DHX15
entrez
1665
canonical
uniprot
O43143
canonical
ensembl
ENSG00000109606
resolver
ensp
ENSP00000336741
resolver
ensp
ENSP00000649386
resolver
ensp
ENSP00000649387
resolver
enst
ENST00000336812
resolver
genesymbol
DHX15
resolver
genesymbol_syn
DBP1
resolver
genesymbol_syn
DDX15
resolver
hgnc
HGNC:2738
resolver
uniprot
Q9NQT7
resolver
uniprot_entry
DHX15_HUMAN
resolver
uniprot_sec
Q9NQT7
resolver
activity_regulation
ACTIVITY REGULATION: ATPase activity is enhanced upon binding to G-patch domain-containing proteins (PubMed:32179686). G-patch domain-containing proteins act like a brace that tethers mobile sections of DHX15 together, stabilizing a functional conformation with high RNA affinity, thereby promoting the ATPase activity (PubMed:32179686). {ECO:0000269|PubMed:32179686}.
uniprot
proteins
amino_acid_sequence
MSKRHRLDLGEDYPSGKKRAGTDGKDRDRDRDREDRSKDRDRERDRGDREREREKEKEKELRASTNAMLISAGLPPLKASHSAHSTHSAHSTHSTHSAHSTHAGHAGHTSLPQCINPFTNLPHTPRYYDILKKRLQLPVWEYKDRFTDILVRHQSFVLVGETGSGKTTQIPQWCVEYMRSLPGPKRGVACTQPRRVAAMSVAQRVADEMDVMLGQEVGYSIRFEDCSSAKTILKYMTDGMLLREAMNDPLLERYGVIILDEAHERTLATDILMGVLKEVVRQRSDLKVIVMSATLDAGKFQIYFDNCPLLTIPGRTHPVEIFYTPEPERDYLEAAIRTVIQIHMCEEEEGDLLLFLTGQEEIDEACKRIKREVDDLGPEVGDIKIIPLYSTLPPQQQQRIFEPPPPKKQNGAIGRKVVVSTNIAETSLTIDGVVFVIDPGFAKQKVYNPRIRVESLLVTAISKASAQQRAGRAGRTRPGKCFRLYTEKAYKTEMQDNTYPEILRSNLGSVVLQLKKLGIDDLVHFDFMDPPAPETLMRALELLNYLAALNDDGDLTELGSMMAEFPLDPQLAKMVIASCDYNCSNEVLSITAMLSVPQCFVRPTEAKKAADEAKMRFAHIDGDHLTLLNVYHAFKQNHESVQWCYDNFINYRSLMSADNVRQQLSRIMDRFNLPRRSTDFTSRDYYINIRKALVTGYFMQVAHLERTGHYLTVKDNQVVQLHPSTVLDHKPEWVLYNEFVLTTKNYIRTCTDIKPEWLVKIAPQYYDMSNFPQCEAKRQLDRIIAKLQSKEYSQY
uniprot
proteins
ec_number
3.6.4.13
uniprot
proteins
function
FUNCTION: RNA helicase involved in mRNA processing and antiviral innate immunity (PubMed:19103666, PubMed:19432882, PubMed:24782566, PubMed:24990078, PubMed:32179686, PubMed:34161762). Pre-mRNA processing factor involved in disassembly of spliceosomes after the release of mature mRNA (PubMed:19103666). In cooperation with TFIP11 seem to be involved in the transition of the U2, U5 and U6 snRNP-containing IL complex to the snRNP-free IS complex leading to efficient debranching and turnover of excised introns (PubMed:19103666). Plays a key role in antiviral innate immunity by promoting both MAVS-dependent signaling and NLRP6 inflammasome (PubMed:24782566, PubMed:24990078, PubMed:34161762). Acts as an RNA virus sensor: recognizes and binds viral double stranded RNA (dsRNA) and activates the MAVS-dependent signaling to produce interferon-beta and interferon lambda-3 (IFNL3) (PubMed:24782566, PubMed:24990078, PubMed:34161762). Involved in intestinal antiviral innate immunity together with NLRP6: recognizes and binds viral dsRNA and promotes activation of the NLRP6 inflammasome in intestinal epithelial cells to restrict infection by enteric viruses (PubMed:34161762). The NLRP6 inflammasome acts by promoting maturation and secretion of IL18 in the extracellular milieu (PubMed:34161762). Also involved in antibacterial innate immunity by promoting Wnt-induced antimicrobial protein expression in Paneth cells (By similarity). {ECO:0000250|UniProtKB:O35286, ECO:0000269|PubMed:19103666, ECO:0000269|PubMed:19432882, ECO:0000269|PubMed:24782566, ECO:0000269|PubMed:24990078, ECO:0000269|PubMed:32179686, ECO:0000269|PubMed:34161762}.
uniprot
proteins
mass_dalton
90933
uniprot
proteins
mutagenesis
MUTAGEN 166; /note="K->A: Abolished ATPase activity without affecting ability to activate the MAVS-dependent signaling to produce interferon-beta."; /evidence="ECO:0000269|PubMed:24782566, ECO:0000269|PubMed:24990078"; MUTAGEN 167; /note="T->A: Abolished ATPase activity without affecting ability to activate the MAVS-dependent signaling to produce interferon-beta."; /evidence="ECO:0000269|PubMed:24782566, ECO:0000269|PubMed:24990078"; MUTAGEN 260; /note="D->A: Abolished ATPase activity without affecting ability to activate the MAVS-dependent signaling to produce interferon-beta."; /evidence="ECO:0000269|PubMed:24782566, ECO:0000269|PubMed:24990078"; MUTAGEN 261; /note="E->A: Abolished ATPase activity without affecting ability to activate the MAVS-dependent signaling to produce interferon-beta."; /evidence="ECO:0000269|PubMed:24782566, ECO:0000269|PubMed:24990078"; MUTAGEN 327; /note="P->E: Abolished interaction with NKRF."; /evidence="ECO:0000269|PubMed:32179686"; MUTAGEN 429; /note="T->A: Abolished ATPase activity."; /evidence="ECO:0000269|PubMed:30728453"; MUTAGEN 485; /note="Y->E: Abolished interaction with NKRF."; /evidence="ECO:0000269|PubMed:32179686"; MUTAGEN 489; /note="A->E: Decreased, but not abolished interaction, with NKRF."; /evidence="ECO:0000269|PubMed:32179686"; MUTAGEN 523; /note="V->E: Abolished interaction with NKRF."; /evidence="ECO:0000269|PubMed:32179686"; MUTAGEN 533; /note="P->E: Abolished interaction with NKRF."; /evidence="ECO:0000269|PubMed:32179686"; MUTAGEN 536; /note="L->E: Abolished interaction with NKRF."; /evidence="ECO:0000269|PubMed:32179686"; MUTAGEN 540; /note="L->E: Abolished interaction with NKRF."; /evidence="ECO:0000269|PubMed:32179686
uniprot
proteins
protein_family
DDX15/PRP43 sub-subfamily
uniprot
proteins
protein_family
DEAD box helicase family
uniprot
proteins
protein_family
DEAH subfamily
uniprot
proteins
pubmed
12458796
uniprot
proteins
pubmed
14654843
uniprot
proteins
pubmed
15146077
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
19103666
uniprot
proteins
pubmed
19432882
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22002106
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24782566
uniprot
proteins
pubmed
24990078
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
28580923
uniprot
proteins
pubmed
30728453
uniprot
proteins
pubmed
32179686
uniprot
proteins
pubmed
34161762
uniprot
proteins
pubmed
9388478
uniprot
proteins
sequence_length
795
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12458796}. Nucleus, nucleolus {ECO:0000269|PubMed:12458796}.
uniprot
proteins