P17752 · TPH1_HUMAN
- ProteinTryptophan 5-hydroxylase 1
- GeneTPH1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids444 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Oxidizes L-tryptophan to 5-hydroxy-l-tryptophan in the rate-determining step of serotonin biosynthesis.
Catalytic activity
- (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + L-tryptophan + O2 = (4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin + 5-hydroxy-L-tryptophan
Cofactor
Pathway
Aromatic compound metabolism; serotonin biosynthesis; serotonin from L-tryptophan: step 1/2.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 235 | L-tryptophan (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 257 | L-tryptophan (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 265 | L-tryptophan (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 272 | Fe cation (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 277 | Fe cation (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 317 | Fe cation (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 336 | L-tryptophan (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 366 | L-tryptophan (UniProtKB | ChEBI) | ||||
Sequence: I |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | neuron projection | |
Molecular Function | iron ion binding | |
Molecular Function | tryptophan 5-monooxygenase activity | |
Biological Process | aromatic amino acid metabolic process | |
Biological Process | bone remodeling | |
Biological Process | circadian rhythm | |
Biological Process | mammary gland alveolus development | |
Biological Process | negative regulation of ossification | |
Biological Process | platelet degranulation | |
Biological Process | positive regulation of fat cell differentiation | |
Biological Process | regulation of hemostasis | |
Biological Process | response to immobilization stress | |
Biological Process | serotonin biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTryptophan 5-hydroxylase 1
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP17752
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 478 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000205568 | 1-444 | Tryptophan 5-hydroxylase 1 | |||
Sequence: MIEDNKENKDHSLERGRASLIFSLKNEVGGLIKALKIFQEKHVNLLHIESRKSKRRNSEFEIFVDCDINREQLNDIFHLLKSHTNVLSVNLPDNFTLKEDGMETVPWFPKKISDLDHCANRVLMYGSELDADHPGFKDNVYRKRRKYFADLAMNYKHGDPIPKVEFTEEEIKTWGTVFQELNKLYPTHACREYLKNLPLLSKYCGYREDNIPQLEDVSNFLKERTGFSIRPVAGYLSPRDFLSGLAFRVFHCTQYVRHSSDPFYTPEPDTCHELLGHVPLLAEPSFAQFSQEIGLASLGASEEAVQKLATCYFFTVEFGLCKQDGQLRVFGAGLLSSISELKHALSGHAKVKPFDPKITCKQECLITTFQDVYFVSESFEDAKEKMREFTKTIKRPFGVKYNPYTRSIQILKDTKSITSAMNELQHDLDVVSDALAKVSRKPSI | ||||||
Modified residue | 58 | Phosphoserine; by PKA | ||||
Sequence: S |
Post-translational modification
Ubiquitinated, leading to its degradation by the proteasome. Ubiquitinated is triggered by phosphorylation.
Phosphorylated; triggering degradation by the proteasome.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Homotetramer.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P17752 | BECN1 Q14457 | 3 | EBI-3956833, EBI-949378 | |
BINARY | P17752 | BOD1 Q96IK1-2 | 3 | EBI-3956833, EBI-18924329 | |
BINARY | P17752 | DNAJC12 Q9UKB3 | 3 | EBI-3956833, EBI-2689937 | |
BINARY | P17752 | GORASP2 Q9H8Y8 | 5 | EBI-3956833, EBI-739467 | |
BINARY | P17752 | PSTPIP1 O43586 | 3 | EBI-3956833, EBI-1050964 | |
BINARY | P17752 | ZMYM6 O95789-4 | 3 | EBI-3956833, EBI-12949277 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 19-94 | ACT | ||||
Sequence: SLIFSLKNEVGGLIKALKIFQEKHVNLLHIESRKSKRRNSEFEIFVDCDINREQLNDIFHLLKSHTNVLSVNLPDN |
Sequence similarities
Belongs to the biopterin-dependent aromatic amino acid hydroxylase family.
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
P17752-1
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.
- Name1
- Length444
- Mass (Da)50,985
- Last updated2006-10-17 v4
- ChecksumDFAD501446953A91
P17752-2
- Name2
- Differences from canonical
- 438-444: VSRKPSI → SLNEDVLQVSVFALLLFLPSLHGECHPDT
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0AAQ5BHT3 | A0AAQ5BHT3_HUMAN | TPH1 | 343 | ||
E9PR49 | E9PR49_HUMAN | TPH1 | 454 | ||
E7EMX4 | E7EMX4_HUMAN | TPH1 | 206 |
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 19 | in Ref. 2; AAA67050 | ||||
Sequence: S → T | ||||||
Sequence conflict | 68 | in Ref. 2; AAA67050 | ||||
Sequence: I → T | ||||||
Sequence conflict | 90-91 | in Ref. 2; AAA67050 | ||||
Sequence: NL → TP | ||||||
Sequence conflict | 97 | in Ref. 2; AAA67050 | ||||
Sequence: L → M | ||||||
Sequence conflict | 100 | in Ref. 2; AAA67050 | ||||
Sequence: D → E | ||||||
Sequence conflict | 104 | in Ref. 2; AAA67050 | ||||
Sequence: T → S | ||||||
Sequence conflict | 151 | in Ref. 2; AAA67050 | ||||
Sequence: L → S | ||||||
Sequence conflict | 154 | in Ref. 2; AAA67050 | ||||
Sequence: N → S | ||||||
Sequence conflict | 157 | in Ref. 2; AAA67050 | ||||
Sequence: H → Y | ||||||
Sequence conflict | 179 | in Ref. 2; AAA67050 | ||||
Sequence: Q → R | ||||||
Sequence conflict | 207 | in Ref. 2; AAA67050 | ||||
Sequence: R → Q | ||||||
Sequence conflict | 217 | in Ref. 2; AAA67050 | ||||
Sequence: V → I | ||||||
Sequence conflict | 344 | in Ref. 2; AAA67050 | ||||
Sequence: A → V | ||||||
Sequence conflict | 414 | in Ref. 2; AAA67050 | ||||
Sequence: T → A | ||||||
Sequence conflict | 419 | in Ref. 2; AAA67050 | ||||
Sequence: S → N | ||||||
Sequence conflict | 425 | in Ref. 2; AAA67050 | ||||
Sequence: Q → R | ||||||
Sequence conflict | 436 | in Ref. 2; AAA67050 | ||||
Sequence: A → G | ||||||
Alternative sequence | VSP_000546 | 438-444 | in isoform 2 | |||
Sequence: VSRKPSI → SLNEDVLQVSVFALLLFLPSLHGECHPDT |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X52836 EMBL· GenBank· DDBJ | CAA37018.1 EMBL· GenBank· DDBJ | mRNA | ||
L29306 EMBL· GenBank· DDBJ | AAA67050.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471064 EMBL· GenBank· DDBJ | EAW68421.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471064 EMBL· GenBank· DDBJ | EAW68422.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC106739 EMBL· GenBank· DDBJ | AAI06740.1 EMBL· GenBank· DDBJ | mRNA | ||
AF057280 EMBL· GenBank· DDBJ | AAC69458.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF057280 EMBL· GenBank· DDBJ | AAC69459.1 EMBL· GenBank· DDBJ | Genomic DNA |