Q14839 · CHD4_HUMAN
- ProteinChromodomain-helicase-DNA-binding protein 4
- GeneCHD4
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1912 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin (PubMed:16428440, PubMed:17626165, PubMed:28977666, PubMed:9804427).
Localizes to acetylated damaged chromatin in a ZMYND8-dependent manner, to promote transcriptional repression and double-strand break repair by homologous recombination (PubMed:25593309).
Involved in neurogenesis (By similarity).
Miscellaneous
Catalytic activity
- ATP + H2O = ADP + H+ + phosphate
Cofactor
Features
Showing features for binding site.
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
The subsequence EIILCDTCPRAYHMVCLDPDMEKAPEGKWSCPHCEKEGIQWEAKEDNSEGEEILEEVGGDLEEEDDHHMEFCRVCKDGGE shows transcriptional repressor activity in a high-throughput recruitment assay.
Names & Taxonomy
Protein names
- Recommended nameChromodomain-helicase-DNA-binding protein 4
- EC number
- Short namesCHD-4
- Alternative names
Gene names
- Community suggested namesCHD4
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ14839
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Sifrim-Hitz-Weiss syndrome (SIHIWES)
- Note
- DescriptionAn autosomal dominant syndrome characterized by intellectual disability, variable congenital defects affecting cardiac, skeletal, and urogenital systems. Short stature, macrocephaly, hearing impairment, and facial dysmorphism are present in some patients.
- See alsoMIM:617159
Natural variants in SIHIWES
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_077146 | 851 | S>Y | in SIHIWES; dbSNP:rs886039916 | |
VAR_077147 | 1003 | G>D | in SIHIWES | |
VAR_077148 | 1068 | R>H | in SIHIWES; dbSNP:rs886039915 | |
VAR_077149 | 1127 | R>Q | in SIHIWES; no effect on interaction with HDAC1; no effect on nuclear localization; dbSNP:rs886039917 | |
VAR_077150 | 1148 | W>L | in SIHIWES; dbSNP:rs886039919 | |
VAR_077151 | 1173 | R>L | in SIHIWES; no effect on interaction with HDAC1; no effect on nuclear localization; dbSNP:rs886039918 | |
VAR_077152 | 1608 | V>I | in SIHIWES; uncertain significance; dbSNP:rs201992075 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_031674 | 139 | in dbSNP:rs1639122 | |||
Sequence: E → D | ||||||
Natural variant | VAR_077146 | 851 | in SIHIWES; dbSNP:rs886039916 | |||
Sequence: S → Y | ||||||
Natural variant | VAR_077147 | 1003 | in SIHIWES | |||
Sequence: G → D | ||||||
Natural variant | VAR_077148 | 1068 | in SIHIWES; dbSNP:rs886039915 | |||
Sequence: R → H | ||||||
Natural variant | VAR_077149 | 1127 | in SIHIWES; no effect on interaction with HDAC1; no effect on nuclear localization; dbSNP:rs886039917 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_077150 | 1148 | in SIHIWES; dbSNP:rs886039919 | |||
Sequence: W → L | ||||||
Natural variant | VAR_077151 | 1173 | in SIHIWES; no effect on interaction with HDAC1; no effect on nuclear localization; dbSNP:rs886039918 | |||
Sequence: R → L | ||||||
Natural variant | VAR_077152 | 1608 | in SIHIWES; uncertain significance; dbSNP:rs201992075 | |||
Sequence: V → I | ||||||
Natural variant | VAR_031675 | 1648 | in dbSNP:rs35512811 | |||
Sequence: S → L | ||||||
Natural variant | VAR_031676 | 1655 | in dbSNP:rs16932768 | |||
Sequence: I → V |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,186 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), cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000080228 | 1-1912 | UniProt | Chromodomain-helicase-DNA-binding protein 4 | |||
Sequence: MASGLGSPSPCSAGSEEEDMDALLNNSLPPPHPENEEDPEEDLSETETPKLKKKKKPKKPRDPKIPKSKRQKKERMLLCRQLGDSSGEGPEFVEEEEEVALRSDSEGSDYTPGKKKKKKLGPKKEKKSKSKRKEEEEEEDDDDDSKEPKSSAQLLEDWGMEDIDHVFSEEDYRTLTNYKAFSQFVRPLIAAKNPKIAVSKMMMVLGAKWREFSTNNPFKGSSGASVAAAAAAAVAVVESMVTATEVAPPPPPVEVPIRKAKTKEGKGPNARRKPKGSPRVPDAKKPKPKKVAPLKIKLGGFGSKRKRSSSEDDDLDVESDFDDASINSYSVSDGSTSRSSRSRKKLRTTKKKKKGEEEVTAVDGYETDHQDYCEVCQQGGEIILCDTCPRAYHMVCLDPDMEKAPEGKWSCPHCEKEGIQWEAKEDNSEGEEILEEVGGDLEEEDDHHMEFCRVCKDGGELLCCDTCPSSYHIHCLNPPLPEIPNGEWLCPRCTCPALKGKVQKILIWKWGQPPSPTPVPRPPDADPNTPSPKPLEGRPERQFFVKWQGMSYWHCSWVSELQLELHCQVMFRNYQRKNDMDEPPSGDFGGDEEKSRKRKNKDPKFAEMEERFYRYGIKPEWMMIHRILNHSVDKKGHVHYLIKWRDLPYDQASWESEDVEIQDYDLFKQSYWNHRELMRGEEGRPGKKLKKVKLRKLERPPETPTVDPTVKYERQPEYLDATGGTLHPYQMEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVTYVGDKDSRAIIRENEFSFEDNAIRGGKKASRMKKEASVKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFADIAKEDQIKKLHDMLGPHMLRRLKADVFKNMPSKTELIVRVELSPMQKKYYKYILTRNFEALNARGGGNQVSLLNVVMDLKKCCNHPYLFPVAAMEAPKMPNGMYDGSALIRASGKLLLLQKMLKNLKEGGHRVLIFSQMTKMLDLLEDFLEHEGYKYERIDGGITGNMRQEAIDRFNAPGAQQFCFLLSTRAGGLGINLATADTVIIYDSDWNPHNDIQAFSRAHRIGQNKKVMIYRFVTRASVEERITQVAKKKMMLTHLVVRPGLGSKTGSMSKQELDDILKFGTEELFKDEATDGGGDNKEGEDSSVIHYDDKAIERLLDRNQDETEDTELQGMNEYLSSFKVAQYVVREEEMGEEEEVEREIIKQEESVDPDYWEKLLRHHYEQQQEDLARNLGKGKRIRKQVNYNDGSQEDRDWQDDQSDNQSDYSVASEEGDEDFDERSEAPRRPSRKGLRNDKDKPLPPLLARVGGNIEVLGFNARQRKAFLNAIMRYGMPPQDAFTTQWLVRDLRGKSEKEFKAYVSLFMRHLCEPGADGAETFADGVPREGLSRQHVLTRIGVMSLIRKKVQEFEHVNGRWSMPELAEVEENKKMSQPGSPSPKTPTPSTPGDTQPNTPAPVPPAEDGIKIEENSLKEEESIEGEKEVKSTAPETAIECTQAPAPASEDEKVVVEPPEGEEKVEKAEVKERTEEPMETEPKGAADVEKVEEKSAIDLTPIVVEDKEEKKEEEEKKEVMLQNGETPKDLNDEKQKKNIKQRFMFNIADGGFTELHSLWQNEERAATVTKKTYEIWHRRHDYWLLAGIINHGYARWQDIQNDPRYAILNEPFKGEMNRGNFLEIKNKFLARRFKLLEQALVIEEQLRRAAYLNMSEDPSHPSMALNTRFAEVECLAESHQHLSKESMAGNKPANAVLHKVLKQLEELLSDMKADVTRLPATIARIPPVAVRLQMSERNILSRLANRAPEPTPQQVAQQQ | |||||||
Modified residue | 44 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 85 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 86 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 103 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 105 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 108 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 133 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 146 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 179 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 277 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 297 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 303 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 304 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 308 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 309 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 310 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 319 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 319 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 367 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 367 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 428 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 428 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 515 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 515 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 517 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 517 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 529 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 529 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 531 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 531 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 618 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 696 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 703 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 703 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Cross-link | 711 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate | ||||
Sequence: K | |||||||
Cross-link | 711 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Modified residue | 1209 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 1212 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 1228 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 1239 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 1244 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1245 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 1304 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 1308 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1308 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1349 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1349 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1370 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 1528 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 1529 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 1531 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1531 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1535 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1535 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1537 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1537 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1540 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1542 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1542 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1544 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1545 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1549 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1549 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1553 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1553 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Cross-link | 1565 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 1570 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1570 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 1572 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 1576 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1576 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 1584 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 1602 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1602 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 1606 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 1617 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 1636 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 1643 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Cross-link | 1643 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Cross-link | 1647 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 1648 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1653 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1653 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Cross-link | 1660 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 1670 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 1679 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1679 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Cross-link | 1687 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 1865 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Subunit
The exact stoichiometry of the NuRD complex is unknown, and some subunits such as MBD2 and MBD3, GATAD2A and GATAD2B, and CHD3, CHD4 and CHD5 define mutually exclusive NuRD complexes (PubMed:16428440, PubMed:28977666, PubMed:33283408).
Interacts with IKFZ1; the interaction is direct and when in part of the NuRD complex (By similarity).
Part of a complex containing ATR and HDAC2 (PubMed:10545197).
Interacts with HDAC2; the interaction is direct (PubMed:12198550, PubMed:25593309).
Interacts with the cohesin complex component RAD21; the interaction is direct (PubMed:12198550).
Interacts with the ISWI chromatin remodeling complex component SMARCA5; the interaction is direct (PubMed:12198550).
Interacts with ZGPAT; the interaction is direct (PubMed:19644445).
Interacts with ZMYND8; the interaction is direct, appears to occur with monomeric ZMYND8, and is increased following DNA damage (PubMed:25593309, PubMed:30134174, PubMed:36064715).
Interacts with BCL6 (PubMed:15454082).
Interacts with BRD4 (PubMed:21555454).
Interacts with CBX1 (PubMed:28977666).
Interacts with CBX3 (PubMed:28977666).
Interacts with CBX5 (PubMed:28977666).
Interacts with GATAD2A (PubMed:33283408).
Interacts with HDAC1 (PubMed:25593309, PubMed:27616479, PubMed:28977666, PubMed:36064715).
Interacts with KLF1; the interaction depends on sumoylation of KLF1, and leads to its transcriptional repression (By similarity).
Interacts with MTA1 (PubMed:28977666).
Interacts with PCNT (PubMed:17626165).
Interacts with RBBP7 (PubMed:28977666).
Interacts with SETX (PubMed:23149945).
Interacts with TRIM27 (PubMed:14530259).
Interacts with histone H3 (PubMed:32543371).
Interacts with histone H4 (PubMed:32543371).
Does not interact with PWWP2A (By similarity).
Does not interact with PWWP2B (By similarity).
Interacts (via KIKL motif) with BRD3 (via NET domain) (PubMed:29567837).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q14839 | HDAC1 Q13547 | 15 | EBI-372916, EBI-301834 | |
BINARY | Q14839 | MYC P01106 | 2 | EBI-372916, EBI-447544 | |
XENO | Q14839 | Tbx5 P70326 | 3 | EBI-372916, EBI-8411807 | |
BINARY | Q14839 | ZNF827 Q17R98 | 2 | EBI-372916, EBI-5564776 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, motif, zinc finger, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-157 | Disordered | ||||
Sequence: MASGLGSPSPCSAGSEEEDMDALLNNSLPPPHPENEEDPEEDLSETETPKLKKKKKPKKPRDPKIPKSKRQKKERMLLCRQLGDSSGEGPEFVEEEEEVALRSDSEGSDYTPGKKKKKKLGPKKEKKSKSKRKEEEEEEDDDDDSKEPKSSAQLLED | ||||||
Compositional bias | 52-74 | Basic residues | ||||
Sequence: KKKKKPKKPRDPKIPKSKRQKKE | ||||||
Region | 243-360 | Disordered | ||||
Sequence: ATEVAPPPPPVEVPIRKAKTKEGKGPNARRKPKGSPRVPDAKKPKPKKVAPLKIKLGGFGSKRKRSSSEDDDLDVESDFDDASINSYSVSDGSTSRSSRSRKKLRTTKKKKKGEEEVT | ||||||
Compositional bias | 257-289 | Basic and acidic residues | ||||
Sequence: IRKAKTKEGKGPNARRKPKGSPRVPDAKKPKPK | ||||||
Motif | 295-298 | KIKL | ||||
Sequence: KIKL | ||||||
Compositional bias | 323-337 | Polar residues | ||||
Sequence: DASINSYSVSDGSTS | ||||||
Zinc finger | 370-417 | PHD-type 1 | ||||
Sequence: QDYCEVCQQGGEIILCDTCPRAYHMVCLDPDMEKAPEGKWSCPHCEKE | ||||||
Zinc finger | 449-496 | PHD-type 2 | ||||
Sequence: MEFCRVCKDGGELLCCDTCPSSYHIHCLNPPLPEIPNGEWLCPRCTCP | ||||||
Domain | 494-594 | Chromo 1 | ||||
Sequence: TCPALKGKVQKILIWKWGQPPSPTPVPRPPDADPNTPSPKPLEGRPERQFFVKWQGMSYWHCSWVSELQLELHCQVMFRNYQRKNDMDEPPSGDFGGDEEK | ||||||
Region | 510-538 | Disordered | ||||
Sequence: WGQPPSPTPVPRPPDADPNTPSPKPLEGR | ||||||
Compositional bias | 513-534 | Pro residues | ||||
Sequence: PPSPTPVPRPPDADPNTPSPKP | ||||||
Region | 578-603 | Disordered | ||||
Sequence: NDMDEPPSGDFGGDEEKSRKRKNKDP | ||||||
Domain | 622-697 | Chromo 2 | ||||
Sequence: MMIHRILNHSVDKKGHVHYLIKWRDLPYDQASWESEDVEIQDYDLFKQSYWNHRELMRGEEGRPGKKLKKVKLRKL | ||||||
Domain | 738-922 | Helicase ATP-binding | ||||
Sequence: RFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVTYVGDKDSRAIIRENEFSFEDNAIRGGKKASRMKKEASVKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPE | ||||||
Motif | 873-876 | DEAH box | ||||
Sequence: DEAH | ||||||
Domain | 1054-1203 | Helicase C-terminal | ||||
Sequence: LLQKMLKNLKEGGHRVLIFSQMTKMLDLLEDFLEHEGYKYERIDGGITGNMRQEAIDRFNAPGAQQFCFLLSTRAGGLGINLATADTVIIYDSDWNPHNDIQAFSRAHRIGQNKKVMIYRFVTRASVEERITQVAKKKMMLTHLVVRPGL | ||||||
Compositional bias | 1344-1360 | Basic and acidic residues | ||||
Sequence: NYNDGSQEDRDWQDDQS | ||||||
Region | 1344-1401 | Disordered | ||||
Sequence: NYNDGSQEDRDWQDDQSDNQSDYSVASEEGDEDFDERSEAPRRPSRKGLRNDKDKPLP | ||||||
Compositional bias | 1379-1400 | Basic and acidic residues | ||||
Sequence: ERSEAPRRPSRKGLRNDKDKPL | ||||||
Region | 1525-1562 | Disordered | ||||
Sequence: EENKKMSQPGSPSPKTPTPSTPGDTQPNTPAPVPPAED | ||||||
Compositional bias | 1536-1558 | Pro residues | ||||
Sequence: PSPKTPTPSTPGDTQPNTPAPVP | ||||||
Compositional bias | 1570-1587 | Basic and acidic residues | ||||
Sequence: SLKEEESIEGEKEVKSTA | ||||||
Region | 1570-1589 | Disordered | ||||
Sequence: SLKEEESIEGEKEVKSTAPE | ||||||
Region | 1577-1912 | Required for interaction with PCNT | ||||
Sequence: IEGEKEVKSTAPETAIECTQAPAPASEDEKVVVEPPEGEEKVEKAEVKERTEEPMETEPKGAADVEKVEEKSAIDLTPIVVEDKEEKKEEEEKKEVMLQNGETPKDLNDEKQKKNIKQRFMFNIADGGFTELHSLWQNEERAATVTKKTYEIWHRRHDYWLLAGIINHGYARWQDIQNDPRYAILNEPFKGEMNRGNFLEIKNKFLARRFKLLEQALVIEEQLRRAAYLNMSEDPSHPSMALNTRFAEVECLAESHQHLSKESMAGNKPANAVLHKVLKQLEELLSDMKADVTRLPATIARIPPVAVRLQMSERNILSRLANRAPEPTPQQVAQQQ | ||||||
Region | 1594-1644 | Disordered | ||||
Sequence: CTQAPAPASEDEKVVVEPPEGEEKVEKAEVKERTEEPMETEPKGAADVEKV | ||||||
Compositional bias | 1606-1644 | Basic and acidic residues | ||||
Sequence: KVVVEPPEGEEKVEKAEVKERTEEPMETEPKGAADVEKV |
Domain
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q14839-1
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
- Length1,912
- Mass (Da)218,005
- Last updated2010-11-02 v2
- Checksum765ED8485B7BBB85
Q14839-2
- Name2
- Differences from canonical
- 1353-1353: R → RGVCGRPRPPPMGRSTRAVGPAHLPSLPP
Computationally mapped potential isoform sequences
There are 29 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
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 | ||
A0A2R8Y425 | A0A2R8Y425_HUMAN | CHD4 | 1889 | ||
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 sequence conflict, compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 34-36 | in Ref. 3; AAH38596 | ||||
Sequence: Missing | ||||||
Compositional bias | 52-74 | Basic residues | ||||
Sequence: KKKKKPKKPRDPKIPKSKRQKKE | ||||||
Compositional bias | 257-289 | Basic and acidic residues | ||||
Sequence: IRKAKTKEGKGPNARRKPKGSPRVPDAKKPKPK | ||||||
Compositional bias | 323-337 | Polar residues | ||||
Sequence: DASINSYSVSDGSTS | ||||||
Compositional bias | 513-534 | Pro residues | ||||
Sequence: PPSPTPVPRPPDADPNTPSPKP | ||||||
Compositional bias | 1344-1360 | Basic and acidic residues | ||||
Sequence: NYNDGSQEDRDWQDDQS | ||||||
Alternative sequence | VSP_011416 | 1353 | in isoform 2 | |||
Sequence: R → RGVCGRPRPPPMGRSTRAVGPAHLPSLPP | ||||||
Compositional bias | 1379-1400 | Basic and acidic residues | ||||
Sequence: ERSEAPRRPSRKGLRNDKDKPL | ||||||
Compositional bias | 1536-1558 | Pro residues | ||||
Sequence: PSPKTPTPSTPGDTQPNTPAPVP | ||||||
Compositional bias | 1570-1587 | Basic and acidic residues | ||||
Sequence: SLKEEESIEGEKEVKSTA | ||||||
Compositional bias | 1606-1644 | Basic and acidic residues | ||||
Sequence: KVVVEPPEGEEKVEKAEVKERTEEPMETEPKGAADVEKV |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X86691 EMBL· GenBank· DDBJ | CAA60384.1 EMBL· GenBank· DDBJ | mRNA | ||
AC006064 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC038596 EMBL· GenBank· DDBJ | AAH38596.1 EMBL· GenBank· DDBJ | mRNA |