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P07101 (TY3H_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 168. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tyrosine 3-monooxygenase

EC=1.14.16.2
Alternative name(s):
Tyrosine 3-hydroxylase
Short name=TH
Gene names
Name:TH
Synonyms:TYH
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length528 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays an important role in the physiology of adrenergic neurons.

Catalytic activity

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

Cofactor

Fe2+ ion.

Enzyme regulation

Phosphorylation leads to an increase in the catalytic activity.

Pathway

Catecholamine biosynthesis; dopamine biosynthesis; dopamine from L-tyrosine: step 1/2.

Tissue specificity

Mainly expressed in the brain and adrenal glands.

Involvement in disease

Segawa syndrome autosomal recessive (ARSEGS) [MIM:605407]: A form of DOPA-responsive dystonia presenting in infancy or early childhood. Dystonia is defined by the presence of sustained involuntary muscle contractions, often leading to abnormal postures. Some cases present with parkinsonian symptoms in infancy. Unlike all other forms of dystonia, it is an eminently treatable condition, due to a favorable response to L-DOPA.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12 Ref.13 Ref.15 Ref.16 Ref.17 Ref.19 Ref.22

May play a role in the pathogenesis of Parkinson disease (PD). A genome-wide copy number variation analysis has identified a 34 kilobase deletion over the TH gene in a PD patient but not in any controls. Ref.12

Sequence similarities

Belongs to the biopterin-dependent aromatic amino acid hydroxylase family.

Sequence caution

The sequence AAA61173.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processCatecholamine biosynthesis
Neurotransmitter biosynthesis
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Dystonia
Parkinson disease
Parkinsonism
   LigandIron
Metal-binding
   Molecular functionMonooxygenase
Oxidoreductase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processanatomical structure morphogenesis

Traceable author statement PubMed 7715703. Source: ProtInc

catecholamine biosynthetic process

Traceable author statement. Source: Reactome

cellular nitrogen compound metabolic process

Traceable author statement. Source: Reactome

cellular response to drug

Inferred from electronic annotation. Source: Ensembl

cellular response to glucose stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to growth factor stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to manganese ion

Inferred from electronic annotation. Source: Ensembl

cellular response to nicotine

Inferred from electronic annotation. Source: Ensembl

cerebral cortex development

Inferred from electronic annotation. Source: Ensembl

circadian sleep/wake cycle

Inferred from electronic annotation. Source: Ensembl

dopamine biosynthetic process

Inferred from direct assay PubMed 12457228. Source: BHF-UCL

dopamine biosynthetic process from tyrosine

Non-traceable author statement PubMed 10907721. Source: BHF-UCL

eating behavior

Inferred from electronic annotation. Source: Ensembl

embryonic camera-type eye morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

epinephrine biosynthetic process

Inferred from direct assay PubMed 12457228. Source: BHF-UCL

eye photoreceptor cell development

Inferred from sequence or structural similarity. Source: BHF-UCL

fatty acid metabolic process

Inferred from electronic annotation. Source: Ensembl

glycoside metabolic process

Inferred from electronic annotation. Source: Ensembl

heart development

Inferred from sequence or structural similarity. Source: BHF-UCL

heart morphogenesis

Non-traceable author statement PubMed 12113410. Source: BHF-UCL

isoquinoline alkaloid metabolic process

Inferred from electronic annotation. Source: Ensembl

learning

Inferred from sequence or structural similarity. Source: BHF-UCL

locomotory behavior

Inferred from sequence or structural similarity. Source: BHF-UCL

mating behavior

Inferred from electronic annotation. Source: Ensembl

memory

Inferred from sequence or structural similarity. Source: BHF-UCL

multicellular organismal aging

Inferred from electronic annotation. Source: Ensembl

neurotransmitter biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

norepinephrine biosynthetic process

Inferred from direct assay PubMed 12457228. Source: BHF-UCL

organ morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

phthalate metabolic process

Inferred from electronic annotation. Source: Ensembl

phytoalexin metabolic process

Inferred from electronic annotation. Source: Ensembl

pigmentation

Traceable author statement PubMed 12631248. Source: BHF-UCL

regulation of heart contraction

Inferred from sequence or structural similarity. Source: BHF-UCL

response to activity

Inferred from electronic annotation. Source: Ensembl

response to amphetamine

Inferred from electronic annotation. Source: Ensembl

response to corticosterone

Inferred from electronic annotation. Source: Ensembl

response to electrical stimulus

Inferred from electronic annotation. Source: Ensembl

response to estradiol

Inferred from electronic annotation. Source: Ensembl

response to ethanol

Inferred from direct assay PubMed 18343820. Source: BHF-UCL

response to ether

Inferred from electronic annotation. Source: Ensembl

response to herbicide

Inferred from electronic annotation. Source: Ensembl

response to hypoxia

Inferred from direct assay PubMed 17520326. Source: BHF-UCL

response to light stimulus

Inferred from electronic annotation. Source: Ensembl

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

response to nutrient levels

Inferred from electronic annotation. Source: Ensembl

response to peptide hormone

Inferred from electronic annotation. Source: Ensembl

response to pyrethroid

Inferred from electronic annotation. Source: Ensembl

response to salt stress

Inferred from electronic annotation. Source: Ensembl

response to water deprivation

Inferred from electronic annotation. Source: Ensembl

response to zinc ion

Inferred from electronic annotation. Source: Ensembl

sensory perception of sound

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

social behavior

Inferred from electronic annotation. Source: Ensembl

sphingolipid metabolic process

Inferred from electronic annotation. Source: Ensembl

synaptic transmission, dopaminergic

Inferred from sequence or structural similarity. Source: BHF-UCL

synaptic vesicle amine transport

Inferred from electronic annotation. Source: Ensembl

terpene metabolic process

Inferred from electronic annotation. Source: Ensembl

visual perception

Inferred from sequence or structural similarity. Source: BHF-UCL

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 10907721. Source: UniProtKB

cytoplasmic side of plasma membrane

Inferred from direct assay PubMed 12457228. Source: BHF-UCL

cytoplasmic vesicle

Inferred from direct assay PubMed 12457228. Source: BHF-UCL

cytosol

Traceable author statement. Source: Reactome

dendrite

Inferred from electronic annotation. Source: Ensembl

melanosome membrane

Inferred from direct assay PubMed 12631248. Source: BHF-UCL

mitochondrion

Inferred from electronic annotation. Source: Ensembl

neuron projection

Inferred from direct assay PubMed 17135716. Source: BHF-UCL

nucleus

Inferred from sequence or structural similarity. Source: BHF-UCL

perikaryon

Inferred from sequence or structural similarity. Source: BHF-UCL

smooth endoplasmic reticulum

Inferred from direct assay PubMed 12457228. Source: BHF-UCL

synaptic vesicle

Inferred from electronic annotation. Source: Ensembl

terminal bouton

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionamino acid binding

Inferred from electronic annotation. Source: Ensembl

dopamine binding

Inferred from electronic annotation. Source: Ensembl

ferric iron binding

Inferred from electronic annotation. Source: Ensembl

ferrous iron binding

Inferred from electronic annotation. Source: Ensembl

oxygen binding

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction PubMed 11943812. Source: BHF-UCL

tetrahydrobiopterin binding

Inferred from electronic annotation. Source: Ensembl

tyrosine 3-monooxygenase activity

Inferred from direct assay PubMed 16338639. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]

Note: TH transcripts lacking exons 8 and 9 present concomitant splicing in exons 1b and 2.
Isoform 3 (identifier: P07101-1)

Also known as: TH type 4;

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.
Isoform 1 (identifier: P07101-2)

Also known as: TH type 3;

The sequence of this isoform differs from the canonical sequence as follows:
     31-34: Missing.
Isoform 2 (identifier: P07101-3)

Also known as: HTH-1; hTH-Delta1b,2; TH type 1;

The sequence of this isoform differs from the canonical sequence as follows:
     31-61: Missing.
Isoform 4 (identifier: P07101-4)

Also known as: hTH-Delta2; TH type 2;

The sequence of this isoform differs from the canonical sequence as follows:
     35-61: Missing.
Isoform 5 (identifier: P07101-5)

Also known as: hTH-Delta2,8,9;

The sequence of this isoform differs from the canonical sequence as follows:
     35-61: Missing.
     264-357: Missing.
Note: Lacks catalytic activity.
Isoform 6 (identifier: P07101-6)

Also known as: hTH-Delta1b,2,8,9;

The sequence of this isoform differs from the canonical sequence as follows:
     31-61: Missing.
     264-357: Missing.
Note: Lacks catalytic activity.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 528527Tyrosine 3-monooxygenase
PRO_0000205561

Regions

Compositional bias85 – 906Poly-Ala

Sites

Metal binding3611Iron By similarity
Metal binding3661Iron By similarity
Metal binding4061Iron By similarity

Amino acid modifications

Modified residue191Phosphoserine; by CaMK2 Ref.11
Modified residue621Phosphoserine By similarity
Modified residue711Phosphoserine; by CaMK2 and PKA Ref.11

Natural variations

Alternative sequence31 – 6131Missing in isoform 2 and isoform 6.
VSP_000544
Alternative sequence31 – 344Missing in isoform 1.
VSP_000543
Alternative sequence35 – 6127Missing in isoform 4 and isoform 5.
VSP_000541
Alternative sequence264 – 35794Missing in isoform 5 and isoform 6.
VSP_054338
Natural variant1121V → M Common polymorphism. Ref.8 Ref.14 Ref.17 Ref.20
Corresponds to variant rs6356 [ dbSNP | Ensembl ].
VAR_014025
Natural variant2331R → H in ARSEGS. Ref.19
VAR_014026
Natural variant2361L → P in ARSEGS; severe parkinsonian symptoms in early infancy; strongly reduced stability and catalytic activity; rare mutation. Ref.16 Ref.17
VAR_014027
Natural variant2761T → P in ARSEGS; parkinsonian symptoms in infancy. Ref.22
Corresponds to variant rs28934581 [ dbSNP | Ensembl ].
VAR_014028
Natural variant3141T → M in ARSEGS; parkinsonian symptoms in infancy. Ref.22
VAR_014029
Natural variant3371R → H in ARSEGS; parkinsonian symptoms in infancy. Ref.22
Corresponds to variant rs28934580 [ dbSNP | Ensembl ].
VAR_014030
Natural variant4121Q → K in ARSEGS; reduced affinity for L-tyrosine. Ref.13 Ref.15
VAR_014031
Natural variant4941T → M in ARSEGS; parkinsonian symptoms in infancy. Ref.22
Corresponds to variant rs45471299 [ dbSNP | Ensembl ].
VAR_014032
Natural variant4991V → M. Ref.18
Corresponds to variant rs1800033 [ dbSNP | Ensembl ].
VAR_014033

Experimental info

Sequence conflict3731R → H in AAI43615. Ref.8
Sequence conflict4011Y → S in AAA61179. Ref.1
Sequence conflict4011Y → S in CAA28908. Ref.2
Sequence conflict4011Y → S in CAA68472. Ref.3

Secondary structure

...................................................... 528
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 3 (TH type 4) [UniParc].

Last modified June 16, 2009. Version 5.
Checksum: 31D2D49955ACF070

FASTA52858,600
        10         20         30         40         50         60 
MPTPDATTPQ AKGFRRAVSE LDAKQAEAIM VRGQGAPGPS LTGSPWPGTA APAASYTPTP 

        70         80         90        100        110        120 
RSPRFIGRRQ SLIEDARKER EAAVAAAAAA VPSEPGDPLE AVAFEEKEGK AVLNLLFSPR 

       130        140        150        160        170        180 
ATKPSALSRA VKVFETFEAK IHHLETRPAQ RPRAGGPHLE YFVRLEVRRG DLAALLSGVR 

       190        200        210        220        230        240 
QVSEDVRSPA GPKVPWFPRK VSELDKCHHL VTKFDPDLDL DHPGFSDQVY RQRRKLIAEI 

       250        260        270        280        290        300 
AFQYRHGDPI PRVEYTAEEI ATWKEVYTTL KGLYATHACG EHLEAFALLE RFSGYREDNI 

       310        320        330        340        350        360 
PQLEDVSRFL KERTGFQLRP VAGLLSARDF LASLAFRVFQ CTQYIRHASS PMHSPEPDCC 

       370        380        390        400        410        420 
HELLGHVPML ADRTFAQFSQ DIGLASLGAS DEEIEKLSTL YWFTVEFGLC KQNGEVKAYG 

       430        440        450        460        470        480 
AGLLSSYGEL LHCLSEEPEI RAFDPEAAAV QPYQDQTYQS VYFVSESFSD AKDKLRSYAS 

       490        500        510        520 
RIQRPFSVKF DPYTLAIDVL DSPQAVRRSL EGVQDELDTL AHALSAIG 

« Hide

Isoform 1 (TH type 3) [UniParc].

Checksum: 708422BBD3304A6C
Show »

FASTA52458,160
Isoform 2 (HTH-1) (hTH-Delta1b,2) (TH type 1) [UniParc].

Checksum: 6CB8EDC9C4874288
Show »

FASTA49755,612
Isoform 4 (hTH-Delta2) (TH type 2) [UniParc].

Checksum: B614295B9CB2921F
Show »

FASTA50156,052
Isoform 5 (hTH-Delta2,8,9) [UniParc].

Checksum: 71FB6BA8A6061F44
Show »

FASTA40745,338
Isoform 6 (hTH-Delta1b,2,8,9) [UniParc].

Checksum: DAD3F18191575F99
Show »

FASTA40344,898

References

« Hide 'large scale' references
[1]"Isolation of a novel cDNA clone for human tyrosine hydroxylase: alternative RNA splicing produces four kinds of mRNA from a single gene."
Kaneda N., Kobayashi K., Ichinose H., Kishi F., Nakazawa A., Kurosawa Y., Fujita K., Nagatsu T.
Biochem. Biophys. Res. Commun. 146:971-975(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[2]"A single human gene encoding multiple tyrosine hydroxylases with different predicted functional characteristics."
Grima B., Lamouroux A., Boni C., Julien J.-F., Javoy-Agid F., Mallet J.
Nature 326:707-711(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING.
[3]"Isolation of a full-length cDNA clone encoding human tyrosine hydroxylase type 3."
Kobayashi K., Kaneda N., Ichinose H., Kishi F., Nakazawa A., Kurosawa Y., Fujita K., Nagatsu T.
Nucleic Acids Res. 15:6733-6733(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]"Structure of the human tyrosine hydroxylase gene: alternative splicing from a single gene accounts for generation of four mRNA types."
Kobayashi K., Kaneda N., Ichinose H., Kishi F., Nakazawa A., Kurosawa Y., Fujita K., Nagatsu T.
J. Biochem. 103:907-912(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
[5]"Characterisation of novel splicing variants of the tyrosine hydroxylase C-terminal domain in human neuroblastic tumours."
Roma J., Saus E., Cuadros M., Reventos J., Sanchez de Toledo J., Gallego S.
Biol. Chem. 388:419-426(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5 AND 6), ALTERNATIVE SPLICING.
[6]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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] (ISOFORMS 2 AND 4), VARIANT MET-112.
[9]"Analysis of the 5' region of the human tyrosine hydroxylase gene: combinatorial patterns of exon splicing generate multiple regulated tyrosine hydroxylase isoforms."
le Bourdelles B., Boularand S., Boni C., Horellou P., Dumas S., Grima B., Mallet J.
J. Neurochem. 50:988-991(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[10]"Expression of human tyrosine hydroxylase cDNA in invertebrate cells using a baculovirus vector."
Ginns E.I., Rehavi M., Martin B.M., Weller M., O'Malley K.L., Lamarca M.E., McAllister C.G., Paul S.M.
J. Biol. Chem. 263:7406-7410(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-30.
[11]"Phosphorylation of human recombinant tyrosine hydroxylase isoforms 1 and 2: an additional phosphorylated residue in isoform 2, generated through alternative splicing."
Le Bourdelles B., Horellou P., Le Caer J.P., Denefle P., Latta M., Haavik J., Guibert B., Mayaux J.F., Mallet J.
J. Biol. Chem. 266:17124-17130(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-19 AND SER-71.
[12]"A rare novel deletion of the tyrosine hydroxylase gene in Parkinson disease."
Bademci G., Edwards T.L., Torres A.L., Scott W.K., Zuchner S., Martin E.R., Vance J.M., Wang L.
Hum. Mutat. 31:E1767-E1771(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: POSSIBLE INVOLVEMENT IN PARKINSON DISEASE.
[13]"A point mutation in the tyrosine hydroxylase gene associated with Segawa's syndrome."
Luedecke B., Dworniczak B., Bartholome K.
Hum. Genet. 95:123-125(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ARSEGS LYS-412.
[14]"Frequent sequence variant in the human tyrosine hydroxylase gene."
Luedecke B., Bartholome K.
Hum. Genet. 95:716-716(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MET-112.
[15]"Recessively inherited L-DOPA-responsive dystonia caused by a point mutation (Q381K) in the tyrosine hydroxylase gene."
Knappskog P.M., Flatmark T., Mallet J., Luedecke B., Bartholome K.
Hum. Mol. Genet. 4:1209-1212(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT ARSEGS LYS-412.
[16]"Recessively inherited L-DOPA-responsive parkinsonism in infancy caused by a point mutation (L205P) in the tyrosine hydroxylase gene."
Luedecke B., Knappskog P.M., Clayton P.T., Surtees R.A.H., Clelland J.D., Heales S.J.R., Brand M.P., Bartholome K., Flatmark T.
Hum. Mol. Genet. 5:1023-1028(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT ARSEGS PRO-236.
[17]"Association study of structural mutations of the tyrosine hydroxylase gene with schizophrenia and Parkinson's disease."
Kunugi H., Kawada Y., Hattori M., Ueki A., Otsuka M., Nanko S.
Am. J. Med. Genet. 81:131-133(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ARSEGS PRO-236, VARIANT MET-112.
[18]"Systematic search for variations in the tyrosine hydroxylase gene and their associations with schizophrenia, affective disorders, and alcoholism."
Ishiguro H., Arinami T., Saito T., Akazawa S., Enomoto M., Mitushio H., Fujishiro H., Tada K., Akimoto Y., Mifune H., Shiozuka S., Hamaguchi H., Toru M., Shibuya H.
Am. J. Med. Genet. 81:388-396(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MET-499.
[19]"A common point mutation in the tyrosine hydroxylase gene in autosomal recessive L-DOPA-responsive dystonia in the Dutch population."
van den Heuvel L.P.W.J., Luiten B., Smeitink J.A.M., de Rijk-van Andel J.F., Hyland K., Steenbergen-Spanjers G.C.H., Janssen R.J.T., Wevers R.A.
Hum. Genet. 102:644-646(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ARSEGS HIS-233.
[20]"Characterization of single-nucleotide polymorphisms in coding regions of human genes."
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.
Nat. Genet. 22:231-238(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MET-112.
[21]Erratum
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.
Nat. Genet. 23:373-373(1999)
[22]"Four novel mutations in the tyrosine hydroxylase gene in patients with infantile parkinsonism."
Swaans R.J.M., Rondot P., Renier W.O., Van Den Heuvel L.P.W.J., Steenbergen-Spanjers G.C.H., Wevers R.A.
Ann. Hum. Genet. 64:25-31(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ARSEGS PRO-276; MET-314; HIS-337 AND MET-494.
+Additional computationally mapped references.

Web resources

Wikipedia

Tyrosine hydroxylase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M17589 mRNA. Translation: AAA61179.1.
X05290 mRNA. Translation: CAA28908.1.
Y00414 mRNA. Translation: CAA68472.1.
DQ677336 mRNA. Translation: ABG73364.1.
DQ677337 mRNA. Translation: ABG73365.1.
AC132217 Genomic DNA. No translation available.
M24791, M24787, M24789 Genomic DNA. Translation: AAA61173.1. Sequence problems.
CH471158 Genomic DNA. Translation: EAX02493.1.
BC104967 mRNA. Translation: AAI04968.1.
BC143611 mRNA. Translation: AAI43612.1.
BC143614 mRNA. Translation: AAI43615.1.
M24791, M24787 Genomic DNA. Translation: AAA61170.1.
M20911 mRNA. Translation: AAA61167.1.
CCDSCCDS31338.1. [P07101-2]
CCDS7730.1. [P07101-3]
CCDS7731.1. [P07101-1]
PIRWHHUY4. A30002.
RefSeqNP_000351.2. NM_000360.3. [P07101-3]
NP_954986.2. NM_199292.2. [P07101-1]
NP_954987.2. NM_199293.2. [P07101-2]
UniGeneHs.435609.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2XSNX-ray2.68A/B/C/D193-528[»]
4J6SX-ray3.08E/F/G/H1-74[»]
ProteinModelPortalP07101.
SMRP07101. Positions 95-528.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112912. 4 interactions.
IntActP07101. 4 interactions.
MINTMINT-198913.
STRING9606.ENSP00000370571.

Chemistry

BindingDBP07101.
ChEMBLCHEMBL1969.
DrugBankDB00120. L-Phenylalanine.
DB00135. L-Tyrosine.
DB00765. Metyrosine.
DB00360. Tetrahydrobiopterin.
GuidetoPHARMACOLOGY1243.

PTM databases

PhosphoSiteP07101.

Polymorphism databases

DMDM239938945.

Proteomic databases

PaxDbP07101.
PRIDEP07101.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000333684; ENSP00000328814; ENSG00000180176.
ENST00000352909; ENSP00000325951; ENSG00000180176. [P07101-3]
ENST00000381175; ENSP00000370567; ENSG00000180176. [P07101-2]
ENST00000381178; ENSP00000370571; ENSG00000180176. [P07101-1]
GeneID7054.
KEGGhsa:7054.
UCSCuc001lvp.3. human. [P07101-2]
uc001lvq.3. human. [P07101-1]
uc001lvr.3. human. [P07101-3]
uc010qxj.2. human. [P07101-4]

Organism-specific databases

CTD7054.
GeneCardsGC11M002185.
GeneReviewsTH.
H-InvDBHIX0035928.
HGNCHGNC:11782. TH.
HPACAB002522.
MIM191290. gene.
605407. phenotype.
neXtProtNX_P07101.
Orphanet101150. Autosomal recessive dopa-responsive dystonia.
PharmGKBPA351.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG3186.
HOGENOMHOG000233373.
HOVERGENHBG006841.
InParanoidP07101.
KOK00501.
OMAELDKCHH.
PhylomeDBP07101.
TreeFamTF313327.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
UniPathwayUPA00747; UER00733.

Gene expression databases

ArrayExpressP07101.
BgeeP07101.
CleanExHS_TH.
GenevestigatorP07101.

Family and domain databases

Gene3D1.10.800.10. 1 hit.
InterProIPR001273. ArAA_hydroxylase.
IPR018301. ArAA_hydroxylase_Fe/CU_BS.
IPR019774. Aromatic-AA_hydroxylase_C.
IPR005962. Tyr_3_mOase.
IPR019773. Tyrosine_3-monooxygenase-like.
IPR021164. Tyrosine_hydroxylase_CS.
[Graphical view]
PANTHERPTHR11473. PTHR11473. 1 hit.
PfamPF00351. Biopterin_H. 1 hit.
PF12549. TOH_N. 3 hits.
[Graphical view]
PIRSFPIRSF000336. TH. 1 hit.
PRINTSPR00372. FYWHYDRXLASE.
SUPFAMSSF56534. SSF56534. 1 hit.
TIGRFAMsTIGR01269. Tyr_3_monoox. 1 hit.
PROSITEPS00367. BH4_AAA_HYDROXYL_1. 1 hit.
PS51410. BH4_AAA_HYDROXYL_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiTyrosine_hydroxylase.
GenomeRNAi7054.
NextBio27583.
PROP07101.
SOURCESearch...

Entry information

Entry nameTY3H_HUMAN
AccessionPrimary (citable) accession number: P07101
Secondary accession number(s): B7ZL70 expand/collapse secondary AC list , B7ZL73, Q0PWM2, Q0PWM3, Q15585, Q15588, Q15589, Q2M3B4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: June 16, 2009
Last modified: July 9, 2014
This is version 168 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM