P07101 (TY3H_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tyrosine 3-monooxygenase
EC=1.14.16.2

Alternative name(s):
Tyrosine 3-hydroxylase
Short name=TH

Gene names

Name:	TH
Synonyms:	TYH

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	528 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Plays an important role in the physiology of adrenergic neurons.
Catalytic activity	L-tyrosine + tetrahydrobiopterin + O2 = 3,4-dihydroxy-L-phenylalanine + 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	Defects in TH are the cause of 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=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.10
Sequence similarities	Belongs to the biopterin-dependent aromatic amino acid hydroxylase family.

Ontologies

Keywords
Biological process	Catecholamine biosynthesis Neurotransmitter biosynthesis
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Dystonia Parkinson disease Parkinsonism
Ligand	Iron Metal-binding
Molecular function	Monooxygenase Oxidoreductase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	dopamine biosynthetic process from tyrosine Non-traceable author statement. Source: BHF-UCL embryonic camera-type eye morphogenesis Inferred from sequence or structural similarity. Source: BHF-UCL epinephrine biosynthetic process Inferred from direct assay. Source: BHF-UCL eye photoreceptor cell development Inferred from sequence or structural similarity. Source: BHF-UCL heart morphogenesis Non-traceable author statement. Source: BHF-UCL hormone biosynthetic process Traceable author statement. Source: Reactome learning Inferred from sequence or structural similarity. Source: BHF-UCL locomotory behavior Inferred from sequence or structural similarity. Source: BHF-UCL memory Inferred from sequence or structural similarity. Source: BHF-UCL neurotransmitter biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW neurotransmitter secretion Traceable author statement. Source: Reactome norepinephrine biosynthetic process Inferred from direct assay. Source: BHF-UCL pigmentation Traceable author statement. Source: BHF-UCL regulation of heart contraction Inferred from sequence or structural similarity. Source: BHF-UCL response to ethanol Inferred from direct assay. Source: BHF-UCL response to hypoxia Inferred from direct assay. Source: BHF-UCL synaptic transmission, dopaminergic Inferred from sequence or structural similarity. Source: BHF-UCL visual perception Inferred from sequence or structural similarity. Source: BHF-UCL
Cellular component	cytosol Traceable author statement. Source: Reactome internal side of plasma membrane Inferred from direct assay. Source: BHF-UCL melanosome membrane Inferred from direct assay. 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. Source: BHF-UCL
Molecular function	tyrosine 3-monooxygenase activity Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 3 (identifier: P07101-1)

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)

The sequence of this isoform differs from the canonical sequence as follows:
     31-34: Missing.

Isoform 2 (identifier: P07101-3)

The sequence of this isoform differs from the canonical sequence as follows:
     31-61: Missing.

Isoform 4 (identifier: P07101-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: Missing.
     34-34: Q → M

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 528

527

Tyrosine 3-monooxygenase

PRO_0000205561

Regions

Compositional bias

85 – 90

6

Poly-Ala

Sites

Metal binding

361

1

Iron By similarity

Metal binding

366

1

Iron By similarity

Metal binding

406

1

Iron By similarity

Amino acid modifications

Modified residue

19

1

Phosphoserine By similarity

Modified residue

62

1

Phosphoserine By similarity

Modified residue

71

1

Phosphoserine; by PKA By similarity

Natural variations

Alternative sequence

1 – 33

33

Missing in isoform 4.

VSP_000541

Alternative sequence

31 – 61

31

Missing in isoform 2.

VSP_000544

Alternative sequence

31 – 34

4

Missing in isoform 1.

VSP_000543

Alternative sequence

34

1

Q → M in isoform 4.

VSP_000542

Natural variant

112

1

V → M Common polymorphism. Ref.12 Ref.15 Ref.18
Corresponds to variant rs6356 [ dbSNP | Ensembl ].

VAR_014025

Natural variant

233

1

R → H in ARSEGS.

VAR_014026

Natural variant

236

1

L → P in ARSEGS; severe parkinsonian symptoms in early infancy; strongly reduced stability and catalytic activity; rare mutation.

VAR_014027

Natural variant

276

1

T → P in ARSEGS; parkinsonian symptoms in infancy.
Corresponds to variant rs28934581 [ dbSNP | Ensembl ].

VAR_014028

Natural variant

314

1

T → M in ARSEGS; parkinsonian symptoms in infancy.

VAR_014029

Natural variant

337

1

R → H in ARSEGS; parkinsonian symptoms in infancy.
Corresponds to variant rs28934580 [ dbSNP | Ensembl ].

VAR_014030

Natural variant

412

1

Q → K in ARSEGS; reduced affinity for L-tyrosine.

VAR_014031

Natural variant

494

1

T → M in ARSEGS; parkinsonian symptoms in infancy.
Corresponds to variant rs45471299 [ dbSNP | Ensembl ].

VAR_014032

Natural variant

499

1

V → M. Ref.16
Corresponds to variant rs1800033 [ dbSNP | Ensembl ].

VAR_014033

Experimental info

Sequence conflict

401

1

Y → S in AAA61179. Ref.1

Sequence conflict

401

1

Y → S in CAA28908. Ref.2

Sequence conflict

401

1

Y → S in CAA68472. Ref.3

Secondary structure

1

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528

Helix Strand Turn

Details...

Helix

201 – 206

6

Turn

216 – 218

3

Helix

228 – 243

16

Helix

257 – 270

14

Helix

274 – 277

4

Helix

282 – 292

11

Helix

303 – 313

11

Beta strand

317 – 320

4

Helix

327 – 334

8

Turn

335 – 337

3

Beta strand

338 – 341

4

Helix

359 – 363

5

Helix

367 – 370

4

Helix

374 – 381

8

Helix

391 – 403

13

Turn

404 – 406

3

Beta strand

416 – 418

3

Helix

430 – 433

4

Beta strand

435 – 442

8

Helix

445 – 449

5

Beta strand

455 – 457

3

Beta strand

460 – 466

7

Helix

468 – 480

13

Beta strand

485 – 491

7

Turn

492 – 495

4

Beta strand

496 – 500

5

Helix

503 – 510

8

Helix

514 – 526

13

Sequences

	Sequence		Length	Mass (Da)
	Isoform 3 [UniParc]. Last modified June 16, 2009. Version 5. Checksum: 31D2D49955ACF070	FASTA	528	58,600
	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
	Isoform 1 [UniParc]. Checksum: 708422BBD3304A6C	FASTA	524	58,160
	10 20 30 40 50 60 MPTPDATTPQ AKGFRRAVSE LDAKQAEAIM GAPGPSLTGS PWPGTAAPAA SYTPTPRSPR 70 80 90 100 110 120 FIGRRQSLIE DARKEREAAV AAAAAAVPSE PGDPLEAVAF EEKEGKAVLN LLFSPRATKP 130 140 150 160 170 180 SALSRAVKVF ETFEAKIHHL ETRPAQRPRA GGPHLEYFVR LEVRRGDLAA LLSGVRQVSE 190 200 210 220 230 240 DVRSPAGPKV PWFPRKVSEL DKCHHLVTKF DPDLDLDHPG FSDQVYRQRR KLIAEIAFQY 250 260 270 280 290 300 RHGDPIPRVE YTAEEIATWK EVYTTLKGLY ATHACGEHLE AFALLERFSG YREDNIPQLE 310 320 330 340 350 360 DVSRFLKERT GFQLRPVAGL LSARDFLASL AFRVFQCTQY IRHASSPMHS PEPDCCHELL 370 380 390 400 410 420 GHVPMLADRT FAQFSQDIGL ASLGASDEEI EKLSTLYWFT VEFGLCKQNG EVKAYGAGLL 430 440 450 460 470 480 SSYGELLHCL SEEPEIRAFD PEAAAVQPYQ DQTYQSVYFV SESFSDAKDK LRSYASRIQR 490 500 510 520 PFSVKFDPYT LAIDVLDSPQ AVRRSLEGVQ DELDTLAHAL SAIG
	Isoform 2 [UniParc]. Checksum: 6CB8EDC9C4874288	FASTA	497	55,612
	10 20 30 40 50 60 MPTPDATTPQ AKGFRRAVSE LDAKQAEAIM SPRFIGRRQS LIEDARKERE AAVAAAAAAV 70 80 90 100 110 120 PSEPGDPLEA VAFEEKEGKA VLNLLFSPRA TKPSALSRAV KVFETFEAKI HHLETRPAQR 130 140 150 160 170 180 PRAGGPHLEY FVRLEVRRGD LAALLSGVRQ VSEDVRSPAG PKVPWFPRKV SELDKCHHLV 190 200 210 220 230 240 TKFDPDLDLD HPGFSDQVYR QRRKLIAEIA FQYRHGDPIP RVEYTAEEIA TWKEVYTTLK 250 260 270 280 290 300 GLYATHACGE HLEAFALLER FSGYREDNIP QLEDVSRFLK ERTGFQLRPV AGLLSARDFL 310 320 330 340 350 360 ASLAFRVFQC TQYIRHASSP MHSPEPDCCH ELLGHVPMLA DRTFAQFSQD IGLASLGASD 370 380 390 400 410 420 EEIEKLSTLY WFTVEFGLCK QNGEVKAYGA GLLSSYGELL HCLSEEPEIR AFDPEAAAVQ 430 440 450 460 470 480 PYQDQTYQSV YFVSESFSDA KDKLRSYASR IQRPFSVKFD PYTLAIDVLD SPQAVRRSLE 490 GVQDELDTLA HALSAIG
	Isoform 4 [UniParc]. Checksum: 20B194A87A66BD3D	FASTA	495	55,077
	10 20 30 40 50 60 MGAPGPSLTG SPWPGTAAPA ASYTPTPRSP RFIGRRQSLI EDARKEREAA VAAAAAAVPS 70 80 90 100 110 120 EPGDPLEAVA FEEKEGKAVL NLLFSPRATK PSALSRAVKV FETFEAKIHH LETRPAQRPR 130 140 150 160 170 180 AGGPHLEYFV RLEVRRGDLA ALLSGVRQVS EDVRSPAGPK VPWFPRKVSE LDKCHHLVTK 190 200 210 220 230 240 FDPDLDLDHP GFSDQVYRQR RKLIAEIAFQ YRHGDPIPRV EYTAEEIATW KEVYTTLKGL 250 260 270 280 290 300 YATHACGEHL EAFALLERFS GYREDNIPQL EDVSRFLKER TGFQLRPVAG LLSARDFLAS 310 320 330 340 350 360 LAFRVFQCTQ YIRHASSPMH SPEPDCCHEL LGHVPMLADR TFAQFSQDIG LASLGASDEE 370 380 390 400 410 420 IEKLSTLYWF TVEFGLCKQN GEVKAYGAGL LSSYGELLHC LSEEPEIRAF DPEAAAVQPY 430 440 450 460 470 480 QDQTYQSVYF VSESFSDAKD KLRSYASRIQ RPFSVKFDPY TLAIDVLDSP QAVRRSLEGV 490 QDELDTLAHA LSAIG

References

	« Hide 'large scale' referencesShow '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: 2887169] [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: 2882428] [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: 2888085] [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: 2902075] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
[5]	"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. , 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: 16554811] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	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 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain.
[8]	"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: 2892893] [Abstract] Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[9]	"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: 2896667] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-30.
[10]	"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: 20809526] [Abstract] Cited for: POSSIBLE INVOLVEMENT IN PARKINSON DISEASE.
[11]	"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: 7814018] [Abstract] Cited for: VARIANT ARSEGS LYS-412.
[12]	"Frequent sequence variant in the human tyrosine hydroxylase gene." Luedecke B., Bartholome K. Hum. Genet. 95:716-716(1995) [PubMed: 7789962] [Abstract] Cited for: VARIANT MET-112.
[13]	"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: 8528210] [Abstract] Cited for: CHARACTERIZATION OF VARIANT ARSEGS LYS-412.
[14]	"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: 8817341] [Abstract] Cited for: CHARACTERIZATION OF VARIANT ARSEGS PRO-236.
[15]	"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: 9613851] [Abstract] Cited for: VARIANT ARSEGS PRO-236, VARIANT MET-112.
[16]	"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: 9754624] [Abstract] Cited for: VARIANT MET-499.
[17]	"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: 9703425] [Abstract] Cited for: VARIANT ARSEGS HIS-233.
[18]	"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: 10391209] [Abstract] Cited for: VARIANT MET-112.
[19]	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)
[20]	"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: 11246459] [Abstract] Cited for: VARIANTS ARSEGS PRO-276; MET-314; HIS-337 AND MET-494.
+	Additional computationally mapped references.

Web resources

GeneReviews

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.
AC132217 Genomic DNA. No translation available.
M24791, M24787, M24789 Genomic DNA. Translation: AAA61173.1.
CH471158 Genomic DNA. Translation: EAX02493.1.
BC143611 mRNA. Translation: AAI43612.1.
M24791, M24787 Genomic DNA. Translation: AAA61170.1.
M20911 mRNA. Translation: AAA61167.1.

IPI

IPI00010178.
IPI00218275.
IPI00398179.
IPI00922082.

PIR

WHHUY4. A30002.

RefSeq

NP_000351.2. NM_000360.3.
NP_954986.2. NM_199292.2.
NP_954987.2. NM_199293.2.

UniGene

Hs.435609.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2XSN	X-ray	2.68	A/B/C/D	194-528	[»]

ProteinModelPortal

P07101.

SMR

P07101. Positions 104-528.

ModBase

Search...

Protein-protein interaction databases

STRING

P07101.

PTM databases

PhosphoSite

P07101.

Polymorphism databases

DMDM

239938945.

Proteomic databases

PRIDE

P07101.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000381178; ENSP00000370571; ENSG00000180176.

GeneID

7054.

KEGG

hsa:7054.

UCSC

uc001lvp.1. human.
uc001lvq.1. human.

Organism-specific databases

CTD

7054.

GeneCards

GC11M002185.

HGNC

HGNC:11782. TH.

HPA

CAB002522.

MIM

191290. gene.
605407. phenotype.

neXtProt

NX_P07101.

Orphanet

101150. Autosomal recessive dopa-responsive dystonia.

PharmGKB

PA351.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

HBG484724.

HOVERGEN

HBG006841.

InParanoid

P07101.

OMA

PKVPWFP.

PhylomeDB

P07101.

Enzyme and pathway databases

Pathway_Interaction_DB

alphasynuclein_pathway. Alpha-synuclein signaling.
p38_mk2pathway. p38 signaling mediated by MAPKAP kinases.

Reactome

REACT_111217. Metabolism.

Gene expression databases

ArrayExpress

P07101.

Bgee

P07101.

CleanEx

HS_TH.

Genevestigator

P07101.

GermOnline

ENSG00000180176. Homo sapiens.

Family and domain databases

InterPro

IPR001273. 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]

Gene3D

G3DSA:1.10.800.10. Aaa_hydroxylase. 1 hit.

KO

K00501.

PANTHER

PTHR11473. Aaa_hydroxylase. 1 hit.

Pfam

PF00351. Biopterin_H. 1 hit.
PF12549. TOH_N. 3 hits.
[Graphical view]

PIRSF

PIRSF000336. TH. 1 hit.

PRINTS

PR00372. FYWHYDRXLASE.

SUPFAM

SSF56534. Aaa_hydroxylase. 1 hit.

TIGRFAMs

TIGR01269. Tyr_3_monoox. 1 hit.

PROSITE

PS00367. BH4_AAA_HYDROXYL_1. 1 hit.
PS51410. BH4_AAA_HYDROXYL_2. 1 hit.
[Graphical view]

ProtoNet

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DrugBank

DB00120. L-Phenylalanine.
DB00135. L-Tyrosine.
DB00765. Metyrosine.
DB00360. Tetrahydrobiopterin.

NextBio

27583.

SOURCE

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Entry information

Entry name

TY3H_HUMAN

Accession

Primary (citable) accession number: P07101
Secondary accession number(s): B7ZL70 , Q15585, Q15588, Q15589

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	June 16, 2009
Last modified:	January 25, 2012
This is version 143 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.