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Q93099

- HGD_HUMAN

UniProt

Q93099 - HGD_HUMAN

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Protein

Homogentisate 1,2-dioxygenase

Gene

HGD

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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: UniProtKB
Complete GO annotation...

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

BgeeiQ93099.
CleanExiHS_HGD.
ExpressionAtlasiQ93099. baseline and differential.
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.
GeneTreeiENSGT00390000004601.
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

        10         20         30         40         50
MAELKYISGF GNECSSEDPR CPGSLPEGQN NPQVCPYNLY AEQLSGSAFT
60 70 80 90 100
CPRSTNKRSW LYRILPSVSH KPFESIDEGQ VTHNWDEVDP DPNQLRWKPF
110 120 130 140 150
EIPKASQKKV DFVSGLHTLC GAGDIKSNNG LAIHIFLCNT SMENRCFYNS
160 170 180 190 200
DGDFLIVPQK GNLLIYTEFG KMLVQPNEIC VIQRGMRFSI DVFEETRGYI
210 220 230 240 250
LEVYGVHFEL PDLGPIGANG LANPRDFLIP IAWYEDRQVP GGYTVINKYQ
260 270 280 290 300
GKLFAAKQDV SPFNVVAWHG NYTPYKYNLK NFMVINSVAF DHADPSIFTV
310 320 330 340 350
LTAKSVRPGV AIADFVIFPP RWGVADKTFR PPYYHRNCMS EFMGLIRGHY
360 370 380 390 400
EAKQGGFLPG GGSLHSTMTP HGPDADCFEK ASKVKLAPER IADGTMAFMF
410 420 430 440
ESSLSLAVTK WGLKASRCLD ENYHKCWEPL KSHFTPNSRN PAEPN
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.
GeneTreei ENSGT00390000004601.
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

Bgeei Q93099.
CleanExi HS_HGD.
ExpressionAtlasi Q93099. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 143 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