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Tyrosine 3-monooxygenase (EC 1.14.16.2) (Tyrosine 3-hydroxylase) (TH)

 TY3H_HUMAN              Reviewed;         528 AA.
P07101; B7ZL70; B7ZL73; Q0PWM2; Q0PWM3; Q15585; Q15588; Q15589;
Q2M3B4;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
16-JUN-2009, sequence version 5.
25-OCT-2017, entry version 200.
RecName: Full=Tyrosine 3-monooxygenase;
EC=1.14.16.2;
AltName: Full=Tyrosine 3-hydroxylase;
Short=TH;
Name=TH; Synonyms=TYH;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
PubMed=2887169; DOI=10.1016/0006-291X(87)90742-X;
Kaneda N., Kobayashi K., Ichinose H., Kishi F., Nakazawa A.,
Kurosawa Y., Fujita K., Nagatsu T.;
"Isolation of a novel cDNA clone for human tyrosine hydroxylase:
alternative RNA splicing produces four kinds of mRNA from a single
gene.";
Biochem. Biophys. Res. Commun. 146:971-975(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING.
PubMed=2882428; DOI=10.1038/326707a0;
Grima B., Lamouroux A., Boni C., Julien J.-F., Javoy-Agid F.,
Mallet J.;
"A single human gene encoding multiple tyrosine hydroxylases with
different predicted functional characteristics.";
Nature 326:707-711(1987).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2888085; DOI=10.1093/nar/15.16.6733;
Kobayashi K., Kaneda N., Ichinose H., Kishi F., Nakazawa A.,
Kurosawa Y., Fujita K., Nagatsu T.;
"Isolation of a full-length cDNA clone encoding human tyrosine
hydroxylase type 3.";
Nucleic Acids Res. 15:6733-6733(1987).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
PubMed=2902075; DOI=10.1093/oxfordjournals.jbchem.a122386;
Kobayashi K., Kaneda N., Ichinose H., Kishi F., Nakazawa A.,
Kurosawa Y., Fujita K., Nagatsu T.;
"Structure of the human tyrosine hydroxylase gene: alternative
splicing from a single gene accounts for generation of four mRNA
types.";
J. Biochem. 103:907-912(1988).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5 AND 6), AND ALTERNATIVE
SPLICING.
PubMed=17391063; DOI=10.1515/BC.2007.041;
Roma J., Saus E., Cuadros M., Reventos J., Sanchez de Toledo J.,
Gallego S.;
"Characterisation of novel splicing variants of the tyrosine
hydroxylase C-terminal domain in human neuroblastic tumours.";
Biol. Chem. 388:419-426(2007).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
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., 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.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4), AND VARIANT
MET-112.
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2892893; DOI=10.1111/j.1471-4159.1988.tb03009.x;
le Bourdelles B., Boularand S., Boni C., Horellou P., Dumas S.,
Grima B., Mallet J.;
"Analysis of the 5' region of the human tyrosine hydroxylase gene:
combinatorial patterns of exon splicing generate multiple regulated
tyrosine hydroxylase isoforms.";
J. Neurochem. 50:988-991(1988).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-30.
PubMed=2896667;
Ginns E.I., Rehavi M., Martin B.M., Weller M., O'Malley K.L.,
Lamarca M.E., McAllister C.G., Paul S.M.;
"Expression of human tyrosine hydroxylase cDNA in invertebrate cells
using a baculovirus vector.";
J. Biol. Chem. 263:7406-7410(1988).
[11]
PHOSPHORYLATION AT SER-19 AND SER-71.
PubMed=1680128;
Le Bourdelles B., Horellou P., Le Caer J.P., Denefle P., Latta M.,
Haavik J., Guibert B., Mayaux J.F., Mallet J.;
"Phosphorylation of human recombinant tyrosine hydroxylase isoforms 1
and 2: an additional phosphorylated residue in isoform 2, generated
through alternative splicing.";
J. Biol. Chem. 266:17124-17130(1991).
[12]
POSSIBLE INVOLVEMENT IN PARKINSON DISEASE.
PubMed=20809526; DOI=10.1002/humu.21351;
Bademci G., Edwards T.L., Torres A.L., Scott W.K., Zuchner S.,
Martin E.R., Vance J.M., Wang L.;
"A rare novel deletion of the tyrosine hydroxylase gene in Parkinson
disease.";
Hum. Mutat. 31:E1767-E1771(2010).
[13]
INVOLVEMENT IN ARSEGS, AND VARIANT ARSEGS LYS-412.
PubMed=7814018; DOI=10.1007/BF00225091;
Luedecke B., Dworniczak B., Bartholome K.;
"A point mutation in the tyrosine hydroxylase gene associated with
Segawa's syndrome.";
Hum. Genet. 95:123-125(1995).
[14]
VARIANT MET-112.
PubMed=7789962; DOI=10.1007/BF00209496;
Luedecke B., Bartholome K.;
"Frequent sequence variant in the human tyrosine hydroxylase gene.";
Hum. Genet. 95:716-716(1995).
[15]
CHARACTERIZATION OF VARIANT ARSEGS LYS-412.
PubMed=8528210; DOI=10.1093/hmg/4.7.1209;
Knappskog P.M., Flatmark T., Mallet J., Luedecke B., Bartholome K.;
"Recessively inherited L-DOPA-responsive dystonia caused by a point
mutation (Q381K) in the tyrosine hydroxylase gene.";
Hum. Mol. Genet. 4:1209-1212(1995).
[16]
CHARACTERIZATION OF VARIANT ARSEGS PRO-236.
PubMed=8817341; DOI=10.1093/hmg/5.7.1023;
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.;
"Recessively inherited L-DOPA-responsive parkinsonism in infancy
caused by a point mutation (L205P) in the tyrosine hydroxylase gene.";
Hum. Mol. Genet. 5:1023-1028(1996).
[17]
VARIANT ARSEGS PRO-236, AND VARIANT MET-112.
PubMed=9613851;
DOI=10.1002/(SICI)1096-8628(19980328)81:2<131::AID-AJMG2>3.3.CO;2-X;
Kunugi H., Kawada Y., Hattori M., Ueki A., Otsuka M., Nanko S.;
"Association study of structural mutations of the tyrosine hydroxylase
gene with schizophrenia and Parkinson's disease.";
Am. J. Med. Genet. 81:131-133(1998).
[18]
VARIANT MET-499.
PubMed=9754624;
DOI=10.1002/(SICI)1096-8628(19980907)81:5<388::AID-AJMG7>3.3.CO;2-F;
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.;
"Systematic search for variations in the tyrosine hydroxylase gene and
their associations with schizophrenia, affective disorders, and
alcoholism.";
Am. J. Med. Genet. 81:388-396(1998).
[19]
VARIANT ARSEGS HIS-233.
PubMed=9703425; DOI=10.1007/s004390050756;
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.;
"A common point mutation in the tyrosine hydroxylase gene in autosomal
recessive L-DOPA-responsive dystonia in the Dutch population.";
Hum. Genet. 102:644-646(1998).
[20]
VARIANT ARSEGS PHE-359.
PubMed=10585338;
Braeutigam C., Steenbergen-Spanjers G.C., Hoffmann G.F.,
Dionisi-Vici C., van den Heuvel L.P., Smeitink J.A., Wevers R.A.;
"Biochemical and molecular genetic characteristics of the severe form
of tyrosine hydroxylase deficiency.";
Clin. Chem. 45:2073-2078(1999).
[21]
VARIANT MET-112.
PubMed=10391209; DOI=10.1038/10290;
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.;
"Characterization of single-nucleotide polymorphisms in coding regions
of human genes.";
Nat. Genet. 22:231-238(1999).
[22]
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).
[23]
VARIANTS ARSEGS PRO-276; MET-314; HIS-337 AND MET-494.
PubMed=11246459; DOI=10.1046/j.1469-1809.2000.6410025.x;
Swaans R.J.M., Rondot P., Renier W.O., Van Den Heuvel L.P.W.J.,
Steenbergen-Spanjers G.C.H., Wevers R.A.;
"Four novel mutations in the tyrosine hydroxylase gene in patients
with infantile parkinsonism.";
Ann. Hum. Genet. 64:25-31(2000).
[24]
VARIANT ARSEGS SER-309.
PubMed=11196107; DOI=10.1023/A:1026760602577;
De Lonlay P., Nassogne M.C., van Gennip A.H., van Cruchten A.C.,
Billatte de Villemeur T., Cretz M., Stoll C., Launay J.M.,
Steenberger-Spante G.C., van den Heuvel L.P., Wevers R.A.,
Saudubray J.M., Abeling N.G.;
"Tyrosine hydroxylase deficiency unresponsive to L-dopa treatment with
unusual clinical and biochemical presentation.";
J. Inherit. Metab. Dis. 23:819-825(2000).
[25]
VARIANTS ARSEGS VAL-376 AND GLY-498.
PubMed=15505183; DOI=10.1212/01.WNL.0000142083.47927.0A;
Schiller A., Wevers R.A., Steenbergen G.C., Blau N., Jung H.H.;
"Long-term course of L-dopa-responsive dystonia caused by tyrosine
hydroxylase deficiency.";
Neurology 63:1524-1526(2004).
[26]
VARIANTS ARSEGS TYR-246 AND GLY-498.
PubMed=15747353; DOI=10.1002/mds.20416;
Diepold K., Schuetz B., Rostasy K., Wilken B., Hougaard P.,
Guettler F., Romstad A., Birk Moeller L.;
"Levodopa-responsive infantile parkinsonism due to a novel mutation in
the tyrosine hydroxylase gene and exacerbation by viral infections.";
Mov. Disord. 20:764-767(2005).
[27]
VARIANTS ARSEGS TRP-328 AND MET-399.
PubMed=16049992; DOI=10.1002/pd.1193;
Moeller L.B., Romstad A., Paulsen M., Hougaard P., Ormazabal A.,
Pineda M., Blau N., Guettler F., Artuch R.;
"Pre- and postnatal diagnosis of tyrosine hydroxylase deficiency.";
Prenat. Diagn. 25:671-675(2005).
[28]
VARIANTS ARSEGS MET-387 AND LEU-492.
PubMed=17696123; DOI=10.1002/ana.21199;
Verbeek M.M., Steenbergen-Spanjers G.C., Willemsen M.A., Hol F.A.,
Smeitink J., Seeger J., Grattan-Smith P., Ryan M.M., Hoffmann G.F.,
Donati M.A., Blau N., Wevers R.A.;
"Mutations in the cyclic adenosine monophosphate response element of
the tyrosine hydroxylase gene.";
Ann. Neurol. 62:422-426(2007).
[29]
VARIANTS ARSEGS ARG-414 AND GLN-510.
PubMed=18058633; DOI=10.1055/s-2007-991151;
Giovanniello T., Leuzzi V., Carducci C., Carducci C., Sabato M.L.,
Artiola C., Santagata S., Pozzessere S., Antonozzi I.;
"Tyrosine hydroxylase deficiency presenting with a biphasic clinical
course.";
Neuropediatrics 38:213-215(2007).
[30]
VARIANTS ARSEGS HIS-233 AND SER-247.
PubMed=18554280; DOI=10.1111/j.1399-0004.2008.01039.x;
Wu Z.Y., Lin Y., Chen W.J., Zhao G.X., Xie H., Murong S.X., Wang N.;
"Molecular analyses of GCH-1, TH and parkin genes in Chinese dopa-
responsive dystonia families.";
Clin. Genet. 74:513-521(2008).
[31]
VARIANTS ARSEGS ALA-301; PRO-319; LEU-375; ARG-414 AND GLY-467.
PubMed=19491146; DOI=10.1093/brain/awp084;
Clot F., Grabli D., Cazeneuve C., Roze E., Castelnau P., Chabrol B.,
Landrieu P., Nguyen K., Ponsot G., Abada M., Doummar D., Damier P.,
Gil R., Thobois S., Ward A.J., Hutchinson M., Toutain A., Picard F.,
Camuzat A., Fedirko E., San C., Bouteiller D., LeGuern E., Durr A.,
Vidailhet M., Brice A.;
"Exhaustive analysis of BH4 and dopamine biosynthesis genes in
patients with Dopa-responsive dystonia.";
Brain 132:1753-1763(2009).
[32]
VARIANTS ARSEGS TYR-207; GLY-227; THR-241; GLY-259 AND THR-394.
PubMed=20430833; DOI=10.1093/brain/awq087;
Willemsen M.A., Verbeek M.M., Kamsteeg E.J., de Rijk-van Andel J.F.,
Aeby A., Blau N., Burlina A., Donati M.A., Geurtz B.,
Grattan-Smith P.J., Haeussler M., Hoffmann G.F., Jung H.,
de Klerk J.B., van der Knaap M.S., Kok F., Leuzzi V., de Lonlay P.,
Megarbane A., Monaghan H., Renier W.O., Rondot P., Ryan M.M.,
Seeger J., Smeitink J.A., Steenbergen-Spanjers G.C., Wassmer E.,
Weschke B., Wijburg F.A., Wilcken B., Zafeiriou D.I., Wevers R.A.;
"Tyrosine hydroxylase deficiency: a treatable disorder of brain
catecholamine biosynthesis.";
Brain 133:1810-1822(2010).
[33]
VARIANTS ARSEGS ARG-294; SER-315; VAL-385; THR-394 AND ARG-408.
PubMed=20056467; DOI=10.1016/j.ymgme.2009.12.011;
Mak C.M., Lam C.W., Siu T.S., Chan K.Y., Siu W.K., Yeung W.L., Hui J.,
Wong V.C., Low L.C., Ko C.H., Fung C.W., Chen S.P., Yuen Y.P.,
Lee H.C., Yau E., Chan B., Tong S.F., Tam S., Chan Y.W.;
"Biochemical and molecular characterization of tyrosine hydroxylase
deficiency in Hong Kong Chinese.";
Mol. Genet. Metab. 99:431-433(2010).
[34]
VARIANTS ARSEGS PRO-441 AND GLY-498.
PubMed=23939262; DOI=10.3233/JPD-2011-11006;
Haugarvoll K., Bindoff L.A.;
"A novel compound heterozygous tyrosine hydroxylase mutation (p.R441P)
with complex phenotype.";
J. Parkinson's Dis. 1:119-122(2011).
[35]
VARIANTS ARSEGS LEU-251; PHE-279 AND GLN-296, AND VARIANT MET-112.
PubMed=21940685; DOI=10.1177/0883073811420717;
Giovanniello T., Claps D., Carducci C., Carducci C., Blau N.,
Vigevano F., Antonozzi I., Leuzzi V.;
"A new tyrosine hydroxylase genotype associated with early-onset
severe encephalopathy.";
J. Child Neurol. 27:523-525(2012).
[36]
VARIANT ARSEGS ARG-428.
PubMed=22815559; DOI=10.1212/WNL.0b013e318261714a;
Stamelou M., Mencacci N.E., Cordivari C., Batla A., Wood N.W.,
Houlden H., Hardy J., Bhatia K.P.;
"Myoclonus-dystonia syndrome due to tyrosine hydroxylase deficiency.";
Neurology 79:435-441(2012).
[37]
VARIANTS ARSEGS HIS-233; SER-315 AND THR-382.
PubMed=22264700; DOI=10.1016/j.pediatrneurol.2011.11.012;
Chi C.S., Lee H.F., Tsai C.R.;
"Tyrosine hydroxylase deficiency in Taiwanese infants.";
Pediatr. Neurol. 46:77-82(2012).
[38]
VARIANTS CYS-19 AND ARG-428.
PubMed=23762320; DOI=10.1371/journal.pone.0065215;
Cai C., Shi W., Zeng Z., Zhang M., Ling C., Chen L., Cai C., Zhang B.,
Li W.D.;
"GTP cyclohydrolase I and tyrosine hydroxylase gene mutations in
familial and sporadic dopa-responsive dystonia patients.";
PLoS ONE 8:E65215-E65215(2013).
[39]
CHARACTERIZATION OF VARIANTS ARSEGS TYR-207; GLY-227; HIS-233;
PRO-236; THR-241; TYR-246; SER-247; GLY-259; PRO-276; ALA-301;
SER-309; MET-314; PRO-319; TRP-328; HIS-337; PHE-359; LEU-375;
VAL-376; MET-387; THR-394; MET-399; LYS-412; ARG-414; PRO-441;
GLY-467; LEU-492; MET-494; GLY-498 AND GLN-510.
PubMed=24753243; DOI=10.1002/humu.22565;
Fossbakk A., Kleppe R., Knappskog P.M., Martinez A., Haavik J.;
"Functional studies of tyrosine hydroxylase missense variants reveal
distinct patterns of molecular defects in Dopa-responsive dystonia.";
Hum. Mutat. 35:880-890(2014).
-!- FUNCTION: Plays an important role in the physiology of adrenergic
neurons.
-!- CATALYTIC ACTIVITY: L-tyrosine + tetrahydrobiopterin + O(2) = L-
dopa + 4a-hydroxytetrahydrobiopterin.
-!- COFACTOR:
Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
-!- ENZYME REGULATION: Phosphorylation leads to an increase in the
catalytic activity.
-!- PATHWAY: Catecholamine biosynthesis; dopamine biosynthesis;
dopamine from L-tyrosine: step 1/2.
-!- INTERACTION:
P29762:CRABP1; NbExp=4; IntAct=EBI-12001016, EBI-725950;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Comment=TH transcripts lacking exons 8 and 9 present concomitant
splicing in exons 1b and 2.;
Name=3; Synonyms=TH type 4;
IsoId=P07101-1; Sequence=Displayed;
Name=1; Synonyms=TH type 3;
IsoId=P07101-2; Sequence=VSP_000543;
Name=2; Synonyms=HTH-1, hTH-Delta1b,2, TH type 1;
IsoId=P07101-3; Sequence=VSP_000544;
Name=4; Synonyms=hTH-Delta2, TH type 2;
IsoId=P07101-4; Sequence=VSP_000541;
Name=5; Synonyms=hTH-Delta2,8,9;
IsoId=P07101-5; Sequence=VSP_000541, VSP_054338;
Note=Lacks catalytic activity.;
Name=6; Synonyms=hTH-Delta1b,2,8,9;
IsoId=P07101-6; Sequence=VSP_000544, VSP_054338;
Note=Lacks catalytic activity.;
-!- TISSUE SPECIFICITY: Mainly expressed in the brain and adrenal
glands.
-!- 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.
{ECO:0000269|PubMed:10585338, ECO:0000269|PubMed:11196107,
ECO:0000269|PubMed:11246459, ECO:0000269|PubMed:15505183,
ECO:0000269|PubMed:15747353, ECO:0000269|PubMed:16049992,
ECO:0000269|PubMed:17696123, ECO:0000269|PubMed:18058633,
ECO:0000269|PubMed:18554280, ECO:0000269|PubMed:19491146,
ECO:0000269|PubMed:20056467, ECO:0000269|PubMed:20430833,
ECO:0000269|PubMed:21940685, ECO:0000269|PubMed:22264700,
ECO:0000269|PubMed:22815559, ECO:0000269|PubMed:23762320,
ECO:0000269|PubMed:23939262, ECO:0000269|PubMed:24753243,
ECO:0000269|PubMed:7814018, ECO:0000269|PubMed:8528210,
ECO:0000269|PubMed:8817341, ECO:0000269|PubMed:9613851,
ECO:0000269|PubMed:9703425}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Note=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. {ECO:0000269|PubMed:20809526}.
-!- SIMILARITY: Belongs to the biopterin-dependent aromatic amino acid
hydroxylase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA61173.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Wikipedia; Note=Tyrosine hydroxylase entry;
URL="https://en.wikipedia.org/wiki/Tyrosine_hydroxylase";
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EMBL; M17589; AAA61179.1; -; mRNA.
EMBL; X05290; CAA28908.1; -; mRNA.
EMBL; Y00414; CAA68472.1; -; mRNA.
EMBL; DQ677336; ABG73364.1; -; mRNA.
EMBL; DQ677337; ABG73365.1; -; mRNA.
EMBL; AC132217; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; M24791; AAA61173.1; ALT_SEQ; Genomic_DNA.
EMBL; M24787; AAA61173.1; JOINED; Genomic_DNA.
EMBL; M24789; AAA61173.1; JOINED; Genomic_DNA.
EMBL; CH471158; EAX02493.1; -; Genomic_DNA.
EMBL; BC104967; AAI04968.1; -; mRNA.
EMBL; BC143611; AAI43612.1; -; mRNA.
EMBL; BC143614; AAI43615.1; -; mRNA.
EMBL; M24791; AAA61170.1; -; Genomic_DNA.
EMBL; M24787; AAA61170.1; JOINED; Genomic_DNA.
EMBL; M20911; AAA61167.1; -; mRNA.
CCDS; CCDS31338.1; -. [P07101-2]
CCDS; CCDS7730.1; -. [P07101-3]
CCDS; CCDS7731.1; -. [P07101-1]
PIR; A30002; WHHUY4.
RefSeq; NP_000351.2; NM_000360.3. [P07101-3]
RefSeq; NP_954986.2; NM_199292.2. [P07101-1]
RefSeq; NP_954987.2; NM_199293.2. [P07101-2]
RefSeq; XP_011518637.1; XM_011520335.2. [P07101-4]
UniGene; Hs.435609; -.
PDB; 2XSN; X-ray; 2.68 A; A/B/C/D=193-528.
PDB; 4J6S; X-ray; 3.08 A; E/F/G/H=1-74.
PDBsum; 2XSN; -.
PDBsum; 4J6S; -.
ProteinModelPortal; P07101; -.
SMR; P07101; -.
BioGrid; 112912; 13.
ELM; P07101; -.
IntAct; P07101; 12.
MINT; MINT-198913; -.
STRING; 9606.ENSP00000370571; -.
BindingDB; P07101; -.
ChEMBL; CHEMBL1969; -.
DrugBank; DB00120; L-Phenylalanine.
DrugBank; DB00135; L-Tyrosine.
DrugBank; DB03552; Meta-Tyrosine.
DrugBank; DB00765; Metyrosine.
DrugBank; DB00360; Sapropterin.
iPTMnet; P07101; -.
PhosphoSitePlus; P07101; -.
BioMuta; TH; -.
DMDM; 239938945; -.
PaxDb; P07101; -.
PeptideAtlas; P07101; -.
PRIDE; P07101; -.
Ensembl; ENST00000333684; ENSP00000328814; ENSG00000180176. [P07101-6]
Ensembl; ENST00000352909; ENSP00000325951; ENSG00000180176. [P07101-3]
Ensembl; ENST00000381175; ENSP00000370567; ENSG00000180176. [P07101-2]
Ensembl; ENST00000381178; ENSP00000370571; ENSG00000180176. [P07101-1]
GeneID; 7054; -.
KEGG; hsa:7054; -.
UCSC; uc001lvp.3; human. [P07101-1]
CTD; 7054; -.
DisGeNET; 7054; -.
EuPathDB; HostDB:ENSG00000180176.14; -.
GeneCards; TH; -.
GeneReviews; TH; -.
H-InvDB; HIX0035928; -.
HGNC; HGNC:11782; TH.
HPA; CAB002522; -.
HPA; CAB072340; -.
HPA; HPA061003; -.
MalaCards; TH; -.
MIM; 191290; gene.
MIM; 605407; phenotype.
neXtProt; NX_P07101; -.
OpenTargets; ENSG00000180176; -.
Orphanet; 101150; Autosomal recessive dopa-responsive dystonia.
PharmGKB; PA351; -.
eggNOG; KOG3820; Eukaryota.
eggNOG; COG3186; LUCA.
GeneTree; ENSGT00390000010268; -.
HOGENOM; HOG000233373; -.
HOVERGEN; HBG006841; -.
InParanoid; P07101; -.
KO; K00501; -.
OMA; PKHASEL; -.
OrthoDB; EOG091G05MZ; -.
PhylomeDB; P07101; -.
TreeFam; TF313327; -.
BRENDA; 1.14.16.2; 2681.
Reactome; R-HSA-209905; Catecholamine biosynthesis.
SIGNOR; P07101; -.
UniPathway; UPA00747; UER00733.
GeneWiki; Tyrosine_hydroxylase; -.
GenomeRNAi; 7054; -.
PRO; PR:P07101; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000180176; -.
CleanEx; HS_TH; -.
ExpressionAtlas; P07101; baseline and differential.
Genevisible; P07101; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:BHF-UCL.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0033162; C:melanosome membrane; IDA:BHF-UCL.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0043005; C:neuron projection; IDA:BHF-UCL.
GO; GO:0005634; C:nucleus; ISS:BHF-UCL.
GO; GO:0043204; C:perikaryon; ISS:BHF-UCL.
GO; GO:0005790; C:smooth endoplasmic reticulum; IDA:BHF-UCL.
GO; GO:0008021; C:synaptic vesicle; IEA:Ensembl.
GO; GO:0043195; C:terminal bouton; IEA:Ensembl.
GO; GO:0016597; F:amino acid binding; IEA:Ensembl.
GO; GO:0035240; F:dopamine binding; IEA:Ensembl.
GO; GO:0019899; F:enzyme binding; IPI:ParkinsonsUK-UCL.
GO; GO:0008199; F:ferric iron binding; IEA:Ensembl.
GO; GO:0008198; F:ferrous iron binding; IEA:Ensembl.
GO; GO:0019825; F:oxygen binding; IEA:Ensembl.
GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
GO; GO:0034617; F:tetrahydrobiopterin binding; IEA:Ensembl.
GO; GO:0004511; F:tyrosine 3-monooxygenase activity; IDA:UniProtKB.
GO; GO:0015842; P:aminergic neurotransmitter loading into synaptic vesicle; IEA:Ensembl.
GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
GO; GO:0009887; P:animal organ morphogenesis; ISS:BHF-UCL.
GO; GO:0042423; P:catecholamine biosynthetic process; TAS:Reactome.
GO; GO:0071312; P:cellular response to alkaloid; IEA:Ensembl.
GO; GO:0035690; P:cellular response to drug; IEA:Ensembl.
GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
GO; GO:0071363; P:cellular response to growth factor stimulus; IEA:Ensembl.
GO; GO:0071287; P:cellular response to manganese ion; IEA:Ensembl.
GO; GO:0071316; P:cellular response to nicotine; IEA:Ensembl.
GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
GO; GO:0042745; P:circadian sleep/wake cycle; IEA:Ensembl.
GO; GO:0042416; P:dopamine biosynthetic process; IDA:BHF-UCL.
GO; GO:0006585; P:dopamine biosynthetic process from tyrosine; NAS:BHF-UCL.
GO; GO:0042755; P:eating behavior; IEA:Ensembl.
GO; GO:0048596; P:embryonic camera-type eye morphogenesis; ISS:BHF-UCL.
GO; GO:0042418; P:epinephrine biosynthetic process; IDA:BHF-UCL.
GO; GO:0042462; P:eye photoreceptor cell development; ISS:BHF-UCL.
GO; GO:0006631; P:fatty acid metabolic process; IEA:Ensembl.
GO; GO:0016137; P:glycoside metabolic process; IEA:Ensembl.
GO; GO:0007507; P:heart development; ISS:BHF-UCL.
GO; GO:0003007; P:heart morphogenesis; NAS:BHF-UCL.
GO; GO:0033076; P:isoquinoline alkaloid metabolic process; IEA:Ensembl.
GO; GO:0007612; P:learning; ISS:BHF-UCL.
GO; GO:0007626; P:locomotory behavior; ISS:BHF-UCL.
GO; GO:0007617; P:mating behavior; IEA:Ensembl.
GO; GO:0007613; P:memory; ISS:BHF-UCL.
GO; GO:0010259; P:multicellular organism aging; IEA:Ensembl.
GO; GO:0042136; P:neurotransmitter biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0042421; P:norepinephrine biosynthetic process; IDA:BHF-UCL.
GO; GO:0018963; P:phthalate metabolic process; IEA:Ensembl.
GO; GO:0052314; P:phytoalexin metabolic process; IEA:Ensembl.
GO; GO:0043473; P:pigmentation; TAS:BHF-UCL.
GO; GO:0008016; P:regulation of heart contraction; ISS:BHF-UCL.
GO; GO:0014823; P:response to activity; IEA:Ensembl.
GO; GO:0001975; P:response to amphetamine; IEA:Ensembl.
GO; GO:0051412; P:response to corticosterone; IEA:Ensembl.
GO; GO:0051602; P:response to electrical stimulus; IEA:Ensembl.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0045471; P:response to ethanol; IDA:BHF-UCL.
GO; GO:0045472; P:response to ether; IEA:Ensembl.
GO; GO:0009635; P:response to herbicide; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IDA:BHF-UCL.
GO; GO:0035902; P:response to immobilization stress; IEA:Ensembl.
GO; GO:0035900; P:response to isolation stress; IEA:Ensembl.
GO; GO:0009416; P:response to light stimulus; IEA:Ensembl.
GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl.
GO; GO:0043434; P:response to peptide hormone; IEA:Ensembl.
GO; GO:0046684; P:response to pyrethroid; IEA:Ensembl.
GO; GO:0009651; P:response to salt stress; IEA:Ensembl.
GO; GO:0009414; P:response to water deprivation; IEA:Ensembl.
GO; GO:0010043; P:response to zinc ion; IEA:Ensembl.
GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
GO; GO:0035176; P:social behavior; IEA:Ensembl.
GO; GO:0006665; P:sphingolipid metabolic process; IEA:Ensembl.
GO; GO:0001963; P:synaptic transmission, dopaminergic; ISS:BHF-UCL.
GO; GO:0042214; P:terpene metabolic process; IEA:Ensembl.
GO; GO:0007601; P:visual perception; ISS:BHF-UCL.
Gene3D; 1.10.800.10; -; 1.
InterPro; IPR001273; ArAA_hydroxylase.
InterPro; IPR018301; ArAA_hydroxylase_Fe/CU_BS.
InterPro; IPR036951; ArAA_hydroxylase_sf.
InterPro; IPR036329; Aro-AA_hydroxylase_C_sf.
InterPro; IPR019774; Aromatic-AA_hydroxylase_C.
InterPro; IPR005962; Tyr_3_mOase.
InterPro; IPR019773; Tyrosine_3-monooxygenase-like.
InterPro; IPR021164; Tyrosine_hydroxylase_CS.
PANTHER; PTHR11473; PTHR11473; 1.
Pfam; PF00351; Biopterin_H; 1.
Pfam; PF12549; TOH_N; 3.
PIRSF; PIRSF000336; TH; 1.
PRINTS; PR00372; FYWHYDRXLASE.
SUPFAM; SSF56534; SSF56534; 1.
TIGRFAMs; TIGR01269; Tyr_3_monoox; 1.
PROSITE; PS00367; BH4_AAA_HYDROXYL_1; 1.
PROSITE; PS51410; BH4_AAA_HYDROXYL_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Catecholamine biosynthesis;
Complete proteome; Disease mutation; Dystonia; Iron; Metal-binding;
Monooxygenase; Neurotransmitter biosynthesis; Oxidoreductase;
Parkinson disease; Parkinsonism; Phosphoprotein; Polymorphism;
Reference proteome.
CHAIN 1 528 Tyrosine 3-monooxygenase.
/FTId=PRO_0000205561.
COMPBIAS 85 90 Poly-Ala.
METAL 361 361 Iron. {ECO:0000250}.
METAL 366 366 Iron. {ECO:0000250}.
METAL 406 406 Iron. {ECO:0000250}.
MOD_RES 19 19 Phosphoserine; by CaMK2.
{ECO:0000269|PubMed:1680128}.
MOD_RES 62 62 Phosphoserine.
{ECO:0000250|UniProtKB:P24529}.
MOD_RES 71 71 Phosphoserine; by CaMK2 and PKA.
{ECO:0000269|PubMed:1680128}.
MOD_RES 502 502 Phosphoserine.
{ECO:0000250|UniProtKB:P24529}.
VAR_SEQ 31 61 Missing (in isoform 2 and isoform 6).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17391063,
ECO:0000303|PubMed:2882428}.
/FTId=VSP_000544.
VAR_SEQ 31 34 Missing (in isoform 1).
{ECO:0000303|PubMed:2888085}.
/FTId=VSP_000543.
VAR_SEQ 35 61 Missing (in isoform 4 and isoform 5).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17391063}.
/FTId=VSP_000541.
VAR_SEQ 264 357 Missing (in isoform 5 and isoform 6).
{ECO:0000303|PubMed:17391063}.
/FTId=VSP_054338.
VARIANT 19 19 S -> C (found in a patient with ARSEGS;
unknown pathological significance;
dbSNP:rs766704202).
{ECO:0000269|PubMed:23762320}.
/FTId=VAR_072862.
VARIANT 112 112 V -> M (common polymorphism;
dbSNP:rs6356).
{ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:21940685,
ECO:0000269|PubMed:7789962,
ECO:0000269|PubMed:9613851}.
/FTId=VAR_014025.
VARIANT 207 207 C -> Y (in ARSEGS; loss of over 80% of
tyrosine hydroxylase activity).
{ECO:0000269|PubMed:20430833,
ECO:0000269|PubMed:24753243}.
/FTId=VAR_072863.
VARIANT 227 227 D -> G (in ARSEGS; complete loss of
tyrosine hydroxylase activity).
{ECO:0000269|PubMed:20430833,
ECO:0000269|PubMed:24753243}.
/FTId=VAR_072864.
VARIANT 233 233 R -> H (in ARSEGS; loss of over 80% of
tyrosine hydroxylase activity; shifted
substrate specificity from tyrosine to
phenylalanine and Dopa;
dbSNP:rs80338892).
{ECO:0000269|PubMed:18554280,
ECO:0000269|PubMed:22264700,
ECO:0000269|PubMed:24753243,
ECO:0000269|PubMed:9703425}.
/FTId=VAR_014026.
VARIANT 236 236 L -> P (in ARSEGS; severe parkinsonian
symptoms in early infancy; strongly
reduced stability and catalytic activity;
rare mutation; dbSNP:rs121917763).
{ECO:0000269|PubMed:24753243,
ECO:0000269|PubMed:8817341,
ECO:0000269|PubMed:9613851}.
/FTId=VAR_014027.
VARIANT 241 241 A -> T (in ARSEGS; loss of over 80% of
tyrosine hydroxylase activity).
{ECO:0000269|PubMed:20430833,
ECO:0000269|PubMed:24753243}.
/FTId=VAR_072865.
VARIANT 246 246 H -> Y (in ARSEGS; loss of about 40% of
tyrosine hydroxylase activity).
{ECO:0000269|PubMed:15747353,
ECO:0000269|PubMed:24753243}.
/FTId=VAR_072866.
VARIANT 247 247 G -> S (in ARSEGS; loss of about 50% of
tyrosine hydroxylase activity; shifted
substrate specificity from tyrosine to
phenylalanine and Dopa;
dbSNP:rs762304556).
{ECO:0000269|PubMed:18554280,
ECO:0000269|PubMed:24753243}.
/FTId=VAR_072867.
VARIANT 251 251 P -> L (in ARSEGS).
{ECO:0000269|PubMed:21940685}.
/FTId=VAR_071715.
VARIANT 259 259 E -> G (in ARSEGS; complete loss of
tyrosine hydroxylase activity).
{ECO:0000269|PubMed:20430833,
ECO:0000269|PubMed:24753243}.
/FTId=VAR_072868.
VARIANT 276 276 T -> P (in ARSEGS; parkinsonian symptoms
in infancy; no effect on tyrosine
hydroxylase activity; dbSNP:rs28934581).
{ECO:0000269|PubMed:11246459,
ECO:0000269|PubMed:24753243}.
/FTId=VAR_014028.
VARIANT 279 279 C -> F (in ARSEGS).
{ECO:0000269|PubMed:21940685}.
/FTId=VAR_071716.
VARIANT 294 294 G -> R (in ARSEGS; dbSNP:rs755536257).
{ECO:0000269|PubMed:20056467}.
/FTId=VAR_072869.
VARIANT 296 296 R -> Q (in ARSEGS; dbSNP:rs199961079).
{ECO:0000269|PubMed:21940685}.
/FTId=VAR_071717.
VARIANT 301 301 P -> A (in ARSEGS; loss of over 80% of
tyrosine hydroxylase activity).
{ECO:0000269|PubMed:19491146,
ECO:0000269|PubMed:24753243}.
/FTId=VAR_072870.
VARIANT 309 309 F -> S (in ARSEGS; complete loss of
tyrosine hydroxylase activity).
{ECO:0000269|PubMed:11196107,
ECO:0000269|PubMed:24753243}.
/FTId=VAR_072871.
VARIANT 314 314 T -> M (in ARSEGS; parkinsonian symptoms
in infancy; loss of about 80% of tyrosine
hydroxylase activity; dbSNP:rs121917764).
{ECO:0000269|PubMed:11246459,
ECO:0000269|PubMed:24753243}.
/FTId=VAR_014029.
VARIANT 315 315 G -> S (in ARSEGS).
{ECO:0000269|PubMed:20056467,
ECO:0000269|PubMed:22264700}.
/FTId=VAR_071718.
VARIANT 319 319 R -> P (in ARSEGS; complete loss of
tyrosine hydroxylase activity).
{ECO:0000269|PubMed:19491146,
ECO:0000269|PubMed:24753243}.
/FTId=VAR_072872.
VARIANT 328 328 R -> W (in ARSEGS; complete loss of
tyrosine hydroxylase activity).
{ECO:0000269|PubMed:16049992,
ECO:0000269|PubMed:24753243}.
/FTId=VAR_072873.
VARIANT 337 337 R -> H (in ARSEGS; parkinsonian symptoms
in infancy; no effect on tyrosine
hydroxylase activity; dbSNP:rs28934580).
{ECO:0000269|PubMed:11246459,
ECO:0000269|PubMed:24753243}.
/FTId=VAR_014030.
VARIANT 359 359 C -> F (in ARSEGS; loss of over 80% of
tyrosine hydroxylase activity;
dbSNP:rs121917765).
{ECO:0000269|PubMed:10585338,
ECO:0000269|PubMed:24753243}.
/FTId=VAR_072874.
VARIANT 375 375 F -> L (in ARSEGS; loss of over 80% of
tyrosine hydroxylase activity; shifted
substrate specificity from tyrosine to
phenylalanine and Dopa).
{ECO:0000269|PubMed:19491146,
ECO:0000269|PubMed:24753243}.
/FTId=VAR_072875.
VARIANT 376 376 A -> V (in ARSEGS; loss of over 80% of
tyrosine hydroxylase activity).
{ECO:0000269|PubMed:15505183,
ECO:0000269|PubMed:24753243}.
/FTId=VAR_072876.
VARIANT 382 382 I -> T (in ARSEGS).
{ECO:0000269|PubMed:22264700}.
/FTId=VAR_071719.
VARIANT 385 385 A -> V (in ARSEGS; dbSNP:rs763039181).
{ECO:0000269|PubMed:20056467}.
/FTId=VAR_072877.
VARIANT 387 387 L -> M (in ARSEGS; no effect on tyrosine
hydroxylase activity).
{ECO:0000269|PubMed:17696123,
ECO:0000269|PubMed:24753243}.
/FTId=VAR_072878.
VARIANT 394 394 I -> T (in ARSEGS; complete loss of
tyrosine hydroxylase activity).
{ECO:0000269|PubMed:20056467,
ECO:0000269|PubMed:20430833,
ECO:0000269|PubMed:24753243}.
/FTId=VAR_072879.
VARIANT 399 399 T -> M (in ARSEGS; loss of over 80% of
tyrosine hydroxylase activity).
{ECO:0000269|PubMed:16049992,
ECO:0000269|PubMed:24753243}.
/FTId=VAR_072880.
VARIANT 408 408 G -> R (in ARSEGS; dbSNP:rs745551241).
{ECO:0000269|PubMed:20056467}.
/FTId=VAR_072881.
VARIANT 412 412 Q -> K (in ARSEGS; loss of over 80% of
tyrosine hydroxylase activity; reduced
affinity for L-tyrosine;
dbSNP:rs121917762).
{ECO:0000269|PubMed:24753243,
ECO:0000269|PubMed:7814018,
ECO:0000269|PubMed:8528210}.
/FTId=VAR_014031.
VARIANT 414 414 G -> R (in ARSEGS; loss of over 80% of
tyrosine hydroxylase activity;
dbSNP:rs370962049).
{ECO:0000269|PubMed:18058633,
ECO:0000269|PubMed:19491146,
ECO:0000269|PubMed:24753243}.
/FTId=VAR_072882.
VARIANT 428 428 G -> R (in ARSEGS; phenotype with
prominent levodopa-responsive myoconus-
dystonia (M-D)).
{ECO:0000269|PubMed:22815559,
ECO:0000269|PubMed:23762320}.
/FTId=VAR_071720.
VARIANT 441 441 R -> P (in ARSEGS; complete loss of
tyrosine hydroxylase activity;
dbSNP:rs367874223).
{ECO:0000269|PubMed:23939262,
ECO:0000269|PubMed:24753243}.
/FTId=VAR_072883.
VARIANT 467 467 S -> G (in ARSEGS; loss of over 80% of
tyrosine hydroxylase activity).
{ECO:0000269|PubMed:19491146,
ECO:0000269|PubMed:24753243}.
/FTId=VAR_072884.
VARIANT 492 492 P -> L (in ARSEGS; complete loss of
tyrosine hydroxylase activity;
dbSNP:rs767635052).
{ECO:0000269|PubMed:17696123,
ECO:0000269|PubMed:24753243}.
/FTId=VAR_072885.
VARIANT 494 494 T -> M (in ARSEGS; parkinsonian symptoms
in infancy; no effect on tyrosine
hydroxylase activity; dbSNP:rs45471299).
{ECO:0000269|PubMed:11246459,
ECO:0000269|PubMed:24753243}.
/FTId=VAR_014032.
VARIANT 498 498 D -> G (in ARSEGS; loss of over 80% of
tyrosine hydroxylase activity;
dbSNP:rs771351747).
{ECO:0000269|PubMed:15505183,
ECO:0000269|PubMed:15747353,
ECO:0000269|PubMed:23939262,
ECO:0000269|PubMed:24753243}.
/FTId=VAR_072886.
VARIANT 499 499 V -> M (in dbSNP:rs1800033).
{ECO:0000269|PubMed:9754624}.
/FTId=VAR_014033.
VARIANT 510 510 L -> Q (in ARSEGS; complete loss of
tyrosine hydroxylase activity).
{ECO:0000269|PubMed:18058633,
ECO:0000269|PubMed:24753243}.
/FTId=VAR_072887.
CONFLICT 373 373 R -> H (in Ref. 8; AAI43615).
{ECO:0000305}.
CONFLICT 401 401 Y -> S (in Ref. 1; AAA61179, 2; CAA28908
and 3; CAA68472). {ECO:0000305}.
HELIX 201 206 {ECO:0000244|PDB:2XSN}.
TURN 216 218 {ECO:0000244|PDB:2XSN}.
TURN 223 226 {ECO:0000244|PDB:2XSN}.
HELIX 228 243 {ECO:0000244|PDB:2XSN}.
HELIX 257 277 {ECO:0000244|PDB:2XSN}.
HELIX 280 292 {ECO:0000244|PDB:2XSN}.
HELIX 303 314 {ECO:0000244|PDB:2XSN}.
STRAND 317 320 {ECO:0000244|PDB:2XSN}.
HELIX 327 334 {ECO:0000244|PDB:2XSN}.
TURN 335 337 {ECO:0000244|PDB:2XSN}.
STRAND 338 341 {ECO:0000244|PDB:2XSN}.
HELIX 359 365 {ECO:0000244|PDB:2XSN}.
HELIX 367 370 {ECO:0000244|PDB:2XSN}.
HELIX 373 386 {ECO:0000244|PDB:2XSN}.
HELIX 391 403 {ECO:0000244|PDB:2XSN}.
TURN 404 407 {ECO:0000244|PDB:2XSN}.
STRAND 409 412 {ECO:0000244|PDB:2XSN}.
STRAND 415 418 {ECO:0000244|PDB:2XSN}.
HELIX 421 424 {ECO:0000244|PDB:2XSN}.
HELIX 427 433 {ECO:0000244|PDB:2XSN}.
STRAND 435 442 {ECO:0000244|PDB:2XSN}.
HELIX 445 449 {ECO:0000244|PDB:2XSN}.
STRAND 455 457 {ECO:0000244|PDB:2XSN}.
STRAND 460 466 {ECO:0000244|PDB:2XSN}.
HELIX 468 480 {ECO:0000244|PDB:2XSN}.
STRAND 485 491 {ECO:0000244|PDB:2XSN}.
TURN 492 495 {ECO:0000244|PDB:2XSN}.
STRAND 496 500 {ECO:0000244|PDB:2XSN}.
HELIX 503 526 {ECO:0000244|PDB:2XSN}.
SEQUENCE 528 AA; 58600 MW; 31D2D49955ACF070 CRC64;
MPTPDATTPQ AKGFRRAVSE LDAKQAEAIM VRGQGAPGPS LTGSPWPGTA APAASYTPTP
RSPRFIGRRQ SLIEDARKER EAAVAAAAAA VPSEPGDPLE AVAFEEKEGK AVLNLLFSPR
ATKPSALSRA VKVFETFEAK IHHLETRPAQ RPRAGGPHLE YFVRLEVRRG DLAALLSGVR
QVSEDVRSPA GPKVPWFPRK VSELDKCHHL VTKFDPDLDL DHPGFSDQVY RQRRKLIAEI
AFQYRHGDPI PRVEYTAEEI ATWKEVYTTL KGLYATHACG EHLEAFALLE RFSGYREDNI
PQLEDVSRFL KERTGFQLRP VAGLLSARDF LASLAFRVFQ CTQYIRHASS PMHSPEPDCC
HELLGHVPML ADRTFAQFSQ DIGLASLGAS DEEIEKLSTL YWFTVEFGLC KQNGEVKAYG
AGLLSSYGEL LHCLSEEPEI RAFDPEAAAV QPYQDQTYQS VYFVSESFSD AKDKLRSYAS
RIQRPFSVKF DPYTLAIDVL DSPQAVRRSL EGVQDELDTL AHALSAIG


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E1438h ELISA kit Homo sapiens,Human,TH,TH,TYH,Tyrosine 3-hydroxylase,Tyrosine 3-monooxygenase 96T
E1438h ELISA Homo sapiens,Human,TH,TH,TYH,Tyrosine 3-hydroxylase,Tyrosine 3-monooxygenase 96T
E1438b ELISA Bos taurus,Bovine,TH,TH,Tyrosine 3-hydroxylase,Tyrosine 3-monooxygenase 96T
E1438m ELISA Mouse,Mus musculus,TH,Th,Tyrosine 3-hydroxylase,Tyrosine 3-monooxygenase 96T
U1438r CLIA Rat,Rattus norvegicus,TH,Th,Tyrosine 3-hydroxylase,Tyrosine 3-monooxygenase 96T
U1438b CLIA Bos taurus,Bovine,TH,TH,Tyrosine 3-hydroxylase,Tyrosine 3-monooxygenase 96T
E1438r ELISA kit Rat,Rattus norvegicus,TH,Th,Tyrosine 3-hydroxylase,Tyrosine 3-monooxygenase 96T
E1438m ELISA kit Mouse,Mus musculus,TH,Th,Tyrosine 3-hydroxylase,Tyrosine 3-monooxygenase 96T
E1438r ELISA Rat,Rattus norvegicus,TH,Th,Tyrosine 3-hydroxylase,Tyrosine 3-monooxygenase 96T
U1438m CLIA Mouse,Mus musculus,TH,Th,Tyrosine 3-hydroxylase,Tyrosine 3-monooxygenase 96T
E1438b ELISA kit Bos taurus,Bovine,TH,TH,Tyrosine 3-hydroxylase,Tyrosine 3-monooxygenase 96T
18-662-20085 Tyrosine 3-monooxygenase - EC 1.14.16.2; Tyrosine 3-hydroxylase; TH Polyclonal 0.1 ml
18-662-20084 Tyrosine 3-monooxygenase - EC 1.14.16.2; Tyrosine 3-hydroxylase; TH Polyclonal 0.1 ml
18-662-20086 Tyrosine 3-monooxygenase - EC 1.14.16.2; Tyrosine 3-hydroxylase; TH Polyclonal 0.1 ml
20-662-20108 Tyrosine 3-monooxygenase - EC 1.14.16.2; Tyrosine 3-hydroxylase; TH Monoclonal 0.1 ml
18-662-20023 Tyrosine 3-monooxygenase - EC 1.14.16.2; Tyrosine 3-hydroxylase; TH Polyclonal 0.1 ml
18-662-20022 Tyrosine 3-monooxygenase - EC 1.14.16.2; Tyrosine 3-hydroxylase; TH Polyclonal 0.1 ml
E1438c ELISA Canis familiaris,Canis lupus familiaris,Dog,TH,TH,Tyrosine 3-hydroxylase,Tyrosine 3-monooxygenase 96T
E1438c ELISA kit Canis familiaris,Canis lupus familiaris,Dog,TH,TH,Tyrosine 3-hydroxylase,Tyrosine 3-monooxygenase 96T
U1438c CLIA Canis familiaris,Canis lupus familiaris,Dog,TH,TH,Tyrosine 3-hydroxylase,Tyrosine 3-monooxygenase 96T
MA1100 Monoclonal Antibodies: Tyrosine hydroxylase; reactive species: Human, rat, rabbit.; Clone: TH-100; Isotype: IgG1; Specificity: Tyrosine hydroxylase 100?g
MA1100 Monoclonal Anti-Tyrosine Hydroxylase, Clone number: TH-100, Ig type: mouse IgG1, Immunogen: Rat tyrosine hydroxylase(TH)., Specificity: Human;rat;rabbit. No cross reactivity with other proteins. 100μg/vial
AHP931 RABBIT ANTI TYROSINE HYDROXYLASE, Product Type Polyclonal Antibody, Specificity TYROSINE HYDROXYLASE, Target Species Rat, Host Rabbit, Format Purified, Isotypes Polyclonal IgG, Applications C, 0.1 ml
SCH-AHP1879 SHEEP ANTI RAT TYROSINE HYDROXYLASE , Product Type Polyclonal Antibody, Specificity TYROSINE HYDROXYLASE, Target Species Rat, Host Sheep, Format Purified, Isotypes Polyclonal IgG, Applications 0.1 ml


 

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