Search Results

Overview

Uniprot IDP14618
Protein NamePyruvate kinase PKM
Gene NamePKM
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
115 VAVALDTKGPEIRTG
125 EIRTGLIKGSGTAEV
135 GTAEVELKKGATLKI
136 TAEVELKKGATLKIT
166 LDYKNICKVVEVGSK
186 GLISLQVKQKGADFL
188 ISLQVKQKGADFLVT
206 NGGSLGSKKGVNLPG
207 GGSLGSKKGVNLPGA
224 DLPAVSEKDIQDLKF
247 VFASFIRKASDVHEV
261 VRKVLGEKGKNIKII
266 GEKGKNIKIISKIEN
270 KNIKIISKIENHEGV
3 *****MSKPHSEAGT
305 GIEIPAEKVFLAQKM
322 GRCNRAGKPVICATQ
367 MLSGETAKGDYPLEA
433 GAIIVLTKSGRSAHQ
498 NFAMNVGKARGFFKK
505 KARGFFKKGDVVIVL
62 SRSVETLKEMIKSGM
66 ETLKEMIKSGMNVAR
89 EYHAETIKNVRTATE

Function

Catalyzes the final rate-limiting step of glycolysis by mediating the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP (PubMed:15996096, PubMed:1854723, PubMed:20847263). 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 (PubMed:15996096, PubMed:1854723, PubMed:20847263). The transition between the 2 forms contributes to the control of glycolysis and is important for tumor cell proliferation and survival (PubMed:15996096, PubMed:1854723, PubMed:20847263)

Protein Sequence

10 MSKPHSEAGT 20 AFIQTQQLHA 30 AMADTFLEHM 40 CRLDIDSPPI 50 TARNTGIICT 60 IGPASRSVET 70 LKEMIKSGMN 80 VARLNFSHGT 90 HEYHAETIKN 100 VRTATESFAS 110 DPILYRPVAV 120 ALDTKGPEIR 130 TGLIKGSGTA 140 EVELKKGATL 150 KITLDNAYME 160 KCDENILWLD 170 YKNICKVVEV 180 GSKIYVDDGL 190 ISLQVKQKGA 200 DFLVTEVENG 210 GSLGSKKGVN 220 LPGAAVDLPA 230 VSEKDIQDLK 240 FGVEQDVDMV 250 FASFIRKASD 260 VHEVRKVLGE 270 KGKNIKIISK 280 IENHEGVRRF 290 DEILEASDGI 300 MVARGDLGIE 310 IPAEKVFLAQ 320 KMMIGRCNRA 330 GKPVICATQM 340 LESMIKKPRP 350 TRAEGSDVAN 360 AVLDGADCIM 370 LSGETAKGDY 380 PLEAVRMQHL 390 IAREAEAAIY 400 HLQLFEELRR 410 LAPITSDPTE 420 ATAVGAVEAS 430 FKCCSGAIIV 440 LTKSGRSAHQ 450 VARYRPRAPI 460 IAVTRNPQTA 470 RQAHLYRGIF 480 PVLCKDPVQE 490 AWAEDVDLRV 500 NFAMNVGKAR 510 GFFKKGDVVI 520 VLTGWRPGSG 530 FTNTMRVVPV P

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005929 cilium
Cellular Component GO:0005576 extracellular region
Cellular Component GO:1903561 extracellular vesicle
Cellular Component GO:1904813 ficolin-1-rich granule lumen
Cellular Component GO:0005739 mitochondrion
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0005791 rough endoplasmic reticulum
Cellular Component GO:0034774 secretory granule lumen
Cellular Component GO:0031982 vesicle
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0045296 cadherin binding
Molecular Function GO:0035402 histone H3T11 kinase activity
Molecular Function GO:0000287 magnesium ion binding
Molecular Function GO:0023026 MHC class II protein complex binding
Molecular Function GO:0003729 mRNA binding
Molecular Function GO:0004715 non-membrane spanning protein tyrosine kinase activity
Molecular Function GO:0030955 potassium ion binding
Molecular Function GO:0042803 protein homodimerization activity
Molecular Function GO:0004674 protein serine/threonine kinase activity
Molecular Function GO:0004713 protein tyrosine kinase activity
Molecular Function GO:0004743 pyruvate kinase activity
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0003713 transcription coactivator activity
Biological Process GO:0061621 canonical glycolysis
Biological Process GO:0032869 cellular response to insulin stimulus
Biological Process GO:0006096 glycolytic process
Biological Process GO:2000767 positive regulation of cytoplasmic translation
Biological Process GO:1903672 positive regulation of sprouting angiogenesis
Biological Process GO:0045944 positive regulation of transcription by RNA polymerase II
Biological Process GO:0012501 programmed cell death
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[3] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[4] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.

[5] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.

[6] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[7] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.

[8] Hu J, Jin Z, Gao Y, Liu Q, Yu Y et al.. Global Profiling of Lactylation Proteomics and Specific Lactylated Site Validation in Rheumatoid Arthritis Patients.. J Proteome Res 24(4):1732-1744. 2025 Apr 4. PMID: 40112136.

[9] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[10] Yan M, Tu H, Tang S, Gai Z, Shi Q et al.. Lactylated Proteomic Analysis Reveals Functional Implications of Lysine Lactylation In Asthenozoospermia.. Mol Cell Proteomics 24(12):101439. 2025 Dec. PMID: 41192556.

[11] Chao L, Xu Y, Yang Y, Ao X, Liang J. Identification of lactylation-related biomarkers for diagnosis, prognosis, and treatment responsiveness in triple-negative breast cancer.. World J Surg Oncol 24(1):77. 2026 Jan 22. PMID: 41566505.

[12] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.