Search Results
Overview
| Uniprot ID | A0A4X1TEM7 |
|---|---|
| Protein Name | Pyruvate kinase |
| Gene Name | PKM |
| Organism | Sus scrofa |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 110 | SRSVETLKEMIKSGM |
| 114 | ETLKEMIKSGMNVAR |
| 137 | EYHAETIKNVRAATE |
| 163 | VAVALDTKGPEIRTG |
| 183 | GTAEVELKKGATLKI |
| 214 | LDYKNICKVVDVGSK |
| 255 | GGFLGSKKGVNLPGA |
| 295 | VFASFIRKAADVHEV |
| 309 | VRKVLGEKGKNIKII |
| 314 | GEKGKNIKIISKIEN |
| 318 | KNIKIISKIENHEGV |
| 441 | EAAMFHRKLFEELVR |
| 546 | NLAMNVGKARGFFKK |
Function
Catalyzes the final rate-limiting step of glycolysis by mediating the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. The ratio between the highly active tetrameric form and nearly inactive dimeric form determines whether glucose carbons are channeled to biosynthetic processes or used for glycolytic ATP production. The transition between the 2 forms contributes to the control of glycolysis and is important for tumor cell proliferation and survival
Protein Sequence
10
MALRKILLQG
20
LRLKNKAPWT
30
GHSMCCHQWI
40
CPASTAGLSS
50
SGPKTSEAMP
60
KPHSDAGTAF
70
IQTQQLHAAM
80
ADTFLEHMCR
90
LDIDSPPITA
100
RNTGIICTIG
110
PASRSVETLK
120
EMIKSGMNVA
130
RLNFSHGTHE
140
YHAETIKNVR
150
AATESFASDP
160
ILYRPVAVAL
170
DTKGPEIRTG
180
LIKGSGTAEV
190
ELKKGATLKI
200
TLDNAYMEKC
210
DENVLWLDYK
220
NICKVVDVGS
230
KVYVDDGLIS
240
LLVKQKGPDF
250
LVTEVENGGF
260
LGSKKGVNLP
270
GAAVDLPAVS
280
EKDIQDLKFG
290
VEQDVDMVFA
300
SFIRKAADVH
310
EVRKVLGEKG
320
KNIKIISKIE
330
NHEGVRRFDE
340
ILEASDGIMV
350
ARGDLGIEIP
360
AEKVFLAQKM
370
MIGRCNRAGK
380
PVICATQMLE
390
SMIKKPRPTR
400
AEGSDVANAV
410
LDGADCIMLS
420
GETAKGDYPL
430
EAVRMQHLIA
440
REAEAAMFHR
450
KLFEELVRAS
460
SHSTDLMEAM
470
AMGSVEASYK
480
CLAAALIVLT
490
ESGRSAHQVA
500
RYRPRAPIIA
510
VTRNHQTARQ
520
AHLYRGIFPV
530
VCKDPVQEAW
540
AEDVDLRVNL
550
AMNVGKARGF
560
FKKGDVVIVL
570
TGWRPGSGFT
NTMRVVPVP
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Molecular Function | GO:0005524 | ATP binding |
| Molecular Function | GO:0016301 | kinase activity |
| Molecular Function | GO:0000287 | magnesium ion binding |
| Molecular Function | GO:0030955 | potassium ion binding |
| Molecular Function | GO:0004743 | pyruvate kinase activity |
Reference
[1] Fan S, Zhou R, Wen H, Ye H, Ma S et al.. Global profiling of protein lactylome in porcine granulosa cells.. J Ovarian Res 18(1):177. 2025 Aug 8. PMID: 40781717.