| UniProt ID | PIGH_HUMAN | |
|---|---|---|
| UniProt AC | Q14442 | |
| Protein Name | Phosphatidylinositol N-acetylglucosaminyltransferase subunit H | |
| Gene Name | PIGH | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 188 | |
| Subcellular Localization | Cytoplasm. | |
| Protein Description | Part of the complex catalyzing the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI biosynthesis.. | |
| Protein Sequence | MEDERSFSDICGGRLALQRRYYSPSCREFCLSCPRLSLRSLTAVTCTVWLAAYGLFTLCENSMILSAAIFITLLGLLGYLHFVKIDQETLLIIDSLGIQMTSSYASGKESTTFIEMGKVKDIVINEAIYMQKVIYYLCILLKDPVEPHGISQVVPVFQSAKPRLDCLIEVYRSCQEILAHQKATSTSP | |
| 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 |
|---|---|---|---|---|---|
| 6 | Phosphorylation | --MEDERSFSDICGG --CCCCCCHHHHHCH | 27.36 | 21815630 | |
| 37 | Phosphorylation | CLSCPRLSLRSLTAV HHHCCHHCHHHHHHH | 24.02 | 23532336 | |
| 42 | Phosphorylation | RLSLRSLTAVTCTVW HHCHHHHHHHHHHHH | 21.96 | - | |
| 45 | Phosphorylation | LRSLTAVTCTVWLAA HHHHHHHHHHHHHHH | 10.45 | - | |
| 118 | Ubiquitination | TTFIEMGKVKDIVIN EEEEECCCEEEEEEC | 44.81 | 27667366 | |
| 181 | Ubiquitination | CQEILAHQKATSTSP HHHHHHHHHHCCCCC | 31.32 | 22505724 | |
| 182 | Ubiquitination | QEILAHQKATSTSP- HHHHHHHHHCCCCC- | 43.71 | 22505724 |
| 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 PIGH_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PIGH_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 PIGH_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| PIGA_HUMAN | PIGA | physical | 8900170 |
| 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 |
| "Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, AND MASSSPECTROMETRY. | |