Q8WXI9 · P66B_HUMAN
- ProteinTranscriptional repressor p66-beta
- GeneGATAD2B
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids593 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Transcriptional repressor (PubMed:12183469, PubMed:16415179).
Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin (PubMed:16428440, PubMed:28977666).
Enhances MBD2-mediated repression (PubMed:12183469, PubMed:16415179).
Efficient repression requires the presence of GATAD2A (PubMed:16415179).
Targets MBD3 to discrete loci in the nucleus (PubMed:11756549).
May play a role in synapse development (PubMed:23644463).
Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin (PubMed:16428440, PubMed:28977666).
Enhances MBD2-mediated repression (PubMed:12183469, PubMed:16415179).
Efficient repression requires the presence of GATAD2A (PubMed:16415179).
Targets MBD3 to discrete loci in the nucleus (PubMed:11756549).
May play a role in synapse development (PubMed:23644463).
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 | chromosome, telomeric region | |
Cellular Component | nuclear speck | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Cellular Component | NuRD complex | |
Cellular Component | protein-containing complex | |
Molecular Function | sequence-specific DNA binding | |
Molecular Function | zinc ion binding | |
Biological Process | chromatin remodeling | |
Biological Process | negative regulation of DNA-templated transcription | |
Biological Process | negative regulation of transcription by RNA polymerase II | |
Biological Process | positive regulation of DNA-templated transcription | |
Biological Process | regulation of cell fate specification | |
Biological Process | regulation of stem cell differentiation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
The subsequence PVVQNAASIVQPSPAHVGQQGLSKLPSRPGAQGVEPQNLRTLQGHSVIRSATNTTLPHMLMSQRVIAPNPAQLQGQRGPP shows transcriptional repressor activity in a high-throughput recruitment assay.
Names & Taxonomy
Protein names
- Recommended nameTranscriptional repressor p66-beta
- Alternative names
Gene names
- Community suggested namesGATAD2B
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ8WXI9
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Gand syndrome (GAND)
- Note
- DescriptionAn autosomal dominant syndrome characterized by global developmental delay with motor delay, moderate to severely impaired intellectual development, and poor speech acquisition in most patients. Additional features include hypotonia, feeding difficulties in infancy, and dysmorphic features. More variable features may include seizures, cardiac abnormalities, and non-specific findings on brain imaging.
- See alsoMIM:615074
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_069363 | 316 | ||||
Sequence: I → V | ||||||
Natural variant | VAR_069364 | 586 | ||||
Sequence: S → L |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,014 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, modified residue (large scale data), cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000083502 | 1-593 | UniProt | Transcriptional repressor p66-beta | |||
Sequence: MDRMTEDALRLNLLKRSLDPADERDDVLAKRLKMEGHEAMERLKMLALLKRKDLANLEVPHELPTKQDGSGVKGYEEKLNGNLRPHGDNRTAGRPGKENINDEPVDMSARRSEPERGRLTPSPDIIVLSDNEASSPRSSSRMEERLKAANLEMFKGKGIEERQQLIKQLRDELRLEEARLVLLKKLRQSQLQKENVVQKTPVVQNAASIVQPSPAHVGQQGLSKLPSRPGAQGVEPQNLRTLQGHSVIRSATNTTLPHMLMSQRVIAPNPAQLQGQRGPPKPGLVRTTTPNMNPAINYQPQSSSSVPCQRTTSSAIYMNLASHIQPGTVNRVSSPLPSPSAMTDAANSQAAAKLALRKQLEKTLLEIPPPKPPAPLLHFLPSAANSEFIYMVGLEEVVQSVIDSQGKSCASLLRVEPFVCAQCRTDFTPHWKQEKNGKILCEQCMTSNQKKALKAEHTNRLKNAFVKALQQEQEIEQRLQQQAALSPTTAPAVSSVSKQETIMRHHTLRQAPQPQSSLQRGIPTSARSMLSNFAQAPQLSVPGGLLGMPGVNIAYLNTGIGGHKGPSLADRQREYLLDMIPPRSISQSISGQK | |||||||
Modified residue | 17 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 17 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 33 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 66 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 97 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 112 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 120 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 120 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 122 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 122 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 129 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 129 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 134 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 134 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 135 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 135 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 140 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 147 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 199 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 200 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 208 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 208 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 213 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 281 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 317 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 333 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 333 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 334 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 338 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 338 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 340 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 340 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 353 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 454 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 467 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 486 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 486 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 488 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Cross-link | 498 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Widely expressed.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Homooligomer (PubMed:27732854).
Component of the nucleosome remodeling and deacetylase (NuRD) repressor complex, composed of core proteins MTA1, MTA2, MTA3, RBBP4, RBBP7, HDAC1, HDAC2, MBD2, MBD3, and peripherally associated proteins CDK2AP1, CDK2AP2, GATAD2A, GATAD2B, CHD3, CHD4 and CHD5 (PubMed:16428440, PubMed:28977666, PubMed:33283408).
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:27732854, PubMed:28977666, PubMed:33283408).
Interacts with MBD2; this is required for the enhancement of MBD2-mediated repression and for targeting to the chromatin (PubMed:11756549, PubMed:12183469, PubMed:16415179, PubMed:27732854).
Interacts with MBD3 (PubMed:11756549, PubMed:12183469, PubMed:27732854).
Component of the MeCP1 histone deacetylase complex (PubMed:11756549).
Interacts with histone tails, including that of histones H2A, H2B, H3 and H4 (PubMed:16415179).
Interacts with ERCC6 (PubMed:26030138).
Component of the nucleosome remodeling and deacetylase (NuRD) repressor complex, composed of core proteins MTA1, MTA2, MTA3, RBBP4, RBBP7, HDAC1, HDAC2, MBD2, MBD3, and peripherally associated proteins CDK2AP1, CDK2AP2, GATAD2A, GATAD2B, CHD3, CHD4 and CHD5 (PubMed:16428440, PubMed:28977666, PubMed:33283408).
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:27732854, PubMed:28977666, PubMed:33283408).
Interacts with MBD2; this is required for the enhancement of MBD2-mediated repression and for targeting to the chromatin (PubMed:11756549, PubMed:12183469, PubMed:16415179, PubMed:27732854).
Interacts with MBD3 (PubMed:11756549, PubMed:12183469, PubMed:27732854).
Component of the MeCP1 histone deacetylase complex (PubMed:11756549).
Interacts with histone tails, including that of histones H2A, H2B, H3 and H4 (PubMed:16415179).
Interacts with ERCC6 (PubMed:26030138).
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, coiled coil, zinc finger.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 62-123 | Disordered | ||||
Sequence: ELPTKQDGSGVKGYEEKLNGNLRPHGDNRTAGRPGKENINDEPVDMSARRSEPERGRLTPSP | ||||||
Compositional bias | 79-118 | Basic and acidic residues | ||||
Sequence: LNGNLRPHGDNRTAGRPGKENINDEPVDMSARRSEPERGR | ||||||
Coiled coil | 140-194 | |||||
Sequence: SRMEERLKAANLEMFKGKGIEERQQLIKQLRDELRLEEARLVLLKKLRQSQLQKE | ||||||
Region | 165-195 | CR1; interaction with MBD2 and MBD3 | ||||
Sequence: LIKQLRDELRLEEARLVLLKKLRQSQLQKEN | ||||||
Region | 213-235 | Disordered | ||||
Sequence: SPAHVGQQGLSKLPSRPGAQGVE | ||||||
Region | 340-480 | CR2; histone tail-binding | ||||
Sequence: SAMTDAANSQAAAKLALRKQLEKTLLEIPPPKPPAPLLHFLPSAANSEFIYMVGLEEVVQSVIDSQGKSCASLLRVEPFVCAQCRTDFTPHWKQEKNGKILCEQCMTSNQKKALKAEHTNRLKNAFVKALQQEQEIEQRLQ | ||||||
Zinc finger | 414-467 | GATA-type | ||||
Sequence: RVEPFVCAQCRTDFTPHWKQEKNGKILCEQCMTSNQKKALKAEHTNRLKNAFVK | ||||||
Coiled coil | 449-482 | |||||
Sequence: QKKALKAEHTNRLKNAFVKALQQEQEIEQRLQQQ |
Domain
Both CR1 and CR2 regions are required for speckled nuclear localization.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length593
- Mass (Da)65,261
- Last updated2002-03-01 v1
- Checksum5EB375C7EB24210B
Computationally mapped potential isoform sequences
There are 7 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0U1RR30 | A0A0U1RR30_HUMAN | GATAD2B | 263 | ||
A0A0U1RR34 | A0A0U1RR34_HUMAN | GATAD2B | 187 | ||
A0A0U1RRM1 | A0A0U1RRM1_HUMAN | GATAD2B | 577 | ||
A0A0U1RRK3 | A0A0U1RRK3_HUMAN | GATAD2B | 149 | ||
A0A1B0GW07 | A0A1B0GW07_HUMAN | GATAD2B | 190 | ||
A0A1B0GVS4 | A0A1B0GVS4_HUMAN | GATAD2B | 27 | ||
A0A994J4D5 | A0A994J4D5_HUMAN | GATAD2B | 264 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 79-118 | Basic and acidic residues | ||||
Sequence: LNGNLRPHGDNRTAGRPGKENINDEPVDMSARRSEPERGR |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF411836 EMBL· GenBank· DDBJ | AAL39080.1 EMBL· GenBank· DDBJ | mRNA | ||
AL513523 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471121 EMBL· GenBank· DDBJ | EAW53270.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC069419 EMBL· GenBank· DDBJ | AAH69419.1 EMBL· GenBank· DDBJ | mRNA | ||
BC112052 EMBL· GenBank· DDBJ | AAI12053.1 EMBL· GenBank· DDBJ | mRNA | ||
BC112080 EMBL· GenBank· DDBJ | AAI12081.1 EMBL· GenBank· DDBJ | mRNA | ||
AB032976 EMBL· GenBank· DDBJ | BAA86464.1 EMBL· GenBank· DDBJ | mRNA |