Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Pyruvate kinase isozymes R/L  

UniProtKB / Swiss-Prot ID :  KPYR_HUMAN

Gene Name (Synonyms) : 
PKLR, PK1, PKL  

Species :  Homo sapiens (Human). 

Subcellular Localization :   

Protein Function :  Plays a key role in glycolysis (By similarity). 

Protein Sequence MSIQENISSLQLRSWVSKSQRDLAKSILIGAPGGPAGYLRRASVAQLTQELGTAFFQQQQLPAAMADTFL...
Predicted Secondary Structure CCCCCCCHHHHHHHHHHHHHHHHHHHHEEECCCCCHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHH...
Protein Variant
LocationDescription
37G -> E (in PKHYP). VAR_011435
40R -> W (in PKRD). VAR_058467
48Missing (in PKRD). VAR_058468
73L -> P (in PKRD). VAR_058469
80S -> P (in PKRD). VAR_011436
86R -> P (in PKRD). VAR_011437
90I -> N (in PKRD). VAR_011438
95G -> R (in PKRD). VAR_011439
107M -> T (in PKRD). VAR_004028
111G -> R (in PKRD). VAR_011440
115A -> P (in PKRD; Val de Marne). VAR_011441
120S -> F (in PKRD; Beaujon). VAR_011442
130S -> Y (in PKRD; Conakry). VAR_011443
131Missing (in PKRD). VAR_004029
134V -> D (in PKRD). VAR_004030
153I -> T (in PKRD). VAR_011474
154A -> T (in PKRD). VAR_058470
155L -> P (in PKRD). VAR_004031
159G -> V (in PKRD). VAR_011444
163R -> C (in PKRD; Linz). VAR_004033
163R -> L (in PKRD). VAR_058471
165G -> V (in PKRD). VAR_058472
172E -> Q (in PKRD; Sassari). VAR_004032
219I -> T (in PKRD). VAR_011475
221D -> DD (in PKRD). VAR_004034
222G -> A (in PKRD; Katsushika). VAR_011445
263G -> R (in PKRD). VAR_011447
263G -> W (in PKRD). VAR_011448
272L -> V (in PKRD). VAR_058473
275G -> R (in PKRD). VAR_004035
281D -> N (in PKRD). VAR_004036
287F -> V (in PKRD). VAR_004037
288V -> L (in PKRD; Moriguchi). VAR_011449
293D -> N (in PKRD). VAR_011446
295A -> V (in PKRD). VAR_011450
310I -> N (in PKRD; Dordrecht). VAR_011451
314I -> T (in PKRD; Hong Kong). VAR_004038
315E -> K (in PKRD). VAR_011452
320V -> L (in PKRD). VAR_058474
331D -> E (in PKRD; Parma). VAR_004039
331D -> N (in PKRD). VAR_011453
332G -> S (in PKRD; loss of catalyticalactivity).
335V -> M (in PKRD). VAR_011476
336A -> S (in PKRD). VAR_004041
337R -> P (in PKRD). VAR_004042
337R -> Q (in PKRD). VAR_004043
339D -> H (in PKRD). VAR_004044
341G -> A (in PKRD). VAR_004045
341G -> D (in PKRD). VAR_011454
342I -> F (in PKRD). VAR_011455
348K -> N (in PKRD; Kamata). VAR_011456
348Missing (in PKRD; Brescia). VAR_011457
352A -> D (in PKRD). VAR_011477
354Missing (in PKRD). VAR_004046
357I -> T (in PKRD). VAR_004047
358G -> E (in PKRD). VAR_058475
359R -> C (in PKRD; Aomori). VAR_004048
359R -> H (in PKRD). VAR_004049
361N -> D (in PKRD). VAR_004050
364G -> D (in PKRD; Tjaereborg; unstabilityof the protein and decrease in catalytic
368V -> F (in PKRD; Osaka). VAR_004051
374L -> P (in PKRD). VAR_058476
376S -> I (in PKRD). VAR_011459
384T -> M (in PKRD; Tokyo/Beirut; mostcommon mutation in Japanese population;
385R -> W (in PKRD). VAR_011478
387E -> G (in PKRD). VAR_011460
390D -> N (in PKRD; Mantova; almost completeinactivation).
392A -> T (in PKRD). VAR_004053
393N -> K (in PKRD). VAR_004054
393N -> S (in PKRD; Paris). VAR_004055
394A -> D (in PKRD). VAR_011462
394A -> V (in PKRD). VAR_011463
401C -> CS (in PKRD). VAR_004056
408T -> A (in PKRD; Hirosaki). VAR_011464
408T -> I (in PKRD). VAR_004057
421Q -> K (in PKRD; Fukushima/Maebashi/Sendai).
426R -> Q (in PKRD; Sapporo). VAR_004059
426R -> W (in PKRD; Naniwa). VAR_004060
427E -> A (in PKRD). VAR_011465
427E -> D (in PKRD). VAR_011466
431A -> T (in PKRD). VAR_004061
458G -> D (in PKRD). VAR_004062
459A -> V (in PKRD). VAR_004063
460V -> M (in PKRD). VAR_004064
468A -> G (in PKRD). VAR_011479
468A -> V (in PKRD; Hadano). VAR_004065
477T -> A (in PKRD). VAR_011467
479R -> H (in PKRD; Amish; no conformationalchange).
485S -> F (in PKRD). VAR_011468
486R -> W (in PKRD; frequent mutation; noconformational change).
488R -> Q (in PKRD). VAR_011469
490R -> W (in PKRD). VAR_004067
495A -> T (in PKRD). VAR_011470
495A -> V (in PKRD). VAR_004068
498R -> C (in PKRD). VAR_004069
498R -> H (in PKRD). VAR_004070
504R -> L (in PKRD; instability of theprotein).
506V -> I (in dbSNP:rs8177988). VAR_018848
510R -> Q (in PKRD; the most common mutationin European population).
511G -> R (in PKRD). VAR_011472
531R -> C (in PKRD). VAR_011473
532R -> Q (in PKRD). VAR_004072
532R -> W (in PKRD; Complete loss in theresponsiveness to fructose 1,6-
552V -> M (in PKRD). VAR_004074
557G -> A (in PKRD). VAR_011481
559R -> G (in PKRD). VAR_004075
566N -> K (in PKRD). VAR_004076
569R -> Q (in PKRD). VAR_011482
- top -

Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
- top -

Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
26PhosphoserineDLAKSILIG
HHHHHHEEE
19.61HPRD
Link-
38PhosphotyrosineGPAGYLRRA
CCHHHHHHH
10.11Phosphositeplus
Link-
292PhosphoserineVRKASDVAA
CCCHHHHHH
35.34HPRD
Link
292PhosphoserineVRKASDVAA
CCCHHHHHH
35.34Phosphositeplus
Link
348Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)IPAEKVFLA
CCHHHHHHH
40.15Phosphositeplus
Link
348N6-acetyllysineIPAEKVFLA
CCHHHHHHH
40.15Phosphositeplus
Link
348N6-acetyllysine.IPAEKVFLA
CCHHHHHHH
40.15UniProtKB
Link
354Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)FLAQKMMIG
HHHHHHHHH
25.48Phosphositeplus
Link
556PhosphothreonineVIVVTGWRP
EEEEECCCC
21.82HPRD
Link
556PhosphothreonineVIVVTGWRP
EEEEECCCC
21.82Phosphositeplus
Link
556PhosphothreonineVIVVTGWRP
EEEEECCCC
21.82SysPTM
Link
556Phosphothreonine.VIVVTGWRP
EEEEECCCC
21.82UniProtKB
Link
564PhosphotyrosinePGSGYTNIM
CCCCCCCEE
9.79Phosphositeplus
Link
- top -

Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
DLDH_HUMANENSP00000271946STRING
ODPX_HUMANENSP00000271946STRING
PAXI_HUMANENSP00000271946STRING
ENOG_HUMANENSP00000271946STRING
RIR2B_HUMANENSP00000271946STRING
PNPT1_HUMANENSP00000271946STRING
KAD7_HUMANENSP00000271946STRING
ODP2_HUMANENSP00000271946STRING
ODPAT_HUMANENSP00000271946STRING
ODPAT_HUMANENSP00000271946STRING
ODPAT_HUMANENSP00000271946STRING
LDHD_HUMANENSP00000271946STRING
RIR1_HUMANENSP00000271946STRING
ENTP3_HUMANENSP00000271946STRING
RIR2_HUMANENSP00000271946STRING
ODPB_HUMANENSP00000271946STRING
CANT1_HUMANENSP00000271946STRING
KGUA_HUMANENSP00000271946STRING
PPCKC_HUMANENSP00000271946STRING
WBS14_HUMANENSP00000271946STRING
MAOM_HUMANENSP00000271946STRING
ENOB_HUMANENSP00000271946STRING
ENTP5_HUMANENSP00000271946STRING
FAK1_HUMANENSP00000271946STRING
ENTP8_HUMANENSP00000271946STRING
ENTP8_HUMANENSP00000271946STRING
AP4A_HUMANENSP00000271946STRING
ALAT2_HUMANENSP00000271946STRING
KAD5_HUMANENSP00000271946STRING
ENTP4_HUMANENSP00000271946STRING
- top -

Disease Reference
Kegg disease
OMIM disease
102900Pyruvate kinase hyperactivity (PKHYP)
266200Pyruvate kinase deficiency of red cells (PKRD)
Drug Reference
DrugBank
DB00119Pyruvic acid
- top -
Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-348, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-556, AND MASSSPECTROMETRY.
- top -
Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures