Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P52480

- KPYM_MOUSE

UniProt

P52480 - KPYM_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Pyruvate kinase PKM

Gene

Pkm

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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

Catalytic activityi

ATP + pyruvate = ADP + phosphoenolpyruvate.

Cofactori

Magnesium.
Potassium.

Enzyme 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei70 – 701SerineBy similarity
Binding sitei73 – 731SubstrateBy similarity
Metal bindingi75 – 751PotassiumBy similarity
Metal bindingi77 – 771PotassiumBy similarity
Binding sitei106 – 1061SerineBy similarity
Metal bindingi113 – 1131PotassiumBy similarity
Metal bindingi114 – 1141Potassium; via carbonyl oxygenBy similarity
Sitei270 – 2701Transition state stabilizerBy similarity
Metal bindingi272 – 2721MagnesiumBy similarity
Binding sitei295 – 2951Substrate; via amide nitrogenBy similarity
Metal bindingi296 – 2961MagnesiumBy similarity
Binding sitei296 – 2961Substrate; via amide nitrogenBy similarity
Binding sitei328 – 3281SubstrateBy similarity
Sitei433 – 4331Crucial for phosphotyrosine bindingBy similarity
Binding sitei464 – 4641SerineBy similarity
Binding sitei482 – 4821D-fructose 1,6-bisphosphate; part of allosteric siteBy similarity
Binding sitei489 – 4891D-fructose 1,6-bisphosphate; part of allosteric siteBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. magnesium ion binding Source: InterPro
  3. poly(A) RNA binding Source: Ensembl
  4. potassium ion binding Source: InterPro
  5. pyruvate kinase activity Source: MGI

GO - Biological processi

  1. glycolytic process Source: MGI
  2. programmed cell death Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium, Pyruvate

Enzyme and pathway databases

SABIO-RKP52480.
UniPathwayiUPA00109; UER00188.

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:Pk3, Pkm2, Pykm
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 9

Organism-specific databases

MGIiMGI:97591. Pkm.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity

GO - Cellular componenti

  1. cilium Source: MGI
  2. extracellular matrix Source: UniProtKB
  3. extracellular vesicular exosome Source: Ensembl
  4. mitochondrion Source: MGI
  5. nucleus Source: UniProtKB-KW
  6. plasma membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 531530Pyruvate kinase PKMPRO_0000112089Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei37 – 371PhosphoserineBy similarity
Modified residuei62 – 621N6-acetyllysine1 Publication
Modified residuei66 – 661N6-succinyllysine1 Publication
Modified residuei89 – 891N6-acetyllysineBy similarity
Modified residuei105 – 1051Phosphotyrosine1 Publication
Modified residuei148 – 1481Phosphotyrosine1 Publication
Modified residuei166 – 1661N6-acetyllysine; alternate1 Publication
Modified residuei166 – 1661N6-succinyllysine; alternate1 Publication
Modified residuei175 – 1751PhosphotyrosineBy similarity
Modified residuei195 – 1951PhosphothreonineBy similarity
Modified residuei266 – 2661N6-acetyllysineBy similarity
Modified residuei270 – 2701N6-acetyllysine1 Publication
Modified residuei305 – 3051N6-acetyllysineBy similarity
Modified residuei322 – 3221N6-acetyllysine; alternate1 Publication
Modified residuei322 – 3221N6-succinyllysine; alternate1 Publication
Modified residuei403 – 40314-hydroxyprolineBy similarity
Modified residuei408 – 40814-hydroxyprolineBy similarity
Modified residuei433 – 4331N6-acetyllysineBy similarity
Modified residuei475 – 4751N6-acetyllysine1 Publication
Modified residuei498 – 4981N6-succinyllysine1 Publication

Post-translational modificationi

ISGylated.1 Publication
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, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP52480.
PaxDbiP52480.
PRIDEiP52480.

2D gel databases

REPRODUCTION-2DPAGEIPI00407130.
P52480.
SWISS-2DPAGEP52480.

PTM databases

PhosphoSiteiP52480.

Expressioni

Tissue specificityi

Embryonic stem cells and embryonal carcinoma cells.1 Publication

Gene expression databases

BgeeiP52480.
CleanExiMM_PKM2.
GenevestigatoriP52480.

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. 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.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
P266633EBI-647785,EBI-6857429From a different organism.
Pou5f1P202636EBI-647785,EBI-1606219

Protein-protein interaction databases

BioGridi202191. 15 interactions.
IntActiP52480. 16 interactions.
MINTiMINT-1850796.

Structurei

3D structure databases

ProteinModelPortaliP52480.
SMRiP52480. Positions 13-531.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni307 – 531225Interaction with POU5F1By similarityAdd
BLAST
Regioni389 – 43345Intersubunit contactAdd
BLAST
Regioni432 – 4376D-fructose 1,6-bisphosphate binding; part of allosteric siteBy similarity
Regioni514 – 5218D-fructose 1,6-bisphosphate binding; part of allosteric siteBy similarity

Sequence similaritiesi

Belongs to the pyruvate kinase family.Curated

Phylogenomic databases

eggNOGiCOG0469.
GeneTreeiENSGT00390000008859.
HOVERGENiHBG000941.
InParanoidiP52480.
KOiK00873.
OMAiCIVENAG.
OrthoDBiEOG78M01Q.
PhylomeDBiP52480.
TreeFamiTF300390.

Family and domain databases

Gene3Di2.40.33.10. 1 hit.
3.20.20.60. 2 hits.
3.40.1380.20. 1 hit.
InterProiIPR001697. Pyr_Knase.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
IPR011037. Pyrv_Knase-like_insert_dom.
IPR015794. Pyrv_Knase_a/b.
IPR018209. Pyrv_Knase_AS.
IPR015793. Pyrv_Knase_brl.
IPR015795. Pyrv_Knase_C.
IPR015806. Pyrv_Knase_insert_dom.
[Graphical view]
PANTHERiPTHR11817. PTHR11817. 1 hit.
PfamiPF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view]
PRINTSiPR01050. PYRUVTKNASE.
SUPFAMiSSF50800. SSF50800. 1 hit.
SSF51621. SSF51621. 2 hits.
SSF52935. SSF52935. 1 hit.
TIGRFAMsiTIGR01064. pyruv_kin. 1 hit.
PROSITEiPS00110. PYRUVATE_KINASE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform M2 (identifier: P52480-1) [UniParc]FASTAAdd 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
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
Length:531
Mass (Da):57,845
Last modified:May 1, 2007 - v4
Checksum:i34CBBC01BC0C047D
GO
Isoform M1 (identifier: P52480-2) [UniParc]FASTAAdd to Basket

Also known as: PKM2

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

Show »
Length:531
Mass (Da):57,985
Checksum:iD0D163786CC6D4A6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 81A → V in CAA65761. (PubMed:9545585)Curated
Sequence conflicti121 – 1211T → A in BAE30642. (PubMed:16141072)Curated
Sequence conflicti121 – 1211T → A in BAE32031. (PubMed:16141072)Curated
Sequence conflicti158 – 1581W → R in BAA07457. (PubMed:7612666)Curated
Sequence conflicti166 – 1661K → E in BAE42098. (PubMed:16141072)Curated
Sequence conflicti170 – 1701V → L in BAE30642. (PubMed:16141072)Curated
Sequence conflicti170 – 1701V → L in BAE32031. (PubMed:16141072)Curated
Sequence conflicti177 – 1771D → G in BAE42199. (PubMed:16141072)Curated
Sequence conflicti230 – 2301K → R in BAE30642. (PubMed:16141072)Curated
Sequence conflicti230 – 2301K → R in BAE32031. (PubMed:16141072)Curated
Sequence conflicti299 – 2991I → T in BAA07457. (PubMed:7612666)Curated
Sequence conflicti309 – 3091A → S in BAA07457. (PubMed:7612666)Curated
Sequence conflicti327 – 3271A → S in BAA07457. (PubMed:7612666)Curated
Sequence conflicti327 – 3271A → S in CAA65761. (PubMed:9545585)Curated
Sequence conflicti333 – 3331S → I in BAA07457. (PubMed:7612666)Curated
Sequence conflicti333 – 3331S → I in CAA65761. (PubMed:9545585)Curated
Sequence conflicti485 – 4851D → N in BAE33055. (PubMed:16141072)Curated
Sequence conflicti485 – 4851D → N in BAE42192. (PubMed:16141072)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei389 – 43345IYHLQ…IVLTK → MFHRLLFEELVRASSHSTDL MEAMAMGSVEASYKCLAAAL IVLTE in isoform M1. 1 PublicationVSP_025057Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
CCDSiCCDS40659.1. [P52480-1]
CCDS57681.1. [P52480-2]
PIRiS55921.
RefSeqiNP_001240812.1. NM_001253883.1. [P52480-2]
NP_035229.2. NM_011099.3. [P52480-1]
XP_006510918.1. XM_006510855.1. [P52480-1]
UniGeneiMm.326167.
Mm.488724.

Genome annotation databases

EnsembliENSMUST00000034834; ENSMUSP00000034834; ENSMUSG00000032294. [P52480-1]
ENSMUST00000163694; ENSMUSP00000128770; ENSMUSG00000032294. [P52480-2]
GeneIDi18746.
KEGGimmu:18746.
UCSCiuc009pyf.2. mouse. [P52480-1]
uc009pyh.2. mouse. [P52480-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 ]
UniGenei Mm.326167.
Mm.488724.

3D structure databases

ProteinModelPortali P52480.
SMRi P52480. Positions 13-531.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202191. 15 interactions.
IntActi P52480. 16 interactions.
MINTi MINT-1850796.

PTM databases

PhosphoSitei P52480.

2D gel databases

REPRODUCTION-2DPAGE IPI00407130.
P52480.
SWISS-2DPAGE P52480.

Proteomic databases

MaxQBi P52480.
PaxDbi P52480.
PRIDEi P52480.

Protocols and materials databases

Structural Biology Knowledgebase Search...

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 COG0469.
GeneTreei ENSGT00390000008859.
HOVERGENi HBG000941.
InParanoidi P52480.
KOi K00873.
OMAi CIVENAG.
OrthoDBi EOG78M01Q.
PhylomeDBi P52480.
TreeFami TF300390.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00188 .
SABIO-RK P52480.

Miscellaneous databases

ChiTaRSi PKM2. mouse.
NextBioi 294905.
PROi P52480.
SOURCEi Search...

Gene expression databases

Bgeei P52480.
CleanExi MM_PKM2.
Genevestigatori P52480.

Family and domain databases

Gene3Di 2.40.33.10. 1 hit.
3.20.20.60. 2 hits.
3.40.1380.20. 1 hit.
InterProi IPR001697. Pyr_Knase.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
IPR011037. Pyrv_Knase-like_insert_dom.
IPR015794. Pyrv_Knase_a/b.
IPR018209. Pyrv_Knase_AS.
IPR015793. Pyrv_Knase_brl.
IPR015795. Pyrv_Knase_C.
IPR015806. Pyrv_Knase_insert_dom.
[Graphical view ]
PANTHERi PTHR11817. PTHR11817. 1 hit.
Pfami PF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view ]
PRINTSi PR01050. PYRUVTKNASE.
SUPFAMi SSF50800. SSF50800. 1 hit.
SSF51621. SSF51621. 2 hits.
SSF52935. SSF52935. 1 hit.
TIGRFAMsi TIGR01064. pyruv_kin. 1 hit.
PROSITEi PS00110. PYRUVATE_KINASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of the complementary DNA for the mouse pyruvate kinase M-2 gene whose expression is dependent upon cell differentiation."
    Izumi S., Manabe A., Tomoyasu A., Kihara-Negishi F., Ariga H.
    Biochim. Biophys. Acta 1267:135-138(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM M2).
  2. "Gene expression of mouse M1 and M2 pyruvate kinase isoenzymes correlates with differential poly(A) tract extension of their mRNAs during the development of spermatogenesis."
    de Luis O., del Mazo J.
    Biochim. Biophys. Acta 1396:294-305(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM M2).
    Strain: Swiss.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM M2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-395 (ISOFORM M1).
    Strain: C57BL/6J and NOD.
    Tissue: Bone marrow, Kidney and Muellerian duct.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM M2).
    Strain: C57BL/6 and FVB/N.
    Tissue: Brain and Mammary tumor.
  6. Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 33-56; 67-89; 93-115; 126-136; 142-162; 167-224; 231-246; 248-255; 279-305; 320-336; 343-399; 401-433; 468-498 AND 506-526, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6 and OF1.
    Tissue: Brain and Hippocampus.
  7. Cited for: ISGYLATION.
  8. "Pyruvate kinase isozyme type M2 (PKM2) interacts and cooperates with Oct-4 in regulating transcription."
    Lee J., Kim H.K., Han Y.-M., Kim J.
    Int. J. Biochem. Cell Biol. 40:1043-1054(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  9. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
    Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
    J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-105 AND TYR-148, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  10. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-62; LYS-166; LYS-270; LYS-322 AND LYS-475, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-66; LYS-166; LYS-322 AND LYS-498, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiKPYM_MOUSE
AccessioniPrimary (citable) accession number: P52480
Secondary accession number(s): Q3TBV8
, Q3TBW5, Q3TC59, Q3U1X3, Q3U5P6, Q4VC20, Q64484, Q91YI8, Q9CWB1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 1, 2007
Last modified: October 29, 2014
This is version 153 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3