Search Results

Overview

Uniprot ID	Q08211
Protein Name	ATP-dependent RNA helicase A
Gene Name	DHX9
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
1011	CYHKEKRKILTTEGR
1024	GRNALIHKSSVNCPF
1163	GDGPRPPKMARYDNG
14	FLYAWCGKRKMTPSY
146	WDRGANLKDYYSRKE
16	YAWCGKRKMTPSYEI
191	RLNQYFQKEKIQGEY
193	NQYFQKEKIQGEYKY
236	REHGSNKKLAAQSCA
264	EAYSGLTKKKEGETV
29	EIRAVGNKNRQKFMC
497	TVGVLLRKLEAGIRG
697	IPREEQRKVFDPVPV

Function

Multifunctional ATP-dependent nucleic acid helicase that unwinds DNA and RNA in a 3' to 5' direction and that plays important roles in many processes, such as DNA replication, transcriptional activation, post-transcriptional RNA regulation, mRNA translation and RNA-mediated gene silencing (PubMed:11416126, PubMed:12711669, PubMed:15355351, PubMed:16680162, PubMed:17531811, PubMed:20669935, PubMed:21561811, PubMed:24049074, PubMed:24990949, PubMed:25062910, PubMed:28221134, PubMed:9111062, PubMed:37467750). Requires a 3'-single-stranded tail as entry site for acid nuclei unwinding activities as well as the binding and hydrolyzing of any of the four ribo- or deoxyribo-nucleotide triphosphates (NTPs) (PubMed:1537828). Unwinds numerous nucleic acid substrates such as double-stranded (ds) DNA and RNA, DNA:RNA hybrids, DNA and RNA forks composed of either partially complementary DNA duplexes or DNA:RNA hybrids, respectively, and also DNA and RNA displacement loops (D- and R-loops), triplex-helical DNA (H-DNA) structure and DNA and RNA-based G-quadruplexes (PubMed:20669935, PubMed:21561811, PubMed:24049074). Binds dsDNA, single-stranded DNA (ssDNA), dsRNA, ssRNA and poly(A)-containing RNA (PubMed:10198287, PubMed:9111062). Also binds to circular dsDNA or dsRNA of either linear and/or circular forms and stimulates the relaxation of supercoiled DNAs catalyzed by topoisomerase TOP2A (PubMed:12711669). Plays a role in DNA replication at origins of replication and cell cycle progression (PubMed:24990949). Plays a role as a transcriptional coactivator acting as a bridging factor between polymerase II holoenzyme and transcription factors or cofactors, such as BRCA1, CREBBP, RELA and SMN1 (PubMed:11038348, PubMed:11149922, PubMed:11416126, PubMed:15355351, PubMed:28221134, PubMed:9323138, PubMed:9662397). Binds to the CDKN2A promoter (PubMed:11038348). Plays several roles in post-transcriptional regulation of gene expression (PubMed:28221134, PubMed:28355180). In cooperation with NUP98, promotes pre-mRNA alternative splicing activities of a subset of genes (PubMed:11402034, PubMed:16680162, PubMed:28221134, PubMed:28355180). As component of a large PER complex, is involved in the negative regulation of 3' transcriptional termination of circadian target genes such as PER1 and NR1D1 and the control of the circadian rhythms (By similarity). Also acts as a nuclear resolvase that is able to bind and neutralize harmful massive secondary double-stranded RNA structures formed by inverted-repeat Alu retrotransposon elements that are inserted and transcribed as parts of genes during the process of gene transposition (PubMed:28355180). Involved in the positive regulation of nuclear export of constitutive transport element (CTE)-containing unspliced mRNA (PubMed:10924507, PubMed:11402034, PubMed:9162007). Component of the coding region determinant (CRD)-mediated complex that promotes cytoplasmic MYC mRNA stability (PubMed:19029303). Plays a role in mRNA translation (PubMed:28355180). Positively regulates translation of selected mRNAs through its binding to post-transcriptional control element (PCE) in the 5'-untranslated region (UTR) (PubMed:16680162). Involved with LARP6 in the translation stimulation of type I collagen mRNAs for CO1A1 and CO1A2 through binding of a specific stem-loop structure in their 5'-UTRs (PubMed:22190748). Stimulates LIN28A-dependent mRNA translation probably by facilitating ribonucleoprotein remodeling during the process of translation (PubMed:21247876). Plays also a role as a small interfering (siRNA)-loading factor involved in the RNA-induced silencing complex (RISC) loading complex (RLC) assembly, and hence functions in the RISC-mediated gene silencing process (PubMed:17531811). Binds preferentially to short double-stranded RNA, such as those produced during rotavirus intestinal infection (PubMed:28636595). This interaction may mediate NLRP9 inflammasome activation and trigger inflammatory response, including IL18 release and pyroptosis (PubMed:28636595). Finally, mediates the attachment of heterogeneous nuclear ribonucleoproteins (hnRNPs) to actin filaments in the nucleus (PubMed:11687588)

Protein Sequence

10 MGDVKNFLYA 20 WCGKRKMTPS 30 YEIRAVGNKN 40 RQKFMCEVQV 50 EGYNYTGMGN 60 STNKKDAQSN 70 AARDFVNYLV 80 RINEIKSEEV 90 PAFGVASPPP 100 LTDTPDTTAN 110 AEGDLPTTMG 120 GPLPPHLALK 130 AENNSEVGAS 140 GYGVPGPTWD 150 RGANLKDYYS 160 RKEEQEVQAT 170 LESEEVDLNA 180 GLHGNWTLEN 190 AKARLNQYFQ 200 KEKIQGEYKY 210 TQVGPDHNRS 220 FIAEMTIYIK 230 QLGRRIFARE 240 HGSNKKLAAQ 250 SCALSLVRQL 260 YHLGVVEAYS 270 GLTKKKEGET 280 VEPYKVNLSQ 290 DLEHQLQNII 300 QELNLEILPP 310 PEDPSVPVAL 320 NIGKLAQFEP 330 SQRQNQVGVV 340 PWSPPQSNWN 350 PWTSSNIDEG 360 PLAFATPEQI 370 SMDLKNELMY 380 QLEQDHDLQA 390 ILQERELLPV 400 KKFESEILEA 410 ISQNSVVIIR 420 GATGCGKTTQ 430 VPQFILDDFI 440 QNDRAAECNI 450 VVTQPRRISA 460 VSVAERVAFE 470 RGEEPGKSCG 480 YSVRFESILP 490 RPHASIMFCT 500 VGVLLRKLEA 510 GIRGISHVIV 520 DEIHERDINT 530 DFLLVVLRDV 540 VQAYPEVRIV 550 LMSATIDTSM 560 FCEYFFNCPI 570 IEVYGRTYPV 580 QEYFLEDCIQ 590 MTHFVPPPKD 600 KKKKDKDDDG 610 GEDDDANCNL 620 ICGDEYGPET 630 RLSMSQLNEK 640 ETPFELIEAL 650 LKYIETLNVP 660 GAVLVFLPGW 670 NLIYTMQKHL 680 EMNPHFGSHR 690 YQILPLHSQI 700 PREEQRKVFD 710 PVPVGVTKVI 720 LSTNIAETSI 730 TINDVVYVID 740 SCKQKVKLFT 750 AHNNMTNYAT 760 VWASKTNLEQ 770 RKGRAGRVRP 780 GFCFHLCSRA 790 RFERLETHMT 800 PEMFRTPLHE 810 IALSIKLLRL 820 GGIGQFLAKA 830 IEPPPLDAVI 840 EAEHTLRELD 850 ALDANDELTP 860 LGRILAKLPI 870 EPRFGKMMIM 880 GCIFYVGDAI 890 CTIAAATCFP 900 EPFINEGKRL 910 GYIHRNFAGN 920 RFSDHVALLS 930 VFQAWDDARM 940 GGEEAEIRFC 950 EHKRLNMATL 960 RMTWEAKVQL 970 KEILINSGFP 980 EDCLLTQVFT 990 NTGPDNNLDV 1000 VISLLAFGVY 1010 PNVCYHKEKR 1020 KILTTEGRNA 1030 LIHKSSVNCP 1040 FSSQDMKYPS 1050 PFFVFGEKIR 1060 TRAISAKGMT 1070 LVTPLQLLLF 1080 ASKKVQSDGQ 1090 IVLVDDWIKL 1100 QISHEAAACI 1110 TGLRAAMEAL 1120 VVEVTKQPAI 1130 ISQLDPVNER 1140 MLNMIRQISR 1150 PSAAGINLMI 1160 GSTRYGDGPR 1170 PPKMARYDNG 1180 SGYRRGGSSY 1190 SGGGYGGGYS 1200 SGGYGSGGYG 1210 GSANSFRAGY 1220 GAGVGGGYRG 1230 VSRGGFRGNS 1240 GGDYRGPSGG 1250 YRGSGGFQRG 1260 GGRGAYGTGY 1270 FGQGRGGGGY

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0097165	nuclear stress granule
Cellular Component	GO:0015629	actin cytoskeleton
Cellular Component	GO:0005813	centrosome
Cellular Component	GO:0070937	CRD-mediated mRNA stability complex
Cellular Component	GO:0005737	cytoplasm
Cellular Component	GO:0036464	cytoplasmic ribonucleoprotein granule
Cellular Component	GO:0005829	cytosol
Cellular Component	GO:0016020	membrane
Cellular Component	GO:0016604	nuclear body
Biological Process	GO:0048511	rhythmic process
Biological Process	GO:0070922	RISC complex assembly
Cellular Component	GO:0005730	nucleolus
Cellular Component	GO:0005654	nucleoplasm
Cellular Component	GO:0005634	nucleus
Cellular Component	GO:0005726	perichromatin fibrils
Cellular Component	GO:0032991	protein-containing complex
Cellular Component	GO:1990904	ribonucleoprotein complex
Cellular Component	GO:0016442	RISC complex
Cellular Component	GO:0070578	RISC-loading complex
Molecular Function	GO:0043138	3'-5' DNA helicase activity
Molecular Function	GO:0033679	3'-5' DNA/RNA helicase activity
Molecular Function	GO:0034458	3'-5' RNA helicase activity
Molecular Function	GO:0005524	ATP binding
Molecular Function	GO:0016887	ATP hydrolysis activity
Molecular Function	GO:0031490	chromatin DNA binding
Molecular Function	GO:0003677	DNA binding
Molecular Function	GO:0003678	DNA helicase activity
Molecular Function	GO:0003688	DNA replication origin binding
Molecular Function	GO:0003690	double-stranded DNA binding
Molecular Function	GO:0003725	double-stranded RNA binding
Molecular Function	GO:0160225	G-quadruplex unwinding activity
Molecular Function	GO:0061676	importin-alpha family protein binding
Molecular Function	GO:0046872	metal ion binding
Molecular Function	GO:0003729	mRNA binding
Molecular Function	GO:0047429	nucleoside triphosphate diphosphatase activity
Molecular Function	GO:1990841	promoter-specific chromatin binding
Molecular Function	GO:0001069	regulatory region RNA binding
Molecular Function	GO:0017111	ribonucleoside triphosphate phosphatase activity
Molecular Function	GO:0043022	ribosome binding
Molecular Function	GO:1905172	RISC complex binding
Molecular Function	GO:0003723	RNA binding
Molecular Function	GO:0003724	RNA helicase activity
Molecular Function	GO:0070063	RNA polymerase binding
Molecular Function	GO:0000978	RNA polymerase II cis-regulatory region sequence-specific DNA binding
Molecular Function	GO:0000993	RNA polymerase II complex binding
Molecular Function	GO:0061629	RNA polymerase II-specific DNA-binding transcription factor binding
Molecular Function	GO:0035613	RNA stem-loop binding
Molecular Function	GO:1990825	sequence-specific mRNA binding
Molecular Function	GO:1990518	single-stranded 3'-5' DNA helicase activity
Molecular Function	GO:0003697	single-stranded DNA binding
Molecular Function	GO:0003727	single-stranded RNA binding
Molecular Function	GO:0035197	siRNA binding
Molecular Function	GO:0003713	transcription coactivator activity
Molecular Function	GO:0003712	transcription coregulator activity
Molecular Function	GO:0045142	triplex DNA binding
Biological Process	GO:0000380	alternative mRNA splicing, via spliceosome
Biological Process	GO:0071360	cellular response to exogenous dsRNA
Biological Process	GO:0006325	chromatin organization
Biological Process	GO:0070934	CRD-mediated mRNA stabilization
Biological Process	GO:0006260	DNA replication
Biological Process	GO:0006353	DNA-templated transcription termination
Biological Process	GO:0039695	DNA-templated viral transcription
Biological Process	GO:0045087	innate immune response
Biological Process	GO:0035195	miRNA-mediated post-transcriptional gene silencing
Biological Process	GO:0051028	mRNA transport
Biological Process	GO:1900152	negative regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay
Biological Process	GO:0001649	osteoblast differentiation
Biological Process	GO:2000767	positive regulation of cytoplasmic translation
Biological Process	GO:0045739	positive regulation of DNA repair
Biological Process	GO:0045740	positive regulation of DNA replication
Biological Process	GO:0048146	positive regulation of fibroblast proliferation
Biological Process	GO:0050729	positive regulation of inflammatory response
Biological Process	GO:0045089	positive regulation of innate immune response
Biological Process	GO:0032727	positive regulation of interferon-alpha production
Biological Process	GO:0032728	positive regulation of interferon-beta production
Biological Process	GO:0032741	positive regulation of interleukin-18 production
Biological Process	GO:0032755	positive regulation of interleukin-6 production
Biological Process	GO:0060760	positive regulation of response to cytokine stimulus
Biological Process	GO:0046833	positive regulation of RNA export from nucleus
Biological Process	GO:0045944	positive regulation of transcription by RNA polymerase II
Biological Process	GO:0032760	positive regulation of tumor necrosis factor production
Biological Process	GO:0050434	positive regulation of viral transcription
Biological Process	GO:1903608	protein localization to cytoplasmic stress granule
Biological Process	GO:0065003	protein-containing complex assembly
Biological Process	GO:0070269	pyroptotic inflammatory response
Biological Process	GO:2000765	regulation of cytoplasmic translation
Biological Process	GO:0050691	regulation of defense response to virus by host
Biological Process	GO:0050684	regulation of mRNA processing
Biological Process	GO:0006357	regulation of transcription by RNA polymerase II

Reference

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[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.

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[5] 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.

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[7] 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.

[8] 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.

[9] 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.

[10] 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.

[11] 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.