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Q9UHL4

- DPP2_HUMAN

UniProt

Q9UHL4 - DPP2_HUMAN

Protein

Dipeptidyl peptidase 2

Gene

DPP7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 3 (04 Nov 2008)
      Previous versions | rss
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    Functioni

    Plays an important role in the degradation of some oligopeptides.1 Publication

    Catalytic activityi

    Release of an N-terminal dipeptide, Xaa-Yaa-|-, preferentially when Yaa is Ala or Pro. Substrates are oligopeptides, preferentially tripeptides.1 Publication

    pH dependencei

    Optimum pH is 5.5. Has low activity at pH 7 and is inactive at pH 8.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei162 – 1621Charge relay systemSequence Analysis
    Active sitei418 – 4181Charge relay systemSequence Analysis
    Active sitei443 – 4431Charge relay systemSequence Analysis

    GO - Molecular functioni

    1. dipeptidyl-peptidase activity Source: Ensembl
    2. serine-type peptidase activity Source: ProtInc

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Protease, Serine protease

    Protein family/group databases

    MEROPSiS28.002.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dipeptidyl peptidase 2 (EC:3.4.14.2)
    Alternative name(s):
    Dipeptidyl aminopeptidase II
    Dipeptidyl peptidase 7
    Dipeptidyl peptidase II
    Short name:
    DPP II
    Quiescent cell proline dipeptidase
    Gene namesi
    Name:DPP7
    Synonyms:DPP2, QPP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:14892. DPP7.

    Subcellular locationi

    Lysosome 1 Publication. Cytoplasmic vesicle 1 Publication. Secreted 1 Publication

    GO - Cellular componenti

    1. cytoplasmic membrane-bounded vesicle Source: UniProtKB-SubCell
    2. cytosol Source: Ensembl
    3. extracellular vesicular exosome Source: UniProt
    4. lysosome Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasmic vesicle, Lysosome, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27469.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Sequence AnalysisAdd
    BLAST
    Propeptidei22 – 254Sequence AnalysisPRO_0000027314
    Chaini26 – 492467Dipeptidyl peptidase 2PRO_0000027315Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi50 – 501N-linked (GlcNAc...)2 Publications
    Glycosylationi86 – 861N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi315 – 3151N-linked (GlcNAc...)2 Publications
    Glycosylationi356 – 3561N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi363 – 3631N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi428 – 4281N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    N-glycosylated.2 Publications

    Keywords - PTMi

    Cleavage on pair of basic residues, Glycoprotein, Zymogen

    Proteomic databases

    MaxQBiQ9UHL4.
    PaxDbiQ9UHL4.
    PRIDEiQ9UHL4.

    PTM databases

    PhosphoSiteiQ9UHL4.

    Expressioni

    Tissue specificityi

    Detected in seminal plasma (at protein level).1 Publication

    Gene expression databases

    BgeeiQ9UHL4.
    CleanExiHS_DPP7.
    GenevestigatoriQ9UHL4.

    Organism-specific databases

    HPAiCAB025541.
    HPA021282.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi118989. 10 interactions.
    IntActiQ9UHL4. 8 interactions.
    STRINGi9606.ENSP00000360635.

    Structurei

    Secondary structure

    1
    492
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi32 – 409
    Turni47 – 504
    Beta strandi52 – 609
    Turni66 – 683
    Beta strandi71 – 755
    Helixi81 – 877
    Helixi89 – 9810
    Beta strandi101 – 1055
    Helixi117 – 1215
    Helixi131 – 14818
    Beta strandi156 – 1616
    Helixi163 – 17412
    Turni176 – 1783
    Beta strandi180 – 1856
    Helixi191 – 1933
    Helixi200 – 21011
    Helixi214 – 23320
    Helixi236 – 2438
    Beta strandi245 – 2473
    Helixi252 – 27120
    Beta strandi278 – 2847
    Helixi288 – 29710
    Helixi302 – 31413
    Beta strandi316 – 3183
    Beta strandi321 – 3233
    Helixi325 – 3284
    Helixi342 – 35110
    Turni352 – 3543
    Beta strandi363 – 3686
    Helixi375 – 38612
    Helixi394 – 3996
    Beta strandi409 – 4157
    Helixi421 – 4233
    Beta strandi430 – 4389
    Helixi445 – 4473
    Helixi456 – 47621

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3JYHX-ray2.19A/B/C/D28-492[»]
    3N0TX-ray2.45A/B/C/D28-492[»]
    4EBBX-ray2.00A/B27-492[»]
    ProteinModelPortaliQ9UHL4.
    SMRiQ9UHL4. Positions 28-477.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UHL4.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase S28 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG290141.
    HOGENOMiHOG000238311.
    HOVERGENiHBG005526.
    InParanoidiQ9UHL4.
    KOiK01276.
    OMAiVWPRPDW.
    OrthoDBiEOG78WKRN.
    PhylomeDBiQ9UHL4.
    TreeFamiTF314414.

    Family and domain databases

    Gene3Di3.40.50.1820. 2 hits.
    InterProiIPR029058. AB_hydrolase.
    IPR008758. Peptidase_S28.
    [Graphical view]
    PANTHERiPTHR11010. PTHR11010. 1 hit.
    PfamiPF05577. Peptidase_S28. 1 hit.
    [Graphical view]
    SUPFAMiSSF53474. SSF53474. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q9UHL4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGSAPWAPVL LLALGLRGLQ AGARRAPDPG FQERFFQQRL DHFNFERFGN    50
    KTFPQRFLVS DRFWVRGEGP IFFYTGNEGD VWAFANNSAF VAELAAERGA 100
    LLVFAEHRYY GKSLPFGAQS TQRGHTELLT VEQALADFAE LLRALRRDLG 150
    AQDAPAIAFG GSYGGMLSAY LRMKYPHLVA GALAASAPVL AVAGLGDSNQ 200
    FFRDVTADFE GQSPKCTQGV REAFRQIKDL FLQGAYDTVR WEFGTCQPLS 250
    DEKDLTQLFM FARNAFTVLA MMDYPYPTDF LGPLPANPVK VGCDRLLSEA 300
    QRITGLRALA GLVYNASGSE HCYDIYRLYH SCADPTGCGT GPDARAWDYQ 350
    ACTEINLTFA SNNVTDMFPD LPFTDELRQR YCLDTWGVWP RPDWLLTSFW 400
    GGDLRAASNI IFSNGNLDPW AGGGIRRNLS ASVIAVTIQG GAHHLDLRAS 450
    HPEDPASVVE ARKLEATIIG EWVKAARREQ QPALRGGPRL SL 492
    Length:492
    Mass (Da):54,341
    Last modified:November 4, 2008 - v3
    Checksum:i6C3EDECA90FA7583
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti71 – 711I → T in AAF12747. (PubMed:10567372)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti89 – 891A → G.2 Publications
    Corresponds to variant rs10747049 [ dbSNP | Ensembl ].
    VAR_047087

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF154502 mRNA. Translation: AAF12747.1.
    AK292112 mRNA. Translation: BAF84801.1.
    AL929554 Genomic DNA. Translation: CAH72872.1.
    BC011907 mRNA. Translation: AAH11907.1.
    BC016961 mRNA. Translation: AAH16961.1.
    CCDSiCCDS7030.1.
    PIRiS77568.
    RefSeqiNP_037511.2. NM_013379.2.
    UniGeneiHs.37916.

    Genome annotation databases

    EnsembliENST00000371579; ENSP00000360635; ENSG00000176978.
    GeneIDi29952.
    KEGGihsa:29952.
    UCSCiuc004clh.3. human.

    Polymorphism databases

    DMDMi212276510.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF154502 mRNA. Translation: AAF12747.1 .
    AK292112 mRNA. Translation: BAF84801.1 .
    AL929554 Genomic DNA. Translation: CAH72872.1 .
    BC011907 mRNA. Translation: AAH11907.1 .
    BC016961 mRNA. Translation: AAH16961.1 .
    CCDSi CCDS7030.1.
    PIRi S77568.
    RefSeqi NP_037511.2. NM_013379.2.
    UniGenei Hs.37916.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3JYH X-ray 2.19 A/B/C/D 28-492 [» ]
    3N0T X-ray 2.45 A/B/C/D 28-492 [» ]
    4EBB X-ray 2.00 A/B 27-492 [» ]
    ProteinModelPortali Q9UHL4.
    SMRi Q9UHL4. Positions 28-477.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118989. 10 interactions.
    IntActi Q9UHL4. 8 interactions.
    STRINGi 9606.ENSP00000360635.

    Chemistry

    BindingDBi Q9UHL4.
    ChEMBLi CHEMBL3976.
    GuidetoPHARMACOLOGYi 1605.

    Protein family/group databases

    MEROPSi S28.002.

    PTM databases

    PhosphoSitei Q9UHL4.

    Polymorphism databases

    DMDMi 212276510.

    Proteomic databases

    MaxQBi Q9UHL4.
    PaxDbi Q9UHL4.
    PRIDEi Q9UHL4.

    Protocols and materials databases

    DNASUi 29952.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000371579 ; ENSP00000360635 ; ENSG00000176978 .
    GeneIDi 29952.
    KEGGi hsa:29952.
    UCSCi uc004clh.3. human.

    Organism-specific databases

    CTDi 29952.
    GeneCardsi GC09M140004.
    H-InvDB HIX0017204.
    HIX0025819.
    HGNCi HGNC:14892. DPP7.
    HPAi CAB025541.
    HPA021282.
    MIMi 610537. gene.
    neXtProti NX_Q9UHL4.
    PharmGKBi PA27469.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG290141.
    HOGENOMi HOG000238311.
    HOVERGENi HBG005526.
    InParanoidi Q9UHL4.
    KOi K01276.
    OMAi VWPRPDW.
    OrthoDBi EOG78WKRN.
    PhylomeDBi Q9UHL4.
    TreeFami TF314414.

    Miscellaneous databases

    EvolutionaryTracei Q9UHL4.
    GeneWikii DPP7.
    GenomeRNAii 29952.
    NextBioi 52649.
    PROi Q9UHL4.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9UHL4.
    CleanExi HS_DPP7.
    Genevestigatori Q9UHL4.

    Family and domain databases

    Gene3Di 3.40.50.1820. 2 hits.
    InterProi IPR029058. AB_hydrolase.
    IPR008758. Peptidase_S28.
    [Graphical view ]
    PANTHERi PTHR11010. PTHR11010. 1 hit.
    Pfami PF05577. Peptidase_S28. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53474. SSF53474. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Sequence, purification, and cloning of an intracellular serine protease, quiescent cell proline dipeptidase."
      Underwood R., Chiravuri M., Lee H., Schmitz T., Kabcenell A.K., Yardley Y., Huber B.T.
      J. Biol. Chem. 274:34053-34058(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, VARIANT GLY-89.
    2. "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].
      Tissue: Synovial cell.
    3. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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], VARIANT GLY-89.
      Tissue: Brain.
    5. "Vesicular localization and characterization of a novel post-proline-cleaving aminodipeptidase, quiescent cell proline dipeptidase."
      Chiravuri M., Agarraberes F., Mathieu S.L., Lee H., Huber B.T.
      J. Immunol. 165:5695-5702(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    6. "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-50 AND ASN-315.
      Tissue: Liver.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "Kinetic investigation of human dipeptidyl peptidase II (DPPII)-mediated hydrolysis of dipeptide derivatives and its identification as quiescent cell proline dipeptidase (QPP)/dipeptidyl peptidase 7 (DPP7)."
      Maes M.B., Lambeir A.M., Gilany K., Senten K., Van der Veken P., Leiting B., Augustyns K., Scharpe S., De Meester I.
      Biochem. J. 386:315-324(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS) OF 28-492, PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, GLYCOSYLATION, TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiDPP2_HUMAN
    AccessioniPrimary (citable) accession number: Q9UHL4
    Secondary accession number(s): A8K7U7, Q5VSF1, Q969X4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: November 4, 2008
    Last modified: October 1, 2014
    This is version 128 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Peptidase families
      Classification of peptidase families and list of entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3