Search Results

Overview

Uniprot IDQ9NR30
Protein NameNucleolar RNA helicase 2
Gene NameDDX21
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
113 VVSSKTKKVTKNEEP
116 SKTKKVTKNEEPSEE
131 EIDAPKPKKMKKEKE
132 IDAPKPKKMKKEKEM
18 LESDTAMKKGETLRK
19 ESDTAMKKGETLRKQ
402 EQVDLIGKKTQKTAI
403 QVDLIGKKTQKTAIT
406 LIGKKTQKTAITVEH
54 EEETVFPKAKQVKKK
56 ETVFPKAKQVKKKAE
60 PKAKQVKKKAEPSEV
61 KAKQVKKKAEPSEVD
678 GMVFLKGKLGVCFDV
73 EVDMNSPKSKKAKKK
779 GQKRSFSKAFGQ***
79 PKSKKAKKKEEPSQN
80 KSKKAKKKEEPSQND
91 SQNDISPKTKSLRKK
93 NDISPKTKSLRKKKE

Function

RNA helicase that acts as a sensor of the transcriptional status of both RNA polymerase (Pol) I and II: promotes ribosomal RNA (rRNA) processing and transcription from polymerase II (Pol II) (PubMed:25470060, PubMed:28790157). Binds various RNAs, such as rRNAs, snoRNAs, 7SK and, at lower extent, mRNAs (PubMed:25470060). In the nucleolus, localizes to rDNA locus, where it directly binds rRNAs and snoRNAs, and promotes rRNA transcription, processing and modification. Required for rRNA 2'-O-methylation, possibly by promoting the recruitment of late-acting snoRNAs SNORD56 and SNORD58 with pre-ribosomal complexes (PubMed:25470060, PubMed:25477391). In the nucleoplasm, binds 7SK RNA and is recruited to the promoters of Pol II-transcribed genes: acts by facilitating the release of P-TEFb from inhibitory 7SK snRNP in a manner that is dependent on its helicase activity, thereby promoting transcription of its target genes (PubMed:25470060). Functions as a cofactor for JUN-activated transcription: required for phosphorylation of JUN at 'Ser-77' (PubMed:11823437, PubMed:25260534). Can unwind double-stranded RNA (helicase) and can fold or introduce a secondary structure to a single-stranded RNA (foldase) (PubMed:9461305). Together with SIRT7, required to prevent R-loop-associated DNA damage and transcription-associated genomic instability: deacetylation by SIRT7 activates the helicase activity, thereby overcoming R-loop-mediated stalling of RNA polymerases (PubMed:28790157). Involved in rRNA processing (PubMed:14559904, PubMed:18180292). May bind to specific miRNA hairpins (PubMed:28431233). 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 (By similarity)

Protein Sequence

10 MPGKLRSDAG 20 LESDTAMKKG 30 ETLRKQTEEK 40 EKKEKPKSDK 50 TEEIAEEEET 60 VFPKAKQVKK 70 KAEPSEVDMN 80 SPKSKKAKKK 90 EEPSQNDISP 100 KTKSLRKKKE 110 PIEKKVVSSK 120 TKKVTKNEEP 130 SEEEIDAPKP 140 KKMKKEKEMN 150 GETREKSPKL 160 KNGFPHPEPD 170 CNPSEAASEE 180 SNSEIEQEIP 190 VEQKEGAFSN 200 FPISEETIKL 210 LKGRGVTFLF 220 PIQAKTFHHV 230 YSGKDLIAQA 240 RTGTGKTFSF 250 AIPLIEKLHG 260 ELQDRKRGRA 270 PQVLVLAPTR 280 ELANQVSKDF 290 SDITKKLSVA 300 CFYGGTPYGG 310 QFERMRNGID 320 ILVGTPGRIK 330 DHIQNGKLDL 340 TKLKHVVLDE 350 VDQMLDMGFA 360 DQVEEILSVA 370 YKKDSEDNPQ 380 TLLFSATCPH 390 WVFNVAKKYM 400 KSTYEQVDLI 410 GKKTQKTAIT 420 VEHLAIKCHW 430 TQRAAVIGDV 440 IRVYSGHQGR 450 TIIFCETKKE 460 AQELSQNSAI 470 KQDAQSLHGD 480 IPQKQREITL 490 KGFRNGSFGV 500 LVATNVAARG 510 LDIPEVDLVI 520 QSSPPKDVES 530 YIHRSGRTGR 540 AGRTGVCICF 550 YQHKEEYQLV 560 QVEQKAGIKF 570 KRIGVPSATE 580 IIKASSKDAI 590 RLLDSVPPTA 600 ISHFKQSAEK 610 LIEEKGAVEA 620 LAAALAHISG 630 ATSVDQRSLI 640 NSNVGFVTMI 650 LQCSIEMPNI 660 SYAWKELKEQ 670 LGEEIDSKVK 680 GMVFLKGKLG 690 VCFDVPTASV 700 TEIQEKWHDS 710 RRWQLSVATE 720 QPELEGPREG 730 YGGFRGQREG 740 SRGFRGQRDG 750 NRRFRGQREG 760 SRGPRGQRSG 770 GGNKSNRSQN 780 KGQKRSFSKA FGQ

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005694 chromosome
Cellular Component GO:0005829 cytosol
Cellular Component GO:0016020 membrane
Cellular Component GO:0005739 mitochondrion
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005654 nucleoplasm
Molecular Function GO:0097322 7SK snRNA binding
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0016887 ATP hydrolysis activity
Molecular Function GO:0003725 double-stranded RNA binding
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0035198 miRNA binding
Molecular Function GO:0003729 mRNA binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0003724 RNA helicase activity
Molecular Function GO:0140870 RNA polymerase inhibitor activity
Molecular Function GO:0019843 rRNA binding
Molecular Function GO:0030515 snoRNA binding
Biological Process GO:0006338 chromatin remodeling
Biological Process GO:0051607 defense response to virus
Biological Process GO:0045087 innate immune response
Biological Process GO:0016479 negative regulation of transcription by RNA polymerase I
Biological Process GO:0001649 osteoblast differentiation
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:0045943 positive regulation of transcription by RNA polymerase I
Biological Process GO:0045944 positive regulation of transcription by RNA polymerase II
Biological Process GO:0045945 positive regulation of transcription by RNA polymerase III
Biological Process GO:0062176 R-loop processing
Biological Process GO:0006364 rRNA processing
Biological Process GO:0006366 transcription by RNA polymerase II

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] 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.

[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.