P00518
Gene name |
PHKG1 (PHKG) |
Protein name |
Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoform |
Names |
Phosphorylase kinase subunit gamma-1, Serine/threonine-protein kinase PHKG1 |
Species |
Oryctolagus cuniculus (Rabbit) |
KEGG Pathway |
ocu:100009297 |
EC number |
2.7.11.1: Protein-serine/threonine kinases |
Protein Class |
|
Descriptions
(Annotation from UniProt)
The two calmodulin-binding domains appear to act in concert to bind a single molecule of calmodulin and are pseudosubstrate/autoinhibitory domains.
Autoinhibitory domains (AIDs)
Target domain |
20-288 (Protein kinase domain) |
Relief mechanism |
|
Assay |
|
Target domain |
20-288 (Protein kinase domain) |
Relief mechanism |
|
Assay |
|
Accessory elements
167-189 (Activation loop from InterPro)
Target domain |
20-288 (Protein kinase domain) |
Relief mechanism |
|
Assay |
|
References
Autoinhibited structure
Activated structure
4 structures for P00518
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 1PHK | X-ray | 220 A | A | 2-299 | PDB |
| 1QL6 | X-ray | 240 A | A | 2-299 | PDB |
| 2PHK | X-ray | 260 A | A | 15-291 | PDB |
| AF-P00518-F1 | Predicted | AlphaFoldDB |
No variants for P00518
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P00518 | |||||
No associated diseases with P00518
Functions
| Description | ||
|---|---|---|
| EC Number | 2.7.11.1 | Protein-serine/threonine kinases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| phosphorylase kinase complex | An enzyme complex that catalyzes the phosphorylation of phosphorylase b to form phosphorylase a. |
| skeletal muscle myofibril | A myofibril of a skeletal muscle fiber. |
6 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| calmodulin binding | Binding to calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states. |
| phosphorylase kinase activity | Catalysis of the reaction: 4 ATP + 2 phosphorylase b = 4 ADP + phosphorylase a. |
| protein serine kinase activity | Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate. |
| protein serine/threonine/tyrosine kinase activity | Catalysis of the reactions: ATP + a protein serine = ADP + protein serine phosphate; ATP + a protein threonine = ADP + protein threonine phosphate; and ATP + a protein tyrosine = ADP + protein tyrosine phosphate. |
| tau-protein kinase activity | Catalysis of the reaction: ATP + tau-protein = ADP + O-phospho-tau-protein. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| glycogen biosynthetic process | The chemical reactions and pathways resulting in the formation of glycogen, a polydisperse, highly branched glucan composed of chains of D-glucose residues. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTRDAALPGS | HSTHGFYENY | EPKEILGRGV | SSVVRRCIHK | PTCKEYAVKI | IDVTGGGSFS |
| 70 | 80 | 90 | 100 | 110 | 120 |
| AEEVQELREA | TLKEVDILRK | VSGHPNIIQL | KDTYETNTFF | FLVFDLMKKG | ELFDYLTEKV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| TLSEKETRKI | MRALLEVICA | LHKLNIVHRD | LKPENILLDD | DMNIKLTDFG | FSCQLDPGEK |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LREVCGTPSY | LAPEIIECSM | NDNHPGYGKE | VDMWSTGVIM | YTLLAGSPPF | WHRKQMLMLR |
| 250 | 260 | 270 | 280 | 290 | 300 |
| MIMSGNYQFG | SPEWDDYSDT | VKDLVSRFLV | VQPQKRYTAE | EALAHPFFQQ | YVVEEVRHFS |
| 310 | 320 | 330 | 340 | 350 | 360 |
| PRGKFKVICL | TVLASVRIYY | QYRRVKPVTR | EIVIRDPYAL | RPLRRLIDAY | AFRIYGHWVK |
| 370 | 380 | ||||
| KGQQQNRAAL | FENTPKAVLF | SLAEDDY |