A0A8I5KSH6 · A0A8I5KSH6_HUMAN
- ProteinATP-dependent RNA helicase
- GeneDDX10
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids925 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score2/5
Function
function
RNA helicase.
Catalytic activity
- ATP + H2O = ADP + H+ + phosphate
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Molecular Function | ATP binding | |
Molecular Function | hydrolase activity | |
Molecular Function | RNA binding | |
Molecular Function | RNA helicase activity |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameATP-dependent RNA helicase
- EC number
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionA0A8I5KSH6
Proteomes
Organism-specific databases
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 971 variants from UniProt as well as other sources including ClinVar and dbSNP.
Genetic variation databases
PTM/Processing
Features
Showing features for modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Modified residue (large scale data) | 4 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 7 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 10 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 52 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 197 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 589 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 627 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 656 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 660 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 661 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 767 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 830 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 853 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 854 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 857 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 859 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 879 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 881 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 890 | PRIDE | Phosphoserine | ||||
Sequence: S |
Proteomic databases
Family & Domains
Features
Showing features for region, compositional bias, domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-43 | Disordered | ||||
Sequence: MGKTANSPGSGARPDPVRSFNRWKKKHSHRQNKKKQLRKQLKK | ||||||
Compositional bias | 20-40 | Basic residues | ||||
Sequence: FNRWKKKHSHRQNKKKQLRKQ | ||||||
Domain | 69-97 | DEAD-box RNA helicase Q | ||||
Sequence: TRFSDFPLSKKTLKGLQEAQYRLVTEIQK | ||||||
Motif | 69-97 | Q motif | ||||
Sequence: TRFSDFPLSKKTLKGLQEAQYRLVTEIQK | ||||||
Domain | 100-274 | Helicase ATP-binding | ||||
Sequence: IGLALQGKDVLGAAKTGSGKTLAFLVPVLEALYRLQWTSTDGLGVLIISPTRELAYQTFEVLRKVGKNHDFSAGLIIGGKDLKHEAERINNINILVCTPGRLLQHMDETVSFHATDLQMLVLDEADRILDMGFADTMNAVIENLPKKRQTLLFSATQTKSVKDLARLSLKNPEYV | ||||||
Domain | 337-498 | Helicase C-terminal | ||||
Sequence: TLEQNYIVCELQQKISVLYSFLRSHLKKKSIVFFSSCKEVQYLYRVFCRLRPGVSILALHGRQQQMRRMEVYNEFVRKRAAVLFATDIAARGLDFPAVNWVLQFDCPEDANTYIHRAGRTARYKEDGEALLILLPSEKAMVQQLLQKKVPVKEIKINPEKLI | ||||||
Compositional bias | 612-628 | Basic and acidic residues | ||||
Sequence: GGKRLEGTEHRQDNDTG | ||||||
Region | 612-681 | Disordered | ||||
Sequence: GGKRLEGTEHRQDNDTGNEEQEEEEDDEEEMEEKLAKAKGSQAPSLPNTSEAQKIKEVPTQFLDRDEEEE | ||||||
Compositional bias | 653-667 | Polar residues | ||||
Sequence: QAPSLPNTSEAQKIK | ||||||
Region | 753-900 | Disordered | ||||
Sequence: MQKSAIKDAEEDDDTGGINLHKAKERLQEEDKFDKEEYRKKIKAKHREKRLKEREARREANKRQAKAKDEEEAFLDWSDDDDDDDDGFDPSTLPDPDKYRSSEDSDSEDMENKISDTKKKQGMKKRSNSEVEDVGPTSHNRKKARWDT | ||||||
Compositional bias | 757-793 | Basic and acidic residues | ||||
Sequence: AIKDAEEDDDTGGINLHKAKERLQEEDKFDKEEYRKK | ||||||
Compositional bias | 804-825 | Basic and acidic residues | ||||
Sequence: KEREARREANKRQAKAKDEEEA | ||||||
Compositional bias | 826-842 | Acidic residues | ||||
Sequence: FLDWSDDDDDDDDGFDP | ||||||
Compositional bias | 843-900 | Basic and acidic residues | ||||
Sequence: STLPDPDKYRSSEDSDSEDMENKISDTKKKQGMKKRSNSEVEDVGPTSHNRKKARWDT |
Domain
The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence similarities
Belongs to the DEAD box helicase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length925
- Mass (Da)106,382
- Last updated2022-05-25 v1
- Checksum6F5A2E2D92CACC6E
Computationally mapped potential isoform sequences
There are 7 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
Q13206 | DDX10_HUMAN | DDX10 | 875 | ||
E9PIF2 | E9PIF2_HUMAN | DDX10 | 835 | ||
A0A3B3ISR7 | A0A3B3ISR7_HUMAN | DDX10 | 679 | ||
A0A8I5KPM1 | A0A8I5KPM1_HUMAN | DDX10 | 482 | ||
A0A8I5KQZ1 | A0A8I5KQZ1_HUMAN | DDX10 | 676 | ||
A0A8I5KUU7 | A0A8I5KUU7_HUMAN | DDX10 | 489 | ||
A0A8I5KXY1 | A0A8I5KXY1_HUMAN | DDX10 | 451 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 20-40 | Basic residues | ||||
Sequence: FNRWKKKHSHRQNKKKQLRKQ | ||||||
Compositional bias | 612-628 | Basic and acidic residues | ||||
Sequence: GGKRLEGTEHRQDNDTG | ||||||
Compositional bias | 653-667 | Polar residues | ||||
Sequence: QAPSLPNTSEAQKIK | ||||||
Compositional bias | 757-793 | Basic and acidic residues | ||||
Sequence: AIKDAEEDDDTGGINLHKAKERLQEEDKFDKEEYRKK | ||||||
Compositional bias | 804-825 | Basic and acidic residues | ||||
Sequence: KEREARREANKRQAKAKDEEEA | ||||||
Compositional bias | 826-842 | Acidic residues | ||||
Sequence: FLDWSDDDDDDDDGFDP | ||||||
Compositional bias | 843-900 | Basic and acidic residues | ||||
Sequence: STLPDPDKYRSSEDSDSEDMENKISDTKKKQGMKKRSNSEVEDVGPTSHNRKKARWDT |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AP002453 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AP003027 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AP003387 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |