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P30613

- KPYR_HUMAN

UniProt

P30613 - KPYR_HUMAN

Protein

Pyruvate kinase PKLR

Gene

PKLR

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 175 (01 Oct 2014)
      Sequence version 2 (30 May 2000)
      Previous versions | rss
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    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 stabilizerBy 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

    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

    Pathology & Biotechi

    Involvement in diseasei

    Pyruvate kinase hyperactivity (PKHYP) [MIM:102900]: Autosomal dominant phenotype characterized by increase of red blood cell ATP.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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.16 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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. 2 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.
    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. 2 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.
    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. 1 Publication
    VAR_011480
    Natural varianti485 – 4851S → F in PKRD.
    VAR_011468
    Natural varianti486 – 4861R → W in PKRD; frequent mutation; no conformational change. 3 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.
    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. 1 Publication
    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 PKLRPRO_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

    1
    574
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    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.Curated

    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

    Sequence cautioni

    The sequence BAA02515.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti381 – 3811P → A in BAA02515. 1 PublicationCurated
    Sequence conflicti423 – 4231A → R in AAA60104. (PubMed:3126495)Curated

    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. 2 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.
    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. 2 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.
    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. 1 Publication
    VAR_011480
    Natural varianti485 – 4851S → F in PKRD.
    VAR_011468
    Natural varianti486 – 4861R → W in PKRD; frequent mutation; no conformational change. 3 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.
    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. 1 Publication
    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. CuratedVSP_002883Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB015983 mRNA. Translation: BAA31706.1.
    M15465 mRNA. Translation: AAA60104.1.
    D13243 Genomic DNA. Translation: BAA02515.1. Sequence problems.
    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 .
    D13243 Genomic DNA. Translation: BAA02515.1 . Sequence problems.
    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

    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. "Structural analysis of human pyruvate kinase L-gene and identification of the promoter activity in erythroid cells."
      Kanno H., Fujii H., Miwa S.
      Biochem. Biophys. Res. Commun. 188:516-523(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. NIEHS SNPs program
      Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ILE-506.
    6. "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.
    7. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 470-574.
    8. "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.
    9. Cited for: REVIEW ON VARIANTS.
    10. "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.
    11. "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.
    12. "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.
    13. "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.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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.
    16. "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.
    17. "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.
    18. "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.
    19. "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.
    20. "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.
    21. "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.
    22. "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.
    23. "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.
    24. "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.
    25. Cited for: VARIANTS PKRD GLN-172; GLN-337; HIS-339; THR-357; ILE-408; THR-431; TRP-486 AND GLN-532.
    26. "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.
    27. "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.
    28. "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.
    29. "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.
    30. "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): O75758, P11973
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: May 30, 2000
    Last modified: October 1, 2014
    This is version 175 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