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P32754

- HPPD_HUMAN

UniProt

P32754 - HPPD_HUMAN

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Protein

4-hydroxyphenylpyruvate dioxygenase

Gene

HPD

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

Functioni

Key enzyme in the degradation of tyrosine.

Catalytic activityi

4-hydroxyphenylpyruvate + O2 = homogentisate + CO2.

Cofactori

Fe cationBy similarityNote: Binds 1 Fe cation per subunit.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi183 – 1831IronCurated
Metal bindingi266 – 2661IronCurated
Metal bindingi349 – 3491IronCurated

GO - Molecular functioni

  1. 4-hydroxyphenylpyruvate dioxygenase activity Source: UniProtKB
  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: UniProtKB
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:HS08267-MONOMER.
ReactomeiREACT_1786. Phenylalanine and tyrosine catabolism.
UniPathwayiUPA00139; UER00362.

Names & Taxonomyi

Protein namesi
Recommended name:
4-hydroxyphenylpyruvate dioxygenase (EC:1.13.11.27)
Alternative name(s):
4-hydroxyphenylpyruvic acid oxidase
Short name:
4HPPD
Short name:
HPD
Short name:
HPPDase
Gene namesi
Name:HPD
Synonyms:PPD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:5147. HPD.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Tyrosinemia 3 (TYRSN3) [MIM:276710]: An inborn error of metabolism characterized by elevations of tyrosine in the blood and urine, seizures and mild mental retardation.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti160 – 1601Y → C in TYRSN3. 1 Publication
Corresponds to variant rs28934278 [ dbSNP | Ensembl ].
VAR_015445
Natural varianti268 – 2681A → V in TYRSN3. 1 Publication
VAR_015447
Natural varianti335 – 3351I → M in TYRSN3. 1 Publication
VAR_015448
Hawkinsinuria (HAWK) [MIM:140350]: An inborn error of tyrosine metabolism characterized by failure to thrive, persistent metabolic acidosis, fine and sparse hair, and excretion of the unusual cyclic amino acid metabolite, hawkinsin, in the urine.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

MIMi140350. phenotype.
276710. phenotype.
Orphaneti2118. Hawkinsinuria.
69723. Tyrosinemia type 3.
PharmGKBiPA29420.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 3933924-hydroxyphenylpyruvate dioxygenasePRO_0000088388Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonine1 Publication
Modified residuei132 – 1321N6-succinyllysineBy similarity
Modified residuei211 – 2111PhosphoserineBy similarity
Modified residuei226 – 2261PhosphoserineBy similarity
Modified residuei250 – 2501PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP32754.
PaxDbiP32754.
PRIDEiP32754.

PTM databases

PhosphoSiteiP32754.

Expressioni

Gene expression databases

BgeeiP32754.
CleanExiHS_HPD.
GenevestigatoriP32754.

Organism-specific databases

HPAiHPA038321.
HPA038322.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi109482. 7 interactions.
IntActiP32754. 4 interactions.
STRINGi9606.ENSP00000289004.

Structurei

Secondary structure

1
393
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi15 – 2511Combined sources
Helixi29 – 4012Combined sources
Beta strandi43 – 497Combined sources
Helixi50 – 523Combined sources
Beta strandi56 – 649Combined sources
Beta strandi67 – 7610Combined sources
Helixi80 – 8910Combined sources
Beta strandi91 – 10111Combined sources
Helixi103 – 11311Combined sources
Beta strandi117 – 12610Combined sources
Beta strandi129 – 1379Combined sources
Beta strandi143 – 1519Combined sources
Beta strandi154 – 1563Combined sources
Helixi170 – 1723Combined sources
Beta strandi178 – 18710Combined sources
Helixi193 – 20412Combined sources
Beta strandi207 – 2126Combined sources
Turni214 – 2163Combined sources
Beta strandi223 – 2308Combined sources
Beta strandi237 – 2448Combined sources
Helixi251 – 2599Combined sources
Beta strandi261 – 27212Combined sources
Helixi274 – 28310Combined sources
Helixi293 – 30311Combined sources
Helixi314 – 3207Combined sources
Beta strandi323 – 3264Combined sources
Beta strandi331 – 3377Combined sources
Beta strandi340 – 3445Combined sources
Beta strandi347 – 3559Combined sources
Helixi361 – 37717Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ISQX-ray1.75A8-393[»]
ProteinModelPortaliP32754.
SMRiP32754. Positions 9-384.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32754.

Family & Domainsi

Sequence similaritiesi

Belongs to the 4HPPD family.Curated

Phylogenomic databases

eggNOGiCOG3185.
GeneTreeiENSGT00530000063474.
HOGENOMiHOG000188687.
HOVERGENiHBG005987.
InParanoidiP32754.
KOiK00457.
OrthoDBiEOG75F4D7.
PhylomeDBiP32754.

Family and domain databases

Gene3Di3.10.180.10. 2 hits.
InterProiIPR005956. 4OHPhenylPyrv_dOase.
IPR029068. Glyas_Bleomycin-R_OHBP_Dase.
IPR004360. Glyas_Fos-R_dOase_dom.
[Graphical view]
PANTHERiPTHR11959. PTHR11959. 1 hit.
PfamiPF00903. Glyoxalase. 1 hit.
[Graphical view]
PIRSFiPIRSF009283. HPP_dOase. 1 hit.
SUPFAMiSSF54593. SSF54593. 1 hit.
TIGRFAMsiTIGR01263. 4HPPD. 1 hit.

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: P32754-1) [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

        10         20         30         40         50
MTTYSDKGAK PERGRFLHFH SVTFWVGNAK QAASFYCSKM GFEPLAYRGL
60 70 80 90 100
ETGSREVVSH VIKQGKIVFV LSSALNPWNK EMGDHLVKHG DGVKDIAFEV
110 120 130 140 150
EDCDYIVQKA RERGAKIMRE PWVEQDKFGK VKFAVLQTYG DTTHTLVEKM
160 170 180 190 200
NYIGQFLPGY EAPAFMDPLL PKLPKCSLEM IDHIVGNQPD QEMVSASEWY
210 220 230 240 250
LKNLQFHRFW SVDDTQVHTE YSSLRSIVVA NYEESIKMPI NEPAPGKKKS
260 270 280 290 300
QIQEYVDYNG GAGVQHIALK TEDIITAIRH LRERGLEFLS VPSTYYKQLR
310 320 330 340 350
EKLKTAKIKV KENIDALEEL KILVDYDEKG YLLQIFTKPV QDRPTLFLEV
360 370 380 390
IQRHNHQGFG AGNFNSLFKA FEEEQNLRGN LTNMETNGVV PGM
Length:393
Mass (Da):44,934
Last modified:January 23, 2007 - v2
Checksum:i4314A16532C33A2F
GO
Isoform 2 (identifier: P32754-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-39: Missing.

Show »
Length:354
Mass (Da):40,497
Checksum:i45F3E405EBD38707
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti162 – 1621A → P in AAC73008. (PubMed:9325050)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti33 – 331A → T in two patients with hawkinsinuria. 2 Publications
Corresponds to variant rs1154510 [ dbSNP | Ensembl ].
VAR_015444
Natural varianti113 – 1131R → Q.
Corresponds to variant rs11833399 [ dbSNP | Ensembl ].
VAR_048101
Natural varianti160 – 1601Y → C in TYRSN3. 1 Publication
Corresponds to variant rs28934278 [ dbSNP | Ensembl ].
VAR_015445
Natural varianti267 – 2671I → F.1 Publication
VAR_015446
Natural varianti268 – 2681A → V in TYRSN3. 1 Publication
VAR_015447
Natural varianti335 – 3351I → M in TYRSN3. 1 Publication
VAR_015448
Natural varianti340 – 3401V → L.1 Publication
Corresponds to variant rs36023382 [ dbSNP | Ensembl ].
VAR_015449

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3939Missing in isoform 2. 1 PublicationVSP_044302Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D31628 Genomic DNA. Translation: BAA06498.1.
X72389 mRNA. Translation: CAA51082.1.
U29895 Genomic DNA. Translation: AAC73008.1.
AK057510 mRNA. Translation: BAG51925.1.
AK290826 mRNA. Translation: BAF83515.1.
AC069503 Genomic DNA. No translation available.
AC079360 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW98292.1.
BC024287 mRNA. Translation: AAH24287.1.
CCDSiCCDS53839.1. [P32754-2]
CCDS9224.1. [P32754-1]
PIRiS32458.
RefSeqiNP_001165464.1. NM_001171993.1. [P32754-2]
NP_002141.1. NM_002150.2. [P32754-1]
UniGeneiHs.2899.

Genome annotation databases

EnsembliENST00000543163; ENSP00000441677; ENSG00000158104. [P32754-2]
GeneIDi3242.
KEGGihsa:3242.
UCSCiuc001ubj.3. human. [P32754-1]

Polymorphism databases

DMDMi417144.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D31628 Genomic DNA. Translation: BAA06498.1 .
X72389 mRNA. Translation: CAA51082.1 .
U29895 Genomic DNA. Translation: AAC73008.1 .
AK057510 mRNA. Translation: BAG51925.1 .
AK290826 mRNA. Translation: BAF83515.1 .
AC069503 Genomic DNA. No translation available.
AC079360 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW98292.1 .
BC024287 mRNA. Translation: AAH24287.1 .
CCDSi CCDS53839.1. [P32754-2 ]
CCDS9224.1. [P32754-1 ]
PIRi S32458.
RefSeqi NP_001165464.1. NM_001171993.1. [P32754-2 ]
NP_002141.1. NM_002150.2. [P32754-1 ]
UniGenei Hs.2899.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3ISQ X-ray 1.75 A 8-393 [» ]
ProteinModelPortali P32754.
SMRi P32754. Positions 9-384.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109482. 7 interactions.
IntActi P32754. 4 interactions.
STRINGi 9606.ENSP00000289004.

Chemistry

ChEMBLi CHEMBL1861.
DrugBanki DB00348. Nitisinone.

PTM databases

PhosphoSitei P32754.

Polymorphism databases

DMDMi 417144.

Proteomic databases

MaxQBi P32754.
PaxDbi P32754.
PRIDEi P32754.

Protocols and materials databases

DNASUi 3242.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000543163 ; ENSP00000441677 ; ENSG00000158104 . [P32754-2 ]
GeneIDi 3242.
KEGGi hsa:3242.
UCSCi uc001ubj.3. human. [P32754-1 ]

Organism-specific databases

CTDi 3242.
GeneCardsi GC12M122277.
HGNCi HGNC:5147. HPD.
HPAi HPA038321.
HPA038322.
MIMi 140350. phenotype.
276710. phenotype.
609695. gene.
neXtProti NX_P32754.
Orphaneti 2118. Hawkinsinuria.
69723. Tyrosinemia type 3.
PharmGKBi PA29420.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG3185.
GeneTreei ENSGT00530000063474.
HOGENOMi HOG000188687.
HOVERGENi HBG005987.
InParanoidi P32754.
KOi K00457.
OrthoDBi EOG75F4D7.
PhylomeDBi P32754.

Enzyme and pathway databases

UniPathwayi UPA00139 ; UER00362 .
BioCyci MetaCyc:HS08267-MONOMER.
Reactomei REACT_1786. Phenylalanine and tyrosine catabolism.

Miscellaneous databases

ChiTaRSi HPD. human.
EvolutionaryTracei P32754.
GenomeRNAii 3242.
NextBioi 12905.
PROi P32754.
SOURCEi Search...

Gene expression databases

Bgeei P32754.
CleanExi HS_HPD.
Genevestigatori P32754.

Family and domain databases

Gene3Di 3.10.180.10. 2 hits.
InterProi IPR005956. 4OHPhenylPyrv_dOase.
IPR029068. Glyas_Bleomycin-R_OHBP_Dase.
IPR004360. Glyas_Fos-R_dOase_dom.
[Graphical view ]
PANTHERi PTHR11959. PTHR11959. 1 hit.
Pfami PF00903. Glyoxalase. 1 hit.
[Graphical view ]
PIRSFi PIRSF009283. HPP_dOase. 1 hit.
SUPFAMi SSF54593. SSF54593. 1 hit.
TIGRFAMsi TIGR01263. 4HPPD. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Structure of the human 4-hydroxyphenylpyruvic acid dioxygenase gene (HPD)."
    Awata H., Endo F., Matsuda I.
    Genomics 23:534-539(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
  2. "Regional assignment of the human 4-hydroxyphenylpyruvate dioxygenase gene (HPD) to 12q24-->qter by fluorescence in situ hybridization."
    Stenman G., Roijer E., Rueetschi U., Dellsen A., Rymo L., Lindstedt S.
    Cytogenet. Cell Genet. 71:374-376(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Human 4-hydroxyphenylpyruvate dioxygenase gene (HPD)."
    Ruetschi U., Rymo L., Lindstedt S.
    Genomics 44:292-299(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (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] (ISOFORMS 1 AND 2).
    Tissue: Liver and Testis.
  5. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., 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., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(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: Liver.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  10. "Crystal structure of human 4-hydroxyphenylpyruvate dioxygenase."
    Structural genomics consortium (SGC)
    Submitted (SEP-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 8-393 IN COMPLEX WITH COBALT IONS.
  11. "Mutations in the 4-hydroxyphenylpyruvate dioxygenase gene (HPD) in patients with tyrosinemia type III."
    Rueetschi U., Cerone R., Perez-Cerda C., Schiaffino M.C., Standing S., Ugarte M., Holme E.
    Hum. Genet. 106:654-662(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS TYRSN3 CYS-160 AND MET-335, VARIANTS THR-33; PHE-267 AND LEU-340.
  12. "Mutations in the 4-hydroxyphenylpyruvic acid dioxygenase gene are responsible for tyrosinemia type III and hawkinsinuria."
    Tomoeda K., Awata H., Matsuura T., Matsuda I., Ploechl E., Milovac T., Boneh A., Scott C.R., Danks D.M., Endo F.
    Mol. Genet. Metab. 71:506-510(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT TYRSN3 VAL-268, VARIANT HAWK THR-33.

Entry informationi

Entry nameiHPPD_HUMAN
AccessioniPrimary (citable) accession number: P32754
Secondary accession number(s): A8K461, B3KQ63, Q13234
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 153 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 12
    Human chromosome 12: 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