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P16331

- PH4H_MOUSE

UniProt

P16331 - PH4H_MOUSE

Protein

Phenylalanine-4-hydroxylase

Gene

Pah

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 4 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    L-phenylalanine + tetrahydrobiopterin + O2 = L-tyrosine + 4a-hydroxytetrahydrobiopterin.

    Cofactori

    Fe2+ ion.

    Enzyme regulationi

    N-terminal region of PAH is thought to contain allosteric binding sites for phenylalanine and to constitute an "inhibitory" domain that regulates the activity of a catalytic domain in the C-terminal portion of the molecule.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi285 – 2851IronBy similarity
    Metal bindingi290 – 2901IronBy similarity
    Metal bindingi330 – 3301IronBy similarity

    GO - Molecular functioni

    1. amino acid binding Source: InterPro
    2. iron ion binding Source: InterPro
    3. phenylalanine 4-monooxygenase activity Source: MGI

    GO - Biological processi

    1. L-phenylalanine catabolic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Monooxygenase, Oxidoreductase

    Keywords - Biological processi

    Phenylalanine catabolism

    Keywords - Ligandi

    Iron, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_189094. Abnormal metabolism in phenylketonuria.
    UniPathwayiUPA00139; UER00337.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phenylalanine-4-hydroxylase (EC:1.14.16.1)
    Short name:
    PAH
    Alternative name(s):
    Phe-4-monooxygenase
    Gene namesi
    Name:Pah
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 10

    Organism-specific databases

    MGIiMGI:97473. Pah.

    Pathology & Biotechi

    Involvement in diseasei

    Mouse strains deficient in phenylalanine hydroxylase (Pah) were created as models of phenylketonuria (PKU).

    Keywords - Diseasei

    Disease mutation

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 453452Phenylalanine-4-hydroxylasePRO_0000205549Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei16 – 161Phosphoserine; by PKABy similarity

    Post-translational modificationi

    Phosphorylation at Ser-16 increases basal activity and facilitates activation by the substrate phenylalanine.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP16331.
    PaxDbiP16331.
    PRIDEiP16331.

    PTM databases

    PhosphoSiteiP16331.

    Expressioni

    Gene expression databases

    ArrayExpressiP16331.
    BgeeiP16331.
    CleanExiMM_PAH.
    GenevestigatoriP16331.

    Interactioni

    Subunit structurei

    Homodimer and homotetramer.By similarity

    Protein-protein interaction databases

    IntActiP16331. 3 interactions.
    MINTiMINT-1855311.
    STRINGi10090.ENSMUSP00000020241.

    Structurei

    3D structure databases

    ProteinModelPortaliP16331.
    SMRiP16331. Positions 19-427.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini36 – 11479ACTPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 ACT domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG3186.
    GeneTreeiENSGT00390000010268.
    HOGENOMiHOG000233373.
    HOVERGENiHBG006841.
    InParanoidiQ91WV1.
    KOiK00500.
    OMAiRYNAYTQ.
    OrthoDBiEOG7KM5T1.
    TreeFamiTF313327.

    Family and domain databases

    Gene3Di1.10.800.10. 1 hit.
    InterProiIPR002912. ACT_dom.
    IPR001273. ArAA_hydroxylase.
    IPR018301. ArAA_hydroxylase_Fe/CU_BS.
    IPR019774. Aromatic-AA_hydroxylase_C.
    IPR005961. Phe-4-hydroxylase_tetra.
    IPR019773. Tyrosine_3-monooxygenase-like.
    [Graphical view]
    PANTHERiPTHR11473. PTHR11473. 1 hit.
    PfamiPF01842. ACT. 1 hit.
    PF00351. Biopterin_H. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000336. TH. 1 hit.
    PRINTSiPR00372. FYWHYDRXLASE.
    SUPFAMiSSF56534. SSF56534. 1 hit.
    TIGRFAMsiTIGR01268. Phe4hydrox_tetr. 1 hit.
    PROSITEiPS51671. ACT. 1 hit.
    PS00367. BH4_AAA_HYDROXYL_1. 1 hit.
    PS51410. BH4_AAA_HYDROXYL_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P16331-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAVVLENGV LSRKLSDFGQ ETSYIEDNSN QNGAVSLIFS LKEEVGALAK    50
    VLRLFEENEI NLTHIESRPS RLNKDEYEFF TYLDKRSKPV LGSIIKSLRN 100
    DIGATVHELS RDKEKNTVPW FPRTIQELDR FANQILSYGA ELDADHPGFK 150
    DPVYRARRKQ FADIAYNYRH GQPIPRVEYT EEERKTWGTV FRTLKALYKT 200
    HACYEHNHIF PLLEKYCGFR EDNIPQLEDV SQFLQTCTGF RLRPVAGLLS 250
    SRDFLGGLAF RVFHCTQYIR HGSKPMYTPE PDICHELLGH VPLFSDRSFA 300
    QFSQEIGLAS LGAPDEYIEK LATIYWFTVE FGLCKEGDSI KAYGAGLLSS 350
    FGELQYCLSD KPKLLPLELE KTACQEYTVT EFQPLYYVAE SFNDAKEKVR 400
    TFAATIPRPF SVRYDPYTQR VEVLDNTQQL KILADSINSE VGILCHALQK 450
    IKS 453
    Length:453
    Mass (Da):51,900
    Last modified:July 27, 2011 - v4
    Checksum:i551F181FA59DEA5B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti383 – 3831Q → R in CAA36205. (PubMed:2334400)Curated
    Sequence conflicti432 – 4321I → N in CAA36205. (PubMed:2334400)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti106 – 1061V → A in PAH-ENU1; mild PKU phenotype. 1 Publication
    Natural varianti263 – 2631F → S in PAH-ENU2; severe PKU phenotype. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X51942 mRNA. Translation: CAA36205.1.
    AC122360 Genomic DNA. No translation available.
    BC013458 mRNA. Translation: AAH13458.1.
    CCDSiCCDS24102.1.
    PIRiS15758.
    RefSeqiNP_032803.2. NM_008777.3.
    UniGeneiMm.263539.

    Genome annotation databases

    EnsembliENSMUST00000020241; ENSMUSP00000020241; ENSMUSG00000020051.
    GeneIDi18478.
    KEGGimmu:18478.
    UCSCiuc007gqt.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X51942 mRNA. Translation: CAA36205.1 .
    AC122360 Genomic DNA. No translation available.
    BC013458 mRNA. Translation: AAH13458.1 .
    CCDSi CCDS24102.1.
    PIRi S15758.
    RefSeqi NP_032803.2. NM_008777.3.
    UniGenei Mm.263539.

    3D structure databases

    ProteinModelPortali P16331.
    SMRi P16331. Positions 19-427.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P16331. 3 interactions.
    MINTi MINT-1855311.
    STRINGi 10090.ENSMUSP00000020241.

    PTM databases

    PhosphoSitei P16331.

    Proteomic databases

    MaxQBi P16331.
    PaxDbi P16331.
    PRIDEi P16331.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000020241 ; ENSMUSP00000020241 ; ENSMUSG00000020051 .
    GeneIDi 18478.
    KEGGi mmu:18478.
    UCSCi uc007gqt.2. mouse.

    Organism-specific databases

    CTDi 5053.
    MGIi MGI:97473. Pah.

    Phylogenomic databases

    eggNOGi COG3186.
    GeneTreei ENSGT00390000010268.
    HOGENOMi HOG000233373.
    HOVERGENi HBG006841.
    InParanoidi Q91WV1.
    KOi K00500.
    OMAi RYNAYTQ.
    OrthoDBi EOG7KM5T1.
    TreeFami TF313327.

    Enzyme and pathway databases

    UniPathwayi UPA00139 ; UER00337 .
    Reactomei REACT_189094. Abnormal metabolism in phenylketonuria.

    Miscellaneous databases

    ChiTaRSi PAH. mouse.
    NextBioi 294182.
    PROi P16331.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P16331.
    Bgeei P16331.
    CleanExi MM_PAH.
    Genevestigatori P16331.

    Family and domain databases

    Gene3Di 1.10.800.10. 1 hit.
    InterProi IPR002912. ACT_dom.
    IPR001273. ArAA_hydroxylase.
    IPR018301. ArAA_hydroxylase_Fe/CU_BS.
    IPR019774. Aromatic-AA_hydroxylase_C.
    IPR005961. Phe-4-hydroxylase_tetra.
    IPR019773. Tyrosine_3-monooxygenase-like.
    [Graphical view ]
    PANTHERi PTHR11473. PTHR11473. 1 hit.
    Pfami PF01842. ACT. 1 hit.
    PF00351. Biopterin_H. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000336. TH. 1 hit.
    PRINTSi PR00372. FYWHYDRXLASE.
    SUPFAMi SSF56534. SSF56534. 1 hit.
    TIGRFAMsi TIGR01268. Phe4hydrox_tetr. 1 hit.
    PROSITEi PS51671. ACT. 1 hit.
    PS00367. BH4_AAA_HYDROXYL_1. 1 hit.
    PS51410. BH4_AAA_HYDROXYL_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Mouse phenylalanine hydroxylase. Homology and divergence from human phenylalanine hydroxylase."
      Ledley F.D., Grenett H.E., Dunbar B.S., Woo S.L.C.
      Biochem. J. 267:399-406(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/6J.
      Tissue: Liver.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. "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].
      Strain: FVB/N.
      Tissue: Kidney.
    4. Bienvenut W.V.
      Submitted (JUL-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-13; 54-68; 160-169 AND 253-261, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Liver.
    5. "Amino acid sequence at the phosphorylated site of rat liver phenylalanine hydroxylase and phosphorylation of a corresponding synthetic peptide."
      Wretborn M., Humble E., Ragnarsson U., Engstrom L.
      Biochem. Biophys. Res. Commun. 93:403-408(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 12-21.
    6. "Sequence comparison of rat liver phenylalanine hydroxylase and its cDNA clones."
      Robson K.J.H., Beattie W., James R.J., Cotton R.C.H., Morgan F.J., Woo S.L.C.
      Biochemistry 23:5671-5675(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 277-294.
    7. "Characterization of mutations at the mouse phenylalanine hydroxylase locus."
      McDonald J.D., Charlton C.K.
      Genomics 39:402-405(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS PAH-ENU1 ALA-106 AND PAH-ENU2 SER-263.

    Entry informationi

    Entry nameiPH4H_MOUSE
    AccessioniPrimary (citable) accession number: P16331
    Secondary accession number(s): Q91WV1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 145 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3