A0A2R8Y425 · A0A2R8Y425_HUMAN
- ProteinDNA helicase
- GeneCHD4
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1889 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
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 | |||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Aspect | Term | |
---|---|---|
Cellular Component | nucleoplasm | |
Molecular Function | ATP binding | |
Molecular Function | ATP-dependent chromatin remodeler activity | |
Molecular Function | DNA binding | |
Molecular Function | helicase activity | |
Molecular Function | hydrolase activity | |
Molecular Function | metal ion binding |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDNA 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 accessionA0A2R8Y425
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,141 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) | 61 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 62 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 79 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 81 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 84 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 86 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 253 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 295 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 343 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 404 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 491 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 493 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 505 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 507 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 679 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1220 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1221 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1284 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1325 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1507 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1511 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1513 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1516 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1518 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1520 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1521 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1525 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1529 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1546 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1552 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1578 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1624 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1629 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1655 | PRIDE | Phosphothreonine | ||||
Sequence: T |
Proteomic databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-133 | Disordered | ||||
Sequence: XDMDALLNNSLPPPHPENEEDPEEDLSETETPKLKKKKKPKKPRDPKIPKSKRQKKELGDSSGEGPEFVEEEEEVALRSDSEGSDYTPGKKKKKKLGPKKEKKSKSKRKEEEEEEDDDDDSKEPKSSAQLLED | ||||||
Compositional bias | 35-49 | Basic residues | ||||
Sequence: KKKKKPKKPRDPKIP | ||||||
Compositional bias | 64-78 | Acidic residues | ||||
Sequence: EGPEFVEEEEEVALR | ||||||
Region | 221-327 | Disordered | ||||
Sequence: EVAPPPPPVEVPIRKAKTKEGKGPNARRKPKGSPRVPDAKKPKPKKVAPLKIKLGGFGSKRKRSSSEDDDLDVESDFDDASINSYSVSDGSTSRSSRSRKKLRTTKK | ||||||
Compositional bias | 233-265 | Basic and acidic residues | ||||
Sequence: IRKAKTKEGKGPNARRKPKGSPRVPDAKKPKPK | ||||||
Compositional bias | 299-313 | Polar residues | ||||
Sequence: DASINSYSVSDGSTS | ||||||
Domain | 346-393 | PHD-type | ||||
Sequence: QDYCEVCQQGGEIILCDTCPRAYHMVCLDPDMEKAPEGKWSCPHCEKE | ||||||
Domain | 425-472 | PHD-type | ||||
Sequence: MEFCRVCKDGGELLCCDTCPSSYHIHCLNPPLPEIPNGEWLCPRCTCP | ||||||
Region | 485-514 | Disordered | ||||
Sequence: KWGQPPSPTPVPRPPDADPNTPSPKPLEGR | ||||||
Compositional bias | 489-510 | Pro residues | ||||
Sequence: PPSPTPVPRPPDADPNTPSPKP | ||||||
Domain | 505-562 | Chromo | ||||
Sequence: TPSPKPLEGRPERQFFVKWQGMSYWHCSWVSELQLELHCQVMFRNYQRKNDMDEPPSG | ||||||
Region | 554-579 | Disordered | ||||
Sequence: NDMDEPPSGDFGGDEEKSRKRKNKDP | ||||||
Domain | 598-633 | Chromo | ||||
Sequence: MMIHRILNHSVDKKGHVHYLIKWRDLPYDQASWESE | ||||||
Domain | 714-898 | Helicase ATP-binding | ||||
Sequence: RFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVTYVGDKDSRAIIRENEFSFEDNAIRGGKKASRMKKEASVKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPE | ||||||
Domain | 1030-1179 | Helicase C-terminal | ||||
Sequence: LLQKMLKNLKEGGHRVLIFSQMTKMLDLLEDFLEHEGYKYERIDGGITGNMRQEAIDRFNAPGAQQFCFLLSTRAGGLGINLATADTVIIYDSDWNPHNDIQAFSRAHRIGQNKKVMIYRFVTRASVEERITQVAKKKMMLTHLVVRPGL | ||||||
Compositional bias | 1304-1336 | Basic and acidic residues | ||||
Sequence: DLARNLGKGKRIRKQVNYNDGSQEDRDWQDDQS | ||||||
Region | 1304-1377 | Disordered | ||||
Sequence: DLARNLGKGKRIRKQVNYNDGSQEDRDWQDDQSDNQSDYSVASEEGDEDFDERSEAPRRPSRKGLRNDKDKPLP | ||||||
Compositional bias | 1355-1376 | Basic and acidic residues | ||||
Sequence: ERSEAPRRPSRKGLRNDKDKPL | ||||||
Region | 1496-1582 | Disordered | ||||
Sequence: ELAEVEENKKMSQPGSPSPKTPTPSTPGDTQPNTPAPVPPAEDGIKIEENSLKEEESIEGEKEVKSTAPETAIECTQAPAPASEDEK | ||||||
Compositional bias | 1512-1534 | Pro residues | ||||
Sequence: PSPKTPTPSTPGDTQPNTPAPVP | ||||||
Compositional bias | 1541-1563 | Basic and acidic residues | ||||
Sequence: KIEENSLKEEESIEGEKEVKSTA |
Sequence similarities
Belongs to the SNF2/RAD54 helicase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusFragment
- Length1,889
- Mass (Da)215,608
- Last updated2018-06-20 v1
- ChecksumEBD67B6F89E78AAB
Computationally mapped potential isoform sequences
There are 29 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
Q14839 | CHD4_HUMAN | CHD4 | 1912 | ||
A0A2R8Y212 | A0A2R8Y212_HUMAN | CHD4 | 1914 | ||
A0A2R8Y8B3 | A0A2R8Y8B3_HUMAN | CHD4 | 1147 | ||
A0A2R8Y8C1 | A0A2R8Y8C1_HUMAN | CHD4 | 1669 | ||
A0A2R8Y7X1 | A0A2R8Y7X1_HUMAN | CHD4 | 73 | ||
A0A2R8Y7I0 | A0A2R8Y7I0_HUMAN | CHD4 | 605 | ||
A0A2R8Y7M9 | A0A2R8Y7M9_HUMAN | CHD4 | 560 | ||
A0A2R8Y795 | A0A2R8Y795_HUMAN | CHD4 | 48 | ||
A0A2R8Y6G9 | A0A2R8Y6G9_HUMAN | CHD4 | 103 | ||
A0A2R8Y5Z7 | A0A2R8Y5Z7_HUMAN | CHD4 | 1425 | ||
A0A2R8Y685 | A0A2R8Y685_HUMAN | CHD4 | 1377 | ||
A0A2R8Y5J0 | A0A2R8Y5J0_HUMAN | CHD4 | 1892 | ||
A0A2R8Y5M9 | A0A2R8Y5M9_HUMAN | CHD4 | 554 | ||
A0A2R8Y4X2 | A0A2R8Y4X2_HUMAN | CHD4 | 1262 | ||
A0A2R8Y512 | A0A2R8Y512_HUMAN | CHD4 | 16 | ||
A0A2R8Y521 | A0A2R8Y521_HUMAN | CHD4 | 1920 | ||
A0A2R8Y539 | A0A2R8Y539_HUMAN | CHD4 | 51 | ||
A0A2R8YDW2 | A0A2R8YDW2_HUMAN | CHD4 | 1215 | ||
A0A2R8YE38 | A0A2R8YE38_HUMAN | CHD4 | 458 | ||
A0A2R8YDJ9 | A0A2R8YDJ9_HUMAN | CHD4 | 1554 | ||
A0A2R8YD40 | A0A2R8YD40_HUMAN | CHD4 | 1484 | ||
A0A2R8YFK9 | A0A2R8YFK9_HUMAN | CHD4 | 1899 | ||
A0A2R8YFD8 | A0A2R8YFD8_HUMAN | CHD4 | 1903 | ||
A0A2R8YER1 | A0A2R8YER1_HUMAN | CHD4 | 1645 | ||
A0A2U3TZM0 | A0A2U3TZM0_HUMAN | CHD4 | 1902 | ||
F5GWX5 | F5GWX5_HUMAN | CHD4 | 1905 | ||
F5H6N4 | F5H6N4_HUMAN | CHD4 | 354 | ||
F5H596 | F5H596_HUMAN | CHD4 | 125 | ||
A0A0C4DGG9 | A0A0C4DGG9_HUMAN | CHD4 | 1937 |
Features
Showing features for non-terminal residue, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 1 | |||||
Sequence: X | ||||||
Compositional bias | 35-49 | Basic residues | ||||
Sequence: KKKKKPKKPRDPKIP | ||||||
Compositional bias | 64-78 | Acidic residues | ||||
Sequence: EGPEFVEEEEEVALR | ||||||
Compositional bias | 233-265 | Basic and acidic residues | ||||
Sequence: IRKAKTKEGKGPNARRKPKGSPRVPDAKKPKPK | ||||||
Compositional bias | 299-313 | Polar residues | ||||
Sequence: DASINSYSVSDGSTS | ||||||
Compositional bias | 489-510 | Pro residues | ||||
Sequence: PPSPTPVPRPPDADPNTPSPKP | ||||||
Compositional bias | 1304-1336 | Basic and acidic residues | ||||
Sequence: DLARNLGKGKRIRKQVNYNDGSQEDRDWQDDQS | ||||||
Compositional bias | 1355-1376 | Basic and acidic residues | ||||
Sequence: ERSEAPRRPSRKGLRNDKDKPL | ||||||
Compositional bias | 1512-1534 | Pro residues | ||||
Sequence: PSPKTPTPSTPGDTQPNTPAPVP | ||||||
Compositional bias | 1541-1563 | Basic and acidic residues | ||||
Sequence: KIEENSLKEEESIEGEKEVKSTA |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC006064 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |