Search Results

Overview

Uniprot ID	Q96C86
Protein Name	m7GpppX diphosphatase
Gene Name	DCPS
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
10	DAAPQLGKRKRELDV
12	APQLGKRKRELDVEE
138	VVYPATEKHLQKYLR

Function

Decapping scavenger enzyme that catalyzes the cleavage of a residual cap structure following the degradation of mRNAs by the 3'->5' exosome-mediated mRNA decay pathway. Hydrolyzes cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG) with up to 10 nucleotide substrates (small capped oligoribonucleotides) and specifically releases 5'-phosphorylated RNA fragments and 7-methylguanosine monophosphate (m7GMP). Cleaves cap analog structures like tri-methyl guanosine nucleoside triphosphate (m3(2,2,7)GpppG) with very poor efficiency. Does not hydrolyze unmethylated cap analog (GpppG) and shows no decapping activity on intact m7GpppG-capped mRNA molecules longer than 25 nucleotides. Does not hydrolyze 7-methylguanosine diphosphate (m7GDP) to m7GMP (PubMed:22985415). May also play a role in the 5'->3 mRNA decay pathway; m7GDP, the downstream product released by the 5'->3' mRNA mediated decapping activity, may be also converted by DCPS to m7GMP (PubMed:14523240). Binds to m7GpppG and strongly to m7GDP. Plays a role in first intron splicing of pre-mRNAs. Inhibits activation-induced cell death

Protein Sequence

10 MADAAPQLGK 20 RKRELDVEEA 30 HAASTEEKEA 40 GVGNGTCAPV 50 RLPFSGFRLQ 60 KVLRESARDK 70 IIFLHGKVNE 80 ASGDGDGEDA 90 VVILEKTPFQ 100 VEQVAQLLTG 110 SPELQLQFSN 120 DIYSTYHLFP 130 PRQLNDVKTT 140 VVYPATEKHL 150 QKYLRQDLRL 160 IRETGDDYRN 170 ITLPHLESQS 180 LSIQWVYNIL 190 DKKAEADRIV 200 FENPDPSDGF 210 VLIPDLKWNQ 220 QQLDDLYLIA 230 ICHRRGIRSL 240 RDLTPEHLPL 250 LRNILHQGQE 260 AILQRYRMKG 270 DHLRVYLHYL 280 PSYYHLHVHF 290 TALGFEAPGS 300 GVERAHLLAE 310 VIENLECDPR 320 HYQQRTLTFA 330 LRADDPLLKL LQEAQQS

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0005737	cytoplasm
Cellular Component	GO:0005829	cytosol
Cellular Component	GO:0005654	nucleoplasm
Cellular Component	GO:0005634	nucleus
Cellular Component	GO:0000932	P-body
Cellular Component	GO:0048471	perinuclear region of cytoplasm
Molecular Function	GO:0140932	5'-(N(7)-methyl 5'-triphosphoguanosine)-[mRNA] diphosphatase activity
Molecular Function	GO:0042802	identical protein binding
Molecular Function	GO:0000340	RNA 7-methylguanosine cap binding
Molecular Function	GO:0004532	RNA exonuclease activity
Biological Process	GO:0000290	deadenylation-dependent decapping of nuclear-transcribed mRNA
Biological Process	GO:0045292	mRNA cis splicing, via spliceosome
Biological Process	GO:0110156	mRNA methylguanosine-cap decapping
Biological Process	GO:0000288	nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay

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] 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.

[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] 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.

[6] 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.

[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] 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.

[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.