Th | ENSRNOG00000020410 | NCBI 25085

Details for: Th

Gene ID: 25085

Symbol: Th

Ensembl ID: ENSRNOG00000020410

Description: tyrosine hydroxylase

Associated with

Catecholamine biosynthesis
(R-RNO-209905)
Metabolism
(R-RNO-1430728)
Metabolism of amine-derived hormones
(R-RNO-209776)
Metabolism of amino acids and derivatives
(R-RNO-71291)
Aminergic neurotransmitter loading into synaptic vesicle
(GO:0015842)
Amino acid binding
(GO:0016597)
Animal organ morphogenesis
(GO:0009887)
Aromatic amino acid metabolic process
(GO:0009072)
Axon
(GO:0030424)
Catecholamine biosynthetic process
(GO:0042423)
Cellular response to alkaloid
(GO:0071312)
Cellular response to glucose stimulus
(GO:0071333)
Cellular response to growth factor stimulus
(GO:0071363)
Cellular response to manganese ion
(GO:0071287)
Cellular response to nicotine
(GO:0071316)
Cellular response to xenobiotic stimulus
(GO:0071466)
Cerebral cortex development
(GO:0021987)
Circadian sleep/wake cycle
(GO:0042745)
Cognition
(GO:0050890)
Cytoplasm
(GO:0005737)
Cytoplasmic side of plasma membrane
(GO:0009898)
Dendrite
(GO:0030425)
Dopamine binding
(GO:0035240)
Dopamine biosynthetic process
(GO:0042416)
Dopamine biosynthetic process from tyrosine
(GO:0006585)
Eating behavior
(GO:0042755)
Embryonic camera-type eye morphogenesis
(GO:0048596)
Enzyme binding
(GO:0019899)
Epinephrine biosynthetic process
(GO:0042418)
Eye photoreceptor cell development
(GO:0042462)
Fatty acid metabolic process
(GO:0006631)
Ferric iron binding
(GO:0008199)
Ferrous iron binding
(GO:0008198)
Glycoside metabolic process
(GO:0016137)
Heart development
(GO:0007507)
Hyaloid vascular plexus regression
(GO:1990384)
Identical protein binding
(GO:0042802)
Iron ion binding
(GO:0005506)
Isoquinoline alkaloid metabolic process
(GO:0033076)
Learning
(GO:0007612)
Locomotory behavior
(GO:0007626)
Mating behavior
(GO:0007617)
Memory
(GO:0007613)
Mitochondrion
(GO:0005739)
Monooxygenase activity
(GO:0004497)
Norepinephrine biosynthetic process
(GO:0042421)
Nucleus
(GO:0005634)
Oxygen binding
(GO:0019825)
Phthalate metabolic process
(GO:0018963)
Phytoalexin metabolic process
(GO:0052314)
Protein binding
(GO:0005515)
Protein domain specific binding
(GO:0019904)
Regulation of heart contraction
(GO:0008016)
Response to activity
(GO:0014823)
Response to amphetamine
(GO:0001975)
Response to corticosterone
(GO:0051412)
Response to electrical stimulus
(GO:0051602)
Response to estradiol
(GO:0032355)
Response to ethanol
(GO:0045471)
Response to ether
(GO:0045472)
Response to growth factor
(GO:0070848)
Response to herbicide
(GO:0009635)
Response to hypoxia
(GO:0001666)
Response to immobilization stress
(GO:0035902)
Response to insecticide
(GO:0017085)
Response to isolation stress
(GO:0035900)
Response to light stimulus
(GO:0009416)
Response to lipopolysaccharide
(GO:0032496)
Response to metal ion
(GO:0010038)
Response to nicotine
(GO:0035094)
Response to nutrient levels
(GO:0031667)
Response to organic cyclic compound
(GO:0014070)
Response to peptide hormone
(GO:0043434)
Response to pyrethroid
(GO:0046684)
Response to salt stress
(GO:0009651)
Response to steroid hormone
(GO:0048545)
Response to xenobiotic stimulus
(GO:0009410)
Response to zinc ion
(GO:0010043)
Small molecule binding
(GO:0036094)
Smooth endoplasmic reticulum
(GO:0005790)
Social behavior
(GO:0035176)
Sphingolipid metabolic process
(GO:0006665)
Synaptic transmission, dopaminergic
(GO:0001963)
Synaptic vesicle
(GO:0008021)
Terpene metabolic process
(GO:0042214)
Tetrahydrobiopterin binding
(GO:0034617)
Tyrosine 3-monooxygenase activity
(GO:0004511)
Visual perception
(GO:0007601)

Other Information

Proteins

Tyrosine 3-monooxygenase

Genular Protein ID: 181630070

Symbol: TY3H_RAT

Name: Tyrosine 3-monooxygenase

UniProtKB Accession Codes:

P04177

Database IDs:

Citations:

PubMed ID: 2857492

Title: Complete coding sequence of rat tyrosine hydroxylase mRNA.

PubMed ID: 2857492

DOI: 10.1073/pnas.82.2.617

PubMed ID: 1672315

Title: Tyrosine hydroxylase in rat brain dopaminergic nerve terminals. Multiple-site phosphorylation in vivo and in synaptosomes.

PubMed ID: 1672315

DOI: 10.1016/s0021-9258(19)67644-1

PubMed ID: 11502746

Title: Phosphorylation of Ser(19) alters the conformation of tyrosine hydroxylase to increase the rate of phosphorylation of Ser(40).

PubMed ID: 11502746

DOI: 10.1074/jbc.m105280200

PubMed ID: 9228951

Title: Crystal structure of tyrosine hydroxylase at 2.3 A and its implications for inherited neurodegenerative diseases.

PubMed ID: 9228951

DOI: 10.1038/nsb0797-578

PubMed ID: 10933781

Title: Reversing the substrate specificities of phenylalanine and tyrosine hydroxylase: aspartate 425 of tyrosine hydroxylase is essential for L-DOPA formation.

PubMed ID: 10933781

DOI: 10.1021/bi000493k

PubMed ID: 11922614

Title: Role of tryptophan hydroxylase phe313 in determining substrate specificity.

PubMed ID: 11922614

DOI: 10.1006/bbrc.2002.6719

PubMed ID: 15496595

Title: Isoosmotic isolation of rat brain synaptic vesicles, some of which contain tyrosine hydroxylase.

PubMed ID: 15496595

DOI: 10.1093/jb/mvh113

PubMed ID: 21392500

Title: Phosphorylation of the N-terminal portion of tyrosine hydroxylase triggers proteasomal digestion of the enzyme.

PubMed ID: 21392500

DOI: 10.1016/j.bbrc.2011.03.020

PubMed ID: 9753429

Title: Crystal structure of tyrosine hydroxylase with bound cofactor analogue and iron at 2.3 A resolution: self-hydroxylation of Phe300 and the pterin-binding site.

PubMed ID: 9753429

DOI: 10.1021/bi981462g

PubMed ID: 24361276

Title: The solution structure of the regulatory domain of tyrosine hydroxylase.

PubMed ID: 24361276

DOI: 10.1016/j.jmb.2013.12.015

Sequence Information:

Length: 498
Mass: 55966
Checksum: 17F7E003D29218C5
Sequence:

MPTPSAPSPQ PKGFRRAVSE QDAKQAEAVT SPRFIGRRQS LIEDARKERE AAAAAAAAAV 
ASSEPGNPLE AVVFEERDGN AVLNLLFSLR GTKPSSLSRA VKVFETFEAK IHHLETRPAQ 
RPLAGSPHLE YFVRFEVPSG DLAALLSSVR RVSDDVRSAR EDKVPWFPRK VSELDKCHHL 
VTKFDPDLDL DHPGFSDQVY RQRRKLIAEI AFQYKHGEPI PHVEYTAEEI ATWKEVYVTL 
KGLYATHACR EHLEGFQLLE RYCGYREDSI PQLEDVSRFL KERTGFQLRP VAGLLSARDF 
LASLAFRVFQ CTQYIRHASS PMHSPEPDCC HELLGHVPML ADRTFAQFSQ DIGLASLGAS 
DEEIEKLSTV YWFTVEFGLC KQNGELKAYG AGLLSSYGEL LHSLSEEPEV RAFDPDTAAV 
QPYQDQTYQP VYFVSESFND AKDKLRNYAS RIQRPFSVKF DPYTLAIDVL DSPHTIQRSL 
EGVQDELHTL AHALSAIS

The gene details are incomplete or unavailable at the moment.

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: Th

Associated with

Other Information

Complete coding sequence of rat tyrosine hydroxylase mRNA. PubMed ID: 2857492

Tyrosine hydroxylase in rat brain dopaminergic nerve terminals. Multiple-site phosphorylation in vivo and in synaptosomes. PubMed ID: 1672315

Phosphorylation of Ser(19) alters the conformation of tyrosine hydroxylase to increase the rate of phosphorylation of Ser(40). PubMed ID: 11502746

Crystal structure of tyrosine hydroxylase at 2.3 A and its implications for inherited neurodegenerative diseases. PubMed ID: 9228951

Reversing the substrate specificities of phenylalanine and tyrosine hydroxylase: aspartate 425 of tyrosine hydroxylase is essential for L-DOPA formation. PubMed ID: 10933781

Role of tryptophan hydroxylase phe313 in determining substrate specificity. PubMed ID: 11922614

Isoosmotic isolation of rat brain synaptic vesicles, some of which contain tyrosine hydroxylase. PubMed ID: 15496595

Phosphorylation of the N-terminal portion of tyrosine hydroxylase triggers proteasomal digestion of the enzyme. PubMed ID: 21392500

Crystal structure of tyrosine hydroxylase with bound cofactor analogue and iron at 2.3 A resolution: self-hydroxylation of Phe300 and the pterin-binding site. PubMed ID: 9753429

The solution structure of the regulatory domain of tyrosine hydroxylase. PubMed ID: 24361276