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IID00771
 UniprotP07101
ProteinTyrosine 3-monooxygenase
GeneTH
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
 Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
528
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 1-30,62-74 Hetero dimer : IID00816Complex
 Evidence X-RAY 4j6s E Reference
       Region 4j6s E 1-15 disorder
       Region 4j6s E 16-22 order
       Region 4j6s E 23-30 disorder
       Region 4j6s E 62-74 disorder
 Evidence X-RAY 4j6s F Reference
       Region 4j6s F 1-14 disorder
       Region 4j6s F 15-23 order
       Region 4j6s F 24-30 disorder
       Region 4j6s F 62-74 disorder
 Evidence X-RAY 4j6s G Reference
       Region 4j6s G 1-14 disorder
       Region 4j6s G 15-23 order
       Region 4j6s G 24-30 disorder
       Region 4j6s G 62-74 disorder
 Evidence X-RAY 4j6s H Reference
       Region 4j6s H 1-14 disorder
       Region 4j6s H 15-23 order
       Region 4j6s H 24-30 disorder
       Region 4j6s H 62-74 disorder
Seq 193-528 Homo tetramer :
 Evidence X-RAY 2xsn A Reference
       Region 2xsn A 193-527 order
       Region 2xsn A 528-528 disorder
 Evidence X-RAY 2xsn B Reference
       Region 2xsn B 193-528 order
 Evidence X-RAY 2xsn C Reference
       Region 2xsn C 193-212 order
       Region 2xsn C 213-227 disorder
       Region 2xsn C 228-528 order
 Evidence X-RAY 2xsn D Reference
       Region 2xsn D 193-193 disorder
       Region 2xsn D 194-528 order
SeqProS predicted 15-23 This region is predicted to be disordered by NeProc and AlphaFold (pLDDT < 68.5). Hetero dimer : IID00816Complex
       Region 4j6s E 16-22 order
       Region 4j6s F 15-23 order
       Region 4j6s G 15-23 order
       Region 4j6s H 15-23 order
Seqphosphorylation
    502-502 Phosphoserine
    71-71 Phosphoserine; by CaMK2 and PKA
    62-62 Phosphoserine
    19-19 Phosphoserine; by CaMK2
 
Prediction
NeProc
Disorder 1-15,25-106
Order 16-24,107-528
ProS 12-15,25-49,63-82,94-106
AlphaFold
Disorder 1-102,122-125,150-157,189-193,213-214
Order 103-121,126-149,158-188,194-212,215-528
Pfam Hmmer
PF00351 195-526 8.7e-290
SEG 47-60 ,82-91
Function
Function in SwissProt
Catalyzes the conversion of L-tyrosine to L-dihydroxyphenylalanine (L-Dopa), the rate-limiting step in the biosynthesis of cathecolamines, dopamine, noradrenaline, and adrenaline. Uses tetrahydrobiopterin and molecular oxygen to convert tyrosine to L-Dopa (PubMed:17391063, PubMed:1680128, PubMed:15287903, PubMed:8528210, Ref.18, PubMed:34922205, PubMed:24753243). In addition to tyrosine, is able to catalyze the hydroxylation of phenylalanine and tryptophan with lower specificity (By similarity). Positively regulates the regression of retinal hyaloid vessels during postnatal development (By similarity).
Lacks catalytic activity.
Lacks catalytic activity.