P90980
Gene name |
pkc-2 (kin-11, E01H11.1) |
Protein name |
Protein kinase C-like 2 |
Names |
PKC2 , EC 2.7.11.13 |
Species |
Caenorhabditis elegans |
KEGG Pathway |
|
EC number |
2.7.11.13: Protein-serine/threonine kinases |
Protein Class |
|
Descriptions
Autoinhibitory domains (AIDs)
Target domain |
337-681 (Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha) |
Relief mechanism |
Ligand binding |
Assay |
|
Target domain |
337-681 (Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha) |
Relief mechanism |
Ligand binding |
Assay |
|
Target domain |
350-592 (Protein kinase domain) |
Relief mechanism |
Ligand binding |
Assay |
|
Target domain |
350-592 (Protein kinase domain) |
Relief mechanism |
Ligand binding |
Assay |
|
Accessory elements
489-512 (Activation loop from InterPro)
Target domain |
348-609 (Protein kinase domain) |
Relief mechanism |
|
Assay |
|
489-512 (Activation loop from InterPro)
Target domain |
348-609 (Protein kinase domain) |
Relief mechanism |
|
Assay |
|
References
- Yeon JH et al. (2016) "Systems-wide Identification of cis-Regulatory Elements in Proteins", Cell systems, 2, 89-100
- Steinberg SF (2008) "Structural basis of protein kinase C isoform function", Physiological reviews, 88, 1341-78
- Sommese RF et al. (2017) "The Role of Regulatory Domains in Maintaining Autoinhibition in the Multidomain Kinase PKCα", The Journal of biological chemistry, 292, 2873-2880
- Pears CJ et al. (1990) "Mutagenesis of the pseudosubstrate site of protein kinase C leads to activation", European journal of biochemistry, 194, 89-94
- Smith MK et al. (1990) "Specificities of autoinhibitory domain peptides for four protein kinases. Implications for intact cell studies of protein kinase function", The Journal of biological chemistry, 265, 1837-40
- Slater SJ et al. (2002) "Regulation of PKC alpha activity by C1-C2 domain interactions", The Journal of biological chemistry, 277, 15277-85
- Jones AC et al. (2020) "Hypothesis: Unifying model of domain architecture for conventional and novel protein kinase C isozymes", IUBMB life, 72, 2584-2590
- Kirwan AF et al. (2003) "Inhibition of protein kinase C catalytic activity by additional regions within the human protein kinase Calpha-regulatory domain lying outside of the pseudosubstrate sequence", The Biochemical journal, 373, 571-81
- Huang X et al. (2003) "Crystal structure of an inactive Akt2 kinase domain", Structure (London, England : 1993), 11, 21-30
- Truebestein L et al. (2021) "Structure of autoinhibited Akt1 reveals mechanism of PIP(3)-mediated activation", Proceedings of the National Academy of Sciences of the United States of America, 118,
- Lučić I et al. (2018) "Conformational sampling of membranes by Akt controls its activation and inactivation", Proceedings of the National Academy of Sciences of the United States of America, 115, E3940-E3949
- Wagner J et al. (2009) "Discovery of 3-(1H-indol-3-yl)-4-[2-(4-methylpiperazin-1-yl)quinazolin-4-yl]pyrrole-2,5-dione (AEB071), a potent and selective inhibitor of protein kinase C isotypes", Journal of medicinal chemistry, 52, 6193-6
Autoinhibited structure
Activated structure
1 structures for P90980
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P90980-F1 | Predicted | AlphaFoldDB |
No variants for P90980
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P90980 | |||||
No associated diseases with P90980
12 regional properties for P90980
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | C2 domain | 160 - 280 | IPR000008 |
| domain | Protein kinase domain | 348 - 609 | IPR000719 |
| domain | AGC-kinase, C-terminal | 610 - 681 | IPR000961 |
| domain | Protein kinase C-like, phorbol ester/diacylglycerol-binding domain | 38 - 89 | IPR002219-1 |
| domain | Protein kinase C-like, phorbol ester/diacylglycerol-binding domain | 103 - 155 | IPR002219-2 |
| active_site | Serine/threonine-protein kinase, active site | 468 - 480 | IPR008271 |
| binding_site | Protein kinase, ATP binding site | 354 - 377 | IPR017441 |
| domain | Protein kinase, C-terminal | 631 - 671 | IPR017892 |
| domain | Diacylglycerol/phorbol-ester binding | 36 - 50 | IPR020454-1 |
| domain | Diacylglycerol/phorbol-ester binding | 52 - 61 | IPR020454-2 |
| domain | Diacylglycerol/phorbol-ester binding | 65 - 76 | IPR020454-3 |
| domain | Diacylglycerol/phorbol-ester binding | 142 - 154 | IPR020454-4 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.7.11.13 | Protein-serine/threonine kinases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
4 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| membrane | A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. |
| neuron projection | A prolongation or process extending from a nerve cell, e.g. an axon or dendrite. |
| neuronal cell body | The portion of a neuron that includes the nucleus, but excludes cell projections such as axons and dendrites. |
6 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| calcium,diacylglycerol-dependent serine/threonine kinase activity | Calcium-dependent catalysis of the reaction |
| diacylglycerol-dependent serine/threonine kinase activity | Catalysis of the reaction |
| protein serine kinase activity | Catalysis of the reactions |
| protein serine/threonine kinase activity | Catalysis of the reactions |
| zinc ion binding | Binding to a zinc ion (Zn). |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| intracellular signal transduction | The process in which a signal is passed on to downstream components within the cell, which become activated themselves to further propagate the signal and finally trigger a change in the function or state of the cell. |
| 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. |
28 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P24583 | PKC1 | Protein kinase C-like 1 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | SS |
| P05126 | PRKCB | Protein kinase C beta type | Bos taurus (Bovine) | SS |
| P04409 | PRKCA | Protein kinase C alpha type | Bos taurus (Bovine) | EV SS |
| P05128 | PRKCG | Protein kinase C gamma type | Bos taurus (Bovine) | SS |
| P05130 | Pkc53E | Protein kinase C, brain isozyme | Drosophila melanogaster (Fruit fly) | SS |
| P13677 | inaC | Protein kinase C, eye isozyme | Drosophila melanogaster (Fruit fly) | SS |
| P05129 | PRKCG | Protein kinase C gamma type | Homo sapiens (Human) | SS |
| Q02156 | PRKCE | Protein kinase C epsilon type | Homo sapiens (Human) | SS |
| P24723 | PRKCH | Protein kinase C eta type | Homo sapiens (Human) | SS |
| P17252 | PRKCA | Protein kinase C alpha type | Homo sapiens (Human) | EV |
| P05771 | PRKCB | Protein kinase C beta type | Homo sapiens (Human) | SS |
| P63318 | Prkcg | Protein kinase C gamma type | Mus musculus (Mouse) | SS |
| P16054 | Prkce | Protein kinase C epsilon type | Mus musculus (Mouse) | PR |
| P68404 | Prkcb | Protein kinase C beta type | Mus musculus (Mouse) | SS |
| P23298 | Prkch | Protein kinase C eta type | Mus musculus (Mouse) | PR |
| P20444 | Prkca | Protein kinase C alpha type | Mus musculus (Mouse) | SS |
| Q64617 | Prkch | Protein kinase C eta type | Rattus norvegicus (Rat) | PR |
| P63319 | Prkcg | Protein kinase C gamma type | Rattus norvegicus (Rat) | SS |
| P05696 | Prkca | Protein kinase C alpha type | Rattus norvegicus (Rat) | SS |
| P68403 | Prkcb | Protein kinase C beta type | Rattus norvegicus (Rat) | SS |
| Q9Y1J3 | pdk-1 | 3-phosphoinositide-dependent protein kinase 1 | Caenorhabditis elegans | SS |
| Q19266 | pkc-3 | Protein kinase C-like 3 | Caenorhabditis elegans | SS |
| P34722 | tpa-1 | Protein kinase C-like 1 | Caenorhabditis elegans | PR |
| Q9XTG7 | akt-2 | Serine/threonine-protein kinase akt-2 | Caenorhabditis elegans | SS |
| Q17941 | akt-1 | Serine/threonine-protein kinase akt-1 | Caenorhabditis elegans | PR |
| Q2L6W9 | sax-1 | Serine/threonine-protein kinase sax-1 | Caenorhabditis elegans | SS |
| A8KBH6 | prkcb | Protein kinase C beta type | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) | SS |
| Q7SY24 | prkcbb | Protein kinase C beta type | Danio rerio (Zebrafish) (Brachydanio rerio) | SS |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSLSTNSSVK | EDEAQRIEGK | AFVRRGALRQ | KNVHEIKSHK | FIARFFKQPT | FCSHCKDFLW |
| 70 | 80 | 90 | 100 | 110 | 120 |
| GITKQGFQCQ | VCTLVVHKRC | HEFVNFACPG | ADKGVDTDDP | RQQHKWKVQT | YSSPTFCDHC |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GSLLYGILHQ | GMKCQSCDTN | VHHRCVKNVP | NMCGTDNTEK | RGRLRIEAHI | ENDQLTIKIL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| EAKNLIPMDP | NGLSDPYVKC | KLIPEDSGCK | SKQKTKTLRA | TLNPQWNETF | TYKLLPGDKD |
| 250 | 260 | 270 | 280 | 290 | 300 |
| RRLSIEVWDW | DRTSRNDFMG | SLSFGISELM | KEAASGWYKL | LSAEEGEFYN | INITPEYDED |
| 310 | 320 | 330 | 340 | 350 | 360 |
| MEKVRKKMNE | NFITRDNSSS | KPKDPAAPRA | STLPLGSSNH | NVIKASDFNF | LTVLGKGSFG |
| 370 | 380 | 390 | 400 | 410 | 420 |
| KVLLGEQKTT | KELFAIKVLK | KDVIIQDDDV | ECTMTEKRVL | ALPEKPSFLV | ALHSCFQTMD |
| 430 | 440 | 450 | 460 | 470 | 480 |
| RLYFVMEFVN | GGDLMYQIQQ | VGKFKEPVAV | FYAAEIAVGL | FFLHSKGIIY | RDLKLDNVML |
| 490 | 500 | 510 | 520 | 530 | 540 |
| ERDGHIKITD | FGMCKENIFG | DATTKTFCGT | PDYIAPEIIL | YQPYGKSVDW | WAYGVLLFEM |
| 550 | 560 | 570 | 580 | 590 | 600 |
| LAGQPPFDGE | DEDELFTAIT | EHNVSYPKSL | SKEAVSLCKA | LLIKNPSKRL | GCTGDDESAS |
| 610 | 620 | 630 | 640 | 650 | 660 |
| RDIKEHPFFR | RIDWFKIETR | QIQPPFKPKL | KTDRSTENFD | HSFLKLPTKM | TPPDWEVLEN |
| 670 | 680 | ||||
| LKGDEFSNFS | FVNPFYVKDV | EP |