Q61656 · DDX5_MOUSE
- ProteinProbable ATP-dependent RNA helicase DDX5
- GeneDdx5
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids614 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in the alternative regulation of pre-mRNA splicing; its RNA helicase activity is necessary for increasing tau exon 10 inclusion and occurs in a RBM4-dependent manner. Binds to the tau pre-mRNA in the stem-loop region downstream of exon 10. The rate of ATP hydrolysis is highly stimulated by single-stranded RNA. Involved in transcriptional regulation; the function is independent of the RNA helicase activity. Transcriptional coactivator for androgen receptor AR but probably not ESR1. Synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and involved in skeletal muscle differentiation. Transcriptional coactivator for p53/TP53 and involved in p53/TP53 transcriptional response to DNA damage and p53/TP53-dependent apoptosis. Transcriptional coactivator for RUNX2 and involved in regulation of osteoblast differentiation. Acts as a transcriptional repressor in a promoter-specific manner; the function probably involves association with histone deacetylases, such as HDAC1. As component of a large PER complex is involved in the inhibition of 3' transcriptional termination of circadian target genes such as PER1 and NR1D1 and the control of the circadian rhythms.
Catalytic activity
- ATP + H2O = ADP + H+ + phosphate
Features
Showing features for binding site.
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProbable ATP-dependent RNA helicase DDX5
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ61656
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: During the G0 phase, predominantly located in the nucleus. Cytoplasmic levels increase during the G1/S phase. During the M phase, located at the vicinity of the condensed chromosomes. At G1, localizes in the cytoplasm.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000054992 | 1-614 | Probable ATP-dependent RNA helicase DDX5 | |||
Sequence: MSSYSSDRDRGRDRGFGAPRFGGSRTGPLSGKKFGNPGEKLVKKKWNLDELPKFEKNFYQEHPDLARRTAQEVDTYRRSKEITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERGDGPICLVLAPTRELAQQVQQVAAEYCRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLECGKTNLRRTTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIGALELSANHNILQIVDVCHDVEKDEKLIRLMEEIMSEKENKTIVFVETKRRCDELTRKMRRDGWPAMGIHGDKSQQERDWVLNEFKHGKAPILIATDVASRGLDVEDVKFVINYDYPNSSEDYIHRIGRTARSTKTGTAYTFFTPNNIKQVSDLISVLREANQAINPKLLQLVEDRGSGRSRGRGGMKDDRRDRYSAGKRGGFNTFRDRENYDRGYSNLLKRDFGAKTQNGVYSAANYTNGSFGSNFVSAGIQTSFRTGNPTGTYQNGYDSTQQYGSNVANMHNGMNQQAYAYPLPQAAPMIGYPMPTGYSQ | ||||||
Modified residue | 24 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 32 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Cross-link | 32 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | ||||||
Modified residue | 33 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 40 | N6-acetyllysine | ||||
Sequence: K | ||||||
Cross-link | 45 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 53 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate | ||||
Sequence: K | ||||||
Cross-link | 53 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate | ||||
Sequence: K | ||||||
Cross-link | 53 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | ||||||
Modified residue | 236 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 297 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Cross-link | 340 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 343 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 388 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 391 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 411 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 437 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 451 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 470 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 480 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 523 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K |
Post-translational modification
Sumoylated; sumoylation, promoted by PIAS1, promotes interaction with HDAC1 and transcriptional repression activity. Sumoylation also significantly increases stability, and reduces polyubiquitination (By similarity).
Polyubiquitinated, leading to proteasomal degradation.
Weakly phosphorylated in the G1/S phase of the cell cycle and much more at G2/M, especially at Thr and Tyr residues.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Identified in the spliceosome C complex. Component of a ribonucleoprotein complex containing mRNAs and RNA-binding proteins including DDX5, HNRNPH2 and SRSF1 as well as splicing regulator ARVCF (By similarity).
Interacts with RBM4; the interaction occurs in an RNA-independent manner. Interacts with AGO1 and AGO2. Interacts with ESR1, AR, EP300, CREBBP, POLR2A, TP53, RUNX2 and HDAC1. Self-associates. Interacts with DDX17. Interacts with BRDT. The large PER complex involved in the repression of transcriptional termination is composed of at least PER2, CDK9, DDX5, DHX9, NCBP1 and POLR2A (active). Interacts with DHX36; this interaction occurs in a RNA-dependent manner (By similarity).
Interacts with NUPR1 (PubMed:19723804).
Interacts with ERCC6 (By similarity).
Interacts with DDX3X in the cytoplasm; this interaction may be more efficient when both proteins are unphosphorylated (By similarity).
Interacts with RBM4; the interaction occurs in an RNA-independent manner. Interacts with AGO1 and AGO2. Interacts with ESR1, AR, EP300, CREBBP, POLR2A, TP53, RUNX2 and HDAC1. Self-associates. Interacts with DDX17. Interacts with BRDT. The large PER complex involved in the repression of transcriptional termination is composed of at least PER2, CDK9, DDX5, DHX9, NCBP1 and POLR2A (active). Interacts with DHX36; this interaction occurs in a RNA-dependent manner (By similarity).
Interacts with NUPR1 (PubMed:19723804).
Interacts with ERCC6 (By similarity).
Interacts with DDX3X in the cytoplasm; this interaction may be more efficient when both proteins are unphosphorylated (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | Q61656 | Akap8 Q63014 | 4 | EBI-643076, EBI-11617845 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region, motif, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-16 | Basic and acidic residues | ||||
Sequence: MSSYSSDRDRGRDRGF | ||||||
Region | 1-39 | Disordered | ||||
Sequence: MSSYSSDRDRGRDRGFGAPRFGGSRTGPLSGKKFGNPGE | ||||||
Motif | 94-122 | Q motif | ||||
Sequence: LNFYEANFPANVMDVIARQNFTEPTAIQA | ||||||
Domain | 125-300 | Helicase ATP-binding | ||||
Sequence: WPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERGDGPICLVLAPTRELAQQVQQVAAEYCRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLECGKTNLRRTTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHI | ||||||
Motif | 248-251 | DEAD box | ||||
Sequence: DEAD | ||||||
Domain | 328-475 | Helicase C-terminal | ||||
Sequence: KLIRLMEEIMSEKENKTIVFVETKRRCDELTRKMRRDGWPAMGIHGDKSQQERDWVLNEFKHGKAPILIATDVASRGLDVEDVKFVINYDYPNSSEDYIHRIGRTARSTKTGTAYTFFTPNNIKQVSDLISVLREANQAINPKLLQLV | ||||||
Region | 477-504 | Disordered | ||||
Sequence: DRGSGRSRGRGGMKDDRRDRYSAGKRGG | ||||||
Region | 477-614 | Transactivation domain | ||||
Sequence: DRGSGRSRGRGGMKDDRRDRYSAGKRGGFNTFRDRENYDRGYSNLLKRDFGAKTQNGVYSAANYTNGSFGSNFVSAGIQTSFRTGNPTGTYQNGYDSTQQYGSNVANMHNGMNQQAYAYPLPQAAPMIGYPMPTGYSQ |
Sequence similarities
Belongs to the DEAD box helicase family. DDX5/DBP2 subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length614
- Mass (Da)69,290
- Last updated2011-07-27 v2
- ChecksumA9BBB25D9B7B8819
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-16 | Basic and acidic residues | ||||
Sequence: MSSYSSDRDRGRDRGF | ||||||
Sequence conflict | 112 | in Ref. 1; CAA46581 | ||||
Sequence: Q → H | ||||||
Sequence conflict | 159 | in Ref. 1; CAA46581 | ||||
Sequence: Q → H | ||||||
Sequence conflict | 597 | in Ref. 1; CAA46581 | ||||
Sequence: L → V | ||||||
Sequence conflict | 600 | in Ref. 1; CAA46581 | ||||
Sequence: A → P |
Keywords
- Technical term