UniProtKB - P52480 (KPYM_MOUSE)
Pyruvate kinase PKM
Pkm
Functioni
Miscellaneous
Catalytic activityi
- EC:2.7.1.40By similarity
Cofactori
Protein has several cofactor binding sites:Activity regulationi
: glycolysis Pathwayi
This protein is involved in step 5 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.Proteins known to be involved in the 5 steps of the subpathway in this organism are:
- Glyceraldehyde-3-phosphate dehydrogenase (Gapdh), Glyceraldehyde-3-phosphate dehydrogenase (Gapdh), Glyceraldehyde-3-phosphate dehydrogenase (Gapdh), Glyceraldehyde-3-phosphate dehydrogenase (Gapdh), Glyceraldehyde-3-phosphate dehydrogenase (Gapdhs), Glyceraldehyde-3-phosphate dehydrogenase (Gapdhs), Glyceraldehyde-3-phosphate dehydrogenase (Gm10358), Glyceraldehyde-3-phosphate dehydrogenase (Gm3839), Glyceraldehyde-3-phosphate dehydrogenase, testis-specific (Gapdhs)
- Phosphoglycerate kinase 1 (Pgk1), Phosphoglycerate kinase (Pgk1), Phosphoglycerate kinase (Pgk1), Phosphoglycerate kinase 2 (Pgk2)
- no protein annotated in this organism
- 2-phospho-D-glycerate hydro-lyase (Eno2), 2-phospho-D-glycerate hydro-lyase, 2-phospho-D-glycerate hydro-lyase (Eno3), 2-phospho-D-glycerate hydro-lyase (Eno4), 2-phospho-D-glycerate hydro-lyase (Eno2), 2-phospho-D-glycerate hydro-lyase (Eno4), 2-phospho-D-glycerate hydro-lyase (Eno2), 2-phospho-D-glycerate hydro-lyase (Eno1), 2-phospho-D-glycerate hydro-lyase (EG433182), 2-phospho-D-glycerate hydro-lyase (Eno2), 2-phospho-D-glycerate hydro-lyase (Eno4), Gamma-enolase (Eno2), 2-phospho-D-glycerate hydro-lyase (Eno3), Alpha-enolase (Eno1), Beta-enolase (Eno3), 2-phospho-D-glycerate hydro-lyase (Eno2), 2-phospho-D-glycerate hydro-lyase (Eno2), 2-phospho-D-glycerate hydro-lyase (Eno3), 2-phospho-D-glycerate hydro-lyase (Eno1), Enolase 4 (Eno4)
- Pyruvate kinase (Pkm), Pyruvate kinase (Pkm), Pyruvate kinase (Pkm), Pyruvate kinase (Pklr), Pyruvate kinase (Pkm), Pyruvate kinase (Pklr), Pyruvate kinase (Pkm), Pyruvate kinase PKLR (Pklr), Pyruvate kinase (Pkm), Pyruvate kinase (Pklr), Pyruvate kinase (Pklr), Pyruvate kinase (Pklr), Pyruvate kinase (Pklr), Pyruvate kinase PKM (Pkm)
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 70 | SerineBy similarity | 1 | |
Binding sitei | 73 | SubstrateBy similarity | 1 | |
Metal bindingi | 75 | PotassiumBy similarity | 1 | |
Metal bindingi | 77 | PotassiumBy similarity | 1 | |
Binding sitei | 106 | SerineBy similarity | 1 | |
Metal bindingi | 113 | PotassiumBy similarity | 1 | |
Metal bindingi | 114 | Potassium; via carbonyl oxygenBy similarity | 1 | |
Binding sitei | 120 | ATPBy similarity | 1 | |
Binding sitei | 207 | ATPBy similarity | 1 | |
Binding sitei | 270 | Substrate; via amide nitrogenBy similarity | 1 | |
Sitei | 270 | Transition state stabilizerBy similarity | 1 | |
Metal bindingi | 272 | MagnesiumBy similarity | 1 | |
Binding sitei | 295 | Substrate; via amide nitrogenBy similarity | 1 | |
Metal bindingi | 296 | MagnesiumBy similarity | 1 | |
Binding sitei | 296 | Substrate; via amide nitrogenBy similarity | 1 | |
Binding sitei | 328 | SubstrateBy similarity | 1 | |
Sitei | 433 | Crucial for phosphotyrosine bindingBy similarity | 1 | |
Binding sitei | 464 | SerineBy similarity | 1 | |
Binding sitei | 482 | D-fructose 1,6-bisphosphate; part of allosteric siteBy similarity | 1 | |
Binding sitei | 489 | D-fructose 1,6-bisphosphate; part of allosteric siteBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 75 – 78 | ATPBy similarity | 4 |
GO - Molecular functioni
- ADP binding Source: MGI
- ATP binding Source: UniProtKB-KW
- identical protein binding Source: MGI
- kinase activity Source: UniProtKB-KW
- magnesium ion binding Source: InterPro
- mRNA binding Source: UniProtKB
- potassium ion binding Source: InterPro
- pyruvate kinase activity Source: MGI
- thyroid hormone binding Source: MGI
GO - Biological processi
- animal organ regeneration Source: MGI
- ATP biosynthetic process Source: MGI
- cellular response to insulin stimulus Source: GO_Central
- glucose metabolic process Source: MGI
- glycolytic process Source: MGI
- liver development Source: MGI
- positive regulation of cytoplasmic translation Source: UniProtKB
- positive regulation of sprouting angiogenesis Source: UniProtKB
- programmed cell death Source: MGI
- pyruvate biosynthetic process Source: MGI
- skeletal muscle tissue regeneration Source: MGI
Keywordsi
Molecular function | Allosteric enzyme, Kinase, Transferase |
Biological process | Glycolysis, Translation regulation |
Ligand | ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium, Pyruvate |
Enzyme and pathway databases
Reactomei | R-MMU-6798695, Neutrophil degranulation R-MMU-70171, Glycolysis |
SABIO-RKi | P52480 |
UniPathwayi | UPA00109;UER00188 |
Names & Taxonomyi
Protein namesi | Recommended name: Pyruvate kinase PKM (EC:2.7.1.40By similarity)Alternative name(s): Pyruvate kinase muscle isozyme |
Gene namesi | Name:Pkm Synonyms:Pk3, Pkm2, Pykm |
Organismi | Mus musculus (Mouse) |
Taxonomic identifieri | 10090 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:97591, Pkm |
Subcellular locationi
Nucleus
- Nucleus By similarity
Cytoplasm and Cytosol
- Cytoplasm By similarity
Note: Translocates to the nucleus in response to different apoptotic stimuli. Nuclear translocation is sufficient to induce cell death that is caspase independent, isoform-specific and independent of its enzymatic activity.By similarity
Cytosol
- cytosol Source: MGI
Endoplasmic reticulum
- rough endoplasmic reticulum Source: UniProtKB
Mitochondrion
- mitochondrion Source: MGI
Nucleus
- nucleus Source: MGI
Other locations
- cilium Source: MGI
- collagen-containing extracellular matrix Source: UniProtKB
- cytoplasm Source: MGI
- myelin sheath Source: UniProtKB
- photoreceptor inner segment Source: MGI
- pyruvate kinase complex Source: MGI
Keywords - Cellular componenti
Cytoplasm, NucleusPathology & Biotechi
Disruption phenotypei
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 367 | K → M: Abolishes pyruvate kinase activity without affecting interaction with the ribosome. 1 Publication | 1 | |
Mutagenesisi | 464 | H → A: Abolishes amino-acid binding without affecting interaction with the translating ribosome. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000112089 | 1 – 531 | Pyruvate kinase PKMAdd BLAST | 531 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 3 | N6,N6,N6-trimethyllysineBy similarity | 1 | |
Modified residuei | 37 | PhosphoserineBy similarity | 1 | |
Modified residuei | 41 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 62 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 66 | N6-succinyllysineCombined sources | 1 | |
Modified residuei | 89 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 97 | PhosphoserineBy similarity | 1 | |
Modified residuei | 100 | PhosphoserineBy similarity | 1 | |
Modified residuei | 105 | PhosphotyrosineCombined sources | 1 | |
Cross-linki | 115 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity | ||
Modified residuei | 127 | PhosphoserineBy similarity | 1 | |
Modified residuei | 148 | PhosphotyrosineCombined sources | 1 | |
Modified residuei | 166 | N6-acetyllysine; alternateCombined sources | 1 | |
Modified residuei | 166 | N6-succinyllysine; alternateCombined sources | 1 | |
Cross-linki | 166 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity | ||
Modified residuei | 175 | PhosphotyrosineBy similarity | 1 | |
Modified residuei | 195 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 266 | N6-acetyllysine; alternateBy similarity | 1 | |
Cross-linki | 266 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity | ||
Modified residuei | 270 | N6-acetyllysine; alternateCombined sources | 1 | |
Cross-linki | 270 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity | ||
Modified residuei | 305 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 322 | N6-acetyllysine; alternateCombined sources | 1 | |
Modified residuei | 322 | N6-succinyllysine; alternateCombined sources | 1 | |
Modified residuei | 403 | 4-hydroxyprolineBy similarity | 1 | |
Modified residuei | 408 | 4-hydroxyprolineBy similarity | 1 | |
Modified residuei | 433 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 475 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 498 | N6-succinyllysineCombined sources | 1 |
Post-translational modificationi
Keywords - PTMi
Acetylation, Hydroxylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugationProteomic databases
CPTACi | non-CPTAC-3588 non-CPTAC-3654 |
EPDi | P52480 |
jPOSTi | P52480 |
MaxQBi | P52480 |
PaxDbi | P52480 |
PeptideAtlasi | P52480 |
PRIDEi | P52480 |
ProteomicsDBi | 263452 [P52480-1] 263453 [P52480-2] |
2D gel databases
REPRODUCTION-2DPAGEi | IPI00407130 P52480 |
SWISS-2DPAGEi | P52480 |
PTM databases
iPTMneti | P52480 |
PhosphoSitePlusi | P52480 |
SwissPalmi | P52480 |
Expressioni
Tissue specificityi
Gene expression databases
Bgeei | ENSMUSG00000032294, Expressed in retinal neural layer and 116 other tissues |
ExpressionAtlasi | P52480, baseline and differential |
Genevisiblei | P52480, MM |
Interactioni
Subunit structurei
Monomer and homotetramer. Exists as a monomer in the absence of fructose 1,6 bi-phosphate (FBP), and reversibly associates to form a homotetramer in the presence of FBP. The monomeric form binds T3. Tetramer formation induces pyruvate kinase activity. FBP stimulates the formation of tetramers from dimers.
Interacts with HERC1, POU5F1 and PML.
Interacts (isoform M2) with EGLN3; the interaction hydroxylates PKM under hypoxia and enhances binding to HIF1A.
Interacts (isoform M2) with HIF1A; the interaction is enhanced by binding of EGLN3, promoting enhanced transcription activity under hypoxia (By similarity).
Interacts (isoform M2, but not isoform M1) with TRIM35; this interaction prevents FGFR1-dependent tyrosine phosphorylation (By similarity).
Interacts with JMJD8 (By similarity).
By similarityBinary interactionsi
Hide detailsP52480
GO - Molecular functioni
- identical protein binding Source: MGI
Protein-protein interaction databases
BioGRIDi | 202191, 54 interactors |
ComplexPortali | CPX-3059, PKM2 pyruvate kinase complex (tetramer) [P52480-1] CPX-3060, PKM2 pyruvate kinase complex (dimer) [P52480-1] CPX-3096, PKM1 pyruvate kinase complex [P52480-2] |
DIPi | DIP-40536N |
IntActi | P52480, 33 interactors |
MINTi | P52480 |
STRINGi | 10090.ENSMUSP00000034834 |
Miscellaneous databases
RNActi | P52480, protein |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 307 – 531 | Interaction with POU5F1By similarityAdd BLAST | 225 | |
Regioni | 389 – 433 | Intersubunit contactAdd BLAST | 45 | |
Regioni | 432 – 437 | D-fructose 1,6-bisphosphate binding; part of allosteric siteBy similarity | 6 | |
Regioni | 516 – 521 | D-fructose 1,6-bisphosphate binding; part of allosteric siteBy similarity | 6 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG2323, Eukaryota |
GeneTreei | ENSGT00390000008859 |
HOGENOMi | CLU_015439_0_1_1 |
InParanoidi | P52480 |
OMAi | QVPIVQK |
OrthoDBi | 933620at2759 |
PhylomeDBi | P52480 |
TreeFami | TF300390 |
Family and domain databases
CDDi | cd00288, Pyruvate_Kinase, 1 hit |
Gene3Di | 2.40.33.10, 1 hit 3.20.20.60, 1 hit 3.40.1380.20, 1 hit |
InterProi | View protein in InterPro IPR001697, Pyr_Knase IPR015813, Pyrv/PenolPyrv_Kinase-like_dom IPR040442, Pyrv_Kinase-like_dom_sf IPR011037, Pyrv_Knase-like_insert_dom_sf IPR018209, Pyrv_Knase_AS IPR015793, Pyrv_Knase_brl IPR015795, Pyrv_Knase_C IPR036918, Pyrv_Knase_C_sf IPR015806, Pyrv_Knase_insert_dom_sf |
PANTHERi | PTHR11817, PTHR11817, 1 hit |
Pfami | View protein in Pfam PF00224, PK, 1 hit PF02887, PK_C, 1 hit |
PRINTSi | PR01050, PYRUVTKNASE |
SUPFAMi | SSF50800, SSF50800, 1 hit SSF51621, SSF51621, 1 hit SSF52935, SSF52935, 1 hit |
TIGRFAMsi | TIGR01064, pyruv_kin, 1 hit |
PROSITEi | View protein in PROSITE PS00110, PYRUVATE_KINASE, 1 hit |
s (2+)i Sequence
Sequence statusi: Complete.
This entry describes 2 produced by isoformsialternative splicing. AlignAdd to basketThis entry has 2 described isoforms and 7 potential isoforms that are computationally mapped.Show allAlign All
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MPKPHSEAGT AFIQTQQLHA AMADTFLEHM CRLDIDSAPI TARNTGIICT
60 70 80 90 100
IGPASRSVEM LKEMIKSGMN VARLNFSHGT HEYHAETIKN VREATESFAS
110 120 130 140 150
DPILYRPVAV ALDTKGPEIR TGLIKGSGTA EVELKKGATL KITLDNAYME
160 170 180 190 200
KCDENILWLD YKNICKVVEV GSKIYVDDGL ISLQVKEKGA DFLVTEVENG
210 220 230 240 250
GSLGSKKGVN LPGAAVDLPA VSEKDIQDLK FGVEQDVDMV FASFIRKAAD
260 270 280 290 300
VHEVRKVLGE KGKNIKIISK IENHEGVRRF DEILEASDGI MVARGDLGIE
310 320 330 340 350
IPAEKVFLAQ KMMIGRCNRA GKPVICATQM LESMIKKPRP TRAEGSDVAN
360 370 380 390 400
AVLDGADCIM LSGETAKGDY PLEAVRMQHL IAREAEAAIY HLQLFEELRR
410 420 430 440 450
LAPITSDPTE AAAVGAVEAS FKCCSGAIIV LTKSGRSAHQ VARYRPRAPI
460 470 480 490 500
IAVTRNPQTA RQAHLYRGIF PVLCKDAVLN AWAEDVDLRV NLAMDVGKAR
510 520 530
GFFKKGDVVI VLTGWRPGSG FTNTMRVVPV P
The sequence of this isoform differs from the canonical sequence as follows:
389-433: IYHLQLFEEL...CSGAIIVLTK → MFHRLLFEEL...LAAALIVLTE
Computationally mapped potential isoform sequencesi
There are 7 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketA0A1L1SQV8 | A0A1L1SQV8_MOUSE | Pyruvate kinase | Pkm | 187 | Annotation score: | ||
A0A1L1SSN6 | A0A1L1SSN6_MOUSE | Pyruvate kinase | Pkm | 176 | Annotation score: | ||
A0A1L1ST52 | A0A1L1ST52_MOUSE | Pyruvate kinase | Pkm | 102 | Annotation score: | ||
A0A1L1STV8 | A0A1L1STV8_MOUSE | Pyruvate kinase | Pkm | 184 | Annotation score: | ||
A0A1L1SU37 | A0A1L1SU37_MOUSE | Pyruvate kinase | Pkm | 232 | Annotation score: | ||
A0A1L1SUV0 | A0A1L1SUV0_MOUSE | Pyruvate kinase | Pkm | 155 | Annotation score: | ||
A0A1L1SVH2 | A0A1L1SVH2_MOUSE | Pyruvate kinase PKM | Pkm | 51 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 8 | A → V in CAA65761 (PubMed:9545585).Curated | 1 | |
Sequence conflicti | 121 | T → A in BAE30642 (PubMed:16141072).Curated | 1 | |
Sequence conflicti | 121 | T → A in BAE32031 (PubMed:16141072).Curated | 1 | |
Sequence conflicti | 158 | W → R in BAA07457 (PubMed:7612666).Curated | 1 | |
Sequence conflicti | 166 | K → E in BAE42098 (PubMed:16141072).Curated | 1 | |
Sequence conflicti | 170 | V → L in BAE30642 (PubMed:16141072).Curated | 1 | |
Sequence conflicti | 170 | V → L in BAE32031 (PubMed:16141072).Curated | 1 | |
Sequence conflicti | 177 | D → G in BAE42199 (PubMed:16141072).Curated | 1 | |
Sequence conflicti | 230 | K → R in BAE30642 (PubMed:16141072).Curated | 1 | |
Sequence conflicti | 230 | K → R in BAE32031 (PubMed:16141072).Curated | 1 | |
Sequence conflicti | 299 | I → T in BAA07457 (PubMed:7612666).Curated | 1 | |
Sequence conflicti | 309 | A → S in BAA07457 (PubMed:7612666).Curated | 1 | |
Sequence conflicti | 327 | A → S in BAA07457 (PubMed:7612666).Curated | 1 | |
Sequence conflicti | 327 | A → S in CAA65761 (PubMed:9545585).Curated | 1 | |
Sequence conflicti | 333 | S → I in BAA07457 (PubMed:7612666).Curated | 1 | |
Sequence conflicti | 333 | S → I in CAA65761 (PubMed:9545585).Curated | 1 | |
Sequence conflicti | 485 | D → N in BAE33055 (PubMed:16141072).Curated | 1 | |
Sequence conflicti | 485 | D → N in BAE42192 (PubMed:16141072).Curated | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_025057 | 389 – 433 | IYHLQ…IVLTK → MFHRLLFEELVRASSHSTDL MEAMAMGSVEASYKCLAAAL IVLTE in isoform M1. 1 PublicationAdd BLAST | 45 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D38379 mRNA Translation: BAA07457.1 X97047 mRNA Translation: CAA65761.1 AK002341 mRNA Translation: BAB22025.1 AK135397 mRNA Translation: BAE22519.1 AK151724 mRNA Translation: BAE30642.1 AK153483 mRNA Translation: BAE32031.1 AK155110 mRNA Translation: BAE33055.1 AK155655 mRNA Translation: BAE33370.1 AK170892 mRNA Translation: BAE42098.1 AK168943 mRNA Translation: BAE40751.1 AK171023 mRNA Translation: BAE42192.1 AK171033 mRNA Translation: BAE42199.1 AC160637 Genomic DNA No translation available. BC016619 mRNA Translation: AAH16619.1 BC094663 mRNA Translation: AAH94663.1 |
CCDSi | CCDS40659.1 [P52480-1] CCDS57681.1 [P52480-2] |
PIRi | S55921 |
RefSeqi | NP_001240812.1, NM_001253883.1 [P52480-2] NP_035229.2, NM_011099.3 [P52480-1] XP_006510918.1, XM_006510855.1 [P52480-1] XP_011240975.1, XM_011242673.1 |
Genome annotation databases
Ensembli | ENSMUST00000034834; ENSMUSP00000034834; ENSMUSG00000032294 [P52480-1] ENSMUST00000163694; ENSMUSP00000128770; ENSMUSG00000032294 [P52480-2] |
GeneIDi | 18746 |
KEGGi | mmu:18746 |
UCSCi | uc009pyf.2, mouse [P52480-1] uc009pyh.2, mouse [P52480-2] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D38379 mRNA Translation: BAA07457.1 X97047 mRNA Translation: CAA65761.1 AK002341 mRNA Translation: BAB22025.1 AK135397 mRNA Translation: BAE22519.1 AK151724 mRNA Translation: BAE30642.1 AK153483 mRNA Translation: BAE32031.1 AK155110 mRNA Translation: BAE33055.1 AK155655 mRNA Translation: BAE33370.1 AK170892 mRNA Translation: BAE42098.1 AK168943 mRNA Translation: BAE40751.1 AK171023 mRNA Translation: BAE42192.1 AK171033 mRNA Translation: BAE42199.1 AC160637 Genomic DNA No translation available. BC016619 mRNA Translation: AAH16619.1 BC094663 mRNA Translation: AAH94663.1 |
CCDSi | CCDS40659.1 [P52480-1] CCDS57681.1 [P52480-2] |
PIRi | S55921 |
RefSeqi | NP_001240812.1, NM_001253883.1 [P52480-2] NP_035229.2, NM_011099.3 [P52480-1] XP_006510918.1, XM_006510855.1 [P52480-1] XP_011240975.1, XM_011242673.1 |
3D structure databases
SMRi | P52480 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 202191, 54 interactors |
ComplexPortali | CPX-3059, PKM2 pyruvate kinase complex (tetramer) [P52480-1] CPX-3060, PKM2 pyruvate kinase complex (dimer) [P52480-1] CPX-3096, PKM1 pyruvate kinase complex [P52480-2] |
DIPi | DIP-40536N |
IntActi | P52480, 33 interactors |
MINTi | P52480 |
STRINGi | 10090.ENSMUSP00000034834 |
PTM databases
iPTMneti | P52480 |
PhosphoSitePlusi | P52480 |
SwissPalmi | P52480 |
2D gel databases
REPRODUCTION-2DPAGEi | IPI00407130 P52480 |
SWISS-2DPAGEi | P52480 |
Proteomic databases
CPTACi | non-CPTAC-3588 non-CPTAC-3654 |
EPDi | P52480 |
jPOSTi | P52480 |
MaxQBi | P52480 |
PaxDbi | P52480 |
PeptideAtlasi | P52480 |
PRIDEi | P52480 |
ProteomicsDBi | 263452 [P52480-1] 263453 [P52480-2] |
Protocols and materials databases
Antibodypediai | 14162, 1177 antibodies |
Genome annotation databases
Ensembli | ENSMUST00000034834; ENSMUSP00000034834; ENSMUSG00000032294 [P52480-1] ENSMUST00000163694; ENSMUSP00000128770; ENSMUSG00000032294 [P52480-2] |
GeneIDi | 18746 |
KEGGi | mmu:18746 |
UCSCi | uc009pyf.2, mouse [P52480-1] uc009pyh.2, mouse [P52480-2] |
Organism-specific databases
CTDi | 5315 |
MGIi | MGI:97591, Pkm |
Phylogenomic databases
eggNOGi | KOG2323, Eukaryota |
GeneTreei | ENSGT00390000008859 |
HOGENOMi | CLU_015439_0_1_1 |
InParanoidi | P52480 |
OMAi | QVPIVQK |
OrthoDBi | 933620at2759 |
PhylomeDBi | P52480 |
TreeFami | TF300390 |
Enzyme and pathway databases
UniPathwayi | UPA00109;UER00188 |
Reactomei | R-MMU-6798695, Neutrophil degranulation R-MMU-70171, Glycolysis |
SABIO-RKi | P52480 |
Miscellaneous databases
BioGRID-ORCSi | 18746, 23 hits in 52 CRISPR screens |
ChiTaRSi | Pkm, mouse |
PROi | PR:P52480 |
RNActi | P52480, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSMUSG00000032294, Expressed in retinal neural layer and 116 other tissues |
ExpressionAtlasi | P52480, baseline and differential |
Genevisiblei | P52480, MM |
Family and domain databases
CDDi | cd00288, Pyruvate_Kinase, 1 hit |
Gene3Di | 2.40.33.10, 1 hit 3.20.20.60, 1 hit 3.40.1380.20, 1 hit |
InterProi | View protein in InterPro IPR001697, Pyr_Knase IPR015813, Pyrv/PenolPyrv_Kinase-like_dom IPR040442, Pyrv_Kinase-like_dom_sf IPR011037, Pyrv_Knase-like_insert_dom_sf IPR018209, Pyrv_Knase_AS IPR015793, Pyrv_Knase_brl IPR015795, Pyrv_Knase_C IPR036918, Pyrv_Knase_C_sf IPR015806, Pyrv_Knase_insert_dom_sf |
PANTHERi | PTHR11817, PTHR11817, 1 hit |
Pfami | View protein in Pfam PF00224, PK, 1 hit PF02887, PK_C, 1 hit |
PRINTSi | PR01050, PYRUVTKNASE |
SUPFAMi | SSF50800, SSF50800, 1 hit SSF51621, SSF51621, 1 hit SSF52935, SSF52935, 1 hit |
TIGRFAMsi | TIGR01064, pyruv_kin, 1 hit |
PROSITEi | View protein in PROSITE PS00110, PYRUVATE_KINASE, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | KPYM_MOUSE | |
Accessioni | P52480Primary (citable) accession number: P52480 Secondary accession number(s): Q3TBV8 Q9CWB1 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 1, 1996 |
Last sequence update: | May 1, 2007 | |
Last modified: | April 7, 2021 | |
This is version 210 of the entry and version 4 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Direct protein sequencing, Reference proteomeDocuments
- MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot - PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families