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Q9H4A9

- DPEP2_HUMAN

UniProt

Q9H4A9 - DPEP2_HUMAN

Protein

Dipeptidase 2

Gene

DPEP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 2 (18 May 2010)
      Previous versions | rss
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    Functioni

    Probable metalloprotease which hydrolyzes leukotriene D4 (LTD4) into leukotriene E4 (LTE4).By similarity

    Catalytic activityi

    Hydrolysis of dipeptides.PROSITE-ProRule annotation

    Cofactori

    Zinc.PROSITE-ProRule annotation

    Enzyme regulationi

    Inhibited by L-penicillamine.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi89 – 891Zinc 1; catalyticPROSITE-ProRule annotation
    Metal bindingi91 – 911Zinc 1; catalyticPROSITE-ProRule annotation
    Metal bindingi188 – 1881Zinc 1; catalyticPROSITE-ProRule annotation
    Metal bindingi188 – 1881Zinc 2; catalyticPROSITE-ProRule annotation
    Binding sitei215 – 2151SubstratePROSITE-ProRule annotation
    Metal bindingi261 – 2611Zinc 2; catalyticPROSITE-ProRule annotation
    Metal bindingi282 – 2821Zinc 2; catalyticPROSITE-ProRule annotation
    Binding sitei293 – 2931SubstratePROSITE-ProRule annotation
    Binding sitei351 – 3511SubstratePROSITE-ProRule annotation

    GO - Molecular functioni

    1. dipeptidase activity Source: UniProtKB-KW
    2. dipeptidyl-peptidase activity Source: InterPro
    3. metal ion binding Source: UniProtKB-KW
    4. metalloexopeptidase activity Source: InterPro

    GO - Biological processi

    1. arachidonic acid metabolic process Source: Reactome
    2. leukotriene metabolic process Source: Reactome
    3. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Dipeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciMetaCyc:HS09532-MONOMER.
    ReactomeiREACT_150420. Synthesis of Leukotrienes (LT) and Eoxins (EX).

    Protein family/group databases

    MEROPSiM19.002.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dipeptidase 2 (EC:3.4.13.19)
    Gene namesi
    Name:DPEP2
    ORF Names:UNQ284/PRO323
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:23028. DPEP2.

    Subcellular locationi

    Membrane By similarity; Lipid-anchorGPI-anchor By similarity

    GO - Cellular componenti

    1. anchored component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134985997.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3232Sequence AnalysisAdd
    BLAST
    Chaini33 – 463431Dipeptidase 2PRO_0000231603Add
    BLAST
    Propeptidei464 – 48623Removed in mature formSequence AnalysisPRO_0000231604Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi111 – 1111N-linked (GlcNAc...)1 Publication
    Disulfide bondi138 ↔ 217PROSITE-ProRule annotation
    Glycosylationi176 – 1761N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi235 – 2351N-linked (GlcNAc...)1 Publication
    Disulfide bondi289 ↔ 321PROSITE-ProRule annotation
    Disulfide bondi426 – 426InterchainPROSITE-ProRule annotation
    Lipidationi463 – 4631GPI-anchor amidated serineSequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

    Proteomic databases

    PaxDbiQ9H4A9.
    PRIDEiQ9H4A9.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9H4A9.
    BgeeiQ9H4A9.
    CleanExiHS_DPEP2.
    GenevestigatoriQ9H4A9.

    Organism-specific databases

    HPAiHPA035644.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked.PROSITE-ProRule annotation

    Protein-protein interaction databases

    BioGridi122097. 1 interaction.
    IntActiQ9H4A9. 1 interaction.
    STRINGi9606.ENSP00000268795.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9H4A9.
    SMRiQ9H4A9. Positions 72-428.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M19 family.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG2355.
    HOGENOMiHOG000072016.
    HOVERGENiHBG002339.
    InParanoidiQ9H4A9.
    OMAiDTQKLAC.
    OrthoDBiEOG7SJD4N.
    PhylomeDBiQ9H4A9.
    TreeFamiTF324523.

    Family and domain databases

    InterProiIPR000180. Dipep_AS.
    IPR028531. Dpep2.
    IPR008257. Renal_dipep_fam.
    [Graphical view]
    PANTHERiPTHR10443. PTHR10443. 1 hit.
    PTHR10443:SF9. PTHR10443:SF9. 1 hit.
    PfamiPF01244. Peptidase_M19. 1 hit.
    [Graphical view]
    PROSITEiPS00869. RENAL_DIPEPTIDASE_1. 1 hit.
    PS51365. RENAL_DIPEPTIDASE_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9H4A9-1) [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

    MQPSGLEGPG TFGRWPLLSL LLLLLLLQPV TCAYTTPGPP RALTTLGAPR    50
    AHTMPGTYAP STTLSSPSTQ GLQEQARALM RDFPLVDGHN DLPLVLRQVY 100
    QKGLQDVNLR NFSYGQTSLD RLRDGLVGAQ FWSAYVPCQT QDRDALRLTL 150
    EQIDLIRRMC ASYSELELVT SAKALNDTQK LACLIGVEGG HSLDNSLSIL 200
    PTFYMLGVRY LTLTHTCNTP WAESSAKGVH SFYNNISGLT DFGEKVVAEM 250
    NRLGMMVDLS HVSDAVARRA LEVSQAPVIF SHSAARGVCN SARNVPDDIL 300
    QLLKKNGGVV MVSLSMGVIQ CNPSANVSTV ADHFDHIKAV IGSKFIGIGG 350
    DYDGAGKFPQ GLEDVSTYPV LIEELLSRGW SEEELQGVLR GNLLRVFRQV 400
    EKVQEENKWQ SPLEDKFPDE QLSSSCHSDL SRLRQRQSLT SGQELTEIPI 450
    HWTAKLPAKW SVSESSPHMA PVLAVVATFP VLILWL 486
    Length:486
    Mass (Da):53,306
    Last modified:May 18, 2010 - v2
    Checksum:iB08130A393809D04
    GO
    Isoform 2 (identifier: Q9H4A9-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         43-129: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:399
    Mass (Da):43,828
    Checksum:i7BB6FA876E7D7B9E
    GO

    Sequence cautioni

    The sequence AAQ88819.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti201 – 2011P → R.5 Publications
    Corresponds to variant rs255051 [ dbSNP | Ensembl ].
    VAR_060230
    Natural varianti468 – 4681H → D.
    Corresponds to variant rs1133090 [ dbSNP | Ensembl ].
    VAR_033894

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei43 – 12987Missing in isoform 2. 1 PublicationVSP_017851Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ295149 mRNA. Translation: CAC14667.1.
    AK315090 mRNA. Translation: BAG37555.1.
    AC040162 Genomic DNA. No translation available.
    CH471092 Genomic DNA. Translation: EAW83200.1.
    BC024021 mRNA. Translation: AAH24021.1.
    AY358454 mRNA. Translation: AAQ88819.1. Different initiation.
    CCDSiCCDS10857.1. [Q9H4A9-1]
    RefSeqiNP_071750.1. NM_022355.3.
    XP_005256142.2. XM_005256085.2.
    XP_005256143.2. XM_005256086.2.
    XP_005256144.2. XM_005256087.2.
    UniGeneiHs.372633.

    Genome annotation databases

    EnsembliENST00000393847; ENSP00000377430; ENSG00000167261. [Q9H4A9-1]
    ENST00000572888; ENSP00000458977; ENSG00000167261. [Q9H4A9-1]
    GeneIDi64174.
    KEGGihsa:64174.
    UCSCiuc002eve.4. human. [Q9H4A9-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ295149 mRNA. Translation: CAC14667.1 .
    AK315090 mRNA. Translation: BAG37555.1 .
    AC040162 Genomic DNA. No translation available.
    CH471092 Genomic DNA. Translation: EAW83200.1 .
    BC024021 mRNA. Translation: AAH24021.1 .
    AY358454 mRNA. Translation: AAQ88819.1 . Different initiation.
    CCDSi CCDS10857.1. [Q9H4A9-1 ]
    RefSeqi NP_071750.1. NM_022355.3.
    XP_005256142.2. XM_005256085.2.
    XP_005256143.2. XM_005256086.2.
    XP_005256144.2. XM_005256087.2.
    UniGenei Hs.372633.

    3D structure databases

    ProteinModelPortali Q9H4A9.
    SMRi Q9H4A9. Positions 72-428.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122097. 1 interaction.
    IntActi Q9H4A9. 1 interaction.
    STRINGi 9606.ENSP00000268795.

    Protein family/group databases

    MEROPSi M19.002.

    Proteomic databases

    PaxDbi Q9H4A9.
    PRIDEi Q9H4A9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000393847 ; ENSP00000377430 ; ENSG00000167261 . [Q9H4A9-1 ]
    ENST00000572888 ; ENSP00000458977 ; ENSG00000167261 . [Q9H4A9-1 ]
    GeneIDi 64174.
    KEGGi hsa:64174.
    UCSCi uc002eve.4. human. [Q9H4A9-1 ]

    Organism-specific databases

    CTDi 64174.
    GeneCardsi GC16M068021.
    HGNCi HGNC:23028. DPEP2.
    HPAi HPA035644.
    MIMi 609925. gene.
    neXtProti NX_Q9H4A9.
    PharmGKBi PA134985997.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2355.
    HOGENOMi HOG000072016.
    HOVERGENi HBG002339.
    InParanoidi Q9H4A9.
    OMAi DTQKLAC.
    OrthoDBi EOG7SJD4N.
    PhylomeDBi Q9H4A9.
    TreeFami TF324523.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS09532-MONOMER.
    Reactomei REACT_150420. Synthesis of Leukotrienes (LT) and Eoxins (EX).

    Miscellaneous databases

    GenomeRNAii 64174.
    NextBioi 66091.
    PROi Q9H4A9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9H4A9.
    Bgeei Q9H4A9.
    CleanExi HS_DPEP2.
    Genevestigatori Q9H4A9.

    Family and domain databases

    InterProi IPR000180. Dipep_AS.
    IPR028531. Dpep2.
    IPR008257. Renal_dipep_fam.
    [Graphical view ]
    PANTHERi PTHR10443. PTHR10443. 1 hit.
    PTHR10443:SF9. PTHR10443:SF9. 1 hit.
    Pfami PF01244. Peptidase_M19. 1 hit.
    [Graphical view ]
    PROSITEi PS00869. RENAL_DIPEPTIDASE_1. 1 hit.
    PS51365. RENAL_DIPEPTIDASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and sequencing of a human homologue of renal membrane dipeptidase."
      Chen J.M., Fortunato M., Barrett A.J.
      Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ARG-201.
      Tissue: Uterus.
    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] (ISOFORM 1), VARIANT ARG-201.
      Tissue: Testis.
    3. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ARG-201.
    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] (ISOFORM 2), VARIANT ARG-201.
      Tissue: Lung.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 18-486 (ISOFORM 1), VARIANT ARG-201.
    7. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-111 AND ASN-235.
      Tissue: Plasma.

    Entry informationi

    Entry nameiDPEP2_HUMAN
    AccessioniPrimary (citable) accession number: Q9H4A9
    Secondary accession number(s): B2RCF8, Q6UX92, Q8TC95
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 4, 2006
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 100 of the entry and version 2 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 16
      Human chromosome 16: 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. Peptidase families
      Classification of peptidase families and list of entries
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3