DDX17
entrez
10521
canonical
uniprot
Q92841
canonical
ensembl
ENSG00000100201
resolver
ensp
ENSP00000380033
resolver
ensp
ENSP00000385536
resolver
enst
ENST00000396821
resolver
genesymbol
DDX17
resolver
hgnc
HGNC:2740
resolver
uniprot
A0A5H1ZRQ2
resolver
uniprot
B1AHM0
resolver
uniprot
H3BLZ8
resolver
uniprot
Q59F66
resolver
uniprot
Q69YT1
resolver
uniprot
Q6ICD6
resolver
uniprot_entry
A0A5H1ZRQ2_HUMAN
resolver
uniprot_entry
DDX17_HUMAN
resolver
uniprot_entry
Q59F66_HUMAN
resolver
uniprot_sec
B1AHM0
resolver
uniprot_sec
H3BLZ8
resolver
uniprot_sec
Q69YT1
resolver
uniprot_sec
Q6ICD6
resolver
amino_acid_sequence
MPTGFVAPILCVLLPSPTREAATVASATGDSASERESAAPAAAPTAEAPPPSVVTRPEPQALPSPAIRAPLPDLYPFGTMRGGGFGDRDRDRDRGGFGARGGGGLPPKKFGNPGERLRKKKWDLSELPKFEKNFYVEHPEVARLTPYEVDELRRKKEITVRGGDVCPKPVFAFHHANFPQYVMDVLMDQHFTEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGDGPICLVLAPTRELAQQVQQVADDYGKCSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLESGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYTQINVGNLELSANHNILQIVDVCMESEKDHKLIQLMEEIMAEKENKTIIFVETKRRCDDLTRRMRRDGWPAMCIHGDKSQPERDWVLNEFRSGKAPILIATDVASRGLDVEDVKFVINYDYPNSSEDYVHRIGRTARSTNKGTAYTFFTPGNLKQARELIKVLEEANQAINPKLMQLVDHRGGGGGGGGRSRYRTTSSANNPNLMYQDECDRRLRGVKDGGRRDSASYRDRSETDRAGYANGSGYGSPNSAFGAQAGQYTYGQGTYGAAAYGTSSYTAQEYGAGTYGASSTTSTGRSSQSSSQQFSGIGRSGQQPQPLMSQQFAQPPGATNMIGYMGQTAYQYPPPPPPPPPSRK
uniprot
proteins
ec_number
3.6.4.13
uniprot
proteins
function
FUNCTION: As an RNA helicase, unwinds RNA and alters RNA structures through ATP binding and hydrolysis. Involved in multiple cellular processes, including pre-mRNA splicing, alternative splicing, ribosomal RNA processing and miRNA processing, as well as transcription regulation. Regulates the alternative splicing of exons exhibiting specific features (PubMed:12138182, PubMed:22266867, PubMed:23022728, PubMed:24910439). For instance, promotes the inclusion of AC-rich alternative exons in CD44 transcripts (PubMed:12138182). This function requires the RNA helicase activity (PubMed:12138182, PubMed:22266867, PubMed:23022728, PubMed:24910439). Affects NFAT5 and histone macro-H2A.1/MACROH2A1 alternative splicing in a CDK9-dependent manner (PubMed:22266867, PubMed:26209609). In NFAT5, promotes the introduction of alternative exon 4, which contains 2 stop codons and may target NFAT5 exon 4-containing transcripts to nonsense-mediated mRNA decay, leading to the down-regulation of NFAT5 protein (PubMed:22266867). Affects splicing of mediators of steroid hormone signaling pathway, including kinases that phosphorylates ESR1, such as CDK2, MAPK1 and GSK3B, and transcriptional regulators, such as CREBBP, MED1, NCOR1 and NCOR2. By affecting GSK3B splicing, participates in ESR1 and AR stabilization (PubMed:24275493). In myoblasts and epithelial cells, cooperates with HNRNPH1 to control the splicing of specific subsets of exons (PubMed:24910439). In addition to binding mature mRNAs, also interacts with certain pri-microRNAs, including MIR663/miR-663a, MIR99B/miR-99b, and MIR6087/miR-6087 (PubMed:25126784). Binds pri-microRNAs on the 3' segment flanking the stem loop via the 5'-[ACG]CAUC[ACU]-3' consensus sequence (PubMed:24581491). Required for the production of subsets of microRNAs, including MIR21 and MIR125B1 (PubMed:24581491, PubMed:27478153). May be involved not only in microRNA primary transcript processing, but also stabilization (By similarity). Participates in MYC down-regulation at high cell density through the production of MYC-targeting microRNAs (PubMed:24581491). Along with DDX5, may be involved in the processing of the 32S intermediate into the mature 28S ribosomal RNA (PubMed:17485482). Promoter-specific transcription regulator, functioning as a coactivator or corepressor depending on the context of the promoter and the transcriptional complex in which it exists (PubMed:15298701). Enhances NFAT5 transcriptional activity (PubMed:22266867). Synergizes with TP53 in the activation of the MDM2 promoter; this activity requires acetylation on lysine residues (PubMed:17226766, PubMed:19995069, PubMed:20663877). May also coactivate MDM2 transcription through a TP53-independent pathway (PubMed:17226766). Coactivates MMP7 transcription (PubMed:17226766). Along with CTNNB1, coactivates MYC, JUN, FOSL1 and cyclin D1/CCND1 transcription (PubMed:17699760). Alone or in combination with DDX5 and/or SRA1 non-coding RNA, plays a critical role in promoting the assembly of proteins required for the formation of the transcription initiation complex and chromatin remodeling leading to coactivation of MYOD1-dependent transcription. This helicase-independent activity is required for skeletal muscle cells to properly differentiate into myotubes (PubMed:17011493, PubMed:24910439). During epithelial-to-mesenchymal transition, coregulates SMAD-dependent transcriptional activity, directly controlling key effectors of differentiation, including miRNAs which in turn directly repress its expression (PubMed:24910439). Plays a role in estrogen and testosterone signaling pathway at several levels. Mediates the use of alternative promoters in estrogen-responsive genes and regulates transcription and splicing of a large number of steroid hormone target genes (PubMed:19995069, PubMed:20406972, PubMed:20663877, PubMed:24275493). Contrary to splicing regulation activity, transcriptional coregulation of the estrogen receptor ESR1 is helicase-independent (PubMed:19718048, PubMed:24275493). Plays a role in innate immunity. Specifically restricts bunyavirus infection, including Rift Valley fever virus (RVFV) or La Crosse virus (LACV), but not vesicular stomatitis virus (VSV), in an interferon- and DROSHA-independent manner (PubMed:25126784). Binds to RVFV RNA, likely via structured viral RNA elements (PubMed:25126784). Promotes mRNA degradation mediated by the antiviral zinc-finger protein ZC3HAV1, in an ATPase-dependent manner (PubMed:18334637). {ECO:0000250|UniProtKB:Q501J6, ECO:0000269|PubMed:12138182, ECO:0000269|PubMed:15298701, ECO:0000269|PubMed:17011493, ECO:0000269|PubMed:17226766, ECO:0000269|PubMed:17485482, ECO:0000269|PubMed:17699760, ECO:0000269|PubMed:18334637, ECO:0000269|PubMed:19718048, ECO:0000269|PubMed:19995069, ECO:0000269|PubMed:20406972, ECO:0000269|PubMed:20663877, ECO:0000269|PubMed:22266867, ECO:0000269|PubMed:23022728, ECO:0000269|PubMed:24275493, ECO:0000269|PubMed:24581491, ECO:0000269|PubMed:24910439, ECO:0000269|PubMed:25126784, ECO:0000269|PubMed:26209609, ECO:0000269|PubMed:27478153, ECO:0000305}.
uniprot
proteins
mass_dalton
80272
uniprot
proteins
mutagenesis
MUTAGEN 108..109; /note="KK->RR: No effect on HDAC1-, HDAC2- nor HDAC3-binding, small decrease in ESR1 coactivation, decreased TP53 coactivation. Complete loss of lysine acetylation, decreased stability, loss of ESR1 and TP53 coactivation and loss of HDAC1- and HDAC3-binding, no effect on HDAC2-binding; when associated with R-121."; /evidence="ECO:0000269|PubMed:20663877"; MUTAGEN 121; /note="K->R: No effect on HDAC1-, HDAC2- nor HDAC3-binding, decreased ESR1 coactivation, strongly decreased TP53 coactivation. Complete loss of lysine acetylation, decreased stability, loss of ESR1 and TP53 coactivation and loss of HDAC1- and HDAC3-binding, no effect on HDAC2-binding; when associated with 108-R-R-109."; /evidence="ECO:0000269|PubMed:20663877"; MUTAGEN 129; /note="K->R: Impaired sumoylation and decreased stability. Impairs interaction with HDAC1, but not with HDAC2, nor HDAC3. No effect on EP300-, ESR1-, DDX5- and YAP1-binding."; /evidence="ECO:0000269|PubMed:19995069, ECO:0000269|PubMed:24581491"; MUTAGEN 221; /note="K->N: No effect on transcription activation, when assayed in luciferase reporter gene assays using MDM2 or FOS promoters, either alone or in the presence of EP300 and KAT2B."; /evidence="ECO:0000269|PubMed:17226766"; MUTAGEN 221; /note="K->R: Loss of helicase activity. Loss of splicing regulation in the estrogen signaling pathway. Reduced CD44 alternative splicing regulation. Does not promote ZCH3HAV1-mediated RNA degradation."; /evidence="ECO:0000269|PubMed:12138182, ECO:0000269|PubMed:18334637, ECO:0000269|PubMed:24275493"; MUTAGEN 222; /note="T->A: Decreased CD44 alternative splicing."; /evidence="ECO:0000269|PubMed:12138182"; MUTAGEN 325; /note="D->N: Loss of helicase activity. No effect on ESR1 coactivation."; /evidence="ECO:0000269|PubMed:19718048"; MUTAGEN 328; /note="D->H: Small decrease in CD44 alternative splicing."; /evidence="ECO:0000269|PubMed:12138182"; MUTAGEN 355; /note="W->G: Small decrease in CD44 alternative splicing."; /evidence="ECO:0000269|PubMed:12138182"; MUTAGEN 356; /note="S->L: Small decrease in CD44 alternative splicing."; /evidence="ECO:0000269|PubMed:12138182
uniprot
proteins
post_translational_modification
PTM: Sumoylation significantly increases stability. It also promotes interaction specifically with HDAC1 (but not HDAC2, nor HDAC3) and strongly stimulates ESR1 and TP53 coactivation. {ECO:0000269|PubMed:19995069}.; PTM: Acetylation at lysine residues stabilizes the protein, stimulates interaction with HDAC1 and HDAC3, but not HDAC2, and represses ESR1 and TP53 coactivation activity. {ECO:0000269|PubMed:20663877}.
uniprot
proteins
protein_family
DDX5/DBP2 subfamily
uniprot
proteins
protein_family
DEAD box helicase family
uniprot
proteins
pubmed
10591208
uniprot
proteins
pubmed
11250900
uniprot
proteins
pubmed
11675387
uniprot
proteins
pubmed
12138182
uniprot
proteins
pubmed
12595555
uniprot
proteins
pubmed
15298701
uniprot
proteins
pubmed
15461802
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15531877
uniprot
proteins
pubmed
15660129
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17011493
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17226766
uniprot
proteins
pubmed
17485482
uniprot
proteins
pubmed
17525332
uniprot
proteins
pubmed
17699760
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18279852
uniprot
proteins
pubmed
18334637
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19718048
uniprot
proteins
pubmed
19995069
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20406972
uniprot
proteins
pubmed
20663877
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21876179
uniprot
proteins
pubmed
22002106
uniprot
proteins
pubmed
22266867
uniprot
proteins
pubmed
23022728
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23788676
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
24275493
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24581491
uniprot
proteins
pubmed
24589731
uniprot
proteins
pubmed
24910439
uniprot
proteins
pubmed
25114211
uniprot
proteins
pubmed
25126784
uniprot
proteins
pubmed
25218447
uniprot
proteins
pubmed
25452582
uniprot
proteins
pubmed
25755297
uniprot
proteins
pubmed
25772364
uniprot
proteins
pubmed
26030138
uniprot
proteins
pubmed
26209609
uniprot
proteins
pubmed
27478153
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
8871553
uniprot
proteins
sequence_length
729
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12138182, ECO:0000269|PubMed:12595555, ECO:0000269|PubMed:17226766, ECO:0000269|PubMed:17699760, ECO:0000269|PubMed:19995069, ECO:0000269|PubMed:22002106, ECO:0000269|PubMed:24581491, ECO:0000269|PubMed:25126784}. Nucleus, nucleolus {ECO:0000269|PubMed:17226766, ECO:0000269|PubMed:22002106}. Cytoplasm, cytosol {ECO:0000269|PubMed:25126784}. Note=In the course of bunyavirus infection, relocalizes from the nucleus to the cytosol where it binds viral RNA to antagonize replication. {ECO:0000269|PubMed:25126784}.
uniprot
proteins