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 | ||
|
* 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. |
loading...
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. |