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P16331

- PH4H_MOUSE

UniProt

P16331 - PH4H_MOUSE

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Protein
Phenylalanine-4-hydroxylase
Gene
Pah
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 – 2851Iron By similarity
Metal bindingi290 – 2901Iron By similarity
Metal bindingi330 – 3301Iron By 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
Complete GO annotation...

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-hydroxylase
PRO_0000205549Add
BLAST

Amino acid modifications

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini36 – 11479ACT
Add
BLAST

Sequence similaritiesi

Contains 1 ACT domain.

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

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti383 – 3831Q → R in CAA36205. 1 Publication
Sequence conflicti432 – 4321I → N in CAA36205. 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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 144 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

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