O14647 · CHD2_HUMAN
- ProteinChromodomain-helicase-DNA-binding protein 2
- GeneCHD2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1828 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalytic activity
- ATP + H2O = ADP + H+ + phosphate
Features
Showing features for binding site.
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 | |
---|---|---|
Cellular Component | chromatin | |
Cellular Component | nucleus | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | ATP-dependent chromatin remodeler activity | |
Molecular Function | chromatin binding | |
Molecular Function | DNA binding | |
Molecular Function | helicase activity | |
Molecular Function | histone binding | |
Molecular Function | RNA binding | |
Molecular Function | RNA polymerase II cis-regulatory region sequence-specific DNA binding | |
Biological Process | DNA damage response | |
Biological Process | gene expression | |
Biological Process | hematopoietic stem cell differentiation | |
Biological Process | muscle organ development | |
Biological Process | nucleosome organization |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameChromodomain-helicase-DNA-binding protein 2
- EC number
- Short namesCHD-2
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO14647
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Developmental and epileptic encephalopathy 94 (DEE94)
- Note
- DescriptionA form of epileptic encephalopathy, a heterogeneous group of early-onset epilepsies characterized by refractory seizures, neurodevelopmental impairment, and poor prognosis. Development is normal prior to seizure onset, after which cognitive and motor delays become apparent. DEE94 is an autosomal dominant, severe form characterized by onset of multiple seizure types in the first few years of life.
- See alsoMIM:615369
Natural variants in DEE94
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_078614 | 112-1828 | missing | in DEE94 | |
VAR_078615 | 121-1828 | missing | in DEE94 | |
VAR_070209 | 548 | W>R | in DEE94; dbSNP:rs864309537 | |
VAR_070210 | 823 | L>P | in DEE94; dbSNP:rs864309540 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_078614 | 112-1828 | in DEE94 | |||
Sequence: Missing | ||||||
Natural variant | VAR_078615 | 121-1828 | in DEE94 | |||
Sequence: Missing | ||||||
Natural variant | VAR_085039 | 178-1828 | found in a patient with progressive myoclonus epilepsy; uncertain significance | |||
Sequence: Missing | ||||||
Natural variant | VAR_070209 | 548 | in DEE94; dbSNP:rs864309537 | |||
Sequence: W → R | ||||||
Natural variant | VAR_070210 | 823 | in DEE94; dbSNP:rs864309540 | |||
Sequence: L → P | ||||||
Natural variant | VAR_061099 | 1574 | in dbSNP:rs56227200 | |||
Sequence: G → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,692 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000080226 | 1-1828 | UniProt | Chromodomain-helicase-DNA-binding protein 2 | |||
Sequence: MMRNKDKSQEEDSSLHSNASSHSASEEASGSDSGSQSESEQGSDPGSGHGSESNSSSESSESQSESESESAGSKSQPVLPEAKEKPASKKERIADVKKMWEEYPDVYGVRRSNRSRQEPSRFNIKEEASSGSESGSPKRRGQRQLKKQEKWKQEPSEDEQEQGTSAESEPEQKKVKARRPVPRRTVPKPRVKKQPKTQRGKRKKQDSSDEDDDDDEAPKRQTRRRAAKNVSYKEDDDFETDSDDLIEMTGEGVDEQQDNSETIEKVLDSRLGKKGATGASTTVYAIEANGDPSGDFDTEKDEGEIQYLIKWKGWSYIHSTWESEESLQQQKVKGLKKLENFKKKEDEIKQWLGKVSPEDVEYFNCQQELASELNKQYQIVERVIAVKTSKSTLGQTDFPAHSRKPAPSNEPEYLCKWMGLPYSECSWEDEALIGKKFQNCIDSFHSRNNSKTIPTRECKALKQRPRFVALKKQPAYLGGENLELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLIVVPLSTLTSWQREFEIWAPEINVVVYIGDLMSRNTIREYEWIHSQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGRENGYQSLHKVLEPFLLRRVKKDVEKSLPAKVEQILRVEMSALQKQYYKWILTRNYKALAKGTRGSTSGFLNIVMELKKCCNHCYLIKPPEENERENGQEILLSLIRSSGKLILLDKLLTRLRERGNRVLIFSQMVRMLDILAEYLTIKHYPFQRLDGSIKGEIRKQALDHFNADGSEDFCFLLSTRAGGLGINLASADTVVIFDSDWNPQNDLQAQARAHRIGQKKQVNIYRLVTKGTVEEEIIERAKKKMVLDHLVIQRMDTTGRTILENNSGRSNSNPFNKEELTAILKFGAEDLFKELEGEESEPQEMDIDEILRLAETRENEVSTSATDELLSQFKVANFATMEDEEELEERPHKDWDEIIPEEQRKKVEEEERQKELEEIYMLPRIRSSTKKAQTNDSDSDTESKRQAQRSSASESETEDSDDDKKPKRRGRPRSVRKDLVEGFTDAEIRRFIKAYKKFGLPLERLECIARDAELVDKSVADLKRLGELIHNSCVSAMQEYEEQLKENASEGKGPGKRRGPTIKISGVQVNVKSIIQHEEEFEMLHKSIPVDPEEKKKYCLTCRVKAAHFDVEWGVEDDSRLLLGIYEHGYGNWELIKTDPELKLTDKILPVETDKKPQGKQLQTRADYLLKLLRKGLEKKGAVTGGEEAKLKKRKPRVKKENKVPRLKEEHGIELSSPRHSDNPSEEGEVKDDGLEKSPMKKKQKKKENKENKEKQMSSRKDKEGDKERKKSKDKKEKPKSGDAKSSSKSKRSQGPVHITAGSEPVPIGEDEDDDLDQETFSICKERMRPVKKALKQLDKPDKGLNVQEQLEHTRNCLLKIGDRIAECLKAYSDQEHIKLWRRNLWIFVSKFTEFDARKLHKLYKMAHKKRSQEEEEQKKKDDVTGGKKPFRPEASGSSRDSLISQSHTSHNLHPQKPHLPASHGPQMHGHPRDNYNHPNKRHFSNADRGDWQRERKFNYGGGNNNPPWGSDRHHQYEQHWYKDHHYGDRRHMDAHRSGSYRPNNMSRKRPYDQYSSDRDHRGHRDYYDRHHHDSKRRRSDEFRPQNYHQQDFRRMSDHRPAMGYHGQGPSDHYRSFHTDKLGEYKQPLPPLHPAVSDPRSPPSQKSPHDSKSPLDHRSPLERSLEQKNNPDYNWNVRKT | |||||||
Modified residue (large scale data) | 129 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 130 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 132 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 156 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 207 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 207 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 208 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 208 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 240 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 242 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1068 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 1085 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1085 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1087 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1087 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1364 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1365 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1365 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1369 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1373 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1386 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1386 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1441 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1586 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1728 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1767 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1785 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1789 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1795 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1799 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1801 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1807 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1807 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O14647 | BEND7 Q8N7W2-2 | 3 | EBI-1210503, EBI-10181188 | |
BINARY | O14647 | MID2 Q9UJV3-2 | 3 | EBI-1210503, EBI-10172526 | |
BINARY | O14647 | TARDBP Q13148 | 2 | EBI-1210503, EBI-372899 | |
BINARY | O14647 | TEKT1 Q969V4 | 3 | EBI-1210503, EBI-10180409 | |
BINARY | O14647 | THAP1 Q9NVV9 | 3 | EBI-1210503, EBI-741515 | |
BINARY | O14647 | TRIM41 Q8WV44 | 4 | EBI-1210503, EBI-725997 | |
BINARY | O14647-3 | ELOA2 Q8IYF1 | 3 | EBI-11985957, EBI-741705 | |
BINARY | O14647-3 | MEOX2 Q6FHY5 | 3 | EBI-11985957, EBI-16439278 | |
BINARY | O14647-3 | TRIM54 Q9BYV2 | 3 | EBI-11985957, EBI-2130429 | |
BINARY | O14647-3 | ZNF398 Q8TD17 | 3 | EBI-11985957, EBI-8643207 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-243 | Disordered | ||||
Sequence: MMRNKDKSQEEDSSLHSNASSHSASEEASGSDSGSQSESEQGSDPGSGHGSESNSSSESSESQSESESESAGSKSQPVLPEAKEKPASKKERIADVKKMWEEYPDVYGVRRSNRSRQEPSRFNIKEEASSGSESGSPKRRGQRQLKKQEKWKQEPSEDEQEQGTSAESEPEQKKVKARRPVPRRTVPKPRVKKQPKTQRGKRKKQDSSDEDDDDDEAPKRQTRRRAAKNVSYKEDDDFETDSD | ||||||
Compositional bias | 14-75 | Polar residues | ||||
Sequence: SLHSNASSHSASEEASGSDSGSQSESEQGSDPGSGHGSESNSSSESSESQSESESESAGSKS | ||||||
Compositional bias | 83-123 | Basic and acidic residues | ||||
Sequence: KEKPASKKERIADVKKMWEEYPDVYGVRRSNRSRQEPSRFN | ||||||
Compositional bias | 124-138 | Polar residues | ||||
Sequence: IKEEASSGSESGSPK | ||||||
Compositional bias | 139-159 | Basic and acidic residues | ||||
Sequence: RRGQRQLKKQEKWKQEPSEDE | ||||||
Compositional bias | 177-200 | Basic residues | ||||
Sequence: ARRPVPRRTVPKPRVKKQPKTQRG | ||||||
Compositional bias | 216-235 | Basic and acidic residues | ||||
Sequence: EAPKRQTRRRAAKNVSYKED | ||||||
Domain | 261-353 | Chromo 1 | ||||
Sequence: ETIEKVLDSRLGKKGATGASTTVYAIEANGDPSGDFDTEKDEGEIQYLIKWKGWSYIHSTWESEESLQQQKVKGLKKLENFKKKEDEIKQWLG | ||||||
Domain | 378-456 | Chromo 2 | ||||
Sequence: QIVERVIAVKTSKSTLGQTDFPAHSRKPAPSNEPEYLCKWMGLPYSECSWEDEALIGKKFQNCIDSFHSRNNSKTIPTR | ||||||
Domain | 496-666 | Helicase ATP-binding | ||||
Sequence: AHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLIVVPLSTLTSWQREFEIWAPEINVVVYIGDLMSRNTIREYEWIHSQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPE | ||||||
Motif | 617-620 | DEAH box | ||||
Sequence: DEAH | ||||||
Domain | 795-946 | Helicase C-terminal | ||||
Sequence: LLDKLLTRLRERGNRVLIFSQMVRMLDILAEYLTIKHYPFQRLDGSIKGEIRKQALDHFNADGSEDFCFLLSTRAGGLGINLASADTVVIFDSDWNPQNDLQAQARAHRIGQKKQVNIYRLVTKGTVEEEIIERAKKKMVLDHLVIQRMDTT | ||||||
Compositional bias | 1030-1069 | Basic and acidic residues | ||||
Sequence: EDEEELEERPHKDWDEIIPEEQRKKVEEEERQKELEEIYM | ||||||
Region | 1030-1124 | Disordered | ||||
Sequence: EDEEELEERPHKDWDEIIPEEQRKKVEEEERQKELEEIYMLPRIRSSTKKAQTNDSDSDTESKRQAQRSSASESETEDSDDDKKPKRRGRPRSVR | ||||||
Compositional bias | 1079-1124 | Basic and acidic residues | ||||
Sequence: KAQTNDSDSDTESKRQAQRSSASESETEDSDDDKKPKRRGRPRSVR | ||||||
Region | 1331-1462 | Disordered | ||||
Sequence: VTGGEEAKLKKRKPRVKKENKVPRLKEEHGIELSSPRHSDNPSEEGEVKDDGLEKSPMKKKQKKKENKENKEKQMSSRKDKEGDKERKKSKDKKEKPKSGDAKSSSKSKRSQGPVHITAGSEPVPIGEDEDD | ||||||
Compositional bias | 1350-1435 | Basic and acidic residues | ||||
Sequence: NKVPRLKEEHGIELSSPRHSDNPSEEGEVKDDGLEKSPMKKKQKKKENKENKEKQMSSRKDKEGDKERKKSKDKKEKPKSGDAKSS | ||||||
Region | 1464-1566 | CHD1 helical C-terminal domain (CHCT) | ||||
Sequence: LDQETFSICKERMRPVKKALKQLDKPDKGLNVQEQLEHTRNCLLKIGDRIAECLKAYSDQEHIKLWRRNLWIFVSKFTEFDARKLHKLYKMAHKKRSQEEEEQ | ||||||
Compositional bias | 1556-1577 | Basic and acidic residues | ||||
Sequence: HKKRSQEEEEQKKKDDVTGGKK | ||||||
Region | 1556-1638 | Disordered | ||||
Sequence: HKKRSQEEEEQKKKDDVTGGKKPFRPEASGSSRDSLISQSHTSHNLHPQKPHLPASHGPQMHGHPRDNYNHPNKRHFSNADRG | ||||||
Compositional bias | 1586-1604 | Polar residues | ||||
Sequence: SSRDSLISQSHTSHNLHPQ | ||||||
Compositional bias | 1622-1638 | Basic and acidic residues | ||||
Sequence: DNYNHPNKRHFSNADRG | ||||||
Region | 1680-1828 | Disordered | ||||
Sequence: HMDAHRSGSYRPNNMSRKRPYDQYSSDRDHRGHRDYYDRHHHDSKRRRSDEFRPQNYHQQDFRRMSDHRPAMGYHGQGPSDHYRSFHTDKLGEYKQPLPPLHPAVSDPRSPPSQKSPHDSKSPLDHRSPLERSLEQKNNPDYNWNVRKT | ||||||
Compositional bias | 1700-1749 | Basic and acidic residues | ||||
Sequence: YDQYSSDRDHRGHRDYYDRHHHDSKRRRSDEFRPQNYHQQDFRRMSDHRP | ||||||
Compositional bias | 1798-1813 | Basic and acidic residues | ||||
Sequence: DSKSPLDHRSPLERSL | ||||||
Compositional bias | 1814-1828 | Polar residues | ||||
Sequence: EQKNNPDYNWNVRKT |
Domain
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
O14647-1
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
- Length1,828
- Mass (Da)211,344
- Last updated2006-12-12 v2
- Checksum13139D6059210F00
O14647-2
- Name2
- Differences from canonical
- 1719-1739: HHHDSKRRRSDEFRPQNYHQQ → YAKGCETPGANLCQELFLGRK
- 1740-1828: Missing
O14647-3
- Name3
- Differences from canonical
- 502-1828: Missing
Computationally mapped potential isoform sequences
There are 19 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A1B0GU59 | A0A1B0GU59_HUMAN | CHD2 | 219 | ||
A0A1B0GTU9 | A0A1B0GTU9_HUMAN | CHD2 | 954 | ||
A0A1B0GTM9 | A0A1B0GTM9_HUMAN | CHD2 | 98 | ||
B7Z3I4 | B7Z3I4_HUMAN | CHD2 | 514 | ||
A0A0D9SEH6 | A0A0D9SEH6_HUMAN | CHD2 | 35 | ||
A0A0D9SEP7 | A0A0D9SEP7_HUMAN | CHD2 | 704 | ||
A0A0D9SGK0 | A0A0D9SGK0_HUMAN | CHD2 | 425 | ||
A0A0D9SFV4 | A0A0D9SFV4_HUMAN | CHD2 | 45 | ||
A0A0D9SFV8 | A0A0D9SFV8_HUMAN | CHD2 | 71 | ||
A0A0D9SGA6 | A0A0D9SGA6_HUMAN | CHD2 | 31 | ||
A0A0D9SET4 | A0A0D9SET4_HUMAN | CHD2 | 34 | ||
A0A0D9SEU0 | A0A0D9SEU0_HUMAN | CHD2 | 1149 | ||
A0A0D9SF92 | A0A0D9SF92_HUMAN | CHD2 | 113 | ||
A0A0D9SFA3 | A0A0D9SFA3_HUMAN | CHD2 | 121 | ||
A0A8V8TRB2 | A0A8V8TRB2_HUMAN | CHD2 | 588 | ||
A0A8V8TQC6 | A0A8V8TQC6_HUMAN | CHD2 | 604 | ||
A0A8V8TQD9 | A0A8V8TQD9_HUMAN | CHD2 | 36 | ||
A0A8V8TR03 | A0A8V8TR03_HUMAN | CHD2 | 355 | ||
A0A8V8TPT9 | A0A8V8TPT9_HUMAN | CHD2 | 137 |
Features
Showing features for compositional bias, alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 14-75 | Polar residues | ||||
Sequence: SLHSNASSHSASEEASGSDSGSQSESEQGSDPGSGHGSESNSSSESSESQSESESESAGSKS | ||||||
Compositional bias | 83-123 | Basic and acidic residues | ||||
Sequence: KEKPASKKERIADVKKMWEEYPDVYGVRRSNRSRQEPSRFN | ||||||
Compositional bias | 124-138 | Polar residues | ||||
Sequence: IKEEASSGSESGSPK | ||||||
Compositional bias | 139-159 | Basic and acidic residues | ||||
Sequence: RRGQRQLKKQEKWKQEPSEDE | ||||||
Compositional bias | 177-200 | Basic residues | ||||
Sequence: ARRPVPRRTVPKPRVKKQPKTQRG | ||||||
Compositional bias | 216-235 | Basic and acidic residues | ||||
Sequence: EAPKRQTRRRAAKNVSYKED | ||||||
Alternative sequence | VSP_042791 | 502-1828 | in isoform 3 | |||
Sequence: Missing | ||||||
Compositional bias | 1030-1069 | Basic and acidic residues | ||||
Sequence: EDEEELEERPHKDWDEIIPEEQRKKVEEEERQKELEEIYM | ||||||
Compositional bias | 1079-1124 | Basic and acidic residues | ||||
Sequence: KAQTNDSDSDTESKRQAQRSSASESETEDSDDDKKPKRRGRPRSVR | ||||||
Sequence conflict | 1156 | in Ref. 1; AAB87382 | ||||
Sequence: I → L | ||||||
Compositional bias | 1350-1435 | Basic and acidic residues | ||||
Sequence: NKVPRLKEEHGIELSSPRHSDNPSEEGEVKDDGLEKSPMKKKQKKKENKENKEKQMSSRKDKEGDKERKKSKDKKEKPKSGDAKSS | ||||||
Compositional bias | 1556-1577 | Basic and acidic residues | ||||
Sequence: HKKRSQEEEEQKKKDDVTGGKK | ||||||
Compositional bias | 1586-1604 | Polar residues | ||||
Sequence: SSRDSLISQSHTSHNLHPQ | ||||||
Compositional bias | 1622-1638 | Basic and acidic residues | ||||
Sequence: DNYNHPNKRHFSNADRG | ||||||
Compositional bias | 1700-1749 | Basic and acidic residues | ||||
Sequence: YDQYSSDRDHRGHRDYYDRHHHDSKRRRSDEFRPQNYHQQDFRRMSDHRP | ||||||
Alternative sequence | VSP_021918 | 1719-1739 | in isoform 2 | |||
Sequence: HHHDSKRRRSDEFRPQNYHQQ → YAKGCETPGANLCQELFLGRK | ||||||
Alternative sequence | VSP_021919 | 1740-1828 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 1798-1813 | Basic and acidic residues | ||||
Sequence: DSKSPLDHRSPLERSL | ||||||
Compositional bias | 1814-1828 | Polar residues | ||||
Sequence: EQKNNPDYNWNVRKT |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF006514 EMBL· GenBank· DDBJ | AAB87382.1 EMBL· GenBank· DDBJ | mRNA | ||
BT007050 EMBL· GenBank· DDBJ | AAP35699.1 EMBL· GenBank· DDBJ | mRNA | ||
FJ515838 EMBL· GenBank· DDBJ | ACS13730.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AC013394 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471101 EMBL· GenBank· DDBJ | EAX02160.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC007347 EMBL· GenBank· DDBJ | AAH07347.1 EMBL· GenBank· DDBJ | mRNA | ||
CR978407 EMBL· GenBank· DDBJ | - | mRNA | No translation available. |