Pkm

Functionⁱ

Glycolytic enzyme that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. Stimulates POU5F1-mediated transcriptional activation (By similarity).By similarity

Miscellaneous

There are 4 isozymes of pyruvate kinase in mammals (L, R, M1, M2) encoded by 2 different genes: PKLR and PKM. The L and R isozymes are generated from the PKLR by differential splicing of RNA; the M1 and M2 forms are produced from the PKM gene by differential splicing. L type is major isozyme in the liver, R is found in red cells, M1 is the main form in muscle, heart and brain, and M2 is found in early fetal tissues as well as in most cancer cells.

Catalytic activityⁱ

ATP + pyruvate = ADP + phosphoenolpyruvate.

Cofactorⁱ

Protein has several cofactor binding sites:

Activity regulationⁱ

Allosterically activated by D-fructose 1,6-bisphosphate (FBP). Inhibited by oxalate and 3,3',5-triiodo-L-thyronine (T3). The activity of the tetrameric form is inhibited by PML. Selective binding to tyrosine-phosphorylated peptides releases the allosteric activator FBP, leading to inhibition of PKM enzymatic activity, this diverts glucose metabolites from energy production to anabolic processes when cells are stimulated by certain growth factors. Glycolytic flux are highly dependent on de novo biosynthesis of serine and glycine, and serine is a natural ligand and allosteric activator (By similarity).By similarity

Pathwayⁱ: glycolysis

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: This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
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	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
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
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

GO - Molecular functionⁱ

ADP binding
Source: RGD
Inferred from direct assayⁱ
- 7040662
ATP binding Source: UniProtKB-KW
identical protein binding
Source: CAFA
Inferred from direct assayⁱ
- 1883388
kinase activity Source: UniProtKB-KW
magnesium ion binding Source: InterPro
potassium ion binding Source: InterPro
pyruvate kinase activity
Source: CAFA
Inferred from direct assayⁱ
- 1883388
thyroid hormone binding
Source: CAFA
Inferred from direct assayⁱ
- 1883388

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

animal organ regeneration
Source: RGD
Inferred from direct assayⁱ
- 4005043
ATP biosynthetic process
Source: RGD
Inferred from direct assayⁱ
- 4273555
cellular response to insulin stimulus
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
glucose metabolic process
Source: RGD
Inferred from direct assayⁱ
- 7929251
glycolytic process
Source: CAFA
Inferred from direct assayⁱ
- 1883388
liver development
Source: RGD
Inferred from direct assayⁱ
- 7327170
positive regulation of sprouting angiogenesis Source: UniProtKB
programmed cell death Source: Ensembl
protein homotetramerization
Source: CAFA
Inferred from direct assayⁱ
- 1883388
pyruvate biosynthetic process
Source: RGD
Inferred from direct assayⁱ
- 4273555
response to gravity
Source: RGD
Inferred from expression patternⁱ
- 12165359
response to hypoxia
Source: RGD
Inferred from expression patternⁱ
- 3696161
response to insulin
Source: RGD
Inferred from expression patternⁱ
- 7929251
response to muscle inactivity
Source: RGD
Inferred from expression patternⁱ
- 6331066
response to nutrient
Source: RGD
Inferred from expression patternⁱ
- 7929251
response to organic substance
Source: RGD
Inferred from expression patternⁱ
- 6537126
skeletal muscle tissue regeneration
Source: RGD
Inferred from direct assayⁱ
- 145474

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Allosteric enzyme, Kinase, Transferase
Biological process	Glycolysis
Ligand	ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium, Pyruvate

Enzyme and pathway databases

Reactomeⁱ	R-RNO-6798695 Neutrophil degranulation R-RNO-70171 Glycolysis
SABIO-RKⁱ	P11980
UniPathwayⁱ	UPA00109;UER00188

Protein family/group databases

MoonProtⁱ	P11980

MoonProtⁱ

P11980

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Pyruvate kinase PKM (EC:2.7.1.40) Alternative name(s): Pyruvate kinase muscle isozyme
Gene namesⁱ	Name:Pkm Synonyms:Pkm2, Pykm
Organismⁱ	Rattus norvegicus (Rat)
Taxonomic identifierⁱ	10116 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
Proteomesⁱ	UP000002494 Componentⁱ: Chromosome 8

Organism-specific databases

Rat genome database More...RGDⁱ	3337 Pkm

RGDⁱ

3337 Pkm

Keywords - Cellular componentⁱ

Cytoplasm, Nucleus

Pathology & Biotechⁱ

Chemistry databases

ChEMBLⁱ	CHEMBL4994

ChEMBLⁱ

CHEMBL4994

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000112092	1 – 531	Pyruvate kinase PKMAdd BLAST		531

Amino acid modifications

Feature key	Position(s)	DescriptionActions	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-acetyllysineBy similarity	1
Modified residueⁱ	66	N6-succinyllysineBy similarity	1
Modified residueⁱ	89	N6-acetyllysineBy similarity	1
Modified residueⁱ	97	PhosphoserineCombined sources	1
Modified residueⁱ	100	PhosphoserineCombined sources	1
Modified residueⁱ	105	PhosphotyrosineBy similarity	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	PhosphotyrosineBy similarity	1
Modified residueⁱ	166	N6-acetyllysine; alternateBy similarity	1
Modified residueⁱ	166	N6-succinyllysine; alternateBy similarity	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; alternateBy similarity	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; alternateBy similarity	1
Modified residueⁱ	322	N6-succinyllysine; alternateBy similarity	1
Modified residueⁱ	408	4-hydroxyprolineBy similarity	1
Modified residueⁱ	475	N6-acetyllysineBy similarity	1
Modified residueⁱ	498	N6-succinyllysineBy similarity	1

Post-translational modificationⁱ

ISGylated.By similarity

Under hypoxia, hydroxylated by EGLN3.By similarity

Acetylation at Lys-305 is stimulated by high glucose concentration, it decreases enzyme activity and promotes its lysosomal-dependent degradation via chaperone-mediated autophagy.By similarity

Keywords - PTMⁱ

Acetylation, Hydroxylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbⁱ	P11980
PRIDEⁱ	P11980

2D gel databases

The World-2DPAGE database More...World-2DPAGEⁱ	0004:P11980

World-2DPAGEⁱ

0004:P11980

PTM databases

iPTMnetⁱ	P11980
PhosphoSitePlusⁱ	P11980

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSRNOG00000011329 Expressed in 9 organ(s), highest expression level in skeletal muscle tissue
ExpressionAtlasⁱ	P11980 baseline and differential
Genevisibleⁱ	P11980 RN

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 similarity

GO - Molecular functionⁱ

identical protein binding
Source: CAFA
Inferred from direct assayⁱ
- 1883388

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	247659, 3 interactors
CORUMⁱ	P11980
IntActⁱ	P11980, 4 interactors
STRINGⁱ	10116.ENSRNOP00000015331

Chemistry databases

BindingDBⁱ

P11980

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	P11980
SMRⁱ	P11980
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	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	514 – 521	D-fructose 1,6-bisphosphate binding; part of allosteric siteBy similarity	8

Sequence similaritiesⁱ

Belongs to the pyruvate kinase family.Curated

Phylogenomic databases

eggNOGⁱ	KOG2323 Eukaryota COG0469 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00390000008859
HOGENOMⁱ	HOG000021559
HOVERGENⁱ	HBG000941
InParanoidⁱ	P11980
KEGG Orthology (KO) More...KOⁱ	K00873
OMAⁱ	KHEAIEQ
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0597
PhylomeDBⁱ	P11980
TreeFamⁱ	TF300390

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00288 Pyruvate_Kinase, 1 hit
Gene3Dⁱ	2.40.33.10, 1 hit 3.40.1380.20, 1 hit
InterProⁱ	View protein in InterPro IPR001697 Pyr_Knase IPR015813 Pyrv/PenolPyrv_Kinase-like_dom 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
Pfam protein domain database More...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

Sequences (2+)ⁱ

Sequence statusⁱ: Complete.

This entry describes 2 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show all Align All

Isoform M1 (identifier: P11980-1) [UniParc]FASTA Add to basket

Also known as: PKM1

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPKPDSEAGT AFIQTQQLHA AMADTFLEHM CRLDIDSAPI TARNTGIICT 
        60         70         80         90        100
IGPASRSVEM LKEMIKSGMN VARLNFSHGT HEYHAETIKN VRAATESFAS 
       110        120        130        140        150
DPILYRPVAV ALDTKGPEIR TGLIKGSGTA EVELKKGATL KITLDNAYME 
       160        170        180        190        200
KCDENILWLD YKNICKVVEV GSKIYVDDGL ISLQVKEKGA DYLVTEVENG 
       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 IAREAEAAVF HRLLFEELAR 
       410        420        430        440        450
ASSQSTDPLE AMAMGSVEAS YKCLAAALIV LTESGRSAHQ VARYRPRAPI 
       460        470        480        490        500
IAVTRNPQTA RQAHLYRGIF PVLCKDAVLD AWAEDVDLRV NLAMNVGKAR 
       510        520        530 
GFFKKGDVVI VLTGWRPGSG FTNTMRVVPV P

Length:531

Mass (Da):57,818

Last modified:January 23, 2007 - v3

Checksum:ⁱF0B133FDDD5991A9

GO

Isoform M2 (identifier: P11980-2) [UniParc] [UniParc]FASTA Add to basket

Also known as: PKM2

The sequence of this isoform differs from the canonical sequence as follows:
389-433: VFHRLLFEEL...LAAALIVLTE → IYHLQLFEEL...CSGAIIVLTK

« Hide

        10         20         30         40         50
MPKPDSEAGT AFIQTQQLHA AMADTFLEHM CRLDIDSAPI TARNTGIICT 
        60         70         80         90        100
IGPASRSVEM LKEMIKSGMN VARLNFSHGT HEYHAETIKN VRAATESFAS 
       110        120        130        140        150
DPILYRPVAV ALDTKGPEIR TGLIKGSGTA EVELKKGATL KITLDNAYME 
       160        170        180        190        200
KCDENILWLD YKNICKVVEV GSKIYVDDGL ISLQVKEKGA DYLVTEVENG 
       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 PVLCKDAVLD AWAEDVDLRV NLAMNVGKAR 
       510        520        530 
GFFKKGDVVI VLTGWRPGSG FTNTMRVVPV P

Show »

Length:531

Mass (Da):57,781

Checksum:ⁱ321D9EB3500272DA

GO

Computationally mapped potential isoform sequencesⁱ

There is 1 potential isoform mapped to this entry.BLAST Align Show all Add to basket

	Entry	Entry name		Protein names	Gene names	Length	Annotation

	A0A0G2JVG3	A0A0G2JVG3_RAT		Pyruvate kinase Pyruvate kinase, EC 2.7.1.40	Pkm	489	Annotation score:

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_011107	389 – 433	VFHRL…IVLTE → IYHLQLFEELRRLAPITSDP TEAAAVGAVEASFKCCSGAI IVLTK in isoform M2. CuratedAdd BLAST		45

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M24359 Genomic DNA Translation: AAB93666.1 M24359 Genomic DNA Translation: AAB93667.1 M14377 Genomic DNA No translation available. X15800 mRNA Translation: CAA33799.1
PIRⁱ	A26186 B26186
NCBI Reference Sequences More...RefSeqⁱ	NP_445749.1, NM_053297.2 [P11980-1] XP_006243250.2, XM_006243188.3 [P11980-2]
UniGeneⁱ	Rn.1556

Genome annotation databases

Ensemblⁱ	ENSRNOT00000015332; ENSRNOP00000015331; ENSRNOG00000011329 [P11980-1]
GeneIDⁱ	25630
KEGGⁱ	rno:25630
UCSC genome browser More...UCSCⁱ	RGD:3337 rat [P11980-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P11980	Pyruvate kinase PKM	)	HUMAN		531	UniRef90_P14618
Pyruvate kinase PKM	)	RABIT		531
Pyruvate kinase		PANTR		531
Pyruvate kinase		PANPA		531
Pyruvate kinase		GORGO		531
+135
P11980-2	Pyruvate kinase PKM	)	FELCA		531	UniRef90_P11980-2
Pyruvate kinase PKM		PONAB		531
Pyruvate kinase		LEPWE		610
Pyruvate kinase		MUSPF		579
Pyruvate kinase		AILME		567
+167

Protein	Similar proteins		Species	Score	Length	Source
P11980	Pyruvate kinase PKM	)	HUMAN		531	UniRef50_P14618
Pyruvate kinase PKM	)	RABIT		531
Pyruvate kinase PKM		PONAB		531
Pyruvate kinase PKM	)	FELCA		531
Pyruvate kinase PKM		MOUSE		531
+457

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M24359 Genomic DNA Translation: AAB93666.1 M24359 Genomic DNA Translation: AAB93667.1 M14377 Genomic DNA No translation available. X15800 mRNA Translation: CAA33799.1
PIRⁱ	A26186 B26186
RefSeqⁱ	NP_445749.1, NM_053297.2 [P11980-1] XP_006243250.2, XM_006243188.3 [P11980-2]
UniGeneⁱ	Rn.1556

3D structure databases

ProteinModelPortalⁱ	P11980
SMRⁱ	P11980
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	247659, 3 interactors
CORUMⁱ	P11980
IntActⁱ	P11980, 4 interactors
STRINGⁱ	10116.ENSRNOP00000015331

Chemistry databases

BindingDBⁱ	P11980
ChEMBLⁱ	CHEMBL4994

Protein family/group databases

MoonProtⁱ	P11980

MoonProtⁱ

P11980

PTM databases

iPTMnetⁱ	P11980
PhosphoSitePlusⁱ	P11980

2D gel databases

World-2DPAGEⁱ	0004:P11980

World-2DPAGEⁱ

0004:P11980

Proteomic databases

PaxDbⁱ	P11980
PRIDEⁱ	P11980

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENSRNOT00000015332; ENSRNOP00000015331; ENSRNOG00000011329 [P11980-1]
GeneIDⁱ	25630
KEGGⁱ	rno:25630
UCSCⁱ	RGD:3337 rat [P11980-1]

Organism-specific databases

CTDⁱ	5315
RGDⁱ	3337 Pkm

Phylogenomic databases

eggNOGⁱ	KOG2323 Eukaryota COG0469 LUCA
GeneTreeⁱ	ENSGT00390000008859
HOGENOMⁱ	HOG000021559
HOVERGENⁱ	HBG000941
InParanoidⁱ	P11980
KOⁱ	K00873
OMAⁱ	KHEAIEQ
OrthoDBⁱ	EOG091G0597
PhylomeDBⁱ	P11980
TreeFamⁱ	TF300390

Enzyme and pathway databases

UniPathwayⁱ	UPA00109;UER00188
Reactomeⁱ	R-RNO-6798695 Neutrophil degranulation R-RNO-70171 Glycolysis
SABIO-RKⁱ	P11980

Miscellaneous databases

Protein Ontology More...PROⁱ	PR:P11980

PROⁱ

PR:P11980

Gene expression databases

Bgeeⁱ	ENSRNOG00000011329 Expressed in 9 organ(s), highest expression level in skeletal muscle tissue
ExpressionAtlasⁱ	P11980 baseline and differential
Genevisibleⁱ	P11980 RN

Family and domain databases

CDDⁱ	cd00288 Pyruvate_Kinase, 1 hit
Gene3Dⁱ	2.40.33.10, 1 hit 3.40.1380.20, 1 hit
InterProⁱ	View protein in InterPro IPR001697 Pyr_Knase IPR015813 Pyrv/PenolPyrv_Kinase-like_dom 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...

Entry informationⁱ

Entry nameⁱ	KPYM_RAT
Accessionⁱ	P11980Primary (citable) accession number: P11980 Secondary accession number(s): P11981
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
	Last sequence update:	January 23, 2007
	Last modified:	November 7, 2018
	This is version 176 of the entry and version 3 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P11980 (KPYM_RAT)

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Pyruvate kinase PKM

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: glycolysis

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

Protein family/group databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Nucleus

Other locations

Cytosol

Nucleus

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

2D gel databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

Protein family/group databases

PTM databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

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Functionⁱ

Pathwayⁱ: glycolysis

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ