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Q9NYQ3

- HAOX2_HUMAN

UniProt

Q9NYQ3 - HAOX2_HUMAN

Protein

Hydroxyacid oxidase 2

Gene

HAO2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Catalyzes the oxidation of L-alpha-hydroxy acids as well as, more slowly, that of L-alpha-amino acids.

    Catalytic activityi

    (S)-2-hydroxy acid + O2 = 2-oxo acid + H2O2.

    Cofactori

    FMN.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei106 – 1061FMNPROSITE-ProRule annotation
    Binding sitei128 – 1281FMNPROSITE-ProRule annotation
    Binding sitei130 – 1301SubstratePROSITE-ProRule annotation
    Binding sitei156 – 1561FMNPROSITE-ProRule annotation
    Binding sitei165 – 1651SubstratePROSITE-ProRule annotation
    Binding sitei222 – 2221FMNPROSITE-ProRule annotation
    Active sitei246 – 2461Proton acceptorPROSITE-ProRule annotation
    Binding sitei249 – 2491SubstratePROSITE-ProRule annotation
    Binding sitei301 – 3011FMNPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi277 – 30125FMNPROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. (S)-2-hydroxy-acid oxidase activity Source: UniProtKB
    2. FMN binding Source: Ensembl
    3. long-chain-(S)-2-hydroxy-long-chain-acid oxidase activity Source: UniProtKB
    4. medium-chain-(S)-2-hydroxy-acid oxidase activity Source: UniProtKB-EC
    5. receptor binding Source: UniProtKB
    6. very-long-chain-(S)-2-hydroxy-acid oxidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. fatty acid oxidation Source: UniProtKB
    2. mandelate metabolic process Source: Ensembl
    3. protein homooligomerization Source: Ensembl

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Flavoprotein, FMN

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hydroxyacid oxidase 2 (EC:1.1.3.15)
    Short name:
    HAOX2
    Alternative name(s):
    (S)-2-hydroxy-acid oxidase, peroxisomal
    Cell growth-inhibiting gene 16 protein
    Long chain alpha-hydroxy acid oxidase
    Long-chain L-2-hydroxy acid oxidase
    Gene namesi
    Name:HAO2
    Synonyms:HAOX2
    ORF Names:GIG16
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:4810. HAO2.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. mitochondrion Source: Ensembl
    3. peroxisome Source: UniProtKB

    Keywords - Cellular componenti

    Peroxisome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29186.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 351350Hydroxyacid oxidase 2PRO_0000206320Add
    BLAST

    Proteomic databases

    PaxDbiQ9NYQ3.
    PRIDEiQ9NYQ3.

    PTM databases

    PhosphoSiteiQ9NYQ3.

    Expressioni

    Tissue specificityi

    Liver and kidney.

    Gene expression databases

    ArrayExpressiQ9NYQ3.
    BgeeiQ9NYQ3.
    CleanExiHS_HAO2.
    GenevestigatoriQ9NYQ3.

    Organism-specific databases

    HPAiHPA045773.

    Interactioni

    Subunit structurei

    Homotetramer or homooctamer.By similarity

    Protein-protein interaction databases

    BioGridi119356. 1 interaction.
    IntActiQ9NYQ3. 1 interaction.
    STRINGi9606.ENSP00000316339.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NYQ3.
    SMRiQ9NYQ3. Positions 3-348.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 351350FMN hydroxy acid dehydrogenasePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi349 – 3513Microbody targeting signalSequence Analysis

    Sequence similaritiesi

    Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family.PROSITE-ProRule annotation
    Contains 1 FMN hydroxy acid dehydrogenase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG1304.
    HOGENOMiHOG000217463.
    HOVERGENiHBG051881.
    InParanoidiQ9NYQ3.
    KOiK11517.
    PhylomeDBiQ9NYQ3.
    TreeFamiTF313363.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    InterProiIPR013785. Aldolase_TIM.
    IPR012133. Alpha-hydoxy_acid_DH_FMN.
    IPR000262. FMN-dep_DH.
    IPR008259. FMN_hydac_DH_AS.
    [Graphical view]
    PfamiPF01070. FMN_dh. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000138. Al-hdrx_acd_dh. 1 hit.
    PROSITEiPS00557. FMN_HYDROXY_ACID_DH_1. 1 hit.
    PS51349. FMN_HYDROXY_ACID_DH_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: Q9NYQ3-1) [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

    MSLVCLTDFQ AHAREQLSKS TRDFIEGGAD DSITRDDNIA AFKRIRLRPR    50
    YLRDVSEVDT RTTIQGEEIS APICIAPTGF HCLVWPDGEM STARAAQAAG 100
    ICYITSTFAS CSLEDIVIAA PEGLRWFQLY VHPDLQLNKQ LIQRVESLGF 150
    KALVITLDTP VCGNRRHDIR NQLRRNLTLT DLQSPKKGNA IPYFQMTPIS 200
    TSLCWNDLSW FQSITRLPII LKGILTKEDA ELAVKHNVQG IIVSNHGGRQ 250
    LDEVLASIDA LTEVVAAVKG KIEVYLDGGV RTGNDVLKAL ALGAKCIFLG 300
    RPILWGLACK GEHGVKEVLN ILTNEFHTSM ALTGCRSVAE INRNLVQFSR 350
    L 351
    Length:351
    Mass (Da):38,839
    Last modified:October 1, 2000 - v1
    Checksum:i7330DE44E282947D
    GO
    Isoform 2 (identifier: Q9NYQ3-2) [UniParc]FASTAAdd to Basket

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

    Note: No experimental confirmation available.

    Show »
    Length:364
    Mass (Da):40,391
    Checksum:i13F52C5D431E8B2E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti80 – 801F → Y in AAF14000. 1 PublicationCurated
    Sequence conflicti292 – 2943LGA → HED in AAF14000. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti15 – 151E → K.
    Corresponds to variant rs34638261 [ dbSNP | Ensembl ].
    VAR_049087
    Natural varianti221 – 2211L → M.
    Corresponds to variant rs6661625 [ dbSNP | Ensembl ].
    VAR_049088

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MEDKMWSECEGPEM in isoform 2. 1 PublicationVSP_055095

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF231917 mRNA. Translation: AAF40200.1.
    AF203975 mRNA. Translation: AAF14000.1.
    AY513277 mRNA. Translation: AAT08030.1.
    AK298289 mRNA. Translation: BAG60549.1.
    AL139346 Genomic DNA. No translation available.
    AL359553 Genomic DNA. Translation: CAC19798.1.
    CH471122 Genomic DNA. Translation: EAW56698.1.
    CH471122 Genomic DNA. Translation: EAW56699.1.
    BC020863 mRNA. Translation: AAH20863.1.
    CCDSiCCDS901.1. [Q9NYQ3-1]
    RefSeqiNP_001005783.1. NM_001005783.1.
    NP_057611.1. NM_016527.2.
    XP_005270972.1. XM_005270915.1.
    UniGeneiHs.659767.

    Genome annotation databases

    EnsembliENST00000325945; ENSP00000316339; ENSG00000116882. [Q9NYQ3-1]
    ENST00000361035; ENSP00000354314; ENSG00000116882. [Q9NYQ3-2]
    GeneIDi51179.
    KEGGihsa:51179.
    UCSCiuc001ehq.1. human. [Q9NYQ3-1]

    Polymorphism databases

    DMDMi13124287.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF231917 mRNA. Translation: AAF40200.1 .
    AF203975 mRNA. Translation: AAF14000.1 .
    AY513277 mRNA. Translation: AAT08030.1 .
    AK298289 mRNA. Translation: BAG60549.1 .
    AL139346 Genomic DNA. No translation available.
    AL359553 Genomic DNA. Translation: CAC19798.1 .
    CH471122 Genomic DNA. Translation: EAW56698.1 .
    CH471122 Genomic DNA. Translation: EAW56699.1 .
    BC020863 mRNA. Translation: AAH20863.1 .
    CCDSi CCDS901.1. [Q9NYQ3-1 ]
    RefSeqi NP_001005783.1. NM_001005783.1.
    NP_057611.1. NM_016527.2.
    XP_005270972.1. XM_005270915.1.
    UniGenei Hs.659767.

    3D structure databases

    ProteinModelPortali Q9NYQ3.
    SMRi Q9NYQ3. Positions 3-348.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119356. 1 interaction.
    IntActi Q9NYQ3. 1 interaction.
    STRINGi 9606.ENSP00000316339.

    Chemistry

    ChEMBLi CHEMBL2169732.

    PTM databases

    PhosphoSitei Q9NYQ3.

    Polymorphism databases

    DMDMi 13124287.

    Proteomic databases

    PaxDbi Q9NYQ3.
    PRIDEi Q9NYQ3.

    Protocols and materials databases

    DNASUi 51179.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000325945 ; ENSP00000316339 ; ENSG00000116882 . [Q9NYQ3-1 ]
    ENST00000361035 ; ENSP00000354314 ; ENSG00000116882 . [Q9NYQ3-2 ]
    GeneIDi 51179.
    KEGGi hsa:51179.
    UCSCi uc001ehq.1. human. [Q9NYQ3-1 ]

    Organism-specific databases

    CTDi 51179.
    GeneCardsi GC01P119913.
    HGNCi HGNC:4810. HAO2.
    HPAi HPA045773.
    MIMi 605176. gene.
    neXtProti NX_Q9NYQ3.
    PharmGKBi PA29186.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1304.
    HOGENOMi HOG000217463.
    HOVERGENi HBG051881.
    InParanoidi Q9NYQ3.
    KOi K11517.
    PhylomeDBi Q9NYQ3.
    TreeFami TF313363.

    Miscellaneous databases

    ChiTaRSi HAO2. human.
    GenomeRNAii 51179.
    NextBioi 54141.
    PROi Q9NYQ3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NYQ3.
    Bgeei Q9NYQ3.
    CleanExi HS_HAO2.
    Genevestigatori Q9NYQ3.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    InterProi IPR013785. Aldolase_TIM.
    IPR012133. Alpha-hydoxy_acid_DH_FMN.
    IPR000262. FMN-dep_DH.
    IPR008259. FMN_hydac_DH_AS.
    [Graphical view ]
    Pfami PF01070. FMN_dh. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000138. Al-hdrx_acd_dh. 1 hit.
    PROSITEi PS00557. FMN_HYDROXY_ACID_DH_1. 1 hit.
    PS51349. FMN_HYDROXY_ACID_DH_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification and characterization of HAOX1, HAOX2, and HAOX3, three human peroxisomal 2-hydroxy acid oxidases."
      Jones J.M., Morrell J.C., Gould S.J.
      J. Biol. Chem. 275:12590-12597(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Human long-chain L-2-hydroxy acid oxidase."
      Spielbauer B., Conzelmann E.
      Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Identification of a human cell growth inhibiting gene."
      Kim J.W.
      Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. "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).
      Tissue: Kidney.
    5. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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 1).
      Tissue: Kidney.

    Entry informationi

    Entry nameiHAOX2_HUMAN
    AccessioniPrimary (citable) accession number: Q9NYQ3
    Secondary accession number(s): Q2TU86, Q5QP00, Q9UJS6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 21, 2001
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 114 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 1
      Human chromosome 1: 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