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Q93099

- HGD_HUMAN

UniProt

Q93099 - HGD_HUMAN

Protein

Homogentisate 1,2-dioxygenase

Gene

HGD

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 2 (18 May 2010)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Homogentisate + O2 = 4-maleylacetoacetate.

    Cofactori

    Iron.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi335 – 3351Iron
    Metal bindingi341 – 3411Iron
    Metal bindingi371 – 3711Iron

    GO - Molecular functioni

    1. homogentisate 1,2-dioxygenase activity Source: Reactome
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. cellular nitrogen compound metabolic process Source: Reactome
    2. L-phenylalanine catabolic process Source: Reactome
    3. small molecule metabolic process Source: Reactome
    4. tyrosine catabolic process Source: ProtInc

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase

    Keywords - Biological processi

    Phenylalanine catabolism, Tyrosine catabolism

    Keywords - Ligandi

    Iron, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS03728-MONOMER.
    ReactomeiREACT_1786. Phenylalanine and tyrosine catabolism.
    UniPathwayiUPA00139; UER00339.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Homogentisate 1,2-dioxygenase (EC:1.13.11.5)
    Alternative name(s):
    Homogentisate oxygenase
    Homogentisic acid oxidase
    Homogentisicase
    Gene namesi
    Name:HGD
    Synonyms:HGO
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:4892. HGD.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. extracellular vesicular exosome Source: UniProt

    Pathology & Biotechi

    Involvement in diseasei

    Alkaptonuria (AKU) [MIM:203500]: An autosomal recessive error of metabolism characterized by an increase in the level of homogentisic acid. The clinical manifestations are urine that turns dark on standing and alkalinization, black ochronotic pigmentation of cartilage and collagenous tissues, and spine arthritis.8 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti25 – 251L → P in AKU. 2 Publications
    VAR_009618
    Natural varianti42 – 421E → A in AKU. 1 Publication
    VAR_005272
    Natural varianti60 – 601W → G in AKU. 1 Publication
    VAR_005273
    Natural varianti62 – 621Y → C in AKU. 1 Publication
    VAR_005274
    Natural varianti97 – 971W → G in AKU. 1 Publication
    VAR_005275
    Natural varianti122 – 1221A → D in AKU. 1 Publication
    VAR_005276
    Natural varianti153 – 1531D → G in AKU. 1 Publication
    VAR_005277
    Natural varianti161 – 1611G → R in AKU; loss of activity; most prevalent mutation in Slovak and Czech patients. 2 Publications
    Corresponds to variant rs28941783 [ dbSNP | Ensembl ].
    VAR_005278
    Natural varianti168 – 1681E → K in AKU; loss of activity. 1 Publication
    VAR_009619
    Natural varianti189 – 1891S → I in AKU. 1 Publication
    VAR_005279
    Natural varianti216 – 2161I → T in AKU. 1 Publication
    VAR_005280
    Natural varianti225 – 2251R → H in AKU. 1 Publication
    VAR_005281
    Natural varianti227 – 2271F → S in AKU. 1 Publication
    VAR_005282
    Natural varianti230 – 2301P → S in AKU; complete loss of activity. 2 Publications
    Corresponds to variant rs28942100 [ dbSNP | Ensembl ].
    VAR_005283
    Natural varianti230 – 2301P → T in AKU. 1 Publication
    VAR_005284
    Natural varianti270 – 2701G → R in AKU. 1 Publication
    VAR_009620
    Natural varianti291 – 2911D → E in AKU. 1 Publication
    VAR_005285
    Natural varianti300 – 3001V → G in AKU. 2 Publications
    VAR_005286
    Natural varianti330 – 3301R → S in AKU. 1 Publication
    VAR_008744
    Natural varianti368 – 3681M → V in AKU; loss of activity. 4 Publications
    Corresponds to variant rs120074173 [ dbSNP | Ensembl ].
    VAR_005287
    Natural varianti371 – 3711H → R in AKU. 1 Publication
    VAR_008745

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi203500. phenotype.
    Orphaneti56. Alkaptonuria.
    PharmGKBiPA29268.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 445445Homogentisate 1,2-dioxygenasePRO_0000220240Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei98 – 981N6-acetyllysine1 Publication
    Modified residuei414 – 4141N6-succinyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ93099.
    PaxDbiQ93099.
    PRIDEiQ93099.

    PTM databases

    PhosphoSiteiQ93099.

    Expressioni

    Tissue specificityi

    Highest expression in the prostate, small intestine, colon, kidney and liver.

    Gene expression databases

    ArrayExpressiQ93099.
    BgeeiQ93099.
    CleanExiHS_HGD.
    GenevestigatoriQ93099.

    Organism-specific databases

    HPAiHPA047374.

    Interactioni

    Subunit structurei

    Homohexamer arranged as a dimer of trimers.1 Publication

    Protein-protein interaction databases

    BioGridi109329. 7 interactions.
    IntActiQ93099. 4 interactions.
    MINTiMINT-3049945.
    STRINGi9606.ENSP00000283871.

    Structurei

    Secondary structure

    1
    445
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 83
    Beta strandi14 – 174
    Helixi36 – 383
    Beta strandi40 – 478
    Helixi53 – 553
    Beta strandi58 – 658
    Helixi85 – 873
    Beta strandi95 – 973
    Turni105 – 1073
    Turni112 – 1154
    Beta strandi116 – 1238
    Helixi125 – 1273
    Beta strandi131 – 1388
    Beta strandi144 – 16118
    Beta strandi163 – 1675
    Beta strandi170 – 1745
    Beta strandi178 – 1825
    Beta strandi188 – 1914
    Beta strandi193 – 20513
    Helixi214 – 2163
    Helixi224 – 2263
    Beta strandi227 – 2304
    Beta strandi238 – 24912
    Beta strandi252 – 2609
    Beta strandi265 – 2717
    Beta strandi275 – 2784
    Helixi279 – 2813
    Beta strandi288 – 2914
    Helixi295 – 2984
    Beta strandi299 – 3046
    Beta strandi311 – 3188
    Beta strandi320 – 3234
    Beta strandi326 – 3283
    Beta strandi340 – 3478
    Beta strandi362 – 3654
    Helixi375 – 3839
    Beta strandi389 – 3924
    Beta strandi396 – 4049
    Helixi410 – 4156

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EY2X-ray2.30A1-445[»]
    1EYBX-ray1.90A1-445[»]
    ProteinModelPortaliQ93099.
    SMRiQ93099. Positions 2-440.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ93099.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the homogentisate dioxygenase family.Curated

    Phylogenomic databases

    eggNOGiCOG3508.
    HOGENOMiHOG000139824.
    HOVERGENiHBG005965.
    InParanoidiQ93099.
    KOiK00451.
    OMAiRCFYNSD.
    OrthoDBiEOG7PP58Z.
    PhylomeDBiQ93099.
    TreeFamiTF300490.

    Family and domain databases

    Gene3Di2.60.120.10. 2 hits.
    InterProiIPR005708. Homogentis_dOase.
    IPR014710. RmlC-like_jellyroll.
    IPR011051. RmlC_Cupin.
    [Graphical view]
    PANTHERiPTHR11056. PTHR11056. 1 hit.
    PfamiPF04209. HgmA. 1 hit.
    [Graphical view]
    SUPFAMiSSF51182. SSF51182. 1 hit.
    TIGRFAMsiTIGR01015. hmgA. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q93099-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAELKYISGF GNECSSEDPR CPGSLPEGQN NPQVCPYNLY AEQLSGSAFT    50
    CPRSTNKRSW LYRILPSVSH KPFESIDEGQ VTHNWDEVDP DPNQLRWKPF 100
    EIPKASQKKV DFVSGLHTLC GAGDIKSNNG LAIHIFLCNT SMENRCFYNS 150
    DGDFLIVPQK GNLLIYTEFG KMLVQPNEIC VIQRGMRFSI DVFEETRGYI 200
    LEVYGVHFEL PDLGPIGANG LANPRDFLIP IAWYEDRQVP GGYTVINKYQ 250
    GKLFAAKQDV SPFNVVAWHG NYTPYKYNLK NFMVINSVAF DHADPSIFTV 300
    LTAKSVRPGV AIADFVIFPP RWGVADKTFR PPYYHRNCMS EFMGLIRGHY 350
    EAKQGGFLPG GGSLHSTMTP HGPDADCFEK ASKVKLAPER IADGTMAFMF 400
    ESSLSLAVTK WGLKASRCLD ENYHKCWEPL KSHFTPNSRN PAEPN 445
    Length:445
    Mass (Da):49,964
    Last modified:May 18, 2010 - v2
    Checksum:iF99B51C134FFF965
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti383 – 3831K → R in BAF83471. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti25 – 251L → P in AKU. 2 Publications
    VAR_009618
    Natural varianti42 – 421E → A in AKU. 1 Publication
    VAR_005272
    Natural varianti60 – 601W → G in AKU. 1 Publication
    VAR_005273
    Natural varianti62 – 621Y → C in AKU. 1 Publication
    VAR_005274
    Natural varianti80 – 801Q → H.6 Publications
    Corresponds to variant rs2255543 [ dbSNP | Ensembl ].
    VAR_049353
    Natural varianti97 – 971W → G in AKU. 1 Publication
    VAR_005275
    Natural varianti122 – 1221A → D in AKU. 1 Publication
    VAR_005276
    Natural varianti153 – 1531D → G in AKU. 1 Publication
    VAR_005277
    Natural varianti161 – 1611G → R in AKU; loss of activity; most prevalent mutation in Slovak and Czech patients. 2 Publications
    Corresponds to variant rs28941783 [ dbSNP | Ensembl ].
    VAR_005278
    Natural varianti168 – 1681E → K in AKU; loss of activity. 1 Publication
    VAR_009619
    Natural varianti189 – 1891S → I in AKU. 1 Publication
    VAR_005279
    Natural varianti216 – 2161I → T in AKU. 1 Publication
    VAR_005280
    Natural varianti225 – 2251R → H in AKU. 1 Publication
    VAR_005281
    Natural varianti227 – 2271F → S in AKU. 1 Publication
    VAR_005282
    Natural varianti230 – 2301P → S in AKU; complete loss of activity. 2 Publications
    Corresponds to variant rs28942100 [ dbSNP | Ensembl ].
    VAR_005283
    Natural varianti230 – 2301P → T in AKU. 1 Publication
    VAR_005284
    Natural varianti270 – 2701G → R in AKU. 1 Publication
    VAR_009620
    Natural varianti291 – 2911D → E in AKU. 1 Publication
    VAR_005285
    Natural varianti300 – 3001V → G in AKU. 2 Publications
    VAR_005286
    Natural varianti330 – 3301R → S in AKU. 1 Publication
    VAR_008744
    Natural varianti368 – 3681M → V in AKU; loss of activity. 4 Publications
    Corresponds to variant rs120074173 [ dbSNP | Ensembl ].
    VAR_005287
    Natural varianti371 – 3711H → R in AKU. 1 Publication
    VAR_008745

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U63008 mRNA. Translation: AAB16836.1.
    Z75048 mRNA. Translation: CAA99340.1.
    AF000573 Genomic DNA. Translation: AAC51650.1.
    AF045167 mRNA. Translation: AAC02698.1.
    AK290782 mRNA. Translation: BAF83471.1.
    AK313563 mRNA. Translation: BAG36337.1.
    AC126182 Genomic DNA. No translation available.
    AC133474 Genomic DNA. No translation available.
    CH471052 Genomic DNA. Translation: EAW79524.1.
    BC071757 mRNA. Translation: AAH71757.1.
    CCDSiCCDS3000.1.
    RefSeqiNP_000178.2. NM_000187.3.
    UniGeneiHs.368254.

    Genome annotation databases

    EnsembliENST00000283871; ENSP00000283871; ENSG00000113924.
    GeneIDi3081.
    KEGGihsa:3081.
    UCSCiuc003edv.3. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U63008 mRNA. Translation: AAB16836.1 .
    Z75048 mRNA. Translation: CAA99340.1 .
    AF000573 Genomic DNA. Translation: AAC51650.1 .
    AF045167 mRNA. Translation: AAC02698.1 .
    AK290782 mRNA. Translation: BAF83471.1 .
    AK313563 mRNA. Translation: BAG36337.1 .
    AC126182 Genomic DNA. No translation available.
    AC133474 Genomic DNA. No translation available.
    CH471052 Genomic DNA. Translation: EAW79524.1 .
    BC071757 mRNA. Translation: AAH71757.1 .
    CCDSi CCDS3000.1.
    RefSeqi NP_000178.2. NM_000187.3.
    UniGenei Hs.368254.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EY2 X-ray 2.30 A 1-445 [» ]
    1EYB X-ray 1.90 A 1-445 [» ]
    ProteinModelPortali Q93099.
    SMRi Q93099. Positions 2-440.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109329. 7 interactions.
    IntActi Q93099. 4 interactions.
    MINTi MINT-3049945.
    STRINGi 9606.ENSP00000283871.

    PTM databases

    PhosphoSitei Q93099.

    Proteomic databases

    MaxQBi Q93099.
    PaxDbi Q93099.
    PRIDEi Q93099.

    Protocols and materials databases

    DNASUi 3081.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000283871 ; ENSP00000283871 ; ENSG00000113924 .
    GeneIDi 3081.
    KEGGi hsa:3081.
    UCSCi uc003edv.3. human.

    Organism-specific databases

    CTDi 3081.
    GeneCardsi GC03M120347.
    GeneReviewsi HGD.
    H-InvDB HIX0003593.
    HGNCi HGNC:4892. HGD.
    HPAi HPA047374.
    MIMi 203500. phenotype.
    607474. gene.
    neXtProti NX_Q93099.
    Orphaneti 56. Alkaptonuria.
    PharmGKBi PA29268.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG3508.
    HOGENOMi HOG000139824.
    HOVERGENi HBG005965.
    InParanoidi Q93099.
    KOi K00451.
    OMAi RCFYNSD.
    OrthoDBi EOG7PP58Z.
    PhylomeDBi Q93099.
    TreeFami TF300490.

    Enzyme and pathway databases

    UniPathwayi UPA00139 ; UER00339 .
    BioCyci MetaCyc:HS03728-MONOMER.
    Reactomei REACT_1786. Phenylalanine and tyrosine catabolism.

    Miscellaneous databases

    EvolutionaryTracei Q93099.
    GenomeRNAii 3081.
    NextBioi 12197.
    PROi Q93099.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q93099.
    Bgeei Q93099.
    CleanExi HS_HGD.
    Genevestigatori Q93099.

    Family and domain databases

    Gene3Di 2.60.120.10. 2 hits.
    InterProi IPR005708. Homogentis_dOase.
    IPR014710. RmlC-like_jellyroll.
    IPR011051. RmlC_Cupin.
    [Graphical view ]
    PANTHERi PTHR11056. PTHR11056. 1 hit.
    Pfami PF04209. HgmA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51182. SSF51182. 1 hit.
    TIGRFAMsi TIGR01015. hmgA. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS HIS-80; AKU SER-230 AND GLY-300.
    2. "Homogentisate 1,2-dioxygenase human cDNA sequence."
      Ramos S., Hernandez M., Rozes A., Larruga J., Gonzalez P., Cabrera V.M.
      Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT HIS-80.
      Tissue: Liver.
    3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT HIS-80.
    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], VARIANT HIS-80.
      Tissue: Kidney and Prostate.
    5. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT HIS-80.
    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], VARIANT HIS-80.
    8. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-98, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), METAL-BINDING SITES, SUBUNIT.
    11. "Molecular defects in alkaptonuria."
      Gehrig A., Schmidt S.R., Mueller C.R., Srsen S., Srsnova K., Kress W.
      Cytogenet. Cell Genet. 76:14-16(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT AKU ARG-161.
    12. "Mutation and polymorphism analysis of the human homogentisate 1, 2-dioxygenase gene in alkaptonuria patients."
      Beltran-Valero de Bernabe D., Granadino B., Chiarelli I., Porfirio B., Mayatepek E., Aquaron R., Moore M.M., Festen J.J.M., Sanmarti R., Penalva M.A., de Cordoba S.R.
      Am. J. Hum. Genet. 62:776-784(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS AKU ALA-42; GLY-97; GLY-153; ILE-189; THR-216; HIS-225; SER-227 AND VAL-368.
    13. "A novel point mutation associated with alkaptonuria."
      Higashino K., Liu W., Ohkawa T., Yamamoto T., Fukui K., Ohno M., Imanishi H., Iwasaki A., Amuro Y., Hada T.
      Clin. Genet. 53:228-229(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT AKU LYS-168.
    14. "Analysis of alkaptonuria (AKU) mutations and polymorphisms reveals that the CCC sequence motif is a mutational hot spot in the homogentisate 1,2 dioxygenase gene (HGO)."
      Beltran-Valero de Bernabe D., Jimenez F.J., Aquaron R., Rodriguez de Cordoba S.
      Am. J. Hum. Genet. 64:1316-1322(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS AKU GLY-60; CYS-62; ASP-122; THR-230 AND GLU-291.
    15. "Ocular ochronosis in alkaptonuria patients carrying mutations in the homogentisate 1,2-dioxygenase gene."
      Felbor U., Mutsch Y., Grehn F., Mueller C.R., Kress W.
      Br. J. Ophthalmol. 83:680-683(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS AKU PRO-25 AND VAL-368.
      Tissue: Leukocyte.
    16. Cited for: VARIANTS AKU PRO-25; ARG-161; SER-230; ARG-270; GLY-300 AND VAL-368.
      Tissue: Lymphocyte.
    17. "Mutational analysis of the HGO gene in Finnish alkaptonuria patients."
      Beltran-Valero de Bernabe D., Peterson P., Luopajarvi K., Matintalo P., Alho A., Konttinen Y., Krohn K., Rodriguez de Cordoba S., Ranki A.
      J. Med. Genet. 36:922-923(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS AKU SER-330; VAL-368 AND ARG-371.

    Entry informationi

    Entry nameiHGD_HUMAN
    AccessioniPrimary (citable) accession number: Q93099
    Secondary accession number(s): A8K417, B2R8Z0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 142 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3