Reviewed, UniProtKB/Swiss-Prot P14618 (KPYM_HUMAN)

Names and origin

Protein names

Recommended name:
    Pyruvate kinase isozymes M1/M2
    EC=2.7.1.40
Alternative name(s):
    Pyruvate kinase muscle isozyme
    Pyruvate kinase 2/3
    Cytosolic thyroid hormone-binding protein
      Short name=CTHBP
    THBP1

Gene names

Name:	PKM2
Synonyms:	PK2, PK3, PKM

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	531 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Glycolytic enzyme that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP.
Catalytic activity	ATP + pyruvate = ADP + phosphoenolpyruvate. Ref.11
Cofactor	Magnesium. Potassium.
Enzyme regulation	Isoform M2 is allosterically activated by D-fructose 1,6-biphosphate (FBP). Inhibited by oxalate and 3,3',5-triiodo-L-thyronine (T3). Ref.11 Ref.26
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
Subunit structure	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. Interacts with HERC1. Ref.11 Ref.15
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24
Miscellaneous	There are 4 isozymes of pyruvate kinase in mammals: L, R, M1 and M2. 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.
Sequence similarities	Belongs to the pyruvate kinase family.
biophysicochemical properties	Kinetic parameters: KM=2.7 mM for phosphoenolpyruvate (at 32 degrees Celsius, pH 8.0) KM=0.17 mM for phosphoenolpyruvate (in the presence of 2mM FBP, at 32 degrees Celsius, pH 8.0) KM=0.34 mM for ADP (at 32 degrees Celsius, pH 8.0) KM=0.24 mM for ADP (in the presence of 2mM FBP, at 32 degrees Celsius, pH 8.0) KM=0.13 mM for phosphoenolpyruvate (in the presence of 2mM FBP, at 25 degrees Celsius) KM=0.63 mM for ADP (in the presence of 2mM FBP, at 25 degrees Celsius) pH dependence: 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.

Ontologies

Keywords
Biological process	Glycolysis
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding Pyruvate
Molecular function	Kinase Transferase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Allosteric enzyme Direct protein sequencing
Gene Ontology (GO)
Biological process	glycolysis Non-traceable author statement. Source: UniProtKB
Cellular component	cytosol Ref.2 Ref.3 Non-traceable author statement. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW potassium ion binding Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct pyruvate kinase activity Ref.1 Ref.2 Ref.3 Traceable author statement. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ARRB1	P49407	1	EBI-353408,EBI-743313
ARRB2	P32121	1	EBI-353408,EBI-714559
EXOSC5	Q9NQT4	1	EBI-353408,EBI-371876
NDRG1	Q92597	1	EBI-353408,EBI-716486
RAF1	P04049	3	EBI-353408,EBI-365996

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform M2 (identifier: P14618-1)

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.

Isoform M1 (identifier: P14618-2)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.11 Ref.10 Ref.12

Chain

2 – 531

530

Pyruvate kinase isozymes M1/M2

PRO_0000112088

Regions

Region

389 – 433

45

Intersubunit contact

Region

432 – 437

6

D-fructose 1,6-bisphosphate binding; part of allosteric site

Region

514 – 521

8

D-fructose 1,6-bisphosphate binding; part of allosteric site

Sites

Active site

270

1

Ref.26

Metal binding

113

1

Potassium

Metal binding

114

1

Potassium

Metal binding

272

1

Magnesium

Metal binding

296

1

Magnesium

Binding site

482

1

D-fructose 1,6-bisphosphate; part of allosteric site

Binding site

489

1

D-fructose 1,6-bisphosphate; part of allosteric site

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.10

Modified residue

37

1

Phosphoserine Ref.17 Ref.18 Ref.19 Ref.21 Ref.22 Ref.23 Ref.24

Modified residue

45

1

Phosphothreonine Ref.19

Modified residue

83

1

Phosphotyrosine Ref.16

Modified residue

105

1

Phosphotyrosine Ref.16

Modified residue

148

1

Phosphotyrosine By similarity

Modified residue

328

1

Phosphothreonine Ref.20

Modified residue

390

1

Phosphotyrosine Ref.16

Natural variations

Alternative sequence

389 – 433

45

IYHLQ…IVLTK → MFHRKLFEELVRASSHSTDL MEAMAMGSVEASYKCLAAAL IVLTE in isoform M1.

VSP_011101

Natural variant

204

1

G → V: dbSNP rs17853396. Ref.9

VAR_033067

Experimental info

Sequence conflict

7

1

E → Q in AAH12811. Ref.9

Sequence conflict

54

1

A → T in BAG52542. Ref.4

Sequence conflict

103

1

I → Y in AAA36672. Ref.2

Sequence conflict

132

1

V → L in AAA36672. Ref.2

Sequence conflict

187

1

Q → R in BAD96647. Ref.5

Sequence conflict

252

1

H → R in BAD96647. Ref.5

Sequence conflict

339

1

R → P in CAA39849. Ref.3

Sequence conflict

349

1

A → V in BAG52542. Ref.4

Sequence conflict

379

1

H → N in AAA36449. Ref.1

Sequence conflict

507

1

D → H in AAH12811. Ref.9

Secondary structure

1

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531

Helix Strand Turn

Details...

Helix

18 – 21

4

Helix

26 – 32

7

Beta strand

45 – 50

6

Turn

53 – 55

3

Helix

58 – 66

9

Beta strand

71 – 75

5

Helix

81 – 96

16

Turn

97 – 100

4

Turn

102 – 104

3

Beta strand

109 – 113

5

Beta strand

119 – 121

3

Beta strand

124 – 129

6

Beta strand

139 – 143

5

Helix

146 – 148

3

Beta strand

154 – 160

7

Turn

162 – 166

5

Beta strand

173 – 176

4

Turn

177 – 180

4

Beta strand

181 – 188

8

Beta strand

190 – 196

7

Beta strand

208 – 210

3

Helix

223 – 234

12

Beta strand

238 – 242

5

Helix

248 – 258

11

Helix

260 – 262

3

Beta strand

265 – 271

7

Helix

274 – 278

5

Helix

280 – 286

7

Beta strand

288 – 292

5

Helix

294 – 300

7

Helix

303 – 305

3

Helix

306 – 320

15

Beta strand

324 – 326

3

Beta strand

328 – 331

4

Turn

332 – 335

4

Helix

342 – 354

13

Beta strand

357 – 361

5

Turn

364 – 366

3

Beta strand

367 – 369

3

Helix

371 – 387

17

Helix

391 – 401

11

Helix

408 – 422

15

Beta strand

428 – 431

4

Beta strand

433 – 435

3

Helix

436 – 442

7

Beta strand

450 – 455

6

Helix

457 – 462

6

Helix

463 – 465

3

Beta strand

469 – 473

5

Helix

482 – 499

18

Beta strand

508 – 513

6

Beta strand

515 – 517

3

Beta strand

524 – 529

6

Sequences

	Sequence		Length	Mass (Da)
	Isoform M2 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: AA94D7818ED6BBAD	FASTA	531	57,937
	10 20 30 40 50 60 MSKPHSEAGT AFIQTQQLHA AMADTFLEHM CRLDIDSPPI TARNTGIICT IGPASRSVET 70 80 90 100 110 120 LKEMIKSGMN VARLNFSHGT HEYHAETIKN VRTATESFAS DPILYRPVAV ALDTKGPEIR 130 140 150 160 170 180 TGLIKGSGTA EVELKKGATL KITLDNAYME KCDENILWLD YKNICKVVEV GSKIYVDDGL 190 200 210 220 230 240 ISLQVKQKGA DFLVTEVENG GSLGSKKGVN LPGAAVDLPA VSEKDIQDLK FGVEQDVDMV 250 260 270 280 290 300 FASFIRKASD VHEVRKVLGE KGKNIKIISK IENHEGVRRF DEILEASDGI MVARGDLGIE 310 320 330 340 350 360 IPAEKVFLAQ KMMIGRCNRA GKPVICATQM LESMIKKPRP TRAEGSDVAN AVLDGADCIM 370 380 390 400 410 420 LSGETAKGDY PLEAVRMQHL IAREAEAAIY HLQLFEELRR LAPITSDPTE ATAVGAVEAS 430 440 450 460 470 480 FKCCSGAIIV LTKSGRSAHQ VARYRPRAPI IAVTRNPQTA RQAHLYRGIF PVLCKDPVQE 490 500 510 520 530 AWAEDVDLRV NFAMNVGKAR GFFKKGDVVI VLTGWRPGSG FTNTMRVVPV P
	Isoform M1 [UniParc] [UniParc]. Checksum: AB9B5B2308D26B79	FASTA	531	58,062
	10 20 30 40 50 60 MSKPHSEAGT AFIQTQQLHA AMADTFLEHM CRLDIDSPPI TARNTGIICT IGPASRSVET 70 80 90 100 110 120 LKEMIKSGMN VARLNFSHGT HEYHAETIKN VRTATESFAS DPILYRPVAV ALDTKGPEIR 130 140 150 160 170 180 TGLIKGSGTA EVELKKGATL KITLDNAYME KCDENILWLD YKNICKVVEV GSKIYVDDGL 190 200 210 220 230 240 ISLQVKQKGA DFLVTEVENG GSLGSKKGVN LPGAAVDLPA VSEKDIQDLK FGVEQDVDMV 250 260 270 280 290 300 FASFIRKASD VHEVRKVLGE KGKNIKIISK IENHEGVRRF DEILEASDGI MVARGDLGIE 310 320 330 340 350 360 IPAEKVFLAQ KMMIGRCNRA GKPVICATQM LESMIKKPRP TRAEGSDVAN AVLDGADCIM 370 380 390 400 410 420 LSGETAKGDY PLEAVRMQHL IAREAEAAMF HRKLFEELVR ASSHSTDLME AMAMGSVEAS 430 440 450 460 470 480 YKCLAAALIV LTESGRSAHQ VARYRPRAPI IAVTRNPQTA RQAHLYRGIF PVLCKDPVQE 490 500 510 520 530 AWAEDVDLRV NFAMNVGKAR GFFKKGDVVI VLTGWRPGSG FTNTMRVVPV P

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 2854097] [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: 2813362] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM M2).
[3]	"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: 2040271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
[4]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM M1). Tissue: Astrocyte and Fetal brain.
[5]	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.
[6]	NIEHS SNPs program Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]	"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: 16572171] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM M2), VARIANT VAL-204. Tissue: Kidney, Lung carcinoma, Ovary, Retina and Rhabdomyosarcoma.
[10]	Bienvenut W.V. Unpublished observations (JUL-2005) 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, MASS SPECTROMETRY. Tissue: B-cell lymphoma.
[11]	"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: 1854723] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-18, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICHOCHEMICAL PROPERTIES, SUBUNIT, INTERACTION WITH THYROID HORMONE.
[12]	"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: 12665801] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-32. Tissue: Platelet.
[13]	Lubec G., Vishwanath V. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 74-89, MASS SPECTROMETRY. Tissue: Brain and Cajal-Retzius cell.
[14]	"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: 9466265] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 368-531 (ISOFORM M2).
[15]	"Interaction between HERC1 and M2-type pyruvate kinase." Garcia-Gonzalo F.R., Cruz C., Munoz P., Mazurek S., Eigenbrodt E., Ventura F., Bartrons R., Rosa J.L. FEBS Lett. 539:78-84(2003) [PubMed: 12650930] [Abstract] Cited for: INTERACTION WITH HERC1.
[16]	"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: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-83; TYR-105 AND TYR-390, MASS SPECTROMETRY.
[17]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, MASS SPECTROMETRY. Tissue: Epithelium.
[18]	"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: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, MASS SPECTROMETRY. Tissue: Epithelium.
[19]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37 AND THR-45, MASS SPECTROMETRY.
[20]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-328, MASS SPECTROMETRY.
[21]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, MASS SPECTROMETRY.
[22]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, MASS SPECTROMETRY. Tissue: Platelet.
[23]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, MASS SPECTROMETRY.
[24]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, MASS SPECTROMETRY.
[25]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[26]	"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: 15996096] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.82 ANGSTROMS) OF ISOFORM M2 IN COMPLEX WITH OXALATE AND FBP, ACTIVE SITE, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
[27]	"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).
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

NIEHS-SNPs

Wikipedia

Pyruvate kinase entry

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.
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.

IPI

IPI00220644.
IPI00479186.

PIR

S30038.
S64635.

RefSeq

NP_002645.3.
NP_872270.1.

UniGene

Hs.534770

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1T5A	X-ray	2.80	A/B/C/D	1-531	[»]
1ZJH	X-ray	2.20	A	3-530	[»]
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	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P14618. 10 interactions.

2-D gel databases

Aarhus/Ghent-2DPAGE

3509. NEPHGE.

DOSAC-COBS-2DPAGE

P14618.

OGP

P14618.

REPRODUCTION-2DPAGE

IPI00220644.
IPI00479186.

Proteomic databases

PRIDE

P14618.

Genome annotation databases

Ensembl

ENSG00000067225. Homo sapiens. [Contig view]

GeneID

5315.

KEGG

hsa:5315.

Organism-specific databases

GeneCards

GC15M070278.
GC15M070279.

H-InvDB

HIX0012404.
HIX0077639.
HIX0079720.

HGNC

HGNC:9021. PKM2.

MIM

179050. gene.

Orphanet

766. Hemolytic anemia due to red cell pyruvate kinase deficiency.

PharmGKB

PA33353.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P14618.

OMA

P14618. TMENAVE.

Enzyme and pathway databases

BRENDA

2.7.1.40. 247.

Pathway_Interaction_DB

hif1_tfpathway. HIF-1-alpha transcription factor network.

Reactome

REACT_474. Metabolism of carbohydrates.

Gene expression databases

ArrayExpress

P14618.

Bgee

P14618.

CleanEx

HS_PKM2.

GermOnline

ENSG00000067225. Homo sapiens.

Family and domain databases

InterPro

IPR001697. Pyr_Knase.
IPR015813. Pyrv/PenolPyrv_Kinase_cat.
IPR015794. Pyrv_Knase_a/b.
IPR018209. Pyrv_Knase_AS.
IPR015793. Pyrv_Knase_brl.
[Graphical view]

Gene3D

G3DSA:3.20.20.60. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
G3DSA:3.40.1380.20. Pyrv_Knase_a/b. 1 hit.

PANTHER

PTHR11817. Pyruvate_kinase. 1 hit.

Pfam

PF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view]

PRINTS

PR01050. PYRUVTKNASE.

ProDom

PD001009. Pyruvate_kinase. 2 hits.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR01064. pyruv_kin. 1 hit.

PROSITE

PS00110. PYRUVATE_KINASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00119. Pyruvic acid.

NextBio

20554.

SOURCE

Search...

Entry information

Entry name

KPYM_HUMAN

Accession

Primary (citable) accession number: P14618
Secondary accession number(s): A6NFK3 , B2R5N8, B3KRY0, B4DFX8, P14786, Q53GK4, Q96E76, Q9BWB5, Q9UCV6, Q9UPF2

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 134 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)