P0C5E7
Gene name |
age-1 (CBG02868) |
Protein name |
Phosphatidylinositol 3-kinase age-1 |
Names |
PI3-kinase age-1, PI3K age-1, PtdIns-3-kinase age-1, Aging alteration protein 1 |
Species |
Caenorhabditis briggsae |
KEGG Pathway |
|
EC number |
2.7.1.137: 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 P0C5E7
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P0C5E7-F1 | Predicted | AlphaFoldDB |
No variants for P0C5E7
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P0C5E7 | |||||
No associated diseases with P0C5E7
7 regional properties for P0C5E7
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Phosphatidylinositol 3-kinase Ras-binding (PI3K RBD) domain | 246 - 366 | IPR000341 |
| domain | Phosphatidylinositol 3-/4-kinase, catalytic domain | 858 - 1159 | IPR000403 |
| domain | Phosphoinositide 3-kinase, accessory (PIK) domain | 607 - 803 | IPR001263 |
| domain | C2 phosphatidylinositol 3-kinase-type domain | 422 - 588 | IPR002420 |
| domain | Phosphatidylinositol 3-kinase, adaptor-binding domain | 79 - 182 | IPR003113 |
| conserved_site | Phosphatidylinositol 3/4-kinase, conserved site | 894 - 908 | IPR018936-1 |
| conserved_site | Phosphatidylinositol 3/4-kinase, conserved site | 1016 - 1036 | IPR018936-2 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.7.1.137 | Phosphotransferases with an alcohol group as acceptor |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
4 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| membrane | A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it. |
| phosphatidylinositol 3-kinase complex | A protein complex capable of phosphatidylinositol 3-kinase activity and containing subunits of any phosphatidylinositol 3-kinase (PI3K) enzyme. These complexes are divided in three classes (called I, II and III) that differ for their presence across taxonomic groups and for the type of their constituents. Catalytic subunits of phosphatidylinositol 3-kinase enzymes are present in all 3 classes; regulatory subunits of phosphatidylinositol 3-kinase enzymes are present in classes I and III; adaptor proteins have been observed in class II complexes and may be present in other classes too. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| 1-phosphatidylinositol-3-kinase activity | Catalysis of the reaction: 1-phosphatidyl-1D-myo-inositol + ATP = a 1-phosphatidyl-1D-myo-inositol 3-phosphate + ADP + 2 H(+). |
| 1-phosphatidylinositol-4-phosphate 3-kinase activity | Catalysis of the reaction: 1-phosphatidyl-1D-myo-inositol 4-phosphate + ATP = 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate + ADP + 2 H(+). |
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| phosphatidylinositol kinase activity | Catalysis of the reaction: ATP + a phosphatidylinositol = ADP + a phosphatidylinositol phosphate. |
8 GO annotations of biological process
| Name | Definition |
|---|---|
| aging | A developmental process that is a deterioration and loss of function over time. Aging includes loss of functions such as resistance to disease, homeostasis, and fertility, as well as wear and tear. Aging includes cellular senescence, but is more inclusive. May precede death and may succeed developmental maturation (GO:0021700). |
| cell migration | The controlled self-propelled movement of a cell from one site to a destination guided by molecular cues. Cell migration is a central process in the development and maintenance of multicellular organisms. |
| dauer larval development | The process whose specific outcome is the progression of the dauer larva over time, through the facultative diapause of the dauer (enduring) larval stage, with specialized traits adapted for dispersal and long-term survival, with elevated stress resistance and without feeding. |
| phosphatidylinositol 3-kinase signaling | A series of reactions within the signal-receiving cell, mediated by the intracellular phosphatidylinositol 3-kinase (PI3K). Many cell surface receptor linked signaling pathways signal through PI3K to regulate numerous cellular functions. |
| phosphatidylinositol phosphate biosynthetic process | The chemical reactions and pathways resulting in the formation of phosphatidylinositol phosphate. |
| phosphatidylinositol-3-phosphate biosynthetic process | The chemical reactions and pathways resulting in the formation of phosphatidylinositol-3-phosphate, a phosphatidylinositol monophosphate carrying the phosphate group at the 3-position. |
| 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 |
| MSMGRSSSTT | FRNRTASHGS | RSLGSAETAR | IPRKLSSQLS | HTHANILHPQ | LQTMMEQWQM |
| 70 | 80 | 90 | 100 | 110 | 120 |
| RERPSLETEN | GKGSLLLSSE | GVADMIVLSS | FGEVISVVFP | WFLANVRTSF | DIKLSEFKHQ |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LFEQIGPMKW | GKHSTQPQDY | AFRQLNNFGE | IEVIFNDDQQ | LSCLELHGTF | PMLFLFEPDG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| FNRDKELMCD | ISHCLGYSLD | KLEESIDEEL | RQFRASLWTQ | TKKTCFERGV | DGVDHYAFPE |
| 250 | 260 | 270 | 280 | 290 | 300 |
| EQYFCVGEKC | PTDLESKVKA | AKLDYQLFWT | KRKSEANEVW | EKMYKITIDF | DPEFNPQSLM |
| 310 | 320 | 330 | 340 | 350 | 360 |
| RMFVKELQCM | NLFDPEDPPD | EEWILQLAGR | TSFVTRPEIS | LVSYDGIRSE | LESYRCPGFV |
| 370 | 380 | 390 | 400 | 410 | 420 |
| VRRKSLVLKD | YVRPKPLYEP | HYVRVHERKM | ALDVLSVSIG | TEVKHSGNSD | KVWTDFRPTA |
| 430 | 440 | 450 | 460 | 470 | 480 |
| SLEQITLWDL | DSNLMIRPVN | VTGLPFTASH | DIYLGMEFKV | YVGTLTLATI | KIPRVPTTKL |
| 490 | 500 | 510 | 520 | 530 | 540 |
| VWKREFFTFD | LYMKDMPPSA | ILSVRVYSMK | TTKMKEEIEL | GWVNISLSDW | RDELRQGQIK |
| 550 | 560 | 570 | 580 | 590 | 600 |
| LNLWGPEPSA | NRSRIGHNGA | KIGTSLSVTV | EISSHGRRVK | MPNEAQYKYL | VDHRISWSDT |
| 610 | 620 | 630 | 640 | 650 | 660 |
| VEIVGDDYEA | CIGDPGYKKL | QDLVKKHESG | VILDDSEQRH | VWSWRNYIQK | QEPDLLVVLS |
| 670 | 680 | 690 | 700 | 710 | 720 |
| ELRIVWTDRE | NFSELYVMLE | TWKAPSVAAA | LTLLGKRCTD | RVIRKFAVNK | LNDQLSQFNV |
| 730 | 740 | 750 | 760 | 770 | 780 |
| HLFLLPLIQA | LKYEPRAYSE | VGMMLLTRAL | SSYRIGHRLF | WLLRSEICRL | KDCATNNEEY |
| 790 | 800 | 810 | 820 | 830 | 840 |
| RRISLLMEAY | LRGNEEHIKG | IIRQVDMVDE | LTRISSLVKG | LSKEAAREKL | RDQLRTISHK |
| 850 | 860 | 870 | 880 | 890 | 900 |
| MESIDSPLDP | VYKFGEMVIE | KAIVLGSAKQ | PLRLVWKNKN | PKSDLHLPFC | EVIFKNGDDL |
| 910 | 920 | 930 | 940 | 950 | 960 |
| RQDMLVLQVL | EVMDTIWKAA | NIDCCLSPYG | VLPMGEMIGI | IEVVPNCKTI | FEIQHKAGLV |
| 970 | 980 | 990 | 1000 | 1010 | 1020 |
| NTAARSVDSN | FMNKWIRKQC | GFVDEKKKYK | KGGGPTVDSA | QATKKYFESV | DRFLYSCVGY |
| 1030 | 1040 | 1050 | 1060 | 1070 | 1080 |
| SVATYIMGIK | DRHSDNLMLT | EDGKYFHIDF | GHILGHGKTK | LGIQRDRQPF | ILTEQFLTII |
| 1090 | 1100 | 1110 | 1120 | 1130 | 1140 |
| RSGKPVDGNS | HEIQKFKTLC | LEAYEVMWNN | LKYKFQKTLC | CKGETKEKAR | KFFAGVYEEA |
| 1150 | |||||
| FNGSWSTKTN | WLFHAMKHY |