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P14618

- KPYM_HUMAN

UniProt

P14618 - KPYM_HUMAN

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Protein
Pyruvate kinase PKM
Gene
PKM, OIP3, PK2, PK3, PKM2
Organism
Homo sapiens (Human)
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. Plays a general role in caspase independent cell death of tumor cells. The ratio betwween the highly active tetrameric form and nearly inactive dimeric form determines whether glucose carbons are channeled to biosynthetic processes or used for glycolytic ATP production. The transition between the 2 forms contributes to the control of glycolysis and is important for tumor cell proliferation and survival.3 Publications

Catalytic activityi

ATP + pyruvate = ADP + phosphoenolpyruvate.2 Publications

Cofactori

Magnesium.
Potassium.

Enzyme regulationi

Isoform M2 is 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 of isoform M2.6 Publications

Kineticsi

  1. KM=2.7 mM for phosphoenolpyruvate (at 32 degrees Celsius, pH 8.0)2 Publications
  2. KM=0.17 mM for phosphoenolpyruvate (in the presence of 2 mM FBP, at 32 degrees Celsius, pH 8.0)
  3. KM=0.34 mM for ADP (at 32 degrees Celsius, pH 8.0)
  4. KM=0.24 mM for ADP (in the presence of 2 mM FBP, at 32 degrees Celsius, pH 8.0)
  5. KM=0.13 mM for phosphoenolpyruvate (in the presence of 2 mM FBP, at 25 degrees Celsius)
  6. KM=0.63 mM for ADP (in the presence of 2 mM FBP, at 25 degrees Celsius)

pH dependencei

Optimum pH for T3 binding is 6.0-6.5. Increase in pH causes T3 binding to drop, does not bind T3 above pH 9.0 or below pH 5.0.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei70 – 701Serine
Binding sitei73 – 731Substrate By similarity
Metal bindingi75 – 751Potassium By similarity
Metal bindingi77 – 771Potassium By similarity
Binding sitei106 – 1061Serine
Metal bindingi113 – 1131Potassium
Metal bindingi114 – 1141Potassium; via carbonyl oxygen By similarity
Sitei270 – 2701Transition state stabilizer
Metal bindingi272 – 2721Magnesium
Binding sitei295 – 2951Substrate; via amide nitrogen By similarity
Metal bindingi296 – 2961Magnesium
Binding sitei296 – 2961Substrate; via amide nitrogen By similarity
Binding sitei328 – 3281Substrate By similarity
Sitei433 – 4331Crucial for phosphotyrosine binding
Binding sitei464 – 4641Serine
Binding sitei482 – 4821D-fructose 1,6-bisphosphate; part of allosteric site
Binding sitei489 – 4891D-fructose 1,6-bisphosphate; part of allosteric site

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. MHC class II protein complex binding Source: UniProt
  3. magnesium ion binding Source: InterPro
  4. poly(A) RNA binding Source: UniProtKB
  5. potassium ion binding Source: InterPro
  6. protein binding Source: IntAct
  7. pyruvate kinase activity Source: UniProtKB

GO - Biological processi

  1. carbohydrate metabolic process Source: Reactome
  2. glucose metabolic process Source: Reactome
  3. glycolytic process Source: Reactome
  4. programmed cell death Source: UniProtKB
  5. small molecule metabolic process Source: Reactome
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

BioCyciMetaCyc:HS00906-MONOMER.
ReactomeiREACT_1383. Glycolysis.
SABIO-RKP14618.
UniPathwayiUPA00109; UER00188.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate kinase PKM (EC:2.7.1.40)
Alternative name(s):
Cytosolic thyroid hormone-binding protein
Short name:
CTHBP
Opa-interacting protein 3
Short name:
OIP-3
Pyruvate kinase 2/3
Pyruvate kinase muscle isozyme
Thyroid hormone-binding protein 1
Short name:
THBP1
Tumor M2-PK
p58
Gene namesi
Name:PKM
Synonyms:OIP3, PK2, PK3, PKM2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:9021. PKM.

Subcellular locationi

Cytoplasm. Nucleus
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.4 Publications

GO - Cellular componenti

  1. cilium Source: Ensembl
  2. cytoplasm Source: UniProtKB
  3. cytosol Source: UniProtKB
  4. extracellular vesicular exosome Source: UniProtKB
  5. mitochondrion Source: UniProt
  6. nucleus Source: UniProtKB
  7. plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi403 – 4031P → A: Significant reduction in hydroxylation and in PKM-mediated transcriptional activity of HIF1A; when associated with A-408. 1 Publication
Mutagenesisi408 – 4081P → A: Significant reduction in hydroxylation and in PKM-mediated transcriptional activity of HIF1A; when associated with A-403. 1 Publication
Mutagenesisi437 – 4371S → Y: Unable to bind FBP but still activated by serine. 1 Publication
Mutagenesisi464 – 4641H → A: Abolishes serine binding and allosteric activation. 1 Publication

Organism-specific databases

PharmGKBiPA33353.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 531530Pyruvate kinase PKM
PRO_0000112088Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications
Modified residuei37 – 371Phosphoserine8 Publications
Modified residuei62 – 621N6-acetyllysine1 Publication
Modified residuei66 – 661N6-succinyllysine By similarity
Modified residuei89 – 891N6-acetyllysine1 Publication
Modified residuei105 – 1051Phosphotyrosine1 Publication
Modified residuei148 – 1481Phosphotyrosine By similarity
Modified residuei166 – 1661N6-acetyllysine; alternate1 Publication
Modified residuei166 – 1661N6-succinyllysine; alternate By similarity
Modified residuei175 – 1751Phosphotyrosine1 Publication
Modified residuei195 – 1951Phosphothreonine1 Publication
Modified residuei266 – 2661N6-acetyllysine1 Publication
Modified residuei270 – 2701N6-acetyllysine By similarity
Modified residuei305 – 3051N6-acetyllysine1 Publication
Modified residuei322 – 3221N6-acetyllysine; alternate By similarity
Modified residuei322 – 3221N6-succinyllysine; alternate By similarity
Modified residuei403 – 40314-hydroxyproline1 Publication
Modified residuei408 – 40814-hydroxyproline1 Publication
Modified residuei433 – 4331N6-acetyllysine1 Publication
Modified residuei475 – 4751N6-acetyllysine By similarity
Modified residuei498 – 4981N6-succinyllysine By similarity

Post-translational modificationi

ISGylated.1 Publication
Under hypoxia, hydroxylated by EGLN3.
Acetylation at Lys-305 is stimulated by high glucose concentration, it decreases enzyme activity and promotes its lysosomal-dependent degradation via chaperone-mediated autophagy.2 Publications

Keywords - PTMi

Acetylation, Hydroxylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP14618.
PaxDbiP14618.
PRIDEiP14618.

2D gel databases

DOSAC-COBS-2DPAGEP14618.
OGPiP14618.
REPRODUCTION-2DPAGEIPI00220644.
IPI00479186.
UCD-2DPAGEP14618.

PTM databases

PhosphoSiteiP14618.

Expressioni

Tissue specificityi

Specifically expressed in proliferating cells, such as embryonic stem cells, embryonic carcinoma cells, as well as cancer cells.1 Publication

Gene expression databases

ArrayExpressiP14618.
BgeeiP14618.
CleanExiHS_PKM2.
GenevestigatoriP14618.

Organism-specific databases

HPAiCAB019421.
HPA029501.

Interactioni

Subunit structurei

Monomer and homotetramer. Exists as a monomer in the absence of FBP, and reversibly associates to form a homotetramer in the presence of FBP. The monomeric form binds T3. Tetramer formation induces pyruvate kinase activity. The tetrameric form has high affinity for the substrate and is associated within the glycolytic enzyme complex. Exists in a nearly inactive dimeric form in tumor cells and the dimeric form has less affinity for the substrate. Binding to certain oncoproteins such as HPV-16 E7 oncoprotein can trigger dimerization. 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.9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Q9WMX24EBI-353408,EBI-710918From a different organism.
ARRB1P494073EBI-353408,EBI-743313
ARRB2P321214EBI-353408,EBI-714559
DAPK1P533553EBI-353408,EBI-358616
EGLN3Q9H6Z92EBI-4304679,EBI-1175354
HIF1AQ166657EBI-4304679,EBI-447269
HTTP428583EBI-353408,EBI-466029
RAF1P040493EBI-353408,EBI-365996

Protein-protein interaction databases

BioGridi111332. 106 interactions.
DIPiDIP-31273N.
IntActiP14618. 82 interactions.
MINTiMINT-4998892.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi15 – 173
Helixi18 – 214
Helixi26 – 316
Beta strandi35 – 373
Beta strandi45 – 506
Turni53 – 553
Helixi58 – 6710
Beta strandi71 – 755
Helixi81 – 9616
Turni97 – 1004
Turni102 – 1043
Beta strandi109 – 1135
Beta strandi119 – 1213
Beta strandi127 – 1293
Beta strandi132 – 1343
Beta strandi139 – 1435
Helixi146 – 1483
Beta strandi154 – 1607
Helixi164 – 1674
Beta strandi173 – 1764
Turni177 – 1804
Beta strandi181 – 1888
Beta strandi190 – 19910
Beta strandi201 – 2033
Beta strandi204 – 2063
Beta strandi208 – 2103
Beta strandi212 – 2143
Helixi223 – 23412
Beta strandi238 – 2425
Helixi248 – 25811
Turni259 – 2646
Beta strandi265 – 2717
Helixi274 – 2785
Helixi280 – 2867
Beta strandi287 – 2937
Helixi294 – 3007
Helixi303 – 3053
Helixi306 – 32015
Beta strandi324 – 3296
Helixi332 – 3354
Beta strandi337 – 3393
Helixi342 – 35413
Beta strandi357 – 3626
Helixi363 – 3664
Beta strandi367 – 3693
Helixi371 – 38717
Helixi391 – 40111
Turni402 – 4043
Helixi408 – 42215
Beta strandi428 – 4314
Beta strandi433 – 4353
Helixi436 – 4427
Beta strandi450 – 4556
Helixi457 – 4626
Helixi463 – 4653
Beta strandi469 – 4735
Helixi482 – 49918
Beta strandi508 – 51811
Beta strandi522 – 5298

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1T5AX-ray2.80A/B/C/D1-531[»]
1ZJHX-ray2.20A3-531[»]
3BJFX-ray2.03A/B/C/D14-531[»]
3BJTX-ray2.50A/B/C/D2-531[»]
3G2GX-ray2.00A/B/C/D1-531[»]
3GQYX-ray1.85A/B/C/D1-531[»]
3GR4X-ray1.60A/B/C/D1-531[»]
3H6OX-ray2.00A/B/C/D1-531[»]
3ME3X-ray1.95A/B/C/D1-531[»]
3SRDX-ray2.90A/B/C/D1-531[»]
3SRFX-ray2.84A/B/C/D/E/F/G/H1-531[»]
3SRHX-ray2.60A/B/C/D1-531[»]
3U2ZX-ray2.10A/B/C/D1-531[»]
4B2DX-ray2.30A/B/C/D2-531[»]
4FXFX-ray2.55A/B/C/D1-531[»]
4FXJX-ray2.90A/B/C/D1-531[»]
4G1NX-ray2.30A/B/C/D14-531[»]
4JPGX-ray2.33A/B/C/D1-531[»]
ProteinModelPortaliP14618.
SMRiP14618. Positions 13-531.

Miscellaneous databases

EvolutionaryTraceiP14618.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni307 – 531225Interaction with POU5F1
Add
BLAST
Regioni389 – 43345Intersubunit contact
Add
BLAST
Regioni432 – 4376D-fructose 1,6-bisphosphate binding; part of allosteric site
Regioni514 – 5218D-fructose 1,6-bisphosphate binding; part of allosteric site

Sequence similaritiesi

Belongs to the pyruvate kinase family.

Phylogenomic databases

eggNOGiCOG0469.
HOGENOMiHOG000021559.
HOVERGENiHBG000941.
InParanoidiP14618.
KOiK00873.
OMAiINLFVDY.
OrthoDBiEOG78M01Q.
PhylomeDBiP14618.
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 (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform M2 (identifier: P14618-1) [UniParc]FASTAAdd to Basket

Also known as: M2-PK, PKM2

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

MSKPHSEAGT AFIQTQQLHA AMADTFLEHM CRLDIDSPPI TARNTGIICT    50
IGPASRSVET LKEMIKSGMN VARLNFSHGT HEYHAETIKN VRTATESFAS 100
DPILYRPVAV ALDTKGPEIR TGLIKGSGTA EVELKKGATL KITLDNAYME 150
KCDENILWLD YKNICKVVEV GSKIYVDDGL ISLQVKQKGA DFLVTEVENG 200
GSLGSKKGVN LPGAAVDLPA VSEKDIQDLK FGVEQDVDMV FASFIRKASD 250
VHEVRKVLGE KGKNIKIISK IENHEGVRRF DEILEASDGI MVARGDLGIE 300
IPAEKVFLAQ KMMIGRCNRA GKPVICATQM LESMIKKPRP TRAEGSDVAN 350
AVLDGADCIM LSGETAKGDY PLEAVRMQHL IAREAEAAIY HLQLFEELRR 400
LAPITSDPTE ATAVGAVEAS FKCCSGAIIV LTKSGRSAHQ VARYRPRAPI 450
IAVTRNPQTA RQAHLYRGIF PVLCKDPVQE AWAEDVDLRV NFAMNVGKAR 500
GFFKKGDVVI VLTGWRPGSG FTNTMRVVPV P 531
Length:531
Mass (Da):57,937
Last modified:January 23, 2007 - v4
Checksum:iAA94D7818ED6BBAD
GO
Isoform M1 (identifier: P14618-2) [UniParc] [UniParc]FASTAAdd to Basket

Also known as: M1-PK, PKM1

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

Show »
Length:531
Mass (Da):58,062
Checksum:iAB9B5B2308D26B79
GO
Isoform 3 (identifier: P14618-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-82: MSKPHSEAGT...RLNFSHGTHE → MSPEAQPQRT...PGTLASSVPL

Note: No experimental confirmation available.

Show »
Length:516
Mass (Da):56,273
Checksum:i23200C40C7C42045
GO

Sequence cautioni

The sequence BAG57589.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti204 – 2041G → V.1 Publication
Corresponds to variant rs17853396 [ dbSNP | Ensembl ].
VAR_033067

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8282MSKPH…HGTHE → MSPEAQPQRTKGPQQPCRSP IVKPGLPSFRPSSCTQPWLT HSWSTCAAWTLIHHPSQPGT LASSVPL in isoform 3.
VSP_043370Add
BLAST
Alternative sequencei389 – 43345IYHLQ…IVLTK → MFHRKLFEELVRASSHSTDL MEAMAMGSVEASYKCLAAAL IVLTE in isoform M1.
VSP_011101Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71E → Q in AAH12811. 1 Publication
Sequence conflicti54 – 541A → T in BAG52542. 1 Publication
Sequence conflicti103 – 1031I → Y in AAA36672. 1 Publication
Sequence conflicti132 – 1321V → L in AAA36672. 1 Publication
Sequence conflicti187 – 1871Q → R in BAD96647. 1 Publication
Sequence conflicti252 – 2521H → R in BAD96647. 1 Publication
Sequence conflicti339 – 3391R → P in CAA39849. 1 Publication
Sequence conflicti349 – 3491A → V in BAG52542. 1 Publication
Sequence conflicti379 – 3791H → N in AAA36449. 1 Publication
Sequence conflicti507 – 5071D → H in AAH12811. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M23725 mRNA. Translation: AAA36449.1.
M26252 mRNA. Translation: AAA36672.1.
X56494 Genomic DNA. Translation: CAA39849.1.
AK092369 mRNA. Translation: BAG52542.1.
AK222927 mRNA. Translation: BAD96647.1.
AK294315 mRNA. Translation: BAG57589.1. Different initiation.
AK300800 mRNA. Translation: BAG62458.1.
AK312253 mRNA. Translation: BAG35185.1.
AY352517 Genomic DNA. Translation: AAQ15274.1.
AC020779 Genomic DNA. No translation available.
CH471082 Genomic DNA. Translation: EAW77884.1.
CH471082 Genomic DNA. Translation: EAW77888.1.
BC000481 mRNA. Translation: AAH00481.3.
BC007640 mRNA. Translation: AAH07640.1.
BC007952 mRNA. Translation: AAH07952.3.
BC012811 mRNA. Translation: AAH12811.3.
BC035198 mRNA. Translation: AAH35198.1.
AF025439 mRNA. Translation: AAC39559.1.
CCDSiCCDS32284.1. [P14618-1]
CCDS32285.1. [P14618-2]
CCDS55972.1. [P14618-3]
PIRiS30038.
S64635.
RefSeqiNP_001193725.1. NM_001206796.1.
NP_001193726.1. NM_001206797.1.
NP_001193727.1. NM_001206798.1. [P14618-3]
NP_001193728.1. NM_001206799.1.
NP_002645.3. NM_002654.4. [P14618-1]
NP_872270.1. NM_182470.2. [P14618-2]
NP_872271.1. NM_182471.2. [P14618-2]
XP_005254502.1. XM_005254445.2. [P14618-1]
UniGeneiHs.534770.

Genome annotation databases

EnsembliENST00000319622; ENSP00000320171; ENSG00000067225. [P14618-2]
ENST00000335181; ENSP00000334983; ENSG00000067225. [P14618-1]
ENST00000389093; ENSP00000373745; ENSG00000067225. [P14618-2]
ENST00000449901; ENSP00000403365; ENSG00000067225. [P14618-3]
ENST00000565154; ENSP00000455901; ENSG00000067225. [P14618-2]
ENST00000565184; ENSP00000455736; ENSG00000067225. [P14618-2]
ENST00000568459; ENSP00000456970; ENSG00000067225. [P14618-2]
GeneIDi5315.
KEGGihsa:5315.
UCSCiuc002atv.2. human. [P14618-2]
uc002aty.2. human. [P14618-1]
uc010ukj.2. human. [P14618-3]

Polymorphism databases

DMDMi20178296.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Wikipedia

Pyruvate kinase entry

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M23725 mRNA. Translation: AAA36449.1 .
M26252 mRNA. Translation: AAA36672.1 .
X56494 Genomic DNA. Translation: CAA39849.1 .
AK092369 mRNA. Translation: BAG52542.1 .
AK222927 mRNA. Translation: BAD96647.1 .
AK294315 mRNA. Translation: BAG57589.1 . Different initiation.
AK300800 mRNA. Translation: BAG62458.1 .
AK312253 mRNA. Translation: BAG35185.1 .
AY352517 Genomic DNA. Translation: AAQ15274.1 .
AC020779 Genomic DNA. No translation available.
CH471082 Genomic DNA. Translation: EAW77884.1 .
CH471082 Genomic DNA. Translation: EAW77888.1 .
BC000481 mRNA. Translation: AAH00481.3 .
BC007640 mRNA. Translation: AAH07640.1 .
BC007952 mRNA. Translation: AAH07952.3 .
BC012811 mRNA. Translation: AAH12811.3 .
BC035198 mRNA. Translation: AAH35198.1 .
AF025439 mRNA. Translation: AAC39559.1 .
CCDSi CCDS32284.1. [P14618-1 ]
CCDS32285.1. [P14618-2 ]
CCDS55972.1. [P14618-3 ]
PIRi S30038.
S64635.
RefSeqi NP_001193725.1. NM_001206796.1.
NP_001193726.1. NM_001206797.1.
NP_001193727.1. NM_001206798.1. [P14618-3 ]
NP_001193728.1. NM_001206799.1.
NP_002645.3. NM_002654.4. [P14618-1 ]
NP_872270.1. NM_182470.2. [P14618-2 ]
NP_872271.1. NM_182471.2. [P14618-2 ]
XP_005254502.1. XM_005254445.2. [P14618-1 ]
UniGenei Hs.534770.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1T5A X-ray 2.80 A/B/C/D 1-531 [» ]
1ZJH X-ray 2.20 A 3-531 [» ]
3BJF X-ray 2.03 A/B/C/D 14-531 [» ]
3BJT X-ray 2.50 A/B/C/D 2-531 [» ]
3G2G X-ray 2.00 A/B/C/D 1-531 [» ]
3GQY X-ray 1.85 A/B/C/D 1-531 [» ]
3GR4 X-ray 1.60 A/B/C/D 1-531 [» ]
3H6O X-ray 2.00 A/B/C/D 1-531 [» ]
3ME3 X-ray 1.95 A/B/C/D 1-531 [» ]
3SRD X-ray 2.90 A/B/C/D 1-531 [» ]
3SRF X-ray 2.84 A/B/C/D/E/F/G/H 1-531 [» ]
3SRH X-ray 2.60 A/B/C/D 1-531 [» ]
3U2Z X-ray 2.10 A/B/C/D 1-531 [» ]
4B2D X-ray 2.30 A/B/C/D 2-531 [» ]
4FXF X-ray 2.55 A/B/C/D 1-531 [» ]
4FXJ X-ray 2.90 A/B/C/D 1-531 [» ]
4G1N X-ray 2.30 A/B/C/D 14-531 [» ]
4JPG X-ray 2.33 A/B/C/D 1-531 [» ]
ProteinModelPortali P14618.
SMRi P14618. Positions 13-531.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111332. 106 interactions.
DIPi DIP-31273N.
IntActi P14618. 82 interactions.
MINTi MINT-4998892.

Chemistry

BindingDBi P14618.
ChEMBLi CHEMBL1075189.
DrugBanki DB00119. Pyruvic acid.

PTM databases

PhosphoSitei P14618.

Polymorphism databases

DMDMi 20178296.

2D gel databases

DOSAC-COBS-2DPAGE P14618.
OGPi P14618.
REPRODUCTION-2DPAGE IPI00220644.
IPI00479186.
UCD-2DPAGE P14618.

Proteomic databases

MaxQBi P14618.
PaxDbi P14618.
PRIDEi P14618.

Protocols and materials databases

DNASUi 5315.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000319622 ; ENSP00000320171 ; ENSG00000067225 . [P14618-2 ]
ENST00000335181 ; ENSP00000334983 ; ENSG00000067225 . [P14618-1 ]
ENST00000389093 ; ENSP00000373745 ; ENSG00000067225 . [P14618-2 ]
ENST00000449901 ; ENSP00000403365 ; ENSG00000067225 . [P14618-3 ]
ENST00000565154 ; ENSP00000455901 ; ENSG00000067225 . [P14618-2 ]
ENST00000565184 ; ENSP00000455736 ; ENSG00000067225 . [P14618-2 ]
ENST00000568459 ; ENSP00000456970 ; ENSG00000067225 . [P14618-2 ]
GeneIDi 5315.
KEGGi hsa:5315.
UCSCi uc002atv.2. human. [P14618-2 ]
uc002aty.2. human. [P14618-1 ]
uc010ukj.2. human. [P14618-3 ]

Organism-specific databases

CTDi 5315.
GeneCardsi GC15M072492.
HGNCi HGNC:9021. PKM.
HPAi CAB019421.
HPA029501.
MIMi 179050. gene.
neXtProti NX_P14618.
PharmGKBi PA33353.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0469.
HOGENOMi HOG000021559.
HOVERGENi HBG000941.
InParanoidi P14618.
KOi K00873.
OMAi INLFVDY.
OrthoDBi EOG78M01Q.
PhylomeDBi P14618.
TreeFami TF300390.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00188 .
BioCyci MetaCyc:HS00906-MONOMER.
Reactomei REACT_1383. Glycolysis.
SABIO-RK P14618.

Miscellaneous databases

ChiTaRSi PKM2. human.
EvolutionaryTracei P14618.
GeneWikii PKM2.
GenomeRNAii 5315.
NextBioi 20554.
PROi P14618.
SOURCEi Search...

Gene expression databases

ArrayExpressi P14618.
Bgeei P14618.
CleanExi HS_PKM2.
Genevestigatori P14618.

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. "Human M2-type pyruvate kinase: cDNA cloning, chromosomal assignment and expression in hepatoma."
    Tani K., Yoshida M.C., Satoh H., Mitamura K., Noguchi T., Tanaka T., Fujii H., Miwa S.
    Gene 73:509-516(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM M2).
    Tissue: Liver.
  2. "Cytosolic thyroid hormone-binding protein is a monomer of pyruvate kinase."
    Kato H., Fukuda T., Parkison C., McPhie P., Cheng S.-Y.
    Proc. Natl. Acad. Sci. U.S.A. 86:7861-7865(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM M2), PROTEIN SEQUENCE OF 70-98, SUBUNIT, ENZYME REGULATION.
  3. Erratum
    Kato H., Fukuda T., Parkison C., McPhie P., Cheng S.-Y.
    Proc. Natl. Acad. Sci. U.S.A. 87:1625-1625(1990)
  4. "Isolation and characterization of the human pyruvate kinase M gene."
    Takenaka M., Noguchi T., Sadahiro S., Hirai H., Yamada K., Matsuda T., Imai E., Tanaka T.
    Eur. J. Biochem. 198:101-106(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS M1 AND 3).
    Tissue: Astrocyte and Fetal brain.
  6. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM M2).
    Tissue: Kidney.
  7. NIEHS SNPs program
    Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  8. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "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), VARIANT VAL-204.
    Tissue: Kidney, Lung carcinoma, Ovary, Retina and Rhabdomyosarcoma.
  11. Bienvenut W.V.
    Submitted (JUL-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-43; 57-73; 93-115; 126-135; 167-186; 231-246; 271-311; 401-422; 448-455 AND 490-498, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: B-cell lymphoma.
  12. "An in vitro novel mechanism of regulating the activity of pyruvate kinase M2 by thyroid hormone and fructose 1, 6-bisphosphate."
    Ashizawa K., McPhie P., Lin K.-H., Cheng S.-Y.
    Biochemistry 30:7105-7111(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-18, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, INTERACTION WITH THYROID HORMONE.
  13. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-32.
    Tissue: Platelet.
  14. Lubec G., Vishwanath V.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 74-89, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain and Cajal-Retzius cell.
  15. "Using the yeast two-hybrid system to identify human epithelial cell proteins that bind gonococcal Opa proteins: intracellular gonococci bind pyruvate kinase via their Opa proteins and require host pyruvate for growth."
    Williams J.M., Chen G.-C., Zhu L., Rest R.F.
    Mol. Microbiol. 27:171-186(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 368-531 (ISOFORM M2).
  16. Cited for: INTERACTION WITH HERC1.
  17. Cited for: ISGYLATION.
  18. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  21. "Nuclear translocation of the tumor marker pyruvate kinase M2 induces programmed cell death."
    Stetak A., Veress R., Ovadi J., Csermely P., Keri G., Ullrich A.
    Cancer Res. 67:1602-1608(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  22. "Modulation of M2-type pyruvate kinase activity by the cytoplasmic PML tumor suppressor protein."
    Shimada N., Shinagawa T., Ishii S.
    Genes Cells 13:245-254(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PML, ENZYME REGULATION, SUBUNIT, SUBCELLULAR LOCATION.
  23. "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: INTERACTION WITH POU5F1, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  24. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  25. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  26. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  27. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37; TYR-175 AND THR-195, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  29. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-62; LYS-89; LYS-166; LYS-266 AND LYS-433, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  30. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  31. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  32. "Pyruvate kinase M2 is a PHD3-stimulated coactivator for hypoxia-inducible factor 1."
    Luo W., Hu H., Chang R., Zhong J., Knabel M., O'Meally R., Cole R.N., Pandey A., Semenza G.L.
    Cell 145:732-744(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EGLN3 AND HIF1A, SUBCELLULAR LOCATION, INDUCTION, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, HYDROXYLATION AT PRO-403 AND PRO-408, MUTAGENESIS OF PRO-403 AND PRO-408.
  33. "The oxygen sensor PHD3 limits glycolysis under hypoxia via direct binding to pyruvate kinase."
    Chen N., Rinner O., Czernik D., Nytko K.J., Zheng D., Stiehl D.P., Zamboni N., Gstaiger M., Frei C.
    Cell Res. 21:983-986(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EGLN3.
  34. "Acetylation targets the M2 isoform of pyruvate kinase for degradation through chaperone-mediated autophagy and promotes tumor growth."
    Lv L., Li D., Zhao D., Lin R., Chu Y., Zhang H., Zha Z., Liu Y., Li Z., Xu Y., Wang G., Huang Y., Xiong Y., Guan K.L., Lei Q.Y.
    Mol. Cell 42:719-730(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-305.
  35. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  36. "Structural basis for tumor pyruvate kinase M2 allosteric regulation and catalysis."
    Dombrauckas J.D., Santarsiero B.D., Mesecar A.D.
    Biochemistry 44:9417-9429(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.82 ANGSTROMS) OF ISOFORM M2 IN COMPLEX WITH OXALATE AND FBP, CATALYTIC ACTIVITY, SUBUNIT, ENZYME MECHANISM, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
  37. "Structure of human muscle pyruvate kinase (PKM2)."
    Structural genomics consortium (SGC)
    Submitted (MAY-2005) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
  38. "Pyruvate kinase M2 is a phosphotyrosine-binding protein."
    Christofk H.R., Vander Heiden M.G., Wu N., Asara J.M., Cantley L.C.
    Nature 452:181-186(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 14-531 ALONE AND IN COMPLEX WITH FBP, ENZYME REGULATION.
  39. Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 2-531, ENZYME REGULATION BY SERINE, MAGNESIUM-BINDING SITES, SUBUNIT, MUTAGENESIS OF SER-437 AND HIS-464.

Entry informationi

Entry nameiKPYM_HUMAN
AccessioniPrimary (citable) accession number: P14618
Secondary accession number(s): A6NFK3
, B2R5N8, B3KRY0, B4DFX8, B4DUU6, P14786, Q53GK4, Q96E76, Q9BWB5, Q9UCV6, Q9UPF2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 194 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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

3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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