B2KI64
Gene name |
PI4KB (PIK4CB) |
Protein name |
Phosphatidylinositol 4-kinase beta |
Names |
PI4K-beta, PI4Kbeta, PtdIns 4-kinase beta |
Species |
Rhinolophus ferrumequinum (Greater horseshoe bat) |
KEGG Pathway |
|
EC number |
2.7.1.67: 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
689-711 (Activation loop from InterPro)
Target domain |
529-816 (Catalytic domain of Type III Phosphoinositide 4-kinase beta) |
Relief mechanism |
|
Assay |
|
Autoinhibited structure
Activated structure
1 structures for B2KI64
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-B2KI64-F1 | Predicted | AlphaFoldDB |
No variants for B2KI64
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for B2KI64 | |||||
No associated diseases with B2KI64
Functions
| Description | ||
|---|---|---|
| EC Number | 2.7.1.67 | Phosphotransferases with an alcohol group as acceptor |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| Golgi membrane | The lipid bilayer surrounding any of the compartments of the Golgi apparatus. |
| mitochondrial outer membrane | The outer, i.e. cytoplasm-facing, lipid bilayer of the mitochondrial envelope. |
| rough endoplasmic reticulum membrane | The lipid bilayer surrounding the rough endoplasmic reticulum. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| 1-phosphatidylinositol 4-kinase activity | Catalysis of the reaction: 1-phosphatidyl-1D-myo-inositol + ATP = 1-phosphatidyl-1D-myo-inositol 4-phosphate + ADP + 2 H(+). |
| 14-3-3 protein binding | Binding to a 14-3-3 protein. A 14-3-3 protein is any of a large family of approximately 30kDa acidic proteins which exist primarily as homo- and heterodimers within all eukaryotic cells, and have been implicated in the modulation of distinct biological processes by binding to specific phosphorylated sites on diverse target proteins, thereby forcing conformational changes or influencing interactions between their targets and other molecules. Each 14-3-3 protein sequence can be roughly divided into three sections: a divergent amino terminus, the conserved core region and a divergent carboxy-terminus. The conserved middle core region of the 14-3-3s encodes an amphipathic groove that forms the main functional domain, a cradle for interacting with client proteins. |
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| phosphatidylinositol-mediated signaling | The series of molecular signals in which a cell uses a phosphatidylinositol-mediated signaling to convert a signal into a response. Phosphatidylinositols include phosphatidylinositol (PtdIns) and its phosphorylated derivatives. |
| 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 |
| MGDTVVAPAP | LKPASESTPG | PPGNNGGSLL | SVITEGVGEL | SVIDPEVAQK | ACQEVLQKVK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LSHGGVASSD | RGTPLELVNG | DGVDGEIRCL | DDPPTGIREE | DDETEATVAS | GTAKGARRRR |
| 130 | 140 | 150 | 160 | 170 | 180 |
| QNNSAKQSWL | LRLFESKLFD | ISMAISYLYN | SKEPGVQAYI | GNRLFCFRNE | DVDFYLPQLL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| NMYVHMDEDV | GDAIKPYIVH | RCRQSVDFSL | QCALLLGAYS | SDMHISTQRH | SRGTKLRRLI |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LSDELKPAHR | KRELPSLSPA | PDTGLSPSKR | THQRSKSDAT | ASISLSSSLK | RTASNPKVES |
| 310 | 320 | 330 | 340 | 350 | 360 |
| EDEELSSSTE | SIDNSFSSPV | RLAPEREFIK | SLMAIGKRLA | TLPTKEQKTQ | RLISELSLLN |
| 370 | 380 | 390 | 400 | 410 | 420 |
| HKLPARVWLP | TAGFDHHVVR | VPHTQAVVLN | SKDKAPYLIY | VEVLECENFD | TTSVPARIPE |
| 430 | 440 | 450 | 460 | 470 | 480 |
| NRIRSTRSVE | NLPECGISHE | QRAGSFSTVP | NYDNDDEAWS | VDDIGELQVE | LPEMHTNSCD |
| 490 | 500 | 510 | 520 | 530 | 540 |
| NISQFSVDSI | TSQESKEPVF | IAAGDIRRRL | SEQLAHTPTA | FKRDPEDPSA | VALKEPWQEK |
| 550 | 560 | 570 | 580 | 590 | 600 |
| VRRIREGSPY | GHLPNWRLLS | VIVKCGDDLR | QELLAFQVLK | QLQSIWEQER | VPLWIKPYKI |
| 610 | 620 | 630 | 640 | 650 | 660 |
| LVISADSGMI | EPVVNAVSIH | QVKKQSQLSL | LDYFLQEHGS | YTTEAFLSAQ | RNFVQSCAGY |
| 670 | 680 | 690 | 700 | 710 | 720 |
| CLVCYLLQVK | DRHNGNILLD | AEGHIIHIDF | GFILSSSPRN | LGFETSAFKL | TTEFVDVMGG |
| 730 | 740 | 750 | 760 | 770 | 780 |
| LDGDMFNYYK | MLMLQGLIAA | RKHMDKVVQI | VEIMQQGSQL | PCFHGSSTIR | NLKERFHMSM |
| 790 | 800 | 810 | |||
| TEEQLQLLVE | QMVDGSMRSI | TTKLYDGFQY | LTNGIM |