Search Results

Overview

Uniprot IDQ9GZR7
Protein NameATP-dependent RNA helicase DDX24
Gene NameDDX24
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
105 KIKLKKSKNVATEGT
17 PKQSSCGKFQTKGIK
172 PSQSTAAKVPKKAKT
178 AKVPKKAKTWIPEVH
24 KFQTKGIKVVGKWKE
381 DDKSATCKAYPKRPL
71 NPSSLFSKEAPKRKA
77 SKEAPKRKAQAVSEE
835 SALSCLSKQKKKKTK
837 LSCLSKQKKKKTKKP
838 SCLSKQKKKKTKKPK

Function

ATP-dependent RNA helicase that plays a role in various aspects of RNA metabolism including pre-mRNA splicing and is thereby involved in different biological processes such as cell cycle regulation or innate immunity (PubMed:24204270, PubMed:24980433). Plays an inhibitory role in TP53 transcriptional activity and subsequently in TP53 controlled cell growth arrest and senescence by inhibiting its EP300 mediated acetylation (PubMed:25867071). Negatively regulates cytosolic RNA-mediated innate immune signaling at least in part by affecting RIPK1/IRF7 interactions. Alternatively, possesses antiviral activity by recognizing gammaherpesvirus transcripts in the context of lytic reactivation (PubMed:36298642). Plays an essential role in cell cycle regulation in vascular smooth muscle cells by interacting with and regulating FANCA (Fanconi anemia complementation group A) mRNA (By similarity)

Protein Sequence

10 MKLKDTKSRP 20 KQSSCGKFQT 30 KGIKVVGKWK 40 EVKIDPNMFA 50 DGQMDDLVCF 60 EELTDYQLVS 70 PAKNPSSLFS 80 KEAPKRKAQA 90 VSEEEEEEEG 100 KSSSPKKKIK 110 LKKSKNVATE 120 GTSTQKEFEV 130 KDPELEAQGD 140 DMVCDDPEAG 150 EMTSENLVQT 160 APKKKKNKGK 170 KGLEPSQSTA 180 AKVPKKAKTW 190 IPEVHDQKAD 200 VSAWKDLFVP 210 RPVLRALSFL 220 GFSAPTPIQA 230 LTLAPAIRDK 240 LDILGAAETG 250 SGKTLAFAIP 260 MIHAVLQWQK 270 RNAAPPPSNT 280 EAPPGETRTE 290 AGAETRSPGK 300 AEAESDALPD 310 DTVIESEALP 320 SDIAAEARAK 330 TGGTVSDQAL 340 LFGDDDAGEG 350 PSSLIREKPV 360 PKQNENEEEN 370 LDKEQTGNLK 380 QELDDKSATC 390 KAYPKRPLLG 400 LVLTPTRELA 410 VQVKQHIDAV 420 ARFTGIKTAI 430 LVGGMSTQKQ 440 QRMLNRRPEI 450 VVATPGRLWE 460 LIKEKHYHLR 470 NLRQLRCLVV 480 DEADRMVEKG 490 HFAELSQLLE 500 MLNDSQYNPK 510 RQTLVFSATL 520 TLVHQAPARI 530 LHKKHTKKMD 540 KTAKLDLLMQ 550 KIGMRGKPKV 560 IDLTRNEATV 570 ETLTETKIHC 580 ETDEKDFYLY 590 YFLMQYPGRS 600 LVFANSISCI 610 KRLSGLLKVL 620 DIMPLTLHAC 630 MHQKQRLRNL 640 EQFARLEDCV 650 LLATDVAARG 660 LDIPKVQHVI 670 HYQVPRTSEI 680 YVHRSGRTAR 690 ATNEGLSLML 700 IGPEDVINFK 710 KIYKTLKKDE 720 DIPLFPVQTK 730 YMDVVKERIR 740 LARQIEKSEY 750 RNFQACLHNS 760 WIEQAAAALE 770 IELEEDMYKG 780 GKADQQEERR 790 RQKQMKVLKK 800 ELRHLLSQPL 810 FTESQKTKYP 820 TQSGKPPLLV 830 SAPSKSESAL 840 SCLSKQKKKK 850 TKKPKEPQPE QPQPSTSAN

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0016020 membrane
Cellular Component GO:0005730 nucleolus
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:0016070 RNA metabolic process

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] 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.

[3] 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.

[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.