| UniProt ID | PHS_HUMAN | |
|---|---|---|
| UniProt AC | P61457 | |
| Protein Name | Pterin-4-alpha-carbinolamine dehydratase | |
| Gene Name | PCBD1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 104 | |
| Subcellular Localization | Cytoplasm. Nucleus. Cytoplasmic and/or nuclear. | |
| Protein Description | Involved in tetrahydrobiopterin biosynthesis. Seems to both prevent the formation of 7-pterins and accelerate the formation of quinonoid-BH2. Coactivator for HNF1A-dependent transcription. Regulates the dimerization of homeodomain protein HNF1A and enhances its transcriptional activity.. | |
| Protein Sequence | MAGKAHRLSAEERDQLLPNLRAVGWNELEGRDAIFKQFHFKDFNRAFGFMTRVALQAEKLDHHPEWFNVYNKVHITLSTHECAGLSERDINLASFIEQVAVSMT | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MAGKAHRLS ------CCCCCCCCC | 28.35 | 8444860 | |
| 9 | Phosphorylation | AGKAHRLSAEERDQL CCCCCCCCHHHHHHH | 33.32 | 28102081 | |
| 10 | Ubiquitination | GKAHRLSAEERDQLL CCCCCCCHHHHHHHH | 27.54 | 21890473 | |
| 23 | Ubiquitination | LLPNLRAVGWNELEG HHHHHHHCCCHHHCC | 8.04 | 22053931 | |
| 36 | Ubiquitination | EGRDAIFKQFHFKDF CCCCHHHHHHCCCCH | 46.04 | 23000965 | |
| 36 | 2-Hydroxyisobutyrylation | EGRDAIFKQFHFKDF CCCCHHHHHHCCCCH | 46.04 | - | |
| 36 | Acetylation | EGRDAIFKQFHFKDF CCCCHHHHHHCCCCH | 46.04 | 27178108 | |
| 41 | Acetylation | IFKQFHFKDFNRAFG HHHHHCCCCHHHHHH | 53.49 | 19608861 | |
| 41 | Ubiquitination | IFKQFHFKDFNRAFG HHHHHCCCCHHHHHH | 53.49 | 23000965 | |
| 41 | 2-Hydroxyisobutyrylation | IFKQFHFKDFNRAFG HHHHHCCCCHHHHHH | 53.49 | - | |
| 59 | Ubiquitination | RVALQAEKLDHHPEW HHHHHHHHCCCCHHH | 63.33 | 22817900 | |
| 70 | Phosphorylation | HPEWFNVYNKVHITL CHHHHHHCCEEEEEE | 15.46 | 27732954 | |
| 72 | Ubiquitination | EWFNVYNKVHITLST HHHHHCCEEEEEECH | 19.94 | 21890473 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of PHS_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PHS_HUMAN !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of PHS_HUMAN !! | ||||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| 264070 | Hyperphenylalaninemia, BH4-deficient, D (HPABH4D) | |||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Acetylation | |
| Reference | PubMed |
| "Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-41, AND MASS SPECTROMETRY. | |
