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P30613

- KPYR_HUMAN

UniProt

P30613 - KPYR_HUMAN

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Protein
Pyruvate kinase PKLR
Gene
PKLR, PK1, PKL
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Plays a key role in glycolysis By similarity.

Catalytic activityi

ATP + pyruvate = ADP + phosphoenolpyruvate.

Cofactori

Magnesium.
Potassium.

Enzyme regulationi

Allosterically activated by fructose 1,6-bisphosphate.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei116 – 1161Substrate
Metal bindingi118 – 1181Potassium
Metal bindingi120 – 1201Potassium
Metal bindingi156 – 1561Potassium
Metal bindingi157 – 1571Potassium; via carbonyl oxygen
Sitei313 – 3131Transition state stabilizer By similarity
Metal bindingi315 – 3151Magnesium
Binding sitei338 – 3381Substrate; via amide nitrogen
Metal bindingi339 – 3391Magnesium
Binding sitei339 – 3391Substrate; via amide nitrogen
Binding sitei371 – 3711Substrate
Binding sitei525 – 5251Allosteric activator
Binding sitei532 – 5321Allosteric activator

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. magnesium ion binding Source: InterPro
  3. potassium ion binding Source: InterPro
  4. pyruvate kinase activity Source: ProtInc

GO - Biological processi

  1. ATP biosynthetic process Source: Ensembl
  2. carbohydrate metabolic process Source: Reactome
  3. cellular response to insulin stimulus Source: Ensembl
  4. endocrine pancreas development Source: Reactome
  5. energy reserve metabolic process Source: Reactome
  6. glucose metabolic process Source: Reactome
  7. glycolytic process Source: Reactome
  8. positive regulation of cellular metabolic process Source: Reactome
  9. pyruvate biosynthetic process Source: Ensembl
  10. response to ATP Source: Ensembl
  11. response to cAMP Source: Ensembl
  12. response to glucose Source: Ensembl
  13. response to heat Source: Ensembl
  14. response to hypoxia Source: Ensembl
  15. response to lithium ion Source: Ensembl
  16. response to nutrient Source: Ensembl
  17. response to other organism Source: Ensembl
  18. 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:HS07088-MONOMER.
ReactomeiREACT_13819. Regulation of gene expression in beta cells.
REACT_1383. Glycolysis.
REACT_2122. ChREBP activates metabolic gene expression.
SABIO-RKP30613.
UniPathwayiUPA00109; UER00188.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate kinase PKLR (EC:2.7.1.40)
Alternative name(s):
Pyruvate kinase 1
Pyruvate kinase isozymes L/R
R-type/L-type pyruvate kinase
Red cell/liver pyruvate kinase
Gene namesi
Name:PKLR
Synonyms:PK1, PKL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:9020. PKLR.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Pyruvate kinase hyperactivity (PKHYP) [MIM:102900]: Autosomal dominant phenotype characterized by increase of red blood cell ATP.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti37 – 371G → E in PKHYP. 1 Publication
VAR_011435
Pyruvate kinase deficiency of red cells (PKRD) [MIM:266200]: A frequent cause of hereditary non-spherocytic hemolytic anemia. Clinically, pyruvate kinase-deficient patients suffer from a highly variable degree of chronic hemolysis, ranging from severe neonatal jaundice and fatal anemia at birth, severe transfusion-dependent chronic hemolysis, moderate hemolysis with exacerbation during infection, to a fully compensated hemolysis without apparent anemia.
Note: The disease is caused by mutations affecting the gene represented in this entry.17 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti40 – 401R → W in PKRD. 1 Publication
VAR_058467
Natural varianti48 – 536Missing in PKRD.
VAR_058468
Natural varianti73 – 731L → P in PKRD. 1 Publication
VAR_058469
Natural varianti80 – 801S → P in PKRD.
VAR_011436
Natural varianti86 – 861R → P in PKRD.
VAR_011437
Natural varianti90 – 901I → N in PKRD. 1 Publication
VAR_011438
Natural varianti95 – 951G → R in PKRD.
VAR_011439
Natural varianti107 – 1071M → T in PKRD.
VAR_004028
Natural varianti111 – 1111G → R in PKRD. 1 Publication
VAR_011440
Natural varianti115 – 1151A → P in PKRD; Val de Marne.
VAR_011441
Natural varianti120 – 1201S → F in PKRD; Beaujon.
VAR_011442
Natural varianti130 – 1301S → Y in PKRD; Conakry. 1 Publication
VAR_011443
Natural varianti131 – 1311Missing in PKRD.
VAR_004029
Natural varianti134 – 1341V → D in PKRD. 1 Publication
VAR_004030
Natural varianti153 – 1531I → T in PKRD.
VAR_011474
Natural varianti154 – 1541A → T in PKRD. 1 Publication
VAR_058470
Natural varianti155 – 1551L → P in PKRD. 1 Publication
VAR_004031
Natural varianti159 – 1591G → V in PKRD.
VAR_011444
Natural varianti163 – 1631R → C in PKRD; Linz. 1 Publication
VAR_004033
Natural varianti163 – 1631R → L in PKRD. 1 Publication
VAR_058471
Natural varianti165 – 1651G → V in PKRD. 1 Publication
VAR_058472
Natural varianti172 – 1721E → Q in PKRD; Sassari. 1 Publication
VAR_004032
Natural varianti219 – 2191I → T in PKRD.
VAR_011475
Natural varianti221 – 2211D → DD in PKRD.
VAR_004034
Natural varianti222 – 2221G → A in PKRD; Katsushika.
VAR_011445
Natural varianti263 – 2631G → R in PKRD.
VAR_011447
Natural varianti263 – 2631G → W in PKRD.
VAR_011448
Natural varianti272 – 2721L → V in PKRD. 1 Publication
VAR_058473
Natural varianti275 – 2751G → R in PKRD.
VAR_004035
Natural varianti281 – 2811D → N in PKRD.
VAR_004036
Natural varianti287 – 2871F → V in PKRD.
VAR_004037
Natural varianti288 – 2881V → L in PKRD; Moriguchi.
VAR_011449
Natural varianti293 – 2931D → N in PKRD.
VAR_011446
Natural varianti295 – 2951A → V in PKRD.
VAR_011450
Natural varianti310 – 3101I → N in PKRD; Dordrecht. 1 Publication
VAR_011451
Natural varianti314 – 3141I → T in PKRD; Hong Kong.
VAR_004038
Natural varianti315 – 3151E → K in PKRD.
VAR_011452
Natural varianti320 – 3201V → L in PKRD. 1 Publication
VAR_058474
Natural varianti331 – 3311D → E in PKRD; Parma. 1 Publication
VAR_004039
Natural varianti331 – 3311D → N in PKRD.
VAR_011453
Natural varianti332 – 3321G → S in PKRD; loss of catalytical activity. 3 Publications
VAR_004040
Natural varianti335 – 3351V → M in PKRD. 1 Publication
VAR_011476
Natural varianti336 – 3361A → S in PKRD. 1 Publication
VAR_004041
Natural varianti337 – 3371R → P in PKRD. 1 Publication
VAR_004042
Natural varianti337 – 3371R → Q in PKRD. 1 Publication
VAR_004043
Natural varianti339 – 3391D → H in PKRD. 1 Publication
VAR_004044
Natural varianti341 – 3411G → A in PKRD. 2 Publications
VAR_004045
Natural varianti341 – 3411G → D in PKRD.
VAR_011454
Natural varianti342 – 3421I → F in PKRD.
VAR_011455
Natural varianti348 – 3481K → N in PKRD; Kamata.
VAR_011456
Natural varianti348 – 3481Missing in PKRD; Brescia. 1 Publication
VAR_011457
Natural varianti352 – 3521A → D in PKRD.
VAR_011477
Natural varianti354 – 3541Missing in PKRD. 1 Publication
VAR_004046
Natural varianti357 – 3571I → T in PKRD. 1 Publication
VAR_004047
Natural varianti358 – 3581G → E in PKRD. 1 Publication
VAR_058475
Natural varianti359 – 3591R → C in PKRD; Aomori.
VAR_004048
Natural varianti359 – 3591R → H in PKRD. 1 Publication
VAR_004049
Natural varianti361 – 3611N → D in PKRD. 1 Publication
VAR_004050
Natural varianti364 – 3641G → D in PKRD; Tjaereborg; unstability of the protein and decrease in catalytic activity. 1 Publication
VAR_011458
Natural varianti368 – 3681V → F in PKRD; Osaka. 1 Publication
VAR_004051
Natural varianti374 – 3741L → P in PKRD. 1 Publication
VAR_058476
Natural varianti376 – 3761S → I in PKRD.
VAR_011459
Natural varianti384 – 3841T → M in PKRD; Tokyo/Beirut; most common mutation in Japanese population; no conformational change. 3 Publications
VAR_004052
Natural varianti385 – 3851R → W in PKRD.
VAR_011478
Natural varianti387 – 3871E → G in PKRD. 1 Publication
VAR_011460
Natural varianti390 – 3901D → N in PKRD; Mantova; almost complete inactivation. 1 Publication
VAR_011461
Natural varianti392 – 3921A → T in PKRD. 1 Publication
VAR_004053
Natural varianti393 – 3931N → K in PKRD. 1 Publication
VAR_004054
Natural varianti393 – 3931N → S in PKRD; Paris. 1 Publication
VAR_004055
Natural varianti394 – 3941A → D in PKRD. 1 Publication
VAR_011462
Natural varianti394 – 3941A → V in PKRD. 1 Publication
VAR_011463
Natural varianti401 – 4011C → CS in PKRD.
VAR_004056
Natural varianti408 – 4081T → A in PKRD; Hirosaki.
VAR_011464
Natural varianti408 – 4081T → I in PKRD. 1 Publication
VAR_004057
Natural varianti421 – 4211Q → K in PKRD; Fukushima/Maebashi/Sendai. 1 Publication
VAR_004058
Natural varianti426 – 4261R → Q in PKRD; Sapporo. 1 Publication
VAR_004059
Natural varianti426 – 4261R → W in PKRD; Naniwa.
VAR_004060
Natural varianti427 – 4271E → A in PKRD.
VAR_011465
Natural varianti427 – 4271E → D in PKRD.
VAR_011466
Natural varianti431 – 4311A → T in PKRD. 1 Publication
VAR_004061
Natural varianti458 – 4581G → D in PKRD. 1 Publication
VAR_004062
Natural varianti459 – 4591A → V in PKRD.
VAR_004063
Natural varianti460 – 4601V → M in PKRD. 1 Publication
VAR_004064
Natural varianti468 – 4681A → G in PKRD.
VAR_011479
Natural varianti468 – 4681A → V in PKRD; Hadano.
VAR_004065
Natural varianti477 – 4771T → A in PKRD.
VAR_011467
Natural varianti479 – 4791R → H in PKRD; Amish; no conformational change. 2 Publications
VAR_011480
Natural varianti485 – 4851S → F in PKRD.
VAR_011468
Natural varianti486 – 4861R → W in PKRD; frequent mutation; no conformational change. 4 Publications
Corresponds to variant rs116100695 [ dbSNP | Ensembl ].
VAR_004066
Natural varianti488 – 4881R → Q in PKRD.
VAR_011469
Natural varianti490 – 4901R → W in PKRD.
Corresponds to variant rs200133000 [ dbSNP | Ensembl ].
VAR_004067
Natural varianti495 – 4951A → T in PKRD.
VAR_011470
Natural varianti495 – 4951A → V in PKRD. 1 Publication
VAR_004068
Natural varianti498 – 4981R → C in PKRD. 1 Publication
VAR_004069
Natural varianti498 – 4981R → H in PKRD. 2 Publications
VAR_004070
Natural varianti504 – 5041R → L in PKRD; instability of the protein. 1 Publication
Corresponds to variant rs185753709 [ dbSNP | Ensembl ].
VAR_011471
Natural varianti510 – 5101R → Q in PKRD; the most common mutation in European population. 3 Publications
Corresponds to variant rs113403872 [ dbSNP | Ensembl ].
VAR_004071
Natural varianti511 – 5111G → R in PKRD.
VAR_011472
Natural varianti531 – 5311R → C in PKRD.
VAR_011473
Natural varianti532 – 5321R → Q in PKRD. 1 Publication
VAR_004072
Natural varianti532 – 5321R → W in PKRD; Complete loss in the responsiveness to fructose 1,6-bisphosphate, FBP. 2 Publications
VAR_004073
Natural varianti552 – 5521V → M in PKRD.
VAR_004074
Natural varianti557 – 5571G → A in PKRD.
VAR_011481
Natural varianti559 – 5591R → G in PKRD.
VAR_004075
Natural varianti566 – 5661N → K in PKRD.
VAR_004076
Natural varianti569 – 5691R → Q in PKRD. 1 Publication
Corresponds to variant rs61755431 [ dbSNP | Ensembl ].
VAR_011482

Keywords - Diseasei

Disease mutation, Hereditary hemolytic anemia

Organism-specific databases

MIMi102900. phenotype.
266200. phenotype.
Orphaneti766. Hemolytic anemia due to red cell pyruvate kinase deficiency.
PharmGKBiPA33352.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 574574Pyruvate kinase PKLR
PRO_0000112094Add
BLAST

Proteomic databases

MaxQBiP30613.
PaxDbiP30613.
PRIDEiP30613.

2D gel databases

REPRODUCTION-2DPAGEP30613.
SWISS-2DPAGEP30613.

PTM databases

PhosphoSiteiP30613.

Miscellaneous databases

PMAP-CutDBP30613.

Expressioni

Gene expression databases

ArrayExpressiP30613.
BgeeiP30613.
CleanExiHS_PKLR.
GenevestigatoriP30613.

Organism-specific databases

HPAiCAB034376.
CAB034378.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

BioGridi111330. 12 interactions.
IntActiP30613. 5 interactions.
STRINGi9606.ENSP00000339933.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni49 – 513
Helixi55 – 573
Helixi61 – 644
Helixi69 – 746
Beta strandi88 – 936
Turni96 – 983
Helixi101 – 11010
Beta strandi112 – 1187
Helixi124 – 13916
Turni140 – 1434
Helixi145 – 1473
Beta strandi152 – 1565
Beta strandi162 – 1643
Beta strandi170 – 1723
Beta strandi175 – 1773
Beta strandi182 – 1865
Helixi189 – 1913
Beta strandi199 – 2035
Helixi207 – 2104
Beta strandi216 – 2194
Turni220 – 2234
Beta strandi224 – 2329
Beta strandi235 – 2428
Beta strandi244 – 2463
Beta strandi251 – 2533
Helixi266 – 27712
Beta strandi281 – 2855
Helixi291 – 30111
Helixi303 – 3053
Beta strandi309 – 3146
Helixi317 – 3215
Helixi323 – 3297
Beta strandi330 – 3367
Helixi337 – 3437
Helixi346 – 3483
Helixi349 – 36315
Beta strandi367 – 3726
Helixi375 – 3784
Helixi385 – 39713
Beta strandi400 – 4056
Helixi406 – 4094
Helixi414 – 43017
Helixi434 – 4429
Helixi451 – 46616
Beta strandi469 – 4746
Beta strandi476 – 4783
Helixi479 – 4857
Beta strandi490 – 4989
Helixi500 – 5056
Helixi506 – 5083
Beta strandi512 – 5165
Helixi525 – 54218
Beta strandi551 – 56111
Beta strandi565 – 5728

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VGBX-ray2.73A/B/C/D47-574[»]
2VGFX-ray2.75A/B/C/D47-574[»]
2VGGX-ray2.74A/B/C/D47-574[»]
2VGIX-ray2.87A/B/C/D47-574[»]
4IMAX-ray1.95A/B/C/D34-574[»]
4IP7X-ray1.80A/B/C/D34-574[»]
ProteinModelPortaliP30613.
SMRiP30613. Positions 57-573.

Miscellaneous databases

EvolutionaryTraceiP30613.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni475 – 4806Allosteric activator binding
Regioni559 – 5646Allosteric activator binding

Sequence similaritiesi

Belongs to the pyruvate kinase family.

Phylogenomic databases

eggNOGiCOG0469.
HOGENOMiHOG000021559.
HOVERGENiHBG000941.
KOiK12406.
OMAiCVTRNEQ.
PhylomeDBiP30613.
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.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform R-type (identifier: P30613-1) [UniParc]FASTAAdd to Basket

Also known as: PKR

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

MSIQENISSL QLRSWVSKSQ RDLAKSILIG APGGPAGYLR RASVAQLTQE    50
LGTAFFQQQQ LPAAMADTFL EHLCLLDIDS EPVAARSTSI IATIGPASRS 100
VERLKEMIKA GMNIARLNFS HGSHEYHAES IANVREAVES FAGSPLSYRP 150
VAIALDTKGP EIRTGILQGG PESEVELVKG SQVLVTVDPA FRTRGNANTV 200
WVDYPNIVRV VPVGGRIYID DGLISLVVQK IGPEGLVTQV ENGGVLGSRK 250
GVNLPGAQVD LPGLSEQDVR DLRFGVEHGV DIVFASFVRK ASDVAAVRAA 300
LGPEGHGIKI ISKIENHEGV KRFDEILEVS DGIMVARGDL GIEIPAEKVF 350
LAQKMMIGRC NLAGKPVVCA TQMLESMITK PRPTRAETSD VANAVLDGAD 400
CIMLSGETAK GNFPVEAVKM QHAIAREAEA AVYHRQLFEE LRRAAPLSRD 450
PTEVTAIGAV EAAFKCCAAA IIVLTTTGRS AQLLSRYRPR AAVIAVTRSA 500
QAARQVHLCR GVFPLLYREP PEAIWADDVD RRVQFGIESG KLRGFLRVGD 550
LVIVVTGWRP GSGYTNIMRV LSIS 574
Length:574
Mass (Da):61,830
Last modified:May 30, 2000 - v2
Checksum:i3B430896832032F5
GO
Isoform L-type (identifier: P30613-2) [UniParc]FASTAAdd to Basket

Also known as: PKL

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: MSIQENISSLQLRSWVSKSQRDLAKSILIGAPG → ME

Show »
Length:543
Mass (Da):58,494
Checksum:iCA16D3984B868D9E
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti37 – 371G → E in PKHYP. 1 Publication
VAR_011435
Natural varianti40 – 401R → W in PKRD. 1 Publication
VAR_058467
Natural varianti48 – 536Missing in PKRD.
VAR_058468
Natural varianti73 – 731L → P in PKRD. 1 Publication
VAR_058469
Natural varianti80 – 801S → P in PKRD.
VAR_011436
Natural varianti86 – 861R → P in PKRD.
VAR_011437
Natural varianti90 – 901I → N in PKRD. 1 Publication
VAR_011438
Natural varianti95 – 951G → R in PKRD.
VAR_011439
Natural varianti107 – 1071M → T in PKRD.
VAR_004028
Natural varianti111 – 1111G → R in PKRD. 1 Publication
VAR_011440
Natural varianti115 – 1151A → P in PKRD; Val de Marne.
VAR_011441
Natural varianti120 – 1201S → F in PKRD; Beaujon.
VAR_011442
Natural varianti130 – 1301S → Y in PKRD; Conakry. 1 Publication
VAR_011443
Natural varianti131 – 1311Missing in PKRD.
VAR_004029
Natural varianti134 – 1341V → D in PKRD. 1 Publication
VAR_004030
Natural varianti153 – 1531I → T in PKRD.
VAR_011474
Natural varianti154 – 1541A → T in PKRD. 1 Publication
VAR_058470
Natural varianti155 – 1551L → P in PKRD. 1 Publication
VAR_004031
Natural varianti159 – 1591G → V in PKRD.
VAR_011444
Natural varianti163 – 1631R → C in PKRD; Linz. 1 Publication
VAR_004033
Natural varianti163 – 1631R → L in PKRD. 1 Publication
VAR_058471
Natural varianti165 – 1651G → V in PKRD. 1 Publication
VAR_058472
Natural varianti172 – 1721E → Q in PKRD; Sassari. 1 Publication
VAR_004032
Natural varianti219 – 2191I → T in PKRD.
VAR_011475
Natural varianti221 – 2211D → DD in PKRD.
VAR_004034
Natural varianti222 – 2221G → A in PKRD; Katsushika.
VAR_011445
Natural varianti263 – 2631G → R in PKRD.
VAR_011447
Natural varianti263 – 2631G → W in PKRD.
VAR_011448
Natural varianti272 – 2721L → V in PKRD. 1 Publication
VAR_058473
Natural varianti275 – 2751G → R in PKRD.
VAR_004035
Natural varianti281 – 2811D → N in PKRD.
VAR_004036
Natural varianti287 – 2871F → V in PKRD.
VAR_004037
Natural varianti288 – 2881V → L in PKRD; Moriguchi.
VAR_011449
Natural varianti293 – 2931D → N in PKRD.
VAR_011446
Natural varianti295 – 2951A → V in PKRD.
VAR_011450
Natural varianti310 – 3101I → N in PKRD; Dordrecht. 1 Publication
VAR_011451
Natural varianti314 – 3141I → T in PKRD; Hong Kong.
VAR_004038
Natural varianti315 – 3151E → K in PKRD.
VAR_011452
Natural varianti320 – 3201V → L in PKRD. 1 Publication
VAR_058474
Natural varianti331 – 3311D → E in PKRD; Parma. 1 Publication
VAR_004039
Natural varianti331 – 3311D → N in PKRD.
VAR_011453
Natural varianti332 – 3321G → S in PKRD; loss of catalytical activity. 3 Publications
VAR_004040
Natural varianti335 – 3351V → M in PKRD. 1 Publication
VAR_011476
Natural varianti336 – 3361A → S in PKRD. 1 Publication
VAR_004041
Natural varianti337 – 3371R → P in PKRD. 1 Publication
VAR_004042
Natural varianti337 – 3371R → Q in PKRD. 1 Publication
VAR_004043
Natural varianti339 – 3391D → H in PKRD. 1 Publication
VAR_004044
Natural varianti341 – 3411G → A in PKRD. 2 Publications
VAR_004045
Natural varianti341 – 3411G → D in PKRD.
VAR_011454
Natural varianti342 – 3421I → F in PKRD.
VAR_011455
Natural varianti348 – 3481K → N in PKRD; Kamata.
VAR_011456
Natural varianti348 – 3481Missing in PKRD; Brescia. 1 Publication
VAR_011457
Natural varianti352 – 3521A → D in PKRD.
VAR_011477
Natural varianti354 – 3541Missing in PKRD. 1 Publication
VAR_004046
Natural varianti357 – 3571I → T in PKRD. 1 Publication
VAR_004047
Natural varianti358 – 3581G → E in PKRD. 1 Publication
VAR_058475
Natural varianti359 – 3591R → C in PKRD; Aomori.
VAR_004048
Natural varianti359 – 3591R → H in PKRD. 1 Publication
VAR_004049
Natural varianti361 – 3611N → D in PKRD. 1 Publication
VAR_004050
Natural varianti364 – 3641G → D in PKRD; Tjaereborg; unstability of the protein and decrease in catalytic activity. 1 Publication
VAR_011458
Natural varianti368 – 3681V → F in PKRD; Osaka. 1 Publication
VAR_004051
Natural varianti374 – 3741L → P in PKRD. 1 Publication
VAR_058476
Natural varianti376 – 3761S → I in PKRD.
VAR_011459
Natural varianti384 – 3841T → M in PKRD; Tokyo/Beirut; most common mutation in Japanese population; no conformational change. 3 Publications
VAR_004052
Natural varianti385 – 3851R → W in PKRD.
VAR_011478
Natural varianti387 – 3871E → G in PKRD. 1 Publication
VAR_011460
Natural varianti390 – 3901D → N in PKRD; Mantova; almost complete inactivation. 1 Publication
VAR_011461
Natural varianti392 – 3921A → T in PKRD. 1 Publication
VAR_004053
Natural varianti393 – 3931N → K in PKRD. 1 Publication
VAR_004054
Natural varianti393 – 3931N → S in PKRD; Paris. 1 Publication
VAR_004055
Natural varianti394 – 3941A → D in PKRD. 1 Publication
VAR_011462
Natural varianti394 – 3941A → V in PKRD. 1 Publication
VAR_011463
Natural varianti401 – 4011C → CS in PKRD.
VAR_004056
Natural varianti408 – 4081T → A in PKRD; Hirosaki.
VAR_011464
Natural varianti408 – 4081T → I in PKRD. 1 Publication
VAR_004057
Natural varianti421 – 4211Q → K in PKRD; Fukushima/Maebashi/Sendai. 1 Publication
VAR_004058
Natural varianti426 – 4261R → Q in PKRD; Sapporo. 1 Publication
VAR_004059
Natural varianti426 – 4261R → W in PKRD; Naniwa.
VAR_004060
Natural varianti427 – 4271E → A in PKRD.
VAR_011465
Natural varianti427 – 4271E → D in PKRD.
VAR_011466
Natural varianti431 – 4311A → T in PKRD. 1 Publication
VAR_004061
Natural varianti458 – 4581G → D in PKRD. 1 Publication
VAR_004062
Natural varianti459 – 4591A → V in PKRD.
VAR_004063
Natural varianti460 – 4601V → M in PKRD. 1 Publication
VAR_004064
Natural varianti468 – 4681A → G in PKRD.
VAR_011479
Natural varianti468 – 4681A → V in PKRD; Hadano.
VAR_004065
Natural varianti477 – 4771T → A in PKRD.
VAR_011467
Natural varianti479 – 4791R → H in PKRD; Amish; no conformational change. 2 Publications
VAR_011480
Natural varianti485 – 4851S → F in PKRD.
VAR_011468
Natural varianti486 – 4861R → W in PKRD; frequent mutation; no conformational change. 4 Publications
Corresponds to variant rs116100695 [ dbSNP | Ensembl ].
VAR_004066
Natural varianti488 – 4881R → Q in PKRD.
VAR_011469
Natural varianti490 – 4901R → W in PKRD.
Corresponds to variant rs200133000 [ dbSNP | Ensembl ].
VAR_004067
Natural varianti495 – 4951A → T in PKRD.
VAR_011470
Natural varianti495 – 4951A → V in PKRD. 1 Publication
VAR_004068
Natural varianti498 – 4981R → C in PKRD. 1 Publication
VAR_004069
Natural varianti498 – 4981R → H in PKRD. 2 Publications
VAR_004070
Natural varianti504 – 5041R → L in PKRD; instability of the protein. 1 Publication
Corresponds to variant rs185753709 [ dbSNP | Ensembl ].
VAR_011471
Natural varianti506 – 5061V → I.1 Publication
Corresponds to variant rs8177988 [ dbSNP | Ensembl ].
VAR_018848
Natural varianti510 – 5101R → Q in PKRD; the most common mutation in European population. 3 Publications
Corresponds to variant rs113403872 [ dbSNP | Ensembl ].
VAR_004071
Natural varianti511 – 5111G → R in PKRD.
VAR_011472
Natural varianti531 – 5311R → C in PKRD.
VAR_011473
Natural varianti532 – 5321R → Q in PKRD. 1 Publication
VAR_004072
Natural varianti532 – 5321R → W in PKRD; Complete loss in the responsiveness to fructose 1,6-bisphosphate, FBP. 2 Publications
VAR_004073
Natural varianti552 – 5521V → M in PKRD.
VAR_004074
Natural varianti557 – 5571G → A in PKRD.
VAR_011481
Natural varianti559 – 5591R → G in PKRD.
VAR_004075
Natural varianti566 – 5661N → K in PKRD.
VAR_004076
Natural varianti569 – 5691R → Q in PKRD. 1 Publication
Corresponds to variant rs61755431 [ dbSNP | Ensembl ].
VAR_011482

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3333MSIQE…IGAPG → ME in isoform L-type.
VSP_002883Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti423 – 4231A → R in AAA60104. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB015983 mRNA. Translation: BAA31706.1.
M15465 mRNA. Translation: AAA60104.1.
AY316591 Genomic DNA. Translation: AAP69527.1.
BC025737 mRNA. Translation: AAH25737.1.
S60712 mRNA. Translation: AAB26262.1.
CCDSiCCDS1109.1. [P30613-1]
CCDS44240.1. [P30613-2]
PIRiI52269. KIHUPR.
RefSeqiNP_000289.1. NM_000298.5. [P30613-1]
NP_870986.1. NM_181871.3. [P30613-2]
UniGeneiHs.95990.

Genome annotation databases

EnsembliENST00000342741; ENSP00000339933; ENSG00000143627. [P30613-1]
ENST00000392414; ENSP00000376214; ENSG00000143627. [P30613-2]
ENST00000571194; ENSP00000461487; ENSG00000262785. [P30613-2]
ENST00000572740; ENSP00000459921; ENSG00000262785. [P30613-1]
GeneIDi5313.
KEGGihsa:5313.
UCSCiuc001fka.4. human. [P30613-2]
uc001fkb.4. human. [P30613-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Wikipedia

Pyruvate kinase entry

PKLR Mutation Database

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB015983 mRNA. Translation: BAA31706.1 .
M15465 mRNA. Translation: AAA60104.1 .
AY316591 Genomic DNA. Translation: AAP69527.1 .
BC025737 mRNA. Translation: AAH25737.1 .
S60712 mRNA. Translation: AAB26262.1 .
CCDSi CCDS1109.1. [P30613-1 ]
CCDS44240.1. [P30613-2 ]
PIRi I52269. KIHUPR.
RefSeqi NP_000289.1. NM_000298.5. [P30613-1 ]
NP_870986.1. NM_181871.3. [P30613-2 ]
UniGenei Hs.95990.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2VGB X-ray 2.73 A/B/C/D 47-574 [» ]
2VGF X-ray 2.75 A/B/C/D 47-574 [» ]
2VGG X-ray 2.74 A/B/C/D 47-574 [» ]
2VGI X-ray 2.87 A/B/C/D 47-574 [» ]
4IMA X-ray 1.95 A/B/C/D 34-574 [» ]
4IP7 X-ray 1.80 A/B/C/D 34-574 [» ]
ProteinModelPortali P30613.
SMRi P30613. Positions 57-573.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111330. 12 interactions.
IntActi P30613. 5 interactions.
STRINGi 9606.ENSP00000339933.

Chemistry

ChEMBLi CHEMBL1075126.
DrugBanki DB00119. Pyruvic acid.

PTM databases

PhosphoSitei P30613.

2D gel databases

REPRODUCTION-2DPAGE P30613.
SWISS-2DPAGE P30613.

Proteomic databases

MaxQBi P30613.
PaxDbi P30613.
PRIDEi P30613.

Protocols and materials databases

DNASUi 5313.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000342741 ; ENSP00000339933 ; ENSG00000143627 . [P30613-1 ]
ENST00000392414 ; ENSP00000376214 ; ENSG00000143627 . [P30613-2 ]
ENST00000571194 ; ENSP00000461487 ; ENSG00000262785 . [P30613-2 ]
ENST00000572740 ; ENSP00000459921 ; ENSG00000262785 . [P30613-1 ]
GeneIDi 5313.
KEGGi hsa:5313.
UCSCi uc001fka.4. human. [P30613-2 ]
uc001fkb.4. human. [P30613-1 ]

Organism-specific databases

CTDi 5313.
GeneCardsi GC01M155259.
HGNCi HGNC:9020. PKLR.
HPAi CAB034376.
CAB034378.
MIMi 102900. phenotype.
266200. phenotype.
609712. gene.
neXtProti NX_P30613.
Orphaneti 766. Hemolytic anemia due to red cell pyruvate kinase deficiency.
PharmGKBi PA33352.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0469.
HOGENOMi HOG000021559.
HOVERGENi HBG000941.
KOi K12406.
OMAi CVTRNEQ.
PhylomeDBi P30613.
TreeFami TF300390.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00188 .
BioCyci MetaCyc:HS07088-MONOMER.
Reactomei REACT_13819. Regulation of gene expression in beta cells.
REACT_1383. Glycolysis.
REACT_2122. ChREBP activates metabolic gene expression.
SABIO-RK P30613.

Miscellaneous databases

EvolutionaryTracei P30613.
GeneWikii PKLR.
GenomeRNAii 5313.
NextBioi 20542.
PMAP-CutDB P30613.
PROi P30613.
SOURCEi Search...

Gene expression databases

ArrayExpressi P30613.
Bgeei P30613.
CleanExi HS_PKLR.
Genevestigatori P30613.

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. "cDNA cloning of human R-type pyruvate kinase and identification of a single amino acid substitution (Thr384-->Met) affecting enzymatic stability in a pyruvate kinase variant (PK Tokyo) associated with hereditary hemolytic anemia."
    Kanno H., Fujii H., Hirono A., Miwa S.
    Proc. Natl. Acad. Sci. U.S.A. 88:8218-8221(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT PKRD MET-384.
  2. "Human liver type pyruvate kinase: complete amino acid sequence and the expression in mammalian cells."
    Tani K., Fujii H., Nagata S., Miwa S.
    Proc. Natl. Acad. Sci. U.S.A. 85:1792-1795(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. Kanno H.
    Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 130 AND 232.
  4. NIEHS SNPs program
    Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ILE-506.
  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 R-TYPE).
    Tissue: Pancreas.
  6. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 470-574.
  7. "Molecular basis of impaired pyruvate kinase isozyme conversion in erythroid cells: a single amino acid substitution near the active site and decreased mRNA content of the R-type PK."
    Kanno H., Fujii H., Tsujino G., Miwa S.
    Biochem. Biophys. Res. Commun. 192:46-52(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 365-431, VARIANT PKRD PHE-368.
  8. Cited for: REVIEW ON VARIANTS.
  9. "Hematologically important mutations: red cell pyruvate kinase."
    Baronciani L., Bianchi P., Zanella A.
    Blood Cells Mol. Dis. 22:85-89(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON VARIANTS.
  10. "Hematologically important mutations: red cell pyruvate kinase (1st update)."
    Baronciani L., Bianchi P., Zanella A.
    Blood Cells Mol. Dis. 22:259-264(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON VARIANTS.
  11. "Hematologically important mutations: red cell pyruvate kinase (2nd update)."
    Baronciani L., Bianchi P., Zanella A.
    Blood Cells Mol. Dis. 24:273-279(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON VARIANTS.
  12. "Hematologically important mutations: red cell pyruvate kinase (third update)."
    Bianchi P., Zanella A.
    Blood Cells Mol. Dis. 26:47-53(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON VARIANTS.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Structure and function of human erythrocyte pyruvate kinase. Molecular basis of nonspherocytic hemolytic anemia."
    Valentini G., Chiarelli L.R., Fortin R., Dolzan M., Galizzi A., Abraham D.J., Wang C., Bianchi P., Zanella A., Mattevi A.
    J. Biol. Chem. 277:23807-23814(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.73 ANGSTROMS) OF 47-574 IN COMPLEX WITH FRUCTOSE 1,6-BISPHOSPHATE, ALLOSTERIC ACTIVATION, ENZYME REGULATION, CHARACTERIZATION OF VARIANTS PKRD SER-332; ASP-364; ASN-390; HIS-479; TRP-486; LEU-504 AND TRP-532, CHARACTERIZATION OF VARIANT MET-384, SUBUNIT.
  15. "Point mutations in the L-type pyruvate kinase gene of two children with hemolytic anemia caused by pyruvate kinase deficiency."
    Neubauer B., Lakomek M., Winkler H., Parke M., Hofferbert S., Schroter W.
    Blood 77:1871-1875(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PKRD CYS-163 AND MET-384.
  16. "Identical point mutations of the R-type pyruvate kinase (PK) cDNA found in unrelated PK variants associated with hereditary hemolytic anemia."
    Kanno H., Fujii H., Hirono A., Omine M., Miwa S.
    Blood 79:1347-1350(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PKRD LYS-421.
  17. "Low substrate affinity of pyruvate kinase variant (PK Sapporo) caused by a single amino acid substitution (426 Arg-->Gln) associated with hereditary hemolytic anemia."
    Kanno H., Fujii H., Miwa S.
    Blood 81:2439-2441(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PKRD GLN-426.
  18. "Analysis of pyruvate kinase-deficiency mutations that produce nonspherocytic hemolytic anemia."
    Baronciani L., Beutler E.
    Proc. Natl. Acad. Sci. U.S.A. 90:4324-4327(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PKRD ASP-134; PRO-155; HIS-359; TRP-486; VAL-495 AND GLN-510.
  19. "Molecular abnormality of erythrocyte pyruvate kinase deficiency in the Amish."
    Kanno H., Ballas S.K., Miwa S., Fujii H., Bowman H.S.
    Blood 83:2311-2316(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PKRD HIS-479.
  20. "Mutations in the pyruvate kinase L gene in patients with hereditary hemolytic anemia."
    Lenzner C., Nuernberg P., Thiele B.-J., Reis A., Brabec V., Sakalova A., Jacobasch G.
    Blood 83:2817-2822(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PKRD SER-332; SER-336; LYS-354 DEL; ASP-361; THR-392; HIS-498; GLN-510 AND TRP-532.
  21. "Molecular study of pyruvate kinase deficient patients with hereditary nonspherocytic hemolytic anemia."
    Baronciani L., Beutler E.
    J. Clin. Invest. 95:1702-1709(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PKRD GLU-331; ALA-341; LYS-393; SER-393; ASP-458; MET-460 AND HIS-498.
  22. "Study of the molecular defects in pyruvate kinase (PK) deficient patients affected by hereditary nonspherocytic hemolytic anemia (HNHA)."
    Baronciani L., Westwood B., Beutler E.
    J. Invest. Med. 43:341A-341A(1995)
    Cited for: VARIANTS PKRD.
  23. "G-to-T transition at cDNA nt 110 (K37Q) in the PKLR (pyruvate kinase) gene is the molecular basis of a case of hereditary increase of red blood cell ATP."
    Beutler E., Westwood B., van Zwieten R., Roos D.
    Hum. Mutat. 9:282-285(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PKHYP GLU-37.
  24. Cited for: VARIANTS PKRD GLN-172; GLN-337; HIS-339; THR-357; ILE-408; THR-431; TRP-486 AND GLN-532.
  25. "A new sickle cell disease phenotype associating Hb S trait, severe pyruvate kinase deficiency (PK Conakry), and an alpha-2 globin gene variant (Hb Conakry)."
    Cohen-Solal M., Prehu C., Wajcman H., Poyart C., Bardakdjian-Michau J., Kister J., Prome D., Valentin C., Bachir D., Galacteros F.
    Br. J. Haematol. 103:950-956(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PKRD TYR-130.
  26. "Novel mutations and structural implications in R-type pyruvate kinase-deficient patients from Southern Italy."
    Pastore L., della Morte R., Frisso G., Alfinito F., Vitale D., Calise R.M., Ferraro F., Zagari A., Rotoli B., Salvatore F.
    Hum. Mutat. 11:127-134(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PKRD SER-332; PRO-337; TRP-486; CYS-498 AND GLN-510.
  27. "Molecular characterization of the PK-LR gene in sixteen pyruvate kinase-deficient patients."
    Zanella A., Bianchi P., Fermo E., Iurlo A., Zappa M., Vercellati C., Boschetti C., Baronciani L., Cotton F.
    Br. J. Haematol. 113:43-48(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PKRD MET-335; LYS-348 DEL; GLY-387; ASP-394 AND VAL-394.
  28. "Fifteen novel mutations in PKLR associated with pyruvate kinase (PK) deficiency: structural implications of amino acid substitutions in PK."
    van Wijk R., Huizinga E.G., van Wesel A.C.W., van Oirschot B.A., Hadders M.A., van Solinge W.W.
    Hum. Mutat. 30:446-453(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PKRD TRP-40; 48-THR--THR-53 DEL; PRO-73; ASN-90; ARG-111; THR-154; LEU-163; VAL-165; VAL-272; ASN-310; LEU-320; GLU-358 AND PRO-374.
  29. "Exome sequencing and unrelated findings in the context of complex disease research: ethical and clinical implications."
    Lyon G.J., Jiang T., Van Wijk R., Wang W., Bodily P.M., Xing J., Tian L., Robison R.J., Clement M., Lin Y., Zhang P., Liu Y., Moore B., Glessner J.T., Elia J., Reimherr F., van Solinge W.W., Yandell M.
    , Hakonarson H., Wang J., Johnson W.E., Wei Z., Wang K.
    Discov. Med. 12:41-55(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PKRD ALA-341 AND GLN-569.

Entry informationi

Entry nameiKPYR_HUMAN
AccessioniPrimary (citable) accession number: P30613
Secondary accession number(s): P11973
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: May 30, 2000
Last modified: September 3, 2014
This is version 174 of the entry and version 2 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 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.

Keywords - Technical termi

3D-structure, Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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

Similar proteinsi