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Overview

Uniprot IDQ92499
Protein NameATP-dependent RNA helicase DDX1
Gene NameDDX1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
281 NAQVTQTKFLPNAPK
317 KKYIDNPKLRELLII
493 SEAIKILKGEYAVRA
636 HVCSSRGKGCYNTRL
82 KKGKTTIKTGASVLN

Function

Acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. Possesses 5' single-stranded RNA overhang nuclease activity. Possesses ATPase activity on various RNA, but not DNA polynucleotides. May play a role in RNA clearance at DNA double-strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. Together with RELA, acts as a coactivator to enhance NF-kappa-B-mediated transcriptional activation. Acts as a positive transcriptional regulator of cyclin CCND2 expression. Binds to the cyclin CCND2 promoter region. Associates with chromatin at the NF-kappa-B promoter region via association with RELA. Binds to poly(A) RNA. May be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. It is also an accessory subunit of the tRNA-splicing ligase complex that acts by directly joining spliced tRNA halves to mature-sized tRNAs by incorporating the precursor-derived splice junction phosphate into the mature tRNA as a canonical 3',5'-phosphodiester. Cooperates with ZBTB8OS (also known as archease) for the guanylylation of RTCB, a key intermediate step in activation of the tRNA ligase (PubMed:24870230). Component of a multi-helicase-TICAM1 complex that acts as a cytoplasmic sensor of viral double-stranded RNA (dsRNA) and plays a role in the activation of a cascade of antiviral responses including the induction of pro-inflammatory cytokines via the adapter molecule TICAM1. Specifically binds (via helicase ATP-binding domain) on both short and long poly(I:C) dsRNA (By similarity)

Protein Sequence

10 MAAFSEMGVM 20 PEIAQAVEEM 30 DWLLPTDIQA 40 ESIPLILGGG 50 DVLMAAETGS 60 GKTGAFSIPV 70 IQIVYETLKD 80 QQEGKKGKTT 90 IKTGASVLNK 100 WQMNPYDRGS 110 AFAIGSDGLC 120 CQSREVKEWH 130 GCRATKGLMK 140 GKHYYEVSCH 150 DQGLCRVGWS 160 TMQASLDLGT 170 DKFGFGFGGT 180 GKKSHNKQFD 190 NYGEEFTMHD 200 TIGCYLDIDK 210 GHVKFSKNGK 220 DLGLAFEIPP 230 HMKNQALFPA 240 CVLKNAELKF 250 NFGEEEFKFP 260 PKDGFVALSK 270 APDGYIVKSQ 280 HSGNAQVTQT 290 KFLPNAPKAL 300 IVEPSRELAE 310 QTLNNIKQFK 320 KYIDNPKLRE 330 LLIIGGVAAR 340 DQLSVLENGV 350 DIVVGTPGRL 360 DDLVSTGKLN 370 LSQVRFLVLD 380 EADGLLSQGY 390 SDFINRMHNQ 400 IPQVTSDGKR 410 LQVIVCSATL 420 HSFDVKKLSE 430 KIMHFPTWVD 440 LKGEDSVPDT 450 VHHVVVPVNP 460 KTDRLWERLG 470 KSHIRTDDVH 480 AKDNTRPGAN 490 SPEMWSEAIK 500 ILKGEYAVRA 510 IKEHKMDQAI 520 IFCRTKIDCD 530 NLEQYFIQQG 540 GGPDKKGHQF 550 SCVCLHGDRK 560 PHERKQNLER 570 FKKGDVRFLI 580 CTDVAARGID 590 IHGVPYVINV 600 TLPDEKQNYV 610 HRIGRVGRAE 620 RMGLAISLVA 630 TEKEKVWYHV 640 CSSRGKGCYN 650 TRLKEDGGCT 660 IWYNEMQLLS 670 EIEEHLNCTI 680 SQVEPDIKVP 690 VDEFDGKVTY 700 GQKRAAGGGS 710 YKGHVDILAP 720 TVQELAALEK 730 EAQTSFLHLG 740 YLPNQLFRTF

Gene Ontology

Classification GO ID Description
Cellular Component GO:0071920 cleavage body
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0010494 cytoplasmic stress granule
Cellular Component GO:0005829 cytosol
Cellular Component GO:0016020 membrane
Cellular Component GO:0005739 mitochondrion
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:1990904 ribonucleoprotein complex
Cellular Component GO:0072669 tRNA-splicing ligase complex
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0016887 ATP hydrolysis activity
Molecular Function GO:0003682 chromatin binding
Molecular Function GO:0003677 DNA binding
Molecular Function GO:0033677 DNA/RNA helicase activity
Molecular Function GO:0003725 double-stranded RNA binding
Molecular Function GO:0004527 exonuclease activity
Molecular Function GO:0004518 nuclease activity
Molecular Function GO:0008143 poly(A) binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0003724 RNA helicase activity
Molecular Function GO:0003712 transcription coregulator activity
Biological Process GO:0051607 defense response to virus
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0006302 double-strand break repair
Biological Process GO:0045087 innate immune response
Biological Process GO:0043123 positive regulation of canonical NF-kappaB signal transduction
Biological Process GO:0002735 positive regulation of myeloid dendritic cell cytokine production
Biological Process GO:1903608 protein localization to cytoplasmic stress granule
Biological Process GO:0006446 regulation of translational initiation
Biological Process GO:0000245 spliceosomal complex assembly
Biological Process GO:0006388 tRNA splicing, via endonucleolytic cleavage and ligation

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] 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.

[5] 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.