| UniProt ID | PHYD1_HUMAN | |
|---|---|---|
| UniProt AC | Q5SRE7 | |
| Protein Name | Phytanoyl-CoA dioxygenase domain-containing protein 1 | |
| Gene Name | PHYHD1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 291 | |
| Subcellular Localization | ||
| Protein Description | Isoform 1 has alpha-ketoglutarate-dependent dioxygenase activity. Does not show detectable activity towards fatty acid CoA thioesters. Is not expected to be active with phytanoyl CoA. Isoform 2 and isoform 3 probably lack enzyme activity.. | |
| Protein Sequence | MACLSPSQLQKFQQDGFLVLEGFLSAEECVAMQQRIGEIVAEMDVPLHCRTEFSTQEEEQLRAQGSTDYFLSSGDKIRFFFEKGVFDEKGNFLVPPEKSINKIGHALHAHDPVFKSITHSFKVQTLARSLGLQMPVVVQSMYIFKQPHFGGEVSPHQDASFLYTEPLGRVLGVWIAVEDATLENGCLWFIPGSHTSGVSRRMVRAPVGSAPGTSFLGSEPARDNSLFVPTPVQRGALVLIHGEVVHKSKQNLSDRSRQAYTFHLMEASGTTWSPENWLQPTAELPFPQLYT | |
| 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 |
|---|---|---|---|---|---|
| 5 | Phosphorylation | ---MACLSPSQLQKF ---CCCCCHHHHHHH | 23.53 | 28348404 | |
| 55 | Phosphorylation | HCRTEFSTQEEEQLR EEECCCCCHHHHHHH | 45.37 | 17525332 | |
| 102 | Acetylation | PPEKSINKIGHALHA CCHHHHHHHHHHHHC | 48.68 | 7460727 | |
| 116 | Phosphorylation | AHDPVFKSITHSFKV CCCHHHHHHCHHHHH | 22.66 | 24719451 | |
| 125 | Phosphorylation | THSFKVQTLARSLGL CHHHHHHHHHHHCCC | 25.93 | - | |
| 129 | Phosphorylation | KVQTLARSLGLQMPV HHHHHHHHCCCCCCE | 22.60 | - | |
| 140 | Phosphorylation | QMPVVVQSMYIFKQP CCCEEEEEEEEEECC | 11.27 | - | |
| 154 | Phosphorylation | PHFGGEVSPHQDASF CCCCCCCCCCCCCCE | 16.62 | 28857561 | |
| 160 | Phosphorylation | VSPHQDASFLYTEPL CCCCCCCCEEECCCH | 24.87 | 28348404 |
| 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 PHYD1_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PHYD1_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 PHYD1_HUMAN !! | ||||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| There are no disease associations of PTM sites. | ||||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-55, AND MASSSPECTROMETRY. | |