Q7L2E3 · DHX30_HUMAN
- ProteinATP-dependent RNA helicase DHX30
- GeneDHX30
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1194 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Plays an important role in the assembly of the mitochondrial large ribosomal subunit (PubMed:25683715, PubMed:29100085).
Required for optimal function of the zinc-finger antiviral protein ZC3HAV1 (By similarity).
Associates with mitochondrial DNA (PubMed:18063578).
Involved in nervous system development and differentiation through its involvement in the up-regulation of a number of genes which are required for neurogenesis, including GSC, NCAM1, neurogenin, and NEUROD (By similarity).
Catalytic activity
- ATP + H2O = ADP + H+ + phosphate
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | mitochondrial nucleoid | |
Cellular Component | mitochondrion | |
Cellular Component | nucleus | |
Cellular Component | ribonucleoprotein granule | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | chromatin binding | |
Molecular Function | DNA helicase activity | |
Molecular Function | double-stranded RNA binding | |
Molecular Function | G-quadruplex RNA binding | |
Molecular Function | RNA binding | |
Molecular Function | RNA helicase activity | |
Biological Process | central nervous system development | |
Biological Process | mitochondrial large ribosomal subunit assembly |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameATP-dependent RNA helicase DHX30
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ7L2E3
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Neurodevelopmental disorder with variable motor and language impairment (NEDMIAL)
- Note
- DescriptionAn autosomal dominant neurodevelopmental disorder characterized by global developmental delay, intellectual disability, speech impairment and gait abnormalities.
- See alsoMIM:617804
Natural variants in NEDMIAL
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_080611 | 493 | R>H | in NEDMIAL; changed localization to stress granules; decreased RNA-binding; no effect on RNA-dependent ATPase activity; by inducing the formation of stress granules probably indirectly decreases global protein synthesis; dbSNP:rs1057519436 | |
VAR_080612 | 562 | H>R | in NEDMIAL; changed localization to stress granules; decreased RNA-dependent ATPase activity; by inducing the formation of stress granules probably indirectly decreases global protein synthesis; dbSNP:rs1060499733 | |
VAR_080613 | 781 | G>D | in NEDMIAL; changed localization to stress granules; decreased RNA-dependent ATPase activity; by inducing the formation of stress granules probably indirectly decreases global protein synthesis; dbSNP:rs1553706775 | |
VAR_080614 | 782 | R>W | in NEDMIAL; changed localization to stress granules; decreased RNA-dependent ATPase activity; by inducing the formation of stress granules probably indirectly decreases global protein synthesis; dbSNP:rs753242774 | |
VAR_080615 | 785 | R>C | in NEDMIAL; changed localization to stress granules; decreased RNA-dependent ATPase activity; by inducing the formation of stress granules probably indirectly decreases global protein synthesis; dbSNP:rs1085307451 | |
VAR_080616 | 785 | R>H | in NEDMIAL; changed localization to stress granules; decreased RNA-dependent ATPase activity; by inducing the formation of stress granules probably indirectly decreases global protein synthesis; dbSNP:rs1553706799 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_080611 | 493 | in NEDMIAL; changed localization to stress granules; decreased RNA-binding; no effect on RNA-dependent ATPase activity; by inducing the formation of stress granules probably indirectly decreases global protein synthesis; dbSNP:rs1057519436 | |||
Sequence: R → H | ||||||
Natural variant | VAR_080612 | 562 | in NEDMIAL; changed localization to stress granules; decreased RNA-dependent ATPase activity; by inducing the formation of stress granules probably indirectly decreases global protein synthesis; dbSNP:rs1060499733 | |||
Sequence: H → R | ||||||
Natural variant | VAR_080613 | 781 | in NEDMIAL; changed localization to stress granules; decreased RNA-dependent ATPase activity; by inducing the formation of stress granules probably indirectly decreases global protein synthesis; dbSNP:rs1553706775 | |||
Sequence: G → D | ||||||
Natural variant | VAR_080614 | 782 | in NEDMIAL; changed localization to stress granules; decreased RNA-dependent ATPase activity; by inducing the formation of stress granules probably indirectly decreases global protein synthesis; dbSNP:rs753242774 | |||
Sequence: R → W | ||||||
Natural variant | VAR_080615 | 785 | in NEDMIAL; changed localization to stress granules; decreased RNA-dependent ATPase activity; by inducing the formation of stress granules probably indirectly decreases global protein synthesis; dbSNP:rs1085307451 | |||
Sequence: R → C | ||||||
Natural variant | VAR_080616 | 785 | in NEDMIAL; changed localization to stress granules; decreased RNA-dependent ATPase activity; by inducing the formation of stress granules probably indirectly decreases global protein synthesis; dbSNP:rs1553706799 | |||
Sequence: R → H |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,050 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000245538 | 1-1194 | UniProt | ATP-dependent RNA helicase DHX30 | |||
Sequence: MFSLDSFRKDRAQHRQRQCKLPPPRLPPMCVNPTPGGTISRASRDLLKEFPQPKNLLNSVIGRALGISHAKDKLVYVHTNGPKKKKVTLHIKWPKSVEVEGYGSKKIDAERQAAAAACQLFKGWGLLGPRNELFDAAKYRVLADRFGSPADSWWRPEPTMPPTSWRQLNPESIRPGGPGGLSRSLGREEEEDEEEELEEGTIDVTDFLSMTQQDSHAPLRDSRGSSFEMTDDDSAIRALTQFPLPKNLLAKVIQIATSSSTAKNLMQFHTVGTKTKLSTLTLLWPCPMTFVAKGRRKAEAENKAAALACKKLKSLGLVDRNNEPLTHAMYNLASLRELGETQRRPCTIQVPEPILRKIETFLNHYPVESSWIAPELRLQSDDILPLGKDSGPLSDPITGKPYVPLLEAEEVRLSQSLLELWRRRGPVWQEAPQLPVDPHRDTILNAIEQHPVVVISGDTGCGKTTRIPQLLLERYVTEGRGARCNVIITQPRRISAVSVAQRVSHELGPSLRRNVGFQVRLESKPPSRGGALLFCTVGILLRKLQSNPSLEGVSHVIVDEVHERDVNTDFLLILLKGLQRLNPALRLVLMSATGDNERFSRYFGGCPVIKVPGFMYPVKEHYLEDILAKLGKHQYLHRHRHHESEDECALDLDLVTDLVLHIDARGEPGGILCFLPGWQEIKGVQQRLQEALGMHESKYLILPVHSNIPMMDQKAIFQQPPVGVRKIVLATNIAETSITINDIVHVVDSGLHKEERYDLKTKVSCLETVWVSRANVIQRRGRAGRCQSGFAYHLFPRSRLEKMVPFQVPEILRTPLENLVLQAKIHMPEKTAVEFLSKAVDSPNIKAVDEAVILLQEIGVLDQREYLTTLGQRLAHISTDPRLAKAIVLAAIFRCLHPLLVVVSCLTRDPFSSSLQNRAEVDKVKALLSHDSGSDHLAFVRAVAGWEEVLRWQDRSSRENYLEENLLYAPSLRFIHGLIKQFSENIYEAFLVGKPSDCTLASAQCNEYSEEEELVKGVLMAGLYPNLIQVRQGKVTRQGKFKPNSVTYRTKSGNILLHKSTINREATRLRSRWLTYFMAVKSNGSVFVRDSSQVHPLAVLLLTDGDVHIRDDGRRATISLSDSDLLRLEGDSRTVRLLKELRRALGRMVERSLRSELAALPPSVQEEHGQLLALLAELLRGPCGSFDVRKTADD | |||||||
Modified residue | 6 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 15 | UniProt | In isoform Q7L2E3-2; Phosphoserine | ||||
Sequence: R | |||||||
Modified residue (large scale data) | 225 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 226 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 226 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 380 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 380 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 968 | PRIDE | Phosphotyrosine | ||||
Sequence: Y |
Post-translational modification
Isoform 2
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Found in a complex with GRSF1, DDX28, FASTKD2 and FASTKD5 (PubMed:25683715).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q7L2E3 | CFTR P13569 | 5 | EBI-1211456, EBI-349854 | |
BINARY | Q7L2E3 | DHX58 Q96C10 | 2 | EBI-1211456, EBI-744193 | |
BINARY | Q7L2E3 | EIF2AK2 P19525 | 4 | EBI-1211456, EBI-640775 | |
BINARY | Q7L2E3 | H1-5 P16401 | 2 | EBI-1211456, EBI-5327611 | |
BINARY | Q7L2E3 | OAS3 Q9Y6K5 | 2 | EBI-1211456, EBI-6115729 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-27 | Disordered | ||||
Sequence: MFSLDSFRKDRAQHRQRQCKLPPPRLP | ||||||
Domain | 53-121 | DRBM | ||||
Sequence: PKNLLNSVIGRALGISHAKDKLVYVHTNGPKKKKVTLHIKWPKSVEVEGYGSKKIDAERQAAAAACQLF | ||||||
Region | 150-199 | Disordered | ||||
Sequence: ADSWWRPEPTMPPTSWRQLNPESIRPGGPGGLSRSLGREEEEDEEEELEE | ||||||
Domain | 444-612 | Helicase ATP-binding | ||||
Sequence: LNAIEQHPVVVISGDTGCGKTTRIPQLLLERYVTEGRGARCNVIITQPRRISAVSVAQRVSHELGPSLRRNVGFQVRLESKPPSRGGALLFCTVGILLRKLQSNPSLEGVSHVIVDEVHERDVNTDFLLILLKGLQRLNPALRLVLMSATGDNERFSRYFGGCPVIKVP | ||||||
Motif | 559-562 | DEAH box | ||||
Sequence: DEVH | ||||||
Domain | 654-827 | Helicase C-terminal | ||||
Sequence: LVTDLVLHIDARGEPGGILCFLPGWQEIKGVQQRLQEALGMHESKYLILPVHSNIPMMDQKAIFQQPPVGVRKIVLATNIAETSITINDIVHVVDSGLHKEERYDLKTKVSCLETVWVSRANVIQRRGRAGRCQSGFAYHLFPRSRLEKMVPFQVPEILRTPLENLVLQAKIHM |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing. Additional isoforms seem to exist.
Q7L2E3-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length1,194
- Mass (Da)133,938
- Last updated2004-07-05 v1
- Checksum33D9A08799FE7A02
Q7L2E3-2
- Name2
- Differences from canonical
- 1-41: MFSLDSFRKDRAQHRQRQCKLPPPRLPPMCVNPTPGGTISR → MAAARRLMALAAGISPRLQPLGPRAAGRQGRSRGFSSSCAHPDHTKEAAEAESGMAPGGPGEGDGSLVN
Q7L2E3-3
- Name3
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_036891 | 1-39 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_022118 | 1-41 | in isoform 2 | |||
Sequence: MFSLDSFRKDRAQHRQRQCKLPPPRLPPMCVNPTPGGTISR → MAAARRLMALAAGISPRLQPLGPRAAGRQGRSRGFSSSCAHPDHTKEAAEAESGMAPGGPGEGDGSLVN | ||||||
Alternative sequence | VSP_036892 | 40-41 | in isoform 3 | |||
Sequence: SR → MA | ||||||
Sequence conflict | 557 | in Ref. 2; BAF83955 | ||||
Sequence: I → T | ||||||
Sequence conflict | 1136 | in Ref. 3; AAH14237 | ||||
Sequence: R → W |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB020697 EMBL· GenBank· DDBJ | BAA74913.2 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK002076 EMBL· GenBank· DDBJ | BAA92071.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
AK291266 EMBL· GenBank· DDBJ | BAF83955.1 EMBL· GenBank· DDBJ | mRNA | ||
BC014237 EMBL· GenBank· DDBJ | AAH14237.1 EMBL· GenBank· DDBJ | mRNA | ||
BC015029 EMBL· GenBank· DDBJ | AAH15029.1 EMBL· GenBank· DDBJ | mRNA | ||
BC020126 EMBL· GenBank· DDBJ | AAH20126.1 EMBL· GenBank· DDBJ | mRNA | ||
BC038417 EMBL· GenBank· DDBJ | AAH38417.1 EMBL· GenBank· DDBJ | mRNA |