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Overview

Uniprot IDD4A031
Protein NameATP-dependent RNA helicase DDX42
Gene NameDdx42
OrganismRattus norvegicus

Kla Sites from experimental identification

Position Flanking peptide
650 FKGGKGKKLNIGGGG
701 GDRLTAMKAAFQSQY

Function

ATP-dependent RNA helicase that binds to partially double-stranded RNAs (dsRNAs) in order to unwind RNA secondary structures. Unwinding is promoted in the presence of single-strand binding proteins. Also mediates RNA duplex formation thereby displacing the single-strand RNA binding protein. 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. 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. Involved in the survival of cells by interacting with TP53BP2 and thereby counteracting the apoptosis-stimulating activity of TP53BP2. Relocalizes TP53BP2 to the cytoplasm

Protein Sequence

10 MNWNKGGPGT 20 KRGFGFGGFA 30 ISAGKKEEAK 40 LPQQSHSAFG 50 AASSSSGFGK 60 SAPPQLPSFY 70 KIGSKRANFD 80 EENAYFEDEE 90 EDSSNVDLPY 100 IPAENSPTRQ 110 QFRSKPADSD 120 SDDDPLEAFM 130 AEVEDQAARD 140 MKRLEEKDKE 150 RKNVKGIRDD 160 IEEEDDQEAY 170 FRYMAENPTA 180 GVVQEEEEDN 190 LEYDSDGNPI 200 APSKKIIDPL 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 ILDFKKKDIP 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 SDRGSNNNVM 690 SNYEAYKPST 700 GAMGDRLTAM 710 KAAFQSQYKS 720 HFVAASLSNQ 730 KAGTSTAGAS 740 GWTSAGSLNS 750 VPTNSAQQGH 760 NSPDNPITSS 770 TKNIPGFNNS 780 GNISSAPVTY 790 PSIGAQGVNN 800 TASGSNSREG 810 IGGGNGKRER 820 YTENRGGGRH 830 SHGDSGNRHG 840 DGGRHGDGYR 850 YPESSSRHTD 860 GHRHGETRHG 870 GSASRHGESR 880 GANDGRNGES 890 RKEGFNRENR 900 MDPKVDSSRM 910 DKVDSKTDKT 920 PDGFAVPEPP KRKKSRWDS

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0016607 nuclear speck
Cellular Component GO:0005634 nucleus
Cellular Component GO:0071004 U2-type prespliceosome
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0016787 hydrolase 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] Sheng L, Xu H, Wang Y, Ni J, Xiang T et al.. Systematic analysis of lysine lactylation in nucleus pulposus cells.. iScience 27(11):111157. 2024 Nov 15. PMID: 39524337.