Search Results

Overview

Uniprot IDP55263
Protein NameAdenosine kinase
Gene NameADK
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
11 AEEEPKPKKLKVEAP
12 EEEPKPKKLKVEAPQ
14 EPKPKKLKVEAPQAL
165 ANCYKKEKHLDLEKN
256 REQGFETKDIKEIAK
331 LSQLVSDKPLTECIR
61 DQILAEDKHKELFDE
71 ELFDELVKKFKVEYH

Function

Adenosine kinase that mediates the phosphorylation of the purine nucleoside adenosine at the 5' position in an ATP-dependent manner: catalyzes phosphorylation of both unmodified and modified adenosines (PubMed:21963049, PubMed:40840445, PubMed:6246102, PubMed:8577746, PubMed:9070863). Plays a key role in the detoxification of modified adenosines containing N(6)-methylated adenine (m6A) post-transcriptional modification (PubMed:40840445). Modified nucleosides are derived from the degradation of RNAs (mRNAs, rRNAs and tRNAs) and possess intrinsic cytotoxicity and must be cleared to prevent metabolic dysfunction (PubMed:40840445). Catalyzes the phosphorylation of the free cytosolic methylated adenosine nucleotides N(6)-methyladenosine (m6A), N(6),N(6)-dimethyladenosine (m6,6A) and N(6)-isopentenyladenosine (i6A) into adenosine monophosphate (AMP) intermediates that are further detoxified by MAPDA/ADAL (PubMed:40840445)

Protein Sequence

10 MAAAEEEPKP 20 KKLKVEAPQA 30 LRENILFGMG 40 NPLLDISAVV 50 DKDFLDKYSL 60 KPNDQILAED 70 KHKELFDELV 80 KKFKVEYHAG 90 GSTQNSIKVA 100 QWMIQQPHKA 110 ATFFGCIGID 120 KFGEILKRKA 130 AEAHVDAHYY 140 EQNEQPTGTC 150 AACITGDNRS 160 LIANLAAANC 170 YKKEKHLDLE 180 KNWMLVEKAR 190 VCYIAGFFLT 200 VSPESVLKVA 210 HHASENNRIF 220 TLNLSAPFIS 230 QFYKESLMKV 240 MPYVDILFGN 250 ETEAATFARE 260 QGFETKDIKE 270 IAKKTQALPK 280 MNSKRQRIVI 290 FTQGRDDTIM 300 ATESEVTAFA 310 VLDQDQKEII 320 DTNGAGDAFV 330 GGFLSQLVSD 340 KPLTECIRAG 350 HYAASIIIRR 360 TGCTFPEKPD FH

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Molecular Function GO:0004001 adenosine kinase activity
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0004136 deoxyadenosine kinase activity
Molecular Function GO:0046872 metal ion binding
Molecular Function GO:0003723 RNA binding
Biological Process GO:0044209 AMP salvage
Biological Process GO:0006144 purine nucleobase metabolic process
Biological Process GO:0006166 purine ribonucleoside salvage
Biological Process GO:0009156 ribonucleoside monophosphate biosynthetic process
Biological Process GO:0110052 toxic metabolite repair

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] 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.

[5] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.

[6] 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.

[7] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.

[8] 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.

[9] 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.