Search Results

Overview

Uniprot IDQ86XP3
Protein NameATP-dependent RNA helicase DDX42
Gene NameDDX42
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
195 NPIAPTKKIIDPLPP
61 PQLPSFYKIGSKRAN
650 FKGGKGKKLNIGGGG
700 GDRLTAMKAAFQSQY
708 AAFQSQYKSHFVAAS
806 GTGGSNGKRERYTEN
895 EAFNRESKMEPKMEP
908 EPKVDSSKMDKVDSK
930 FAVPEPPKRKKSRWD

Function

ATP-dependent RNA helicase that binds to partially double-stranded RNAs (dsRNAs) in order to unwind RNA secondary structures (PubMed:16397294). Unwinding is promoted in the presence of single-strand binding proteins (PubMed:16397294). Also mediates RNA duplex formation thereby displacing the single-strand RNA binding protein (PubMed:16397294). ATP and ADP modulate its activity: ATP binding and hydrolysis by DDX42 triggers RNA strand separation, whereas the ADP-bound form of the protein triggers annealing of complementary RNA strands (PubMed:16397294). Required for assembly of the 17S U2 SnRNP complex of the spliceosome, a large ribonucleoprotein complex that removes introns from transcribed pre-mRNAs: DDX42 associates transiently with the SF3B subcomplex of the 17S U2 SnRNP complex and is released after fulfilling its role in the assembly of 17S U2 SnRNP (PubMed:12234937, PubMed:36797247). Involved in the survival of cells by interacting with TP53BP2 and thereby counteracting the apoptosis-stimulating activity of TP53BP2 (PubMed:19377511). Relocalizes TP53BP2 to the cytoplasm (PubMed:19377511)

Protein Sequence

10 MNWNKGGPGT 20 KRGFGFGGFA 30 ISAGKKEEPK 40 LPQQSHSAFG 50 ATSSSSGFGK 60 SAPPQLPSFY 70 KIGSKRANFD 80 EENAYFEDEE 90 EDSSNVDLPY 100 IPAENSPTRQ 110 QFHSKPVDSD 120 SDDDPLEAFM 130 AEVEDQAARD 140 MKRLEEKDKE 150 RKNVKGIRDD 160 IEEEDDQEAY 170 FRYMAENPTA 180 GVVQEEEEDN 190 LEYDSDGNPI 200 APTKKIIDPL 210 PPIDHSEIDY 220 PPFEKNFYNE 230 HEEITNLTPQ 240 QLIDLRHKLN 250 LRVSGAAPPR 260 PGSSFAHFGF 270 DEQLMHQIRK 280 SEYTQPTPIQ 290 CQGVPVALSG 300 RDMIGIAKTG 310 SGKTAAFIWP 320 MLIHIMDQKE 330 LEPGDGPIAV 340 IVCPTRELCQ 350 QIHAECKRFG 360 KAYNLRSVAV 370 YGGGSMWEQA 380 KALQEGAEIV 390 VCTPGRLIDH 400 VKKKATNLQR 410 VSYLVFDEAD 420 RMFDMGFEYQ 430 VRSIASHVRP 440 DRQTLLFSAT 450 FRKKIEKLAR 460 DILIDPIRVV 470 QGDIGEANED 480 VTQIVEILHS 490 GPSKWNWLTR 500 RLVEFTSSGS 510 VLLFVTKKAN 520 AEELANNLKQ 530 EGHNLGLLHG 540 DMDQSERNKV 550 ISDFKKKDIP 560 VLVATDVAAR 570 GLDIPSIKTV 580 INYDVARDID 590 THTHRIGRTG 600 RAGEKGVAYT 610 LLTPKDSNFA 620 GDLVRNLEGA 630 NQHVSKELLD 640 LAMQNAWFRK 650 SRFKGGKGKK 660 LNIGGGGLGY 670 RERPGLGSEN 680 MDRGNNNVMS 690 NYEAYKPSTG 700 AMGDRLTAMK 710 AAFQSQYKSH 720 FVAASLSNQK 730 AGSSAAGASG 740 WTSAGSLNSV 750 PTNSAQQGHN 760 SPDSPVTSAA 770 KGIPGFGNTG 780 NISGAPVTYP 790 SAGAQGVNNT 800 ASGNNSREGT 810 GGSNGKRERY 820 TENRGSSRHS 830 HGETGNRHSD 840 SPRHGDGGRH 850 GDGYRHPESS 860 SRHTDGHRHG 870 ENRHGGSAGR 880 HGENRGANDG 890 RNGESRKEAF 900 NRESKMEPKM 910 EPKVDSSKMD 920 KVDSKTDKTA 930 DGFAVPEPPK RKKSRWDS

Gene Ontology

Classification GO ID Description
Cellular Component GO:0015030 Cajal body
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0016020 membrane
Cellular Component GO:0016607 nuclear speck
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0071004 U2-type prespliceosome
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0016887 ATP hydrolysis activity
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0003724 RNA helicase activity
Biological Process GO:0008104 intracellular protein localization
Biological Process GO:0042981 regulation of apoptotic process
Biological Process GO:1903241 U2-type prespliceosome assembly

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] Cheng Z, Huang H, Li M, Chen Y. Proteomic analysis identifies PFKP lactylation in SW480 colon cancer cells.. iScience 27(1):108645. 2024 Jan 19. PMID: 38155775.

[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.

[10] 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.