P52489
Gene name |
PYK2 (YOR347C, O6342) |
Protein name |
Pyruvate kinase 2 |
Names |
PK 2 , EC 2.7.1.40 |
Species |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
KEGG Pathway |
sce:YOR347C |
EC number |
2.7.1.40: 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 |
22-347 (Pyruvate kinase) |
Relief mechanism |
PTM, Partner binding |
Assay |
|
Accessory elements
No accessory elements
References
- Yeon JH et al. (2016) "Systems-wide Identification of cis-Regulatory Elements in Proteins", Cell systems, 2, 89-100
- Zhang Z et al. (2019) "PKM2, function and expression and regulation", Cell & bioscience, 9, 52
- Zahra K et al. (2020) "Pyruvate Kinase M2 and Cancer: The Role of PKM2 in Promoting Tumorigenesis", Frontiers in oncology, 10, 159
Autoinhibited structure
Activated structure
1 structures for P52489
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P52489-F1 | Predicted | AlphaFoldDB |
10 variants for P52489
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| s15-986347 | 38 | A>V | No | SGRP | |
| s15-986335 | 42 | L>R | No | SGRP | |
| s15-986326 | 45 | A>V | No | SGRP | |
| s15-985888 | 191 | P>L | No | SGRP | |
| s15-985864 | 199 | K>R | No | SGRP | |
| s15-985357 | 368 | D>A | No | SGRP | |
| s15-985133 | 443 | P>A | No | SGRP | |
| s15-985028 | 478 | G>S | No | SGRP | |
| s15-984997 | 488 | K>R | No | SGRP | |
| s15-984989 | 491 | V>I | No | SGRP |
No associated diseases with P52489
5 regional properties for P52489
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | SAP domain | 2 - 36 | IPR003034-1 |
| domain | SAP domain | 69 - 103 | IPR003034-2 |
| domain | Poly(ADP-ribose) polymerase, regulatory domain | 286 - 418 | IPR004102 |
| domain | WGR domain | 158 - 255 | IPR008893 |
| domain | Poly(ADP-ribose) polymerase, catalytic domain | 412 - 637 | IPR012317 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.7.1.40 | Phosphotransferases with an alcohol group as acceptor |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| mitochondrion | A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. |
6 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| kinase activity | Catalysis of the transfer of a phosphate group, usually from ATP, to a substrate molecule. |
| magnesium ion binding | Binding to a magnesium (Mg) ion. |
| melatonin binding | Binding to melatonin. |
| potassium ion binding | Binding to a potassium ion (K+). |
| pyruvate kinase activity | Catalysis of the reaction |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| cellular response to insulin stimulus | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an insulin stimulus. Insulin is a polypeptide hormone produced by the islets of Langerhans of the pancreas in mammals, and by the homologous organs of other organisms. |
| glycolytic process | The chemical reactions and pathways resulting in the breakdown of a carbohydrate into pyruvate, with the concomitant production of a small amount of ATP and the reduction of NAD(P) to NAD(P)H. Glycolysis begins with the metabolism of a carbohydrate to generate products that can enter the pathway and ends with the production of pyruvate. Pyruvate may be converted to acetyl-coenzyme A, ethanol, lactate, or other small molecules. |
| 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. |
| pyruvate metabolic process | The chemical reactions and pathways involving pyruvate, 2-oxopropanoate. |
12 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P00549 | CDC19 | Pyruvate kinase 1 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | SS |
| P11979 | PKM | Pyruvate kinase PKM | Felis catus (Cat) (Felis silvestris catus) | SS |
| P00548 | PKM | Pyruvate kinase PKM | Gallus gallus (Chicken) | SS |
| Q29536 | PKLR | Pyruvate kinase PKLR | Canis lupus familiaris (Dog) (Canis familiaris) | SS |
| O62619 | PyK | Pyruvate kinase | Drosophila melanogaster (Fruit fly) | SS |
| P30613 | PKLR | Pyruvate kinase PKLR | Homo sapiens (Human) | SS |
| P14618 | PKM | Pyruvate kinase PKM | Homo sapiens (Human) | EV |
| P52480 | Pkm | Pyruvate kinase PKM | Mus musculus (Mouse) | SS |
| P53657 | Pklr | Pyruvate kinase PKLR | Mus musculus (Mouse) | SS |
| P12928 | Pklr | Pyruvate kinase PKLR | Rattus norvegicus (Rat) | SS |
| P11980 | Pkm | Pyruvate kinase PKM | Rattus norvegicus (Rat) | SS |
| Q9LIK0 | PKP1 | Plastidial pyruvate kinase 1, chloroplastic | Arabidopsis thaliana (Mouse-ear cress) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MPESRLQRLA | NLKIGTPQQL | RRTSIIGTIG | PKTNSCEAIT | ALRKAGLNII | RLNFSHGSYE |
| 70 | 80 | 90 | 100 | 110 | 120 |
| FHQSVIENAV | KSEQQFPGRP | LAIALDTKGP | EIRTGRTLND | QDLYIPVDHQ | MIFTTDASFA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| NTSNDKIMYI | DYANLTKVIV | PGRFIYVDDG | ILSFKVLQII | DESNLRVQAV | NSGYIASHKG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| VNLPNTDVDL | PPLSAKDMKD | LQFGVRNGIH | IVFASFIRTS | EDVLSIRKAL | GSEGQDIKII |
| 250 | 260 | 270 | 280 | 290 | 300 |
| SKIENQQGLD | NFDEILEVTD | GVMIARGDLG | IEILAPEVLA | IQKKLIAKCN | LAGKPVICAT |
| 310 | 320 | 330 | 340 | 350 | 360 |
| QMLDSMTHNP | RPTRAEVSDV | GNAVLDGADC | VMLSGETAKG | DYPVNAVNIM | AATALIAEST |
| 370 | 380 | 390 | 400 | 410 | 420 |
| IAHLALYDDL | RDATPKPTST | TETVAAAATA | AILEQDGKAI | VVLSTTGNTA | RLLSKYRPSC |
| 430 | 440 | 450 | 460 | 470 | 480 |
| PIILVTRHAR | TARIAHLYRG | VFPFLYEPKR | LDDWGEDVHR | RLKFGVEMAR | SFGMVDNGDT |
| 490 | 500 | ||||
| VVSIQGFKGG | VGHSNTLRIS | TVGQEF |