNEET KLVYFQGTKD TPLEHHLYVV SYEAAGEIVR LTTPGFSHSC 550
    SMSQNFDMFV SHYSSVSTPP CVHVYKLSGP DDDPLHKQPR FWASMMEAAS 600
    CPPDYVPPEI FHFHTRSDVR LYGMIYKPHA LQPGKKHPTV LFVYGGPQVQ 650
    LVNNSFKGIK YLRLNTLASL GYAVVVIDGR GSCQRGLRFE GALKNQMGQV 700
    EIEDQVEGLQ FVAEKYGFID LSRVAIHGWS YGGFLSLMGL IHKPQVFKVA 750
    IAGAPVTVWM AYDTGYTERY MDVPENNQHG YEAGSVALHV EKLPNEPNRL 800
    LILHGFLDEN VHFFHTNFLV SQLIRAGKPY QLQIYPNERH SIRCPESGEH 850
    YEVTLLHFLQ EYL 863
    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: Long

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

    Note: Incomplete sequence.

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

    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:
    EMBL
    GenBank
    DDBJ
    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]
    UniGeneiHs.515081.

    Genome annotation databases

    EnsembliENST00000262960; ENSP00000262960; ENSG00000142002. [Q86TI2-2]
    ENST00000594671; ENSP00000472224; ENSG00000142002. [Q86TI2-4]
    ENST00000598800; ENSP00000469603; ENSG00000142002. [Q86TI2-1]
    GeneIDi91039.
    KEGGihsa:91039.
    UCSCiuc002mba.3. human. [Q86TI2-2]

    Polymorphism databases

    DMDMi67460390.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS45928.1. [Q86TI2-2 ]
    RefSeqi NP_631898.3. NM_139159.4. [Q86TI2-2 ]
    XP_005259730.1. XM_005259673.2. [Q86TI2-2 ]
    UniGenei Hs.515081.

    3D structure databases

    ProteinModelPortali Q86TI2.
    SMRi Q86TI2. Positions 489-861.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 124789. 17 interactions.
    MINTi MINT-4535936.

    Chemistry

    BindingDBi Q86TI2.
    ChEMBLi CHEMBL4793.

    Protein family/group databases

    MEROPSi S09.019.

    PTM databases

    PhosphoSitei Q86TI2.

    Polymorphism databases

    DMDMi 67460390.

    Proteomic databases

    MaxQBi Q86TI2.
    PaxDbi Q86TI2.
    PRIDEi Q86TI2.

    Protocols and materials databases

    DNASUi 91039.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000262960 ; ENSP00000262960 ; ENSG00000142002 . [Q86TI2-2 ]
    ENST00000594671 ; ENSP00000472224 ; ENSG00000142002 . [Q86TI2-4 ]
    ENST00000598800 ; ENSP00000469603 ; ENSG00000142002 . [Q86TI2-1 ]
    GeneIDi 91039.
    KEGGi hsa:91039.
    UCSCi uc002mba.3. human. [Q86TI2-2 ]

    Organism-specific databases

    CTDi 91039.
    GeneCardsi GC19M004675.
    H-InvDB HIX0027578.
    HGNCi HGNC:18648. DPP9.
    HPAi HPA036059.
    MIMi 608258. gene.
    neXtProti NX_Q86TI2.
    Orphaneti 2032. Idiopathic pulmonary fibrosis.
    PharmGKBi PA38620.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1506.
    HOVERGENi HBG061620.
    InParanoidi Q86TI2.
    KOi K08656.
    OMAi FPRVEYI.
    OrthoDBi EOG7XWPN8.
    PhylomeDBi Q86TI2.
    TreeFami TF313309.

    Enzyme and pathway databases

    SABIO-RK Q86TI2.

    Miscellaneous databases

    ChiTaRSi DPP9. human.
    GeneWikii DPP9.
    GenomeRNAii 91039.
    NextBioi 77078.
    PROi Q86TI2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q86TI2.
    Bgeei Q86TI2.
    Genevestigatori Q86TI2.

    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. "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].

    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: October 1, 2014
    This is version 112 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