DDX42
entrez
11325
canonical
uniprot
Q86XP3
canonical
ensembl
ENSG00000198231
resolver
ensp
ENSP00000374574
resolver
ensp
ENSP00000464050
resolver
ensp
ENSP00000548583
resolver
ensp
ENSP00000548585
resolver
genesymbol
DDX42
resolver
hgnc
HGNC:18676
resolver
uniprot
A6NML1
resolver
uniprot
A8KA43
resolver
uniprot
O75619
resolver
uniprot
Q68G51
resolver
uniprot
Q96BK1
resolver
uniprot
Q96HR7
resolver
uniprot
Q9Y3V8
resolver
uniprot_entry
DDX42_HUMAN
resolver
uniprot_sec
A6NML1
resolver
uniprot_sec
A8KA43
resolver
uniprot_sec
O75619
resolver
uniprot_sec
Q68G51
resolver
uniprot_sec
Q96BK1
resolver
uniprot_sec
Q96HR7
resolver
uniprot_sec
Q9Y3V8
resolver
amino_acid_sequence
MNWNKGGPGTKRGFGFGGFAISAGKKEEPKLPQQSHSAFGATSSSSGFGKSAPPQLPSFYKIGSKRANFDEENAYFEDEEEDSSNVDLPYIPAENSPTRQQFHSKPVDSDSDDDPLEAFMAEVEDQAARDMKRLEEKDKERKNVKGIRDDIEEEDDQEAYFRYMAENPTAGVVQEEEEDNLEYDSDGNPIAPTKKIIDPLPPIDHSEIDYPPFEKNFYNEHEEITNLTPQQLIDLRHKLNLRVSGAAPPRPGSSFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDGPIAVIVCPTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVVQGDIGEANEDVTQIVEILHSGPSKWNWLTRRLVEFTSSGSVLLFVTKKANAEELANNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDIDTHTHRIGRTGRAGEKGVAYTLLTPKDSNFAGDLVRNLEGANQHVSKELLDLAMQNAWFRKSRFKGGKGKKLNIGGGGLGYRERPGLGSENMDRGNNNVMSNYEAYKPSTGAMGDRLTAMKAAFQSQYKSHFVAASLSNQKAGSSAAGASGWTSAGSLNSVPTNSAQQGHNSPDSPVTSAAKGIPGFGNTGNISGAPVTYPSAGAQGVNNTASGNNSREGTGGSNGKRERYTENRGSSRHSHGETGNRHSDSPRHGDGGRHGDGYRHPESSSRHTDGHRHGENRHGGSAGRHGENRGANDGRNGESRKEAFNRESKMEPKMEPKVDSSKMDKVDSKTDKTADGFAVPEPPKRKKSRWDS
uniprot
proteins
ec_number
3.6.4.13
uniprot
proteins
function
FUNCTION: ATP-dependent RNA helicase that binds to partially double-stranded RNAs (dsRNAs) in order to unwind RNA secondary structures (PubMed:16397294). Unwinding is promoted in the presence of single-strand binding proteins (PubMed:16397294). Also mediates RNA duplex formation thereby displacing the single-strand RNA binding protein (PubMed:16397294). ATP and ADP modulate its activity: ATP binding and hydrolysis by DDX42 triggers RNA strand separation, whereas the ADP-bound form of the protein triggers annealing of complementary RNA strands (PubMed:16397294). Required for assembly of the 17S U2 SnRNP complex of the spliceosome, a large ribonucleoprotein complex that removes introns from transcribed pre-mRNAs: DDX42 associates transiently with the SF3B subcomplex of the 17S U2 SnRNP complex and is released after fulfilling its role in the assembly of 17S U2 SnRNP (PubMed:12234937, PubMed:36797247). Involved in the survival of cells by interacting with TP53BP2 and thereby counteracting the apoptosis-stimulating activity of TP53BP2 (PubMed:19377511). Relocalizes TP53BP2 to the cytoplasm (PubMed:19377511). {ECO:0000269|PubMed:12234937, ECO:0000269|PubMed:16397294, ECO:0000269|PubMed:19377511, ECO:0000269|PubMed:36797247}.
uniprot
proteins
mass_dalton
102975
uniprot
proteins
protein_family
DDX42 subfamily
uniprot
proteins
protein_family
DEAD box helicase family
uniprot
proteins
pubmed
10727850
uniprot
proteins
pubmed
12234937
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16397294
uniprot
proteins
pubmed
16625196
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19377511
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
23186163
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
36797247
uniprot
proteins
sequence_length
938
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19377511}. Nucleus {ECO:0000269|PubMed:16397294, ECO:0000269|PubMed:19377511}.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus, Cajal body {ECO:0000269|PubMed:12234937}. Nucleus speckle {ECO:0000269|PubMed:12234937}.
uniprot
proteins