DDX21
entrez
9188
canonical
uniprot
Q9NR30
canonical
ensembl
ENSG00000165732
resolver
ensp
ENSP00000346120
resolver
ensp
ENSP00000480334
resolver
ensp
ENSP00000510328
resolver
enst
ENST00000685106
resolver
genesymbol
DDX21
resolver
hgnc
HGNC:2744
resolver
uniprot
A0A8I5KYZ4
resolver
uniprot
B2RDL0
resolver
uniprot
Q13436
resolver
uniprot
Q5VX41
resolver
uniprot
Q68D35
resolver
uniprot_entry
A0A8I5KYZ4_HUMAN
resolver
uniprot_entry
DDX21_HUMAN
resolver
uniprot_sec
B2RDL0
resolver
uniprot_sec
Q13436
resolver
uniprot_sec
Q5VX41
resolver
uniprot_sec
Q68D35
resolver
activity_regulation
ACTIVITY REGULATION: Acetylation inhibits the helicase activity. {ECO:0000269|PubMed:28790157}.
uniprot
proteins
amino_acid_sequence
MPGKLRSDAGLESDTAMKKGETLRKQTEEKEKKEKPKSDKTEEIAEEEETVFPKAKQVKKKAEPSEVDMNSPKSKKAKKKEEPSQNDISPKTKSLRKKKEPIEKKVVSSKTKKVTKNEEPSEEEIDAPKPKKMKKEKEMNGETREKSPKLKNGFPHPEPDCNPSEAASEESNSEIEQEIPVEQKEGAFSNFPISEETIKLLKGRGVTFLFPIQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKLHGELQDRKRGRAPQVLVLAPTRELANQVSKDFSDITKKLSVACFYGGTPYGGQFERMRNGIDILVGTPGRIKDHIQNGKLDLTKLKHVVLDEVDQMLDMGFADQVEEILSVAYKKDSEDNPQTLLFSATCPHWVFNVAKKYMKSTYEQVDLIGKKTQKTAITVEHLAIKCHWTQRAAVIGDVIRVYSGHQGRTIIFCETKKEAQELSQNSAIKQDAQSLHGDIPQKQREITLKGFRNGSFGVLVATNVAARGLDIPEVDLVIQSSPPKDVESYIHRSGRTGRAGRTGVCICFYQHKEEYQLVQVEQKAGIKFKRIGVPSATEIIKASSKDAIRLLDSVPPTAISHFKQSAEKLIEEKGAVEALAAALAHISGATSVDQRSLINSNVGFVTMILQCSIEMPNISYAWKELKEQLGEEIDSKVKGMVFLKGKLGVCFDVPTASVTEIQEKWHDSRRWQLSVATEQPELEGPREGYGGFRGQREGSRGFRGQRDGNRRFRGQREGSRGPRGQRSGGGNKSNRSQNKGQKRSFSKAFGQ
uniprot
proteins
ec_number
3.6.4.13
uniprot
proteins
function
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). {ECO:0000250|UniProtKB:Q9JIK5, ECO:0000269|PubMed:11823437, ECO:0000269|PubMed:14559904, ECO:0000269|PubMed:18180292, ECO:0000269|PubMed:25260534, ECO:0000269|PubMed:25470060, ECO:0000269|PubMed:25477391, ECO:0000269|PubMed:28431233, ECO:0000269|PubMed:28790157, ECO:0000269|PubMed:9461305}.
uniprot
proteins
mass_dalton
87344
uniprot
proteins
mutagenesis
MUTAGEN 18; /note="K->Q: Mimics acetylation; impaired ability to resolve R-loops; when associated with Q-137 and Q-600."; /evidence="ECO:0000269|PubMed:28790157"; MUTAGEN 137; /note="K->Q: Mimics acetylation; impaired ability to resolve R-loops; when associated with Q-18 and Q-600."; /evidence="ECO:0000269|PubMed:28790157"; MUTAGEN 339..340; /note="DE->HG: In mutant DEV; loss of helicase activity. Defects in release of P-TEFb from inhibitory 7SK snRNP."; /evidence="ECO:0000269|PubMed:25470060, ECO:0000269|PubMed:28790157, ECO:0000269|PubMed:9461305"; MUTAGEN 375..376; /note="SA->LE: In mutant SAT; ATPase defective. Defects in release of P-TEFb from inhibitory 7SK snRNP."; /evidence="ECO:0000269|PubMed:25470060, ECO:0000269|PubMed:28790157, ECO:0000269|PubMed:9461305"; MUTAGEN 600; /note="K->Q: Mimics acetylation; impaired ability to resolve R-loops; when associated with Q-18 and Q-137."; /evidence="ECO:0000269|PubMed:28790157
uniprot
proteins
post_translational_modification
PTM: Acetylation by CREBBP/CBP inhibits the helicase activity (PubMed:28790157). Deacetylation by SIRT7 promotes the helicase activity and overcomes R-loop-mediated stalling of RNA polymerases (PubMed:28790157). {ECO:0000269|PubMed:28790157}.
uniprot
proteins
protein_family
DDX21/DDX50 subfamily
uniprot
proteins
protein_family
DEAD box helicase family
uniprot
proteins
pubmed
11237763
uniprot
proteins
pubmed
11823437
uniprot
proteins
pubmed
14559904
uniprot
proteins
pubmed
14654843
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15164054
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16603771
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17924679
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18180292
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21536856
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23652018
uniprot
proteins
pubmed
23848194
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25114211
uniprot
proteins
pubmed
25260534
uniprot
proteins
pubmed
25470060
uniprot
proteins
pubmed
25477391
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
28431233
uniprot
proteins
pubmed
28790157
uniprot
proteins
pubmed
34564892
uniprot
proteins
pubmed
38773330
uniprot
proteins
pubmed
8614622
uniprot
proteins
pubmed
9461305
uniprot
proteins
sequence_length
783
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11823437, ECO:0000269|PubMed:18180292, ECO:0000269|PubMed:23848194, ECO:0000269|PubMed:25260534, ECO:0000269|PubMed:25470060, ECO:0000269|PubMed:28790157, ECO:0000269|PubMed:8614622}. Nucleus, nucleoplasm {ECO:0000269|PubMed:11823437, ECO:0000269|PubMed:18180292, ECO:0000269|PubMed:25260534, ECO:0000269|PubMed:25470060, ECO:0000269|PubMed:28790157}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9JIK5}. Mitochondrion {ECO:0000250|UniProtKB:Q9JIK5}. Note=Present both in nucleolus and nucleoplasm. Interaction with JUN promotes translocation from the nucleolus to the nucleoplasm (PubMed:11823437, PubMed:18180292). Interaction with WDR46 is required for localization to the nucleolus (PubMed:23848194). Colocalizes in the cytosol with DDX1, DHX36 and TICAM1. The multi-helicase-TICAM1 complex may translocate to the mitochondria upon poly(I:C) RNA ligand stimulation (By similarity). {ECO:0000250|UniProtKB:Q9JIK5, ECO:0000269|PubMed:11823437, ECO:0000269|PubMed:18180292, ECO:0000269|PubMed:23848194}.
uniprot
proteins