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Q99489

- OXDD_HUMAN

UniProt

Q99489 - OXDD_HUMAN

Protein

D-aspartate oxidase

Gene

DDO

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
    • BLAST
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      Previous versions | rss
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    Functioni

    Selectively catalyzes the oxidative deamination of D-aspartate and its N-methylated derivative, N-methyl D-aspartate.

    Catalytic activityi

    D-aspartate + H2O + O2 = oxaloacetate + NH3 + H2O2.

    Cofactori

    FAD or 6-hydroxyflavin adenine dinucleotide.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei166 – 1661FAD; via amide nitrogen and carbonyl oxygenBy similarity
    Binding sitei183 – 1831FADBy similarity
    Binding sitei223 – 2231SubstrateBy similarity
    Binding sitei278 – 2781SubstrateBy similarity
    Binding sitei312 – 3121FADBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi6 – 2015FADBy similarityAdd
    BLAST
    Nucleotide bindingi36 – 372FADBy similarity
    Nucleotide bindingi43 – 442FADBy similarity
    Nucleotide bindingi48 – 503FADBy similarity
    Nucleotide bindingi307 – 3115FADBy similarity

    GO - Molecular functioni

    1. cofactor binding Source: UniProtKB
    2. D-aspartate oxidase activity Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. receptor binding Source: UniProtKB

    GO - Biological processi

    1. aspartate catabolic process Source: UniProtKB
    2. aspartate metabolic process Source: Ensembl
    3. D-amino acid catabolic process Source: UniProtKB
    4. grooming behavior Source: Ensembl
    5. hormone metabolic process Source: Ensembl
    6. insemination Source: Ensembl
    7. oxidation-reduction process Source: GOC

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein

    Enzyme and pathway databases

    SABIO-RKQ99489.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    D-aspartate oxidase (EC:1.4.3.1)
    Short name:
    DASOX
    Short name:
    DDO
    Gene namesi
    Name:DDO
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:2727. DDO.

    Subcellular locationi

    GO - Cellular componenti

    1. peroxisome Source: UniProtKB

    Keywords - Cellular componenti

    Peroxisome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27194.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 341341D-aspartate oxidasePRO_0000162770Add
    BLAST

    Proteomic databases

    MaxQBiQ99489.
    PaxDbiQ99489.
    PRIDEiQ99489.

    PTM databases

    PhosphoSiteiQ99489.

    Expressioni

    Gene expression databases

    ArrayExpressiQ99489.
    BgeeiQ99489.
    CleanExiHS_DDO.
    GenevestigatoriQ99489.

    Organism-specific databases

    HPAiHPA037525.
    HPA037526.

    Interactioni

    Protein-protein interaction databases

    BioGridi114098. 3 interactions.
    IntActiQ99489. 1 interaction.
    STRINGi9606.ENSP00000357920.

    Structurei

    3D structure databases

    ProteinModelPortaliQ99489.
    SMRiQ99489. Positions 5-324.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi339 – 3413Microbody targeting signalSequence Analysis

    Sequence similaritiesi

    Belongs to the DAMOX/DASOX family.Curated

    Phylogenomic databases

    eggNOGiCOG0665.
    HOGENOMiHOG000046303.
    HOVERGENiHBG003493.
    InParanoidiQ99489.
    KOiK00272.
    OMAiNFIRDGD.
    OrthoDBiEOG7B31NB.
    PhylomeDBiQ99489.
    TreeFamiTF313887.

    Family and domain databases

    InterProiIPR023209. D-aa_oxidase.
    IPR006181. D-amino_acid_oxidase_CS.
    IPR006076. FAD-dep_OxRdtase.
    [Graphical view]
    PANTHERiPTHR11530. PTHR11530. 1 hit.
    PfamiPF01266. DAO. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000189. D-aa_oxidase. 1 hit.
    PROSITEiPS00677. DAO. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform DDO-1 (identifier: Q99489-1) [UniParc]FASTAAdd to Basket

    Also known as: A

    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

    MDTARIAVVG AGVVGLSTAV CISKLVPRCS VTIISDKFTP DTTSDVAAGM    50
    LIPHTYPDTP IHTQKQWFRE TFNHLFAIAN SAEAGDAGVH LVSGWQIFQS 100
    TPTEEVPFWA DVVLGFRKMT EAELKKFPQY VFGQAFTTLK CECPAYLPWL 150
    EKRIKGSGGW TLTRRIEDLW ELHPSFDIVV NCSGLGSRQL AGDSKIFPVR 200
    GQVLQVQAPW VEHFIRDGSG LTYIYPGTSH VTLGGTRQKG DWNLSPDAEN 250
    SREILSRCCA LEPSLHGACN IREKVGLRPY RPGVRLQTEL LARDGQRLPV 300
    VHHYGHGSGG ISVHWGTALE AARLVSECVH ALRTPIPKSN L 341
    Length:341
    Mass (Da):37,535
    Last modified:May 1, 1997 - v1
    Checksum:i8CAE7501FB7F215C
    GO
    Isoform DDO-2 (identifier: Q99489-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         95-153: Missing.

    Show »
    Length:282
    Mass (Da):30,522
    Checksum:iDBD01D57E5B72F7A
    GO
    Isoform 3 (identifier: Q99489-3) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:369
    Mass (Da):40,993
    Checksum:i4E4C372EE90DD7C5
    GO
    Isoform 4 (identifier: Q99489-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MRPARHWETRFGARDFGGFQDCFFRDRLM
         95-153: Missing.

    Show »
    Length:310
    Mass (Da):33,980
    Checksum:iE74BBF6D27BE5CB3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti278 – 2781R → S in BAF85718. (PubMed:14702039)Curated
    Isoform 4 (identifier: Q99489-4)
    Sequence conflicti9 – 91T → N in DN990727. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti136 – 1361F → L in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036244
    Natural varianti189 – 1891Q → E.
    Corresponds to variant rs17622 [ dbSNP | Ensembl ].
    VAR_014939
    Natural varianti230 – 2301H → Y.
    Corresponds to variant rs17621 [ dbSNP | Ensembl ].
    VAR_014940
    Natural varianti255 – 2551L → R.
    Corresponds to variant rs17623 [ dbSNP | Ensembl ].
    VAR_014941

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MRPARHWETRFGARDFGGFQ DCFFRDRLM in isoform 3 and isoform 4. 3 PublicationsVSP_037664
    Alternative sequencei95 – 15359Missing in isoform DDO-2 and isoform 4. 2 PublicationsVSP_001269Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D89858 mRNA. Translation: BAA14031.1.
    AK293029 mRNA. Translation: BAF85718.1.
    AL050350 Genomic DNA. Translation: CAI42511.1.
    AL050350 Genomic DNA. Translation: CAI42509.1.
    AL050350 Genomic DNA. Translation: CAI42510.1.
    CH471051 Genomic DNA. Translation: EAW48316.1.
    CH471051 Genomic DNA. Translation: EAW48317.1.
    BC032786 mRNA. Translation: AAH32786.3.
    DN990727 mRNA. No translation available.
    CCDSiCCDS5082.1. [Q99489-3]
    CCDS5083.1. [Q99489-4]
    PIRiJC5438.
    JC5439.
    RefSeqiNP_003640.2. NM_003649.2. [Q99489-3]
    NP_004023.2. NM_004032.2. [Q99489-4]
    UniGeneiHs.591348.

    Genome annotation databases

    EnsembliENST00000368923; ENSP00000357919; ENSG00000203797. [Q99489-4]
    ENST00000368924; ENSP00000357920; ENSG00000203797. [Q99489-3]
    GeneIDi8528.
    KEGGihsa:8528.
    UCSCiuc003puc.3. human. [Q99489-3]
    uc003pud.3. human. [Q99489-4]

    Polymorphism databases

    DMDMi2494037.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D89858 mRNA. Translation: BAA14031.1 .
    AK293029 mRNA. Translation: BAF85718.1 .
    AL050350 Genomic DNA. Translation: CAI42511.1 .
    AL050350 Genomic DNA. Translation: CAI42509.1 .
    AL050350 Genomic DNA. Translation: CAI42510.1 .
    CH471051 Genomic DNA. Translation: EAW48316.1 .
    CH471051 Genomic DNA. Translation: EAW48317.1 .
    BC032786 mRNA. Translation: AAH32786.3 .
    DN990727 mRNA. No translation available.
    CCDSi CCDS5082.1. [Q99489-3 ]
    CCDS5083.1. [Q99489-4 ]
    PIRi JC5438.
    JC5439.
    RefSeqi NP_003640.2. NM_003649.2. [Q99489-3 ]
    NP_004023.2. NM_004032.2. [Q99489-4 ]
    UniGenei Hs.591348.

    3D structure databases

    ProteinModelPortali Q99489.
    SMRi Q99489. Positions 5-324.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114098. 3 interactions.
    IntActi Q99489. 1 interaction.
    STRINGi 9606.ENSP00000357920.

    Chemistry

    BindingDBi Q99489.
    ChEMBLi CHEMBL5887.

    PTM databases

    PhosphoSitei Q99489.

    Polymorphism databases

    DMDMi 2494037.

    Proteomic databases

    MaxQBi Q99489.
    PaxDbi Q99489.
    PRIDEi Q99489.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000368923 ; ENSP00000357919 ; ENSG00000203797 . [Q99489-4 ]
    ENST00000368924 ; ENSP00000357920 ; ENSG00000203797 . [Q99489-3 ]
    GeneIDi 8528.
    KEGGi hsa:8528.
    UCSCi uc003puc.3. human. [Q99489-3 ]
    uc003pud.3. human. [Q99489-4 ]

    Organism-specific databases

    CTDi 8528.
    GeneCardsi GC06M110672.
    HGNCi HGNC:2727. DDO.
    HPAi HPA037525.
    HPA037526.
    MIMi 124450. gene.
    neXtProti NX_Q99489.
    PharmGKBi PA27194.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0665.
    HOGENOMi HOG000046303.
    HOVERGENi HBG003493.
    InParanoidi Q99489.
    KOi K00272.
    OMAi NFIRDGD.
    OrthoDBi EOG7B31NB.
    PhylomeDBi Q99489.
    TreeFami TF313887.

    Enzyme and pathway databases

    SABIO-RK Q99489.

    Miscellaneous databases

    GeneWikii DDO_(gene).
    GenomeRNAii 8528.
    NextBioi 31934.
    PROi Q99489.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q99489.
    Bgeei Q99489.
    CleanExi HS_DDO.
    Genevestigatori Q99489.

    Family and domain databases

    InterProi IPR023209. D-aa_oxidase.
    IPR006181. D-amino_acid_oxidase_CS.
    IPR006076. FAD-dep_OxRdtase.
    [Graphical view ]
    PANTHERi PTHR11530. PTHR11530. 1 hit.
    Pfami PF01266. DAO. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000189. D-aa_oxidase. 1 hit.
    PROSITEi PS00677. DAO. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structural and functional characterization of the human brain D-aspartate oxidase."
      Setoyama C., Miura R.
      J. Biochem. 121:798-803(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS DDO-1 AND DDO-2).
      Tissue: Brain.
    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 3).
      Tissue: Uterus.
    3. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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 3).
      Tissue: Brain.
    6. "High-throughput cloning of full-length human cDNAs directly from cDNA libraries optimized for large and rare transcripts."
      Birkett C., Cho J., Gau Y., Hamer R., Kelly S., Kovacs K., Liu L., Liu X., Porter J., Sachs A., Shu Y., Sun Z., Wong J., Wu M., Zhang X., Jay G., He W.
      Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-206 (ISOFORM 4).
    7. Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-136.

    Entry informationi

    Entry nameiOXDD_HUMAN
    AccessioniPrimary (citable) accession number: Q99489
    Secondary accession number(s): A8KAG4
    , Q5JXM4, Q5JXM5, Q5JXM6, Q8N552
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 131 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 6
      Human chromosome 6: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3