Q5PQ01
Gene name |
pip4k2c (pip5k2c) |
Protein name |
Phosphatidylinositol 5-phosphate 4-kinase type-2 gamma |
Names |
Phosphatidylinositol 5-phosphate 4-kinase type II gamma, PI(5)P 4-kinase type II gamma, PIP4KII-gamma |
Species |
Xenopus laevis (African clawed frog) |
KEGG Pathway |
xla:496028 |
EC number |
2.7.1.149: Phosphotransferases with an alcohol group as acceptor |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q5PQ01
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q5PQ01-F1 | Predicted | AlphaFoldDB |
No variants for Q5PQ01
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q5PQ01 | |||||
No associated diseases with Q5PQ01
1 regional properties for Q5PQ01
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Phosphatidylinositol-4-phosphate 5-kinase, core | 46 - 419 | IPR002498 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.7.1.149 | Phosphotransferases with an alcohol group as acceptor |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| endoplasmic reticulum | The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached). |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| 1-phosphatidylinositol-4-phosphate 5-kinase activity | Catalysis of the reaction: 1-phosphatidyl-1D-myo-inositol 4-phosphate + ATP = 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + ADP + 2 H(+). |
| 1-phosphatidylinositol-5-phosphate 4-kinase activity | Catalysis of the reaction: ATP + 1-phosphatidyl-1D-myo-inositol 5-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate. |
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate biosynthetic process | The chemical reactions and pathways resulting in the formation of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate. |
| phosphorylation | The process of introducing a phosphate group into a molecule, usually with the formation of a phosphoric ester, a phosphoric anhydride or a phosphoric amide. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSSSGAMPAV | SSTSSSAAVG | ILSATTAKTK | TKKKHFVQQK | VKVFRASDPL | ISVLMWGVNH |
| 70 | 80 | 90 | 100 | 110 | 120 |
| SVNELIQVPV | PVMLLPDDFK | ANSKIKVTNH | LFNRENLPSH | FKFKDYCPQV | FRNLRERFGI |
| 130 | 140 | 150 | 160 | 170 | 180 |
| DDQDFQVSLT | RSSPYCESEG | HDGRFLLSYD | KTLVIKEISS | EDVADMHIIL | SHYHQHIVKC |
| 190 | 200 | 210 | 220 | 230 | 240 |
| HESTLLPQFL | GMYRLSVDNE | DSYIIVMRNM | FSHRLTVHRK | YDLKGSLVSR | EASDKEKVKE |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LPTLKDMDFL | NKSQKVYVDE | EQKRNFMEKL | KRDVDFLVQL | KLMDYSLLLG | IHEVFRAEQE |
| 310 | 320 | 330 | 340 | 350 | 360 |
| EEEELEEDNA | ENECSPHVNV | GSYGTSPEGI | AGYLNSHKPL | GPGEFEPIID | VYAIKSSDNA |
| 370 | 380 | 390 | 400 | 410 | |
| PQKEVYFMGL | IDILTHYDAK | KKAAHAAKTV | KHGAGAEIST | VHPDQYGKRF | LEFVTNIFA |