Q8C2B3 · HDAC7_MOUSE
- ProteinHistone deacetylase 7
- GeneHdac7
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids938 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4) (PubMed:10640276, PubMed:10984530, PubMed:11279209).
Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events (PubMed:10640276, PubMed:10984530, PubMed:11279209).
Histone deacetylases act via the formation of large multiprotein complexes (PubMed:10640276, PubMed:10984530, PubMed:11279209).
Involved in muscle maturation by repressing transcription of myocyte enhancer factors such as MEF2A, MEF2B and MEF2C (PubMed:11279209).
During muscle differentiation, it shuttles into the cytoplasm, allowing the expression of myocyte enhancer factors (PubMed:11279209).
Positively regulates the transcriptional repressor activity of FOXP3 (By similarity).
Serves as a corepressor of RARA, causing its deacetylation and inhibition of RARE DNA element binding (By similarity).
In association with RARA, plays a role in the repression of microRNA-10a and thereby in the inflammatory response (By similarity).
Also acetylates non-histone proteins, such as ALKBH5 (By similarity).
Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events (PubMed:10640276, PubMed:10984530, PubMed:11279209).
Histone deacetylases act via the formation of large multiprotein complexes (PubMed:10640276, PubMed:10984530, PubMed:11279209).
Involved in muscle maturation by repressing transcription of myocyte enhancer factors such as MEF2A, MEF2B and MEF2C (PubMed:11279209).
During muscle differentiation, it shuttles into the cytoplasm, allowing the expression of myocyte enhancer factors (PubMed:11279209).
Positively regulates the transcriptional repressor activity of FOXP3 (By similarity).
Serves as a corepressor of RARA, causing its deacetylation and inhibition of RARE DNA element binding (By similarity).
In association with RARA, plays a role in the repression of microRNA-10a and thereby in the inflammatory response (By similarity).
Also acetylates non-histone proteins, such as ALKBH5 (By similarity).
Catalytic activity
- H2O + N6-acetyl-L-lysyl-[histone] = acetate + L-lysyl-[histone]
- H2O + N6-acetyl-L-lysyl-[protein] = acetate + L-lysyl-[protein]This reaction proceeds in the forward direction.
Activity regulation
Its activity is inhibited by Trichostatin A (TSA), a known histone deacetylase inhibitor.
Features
Showing features for binding site, active site, site.
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameHistone deacetylase 7
- EC number
- Short namesHD7
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ8C2B3
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: In the nucleus, it associates with distinct subnuclear dot-like structures (PubMed:10640276).
Shuttles between the nucleus and the cytoplasm (PubMed:11279209, PubMed:11585834).
In muscle cells, it shuttles into the cytoplasm during myocyte differentiation (PubMed:11279209).
The export to cytoplasm depends on the interaction with the 14-3-3 protein YWHAE and is due to its phosphorylation (PubMed:11585834).
Shuttles between the nucleus and the cytoplasm (PubMed:11279209, PubMed:11585834).
In muscle cells, it shuttles into the cytoplasm during myocyte differentiation (PubMed:11279209).
The export to cytoplasm depends on the interaction with the 14-3-3 protein YWHAE and is due to its phosphorylation (PubMed:11585834).
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 178 | Strong reduction of CaMK1-dependent nuclear export. Reduces interaction with YWHAE. | ||||
Sequence: S → A | ||||||
Mutagenesis | 344 | Strong reduction of CaMK1-dependent nuclear export. Reduces interaction with YWHAE. | ||||
Sequence: S → A | ||||||
Mutagenesis | 479 | Strong reduction of CaMK1-dependent nuclear export. Reduces interaction with YWHAE. | ||||
Sequence: S → A | ||||||
Mutagenesis | 657 | Abolishes deacetylase activity, but not the interaction with HDAC2 and HDAC3. | ||||
Sequence: H → A | ||||||
Mutagenesis | 692 | Disrupts the dot-like nuclear pattern. | ||||
Sequence: D → A | ||||||
Mutagenesis | 694 | Disrupts the dot-like nuclear pattern. Abolishes deacetylase activity, but not the interaction with HDAC2 and HDAC3. | ||||
Sequence: D → A | ||||||
Mutagenesis | 717 | Abolishes deacetylase activity, but not the interaction with HDAC2 and HDAC3. | ||||
Sequence: H → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 47 variants from UniProt as well as other sources including ClinVar and dbSNP.
Chemistry
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000114706 | 1-938 | Histone deacetylase 7 | |||
Sequence: MHSPGAGCPALQPDTPGSQPQPMDLRVGQRPTVEPPPEPALLTLQHPQRLHRHLFLAGLHQQQRSAEPMRLSMDPPMPELQGGQQEQELRQLLNKDKSKRSAVASSVVKQKLAEVILKKQQAALERTVHPSSPSIPYRTLEPLDTEGAARSVLSSFLPPVPSLPTEPPEHFPLRKTVSEPNLKLRYKPKKSLERRKNPLLRKESAPPSLRRRPAETLGDSSPSSSSTPASGCSSPNDSEHGPNPALGSEADGDRRTHSTLGPRGPVLGNPHAPLFLHHGLEPEAGGTLPSRLQPILLLDPSVSHAPLWTVPGLGPLPFHFAQPLLTTERLSGSGLHRPLNRTRSEPLPPSATASPLLAPLQPRQDRLKPHVQLIKPAISPPQRPAKPSEKPRLRQIPSAEDLETDGGGVGPMANDGLEHRESGRGPPEGRGSISLQQHQQVPPWEQQHLAGRLSQGSPGDSVLIPLAQVGHRPLSRTQSSPAAPVSLLSPEPTCQTQVLNSSETPATGLVYDSVMLKHQCSCGDNSKHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVLLYGTNPLSRLKLDNGKLTGLLAQRTFVMLPCGGVGVDTDTIWNELHSSNAARWAAGSVTDLAFKVASRELKNGFAVVRPPGHHADHSTAMGFCFFNSVAIACRQLQQHGKASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHDDGNFFPGSGAVDEVGTGSGEGFNVNVAWAGGLDPPMGDPEYLAAFRIVVMPIAREFAPDLVLVSAGFDAAEGHPAPLGGYHVSAKCFGYMTQQLMNLAGGAVVLALEGGHDLTAICDASEACVAALLGNKVDPLSEESWKQKPNLSAIRSLEAVVRVHRKYWGCMQRLASCPDSWLPRVPGADAEVEAVTALASLSVGILAEDRPSERLVEEEEPMNL | ||||||
Modified residue | 132 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 178 | Phosphoserine; by MARK2, MARK3 and PKD/PRKD1 | ||||
Sequence: S | ||||||
Modified residue | 204 | Phosphoserine; by PKD/PRKD2 | ||||
Sequence: S | ||||||
Modified residue | 344 | Phosphoserine; by PKD/PRKD1 | ||||
Sequence: S | ||||||
Modified residue | 350 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 398 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 479 | Phosphoserine; by PKD/PRKD1 | ||||
Sequence: S | ||||||
Modified residue | 480 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 582 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
May be phosphorylated by CaMK1. Phosphorylated by the PKC kinases PKN1 and PKN2, impairing nuclear import. Phosphorylation at Ser-178 by MARK2, MARK3 and PRKD1 promotes interaction with 14-3-3 proteins and export from the nucleus. Phosphorylation at Ser-178 is a prerequisite for phosphorylation at Ser-204 (By similarity).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Highly expressed in heart and lung. Expressed at intermediate level in muscle.
Gene expression databases
Interaction
Subunit
Interacts with HDAC1, HDAC2, HDAC3, HDAC4, HDAC5, NCOR1, NCOR2, SIN3A, SIN3B, RBBP4, RBBP7, MTA1L1, SAP30 and MBD3 (PubMed:10640276, PubMed:10984530).
Interacts with KAT5 and EDNRA (By similarity).
Interacts with the 14-3-3 protein YWHAE, MEF2A, MEF2B and MEF2C (PubMed:11279209, PubMed:11585834).
Interacts with ZMYND15 (PubMed:20675388).
Interacts with KDM5B (By similarity).
Interacts with PML (By similarity).
Interacts with FOXP3 (PubMed:19696312).
Interacts with RARA (By similarity).
Interacts with KAT5 and EDNRA (By similarity).
Interacts with the 14-3-3 protein YWHAE, MEF2A, MEF2B and MEF2C (PubMed:11279209, PubMed:11585834).
Interacts with ZMYND15 (PubMed:20675388).
Interacts with KDM5B (By similarity).
Interacts with PML (By similarity).
Interacts with FOXP3 (PubMed:19696312).
Interacts with RARA (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q8C2B3 | Ywhae P62259 | 5 | EBI-643830, EBI-356480 | |
XENO | Q8C2B3-1 | PRKD1 Q15139 | 3 | EBI-15705168, EBI-1181072 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-40 | Disordered | ||||
Sequence: MHSPGAGCPALQPDTPGSQPQPMDLRVGQRPTVEPPPEPA | ||||||
Region | 1-121 | Interaction with MEF2C | ||||
Sequence: MHSPGAGCPALQPDTPGSQPQPMDLRVGQRPTVEPPPEPALLTLQHPQRLHRHLFLAGLHQQQRSAEPMRLSMDPPMPELQGGQQEQELRQLLNKDKSKRSAVASSVVKQKLAEVILKKQQ | ||||||
Region | 2-254 | Transcription repression 1 | ||||
Sequence: HSPGAGCPALQPDTPGSQPQPMDLRVGQRPTVEPPPEPALLTLQHPQRLHRHLFLAGLHQQQRSAEPMRLSMDPPMPELQGGQQEQELRQLLNKDKSKRSAVASSVVKQKLAEVILKKQQAALERTVHPSSPSIPYRTLEPLDTEGAARSVLSSFLPPVPSLPTEPPEHFPLRKTVSEPNLKLRYKPKKSLERRKNPLLRKESAPPSLRRRPAETLGDSSPSSSSTPASGCSSPNDSEHGPNPALGSEADGDR | ||||||
Region | 72-172 | Interaction with MEF2A | ||||
Sequence: SMDPPMPELQGGQQEQELRQLLNKDKSKRSAVASSVVKQKLAEVILKKQQAALERTVHPSSPSIPYRTLEPLDTEGAARSVLSSFLPPVPSLPTEPPEHFP | ||||||
Region | 155-280 | Disordered | ||||
Sequence: SFLPPVPSLPTEPPEHFPLRKTVSEPNLKLRYKPKKSLERRKNPLLRKESAPPSLRRRPAETLGDSSPSSSSTPASGCSSPNDSEHGPNPALGSEADGDRRTHSTLGPRGPVLGNPHAPLFLHHGL | ||||||
Compositional bias | 217-241 | Polar residues | ||||
Sequence: LGDSSPSSSSTPASGCSSPNDSEHG | ||||||
Region | 241-533 | Transcription repression 2 | ||||
Sequence: GPNPALGSEADGDRRTHSTLGPRGPVLGNPHAPLFLHHGLEPEAGGTLPSRLQPILLLDPSVSHAPLWTVPGLGPLPFHFAQPLLTTERLSGSGLHRPLNRTRSEPLPPSATASPLLAPLQPRQDRLKPHVQLIKPAISPPQRPAKPSEKPRLRQIPSAEDLETDGGGVGPMANDGLEHRESGRGPPEGRGSISLQQHQQVPPWEQQHLAGRLSQGSPGDSVLIPLAQVGHRPLSRTQSSPAAPVSLLSPEPTCQTQVLNSSETPATGLVYDSVMLKHQCSCGDNSKHPEHAG | ||||||
Region | 331-361 | Disordered | ||||
Sequence: SGSGLHRPLNRTRSEPLPPSATASPLLAPLQ | ||||||
Region | 373-463 | Disordered | ||||
Sequence: LIKPAISPPQRPAKPSEKPRLRQIPSAEDLETDGGGVGPMANDGLEHRESGRGPPEGRGSISLQQHQQVPPWEQQHLAGRLSQGSPGDSVL | ||||||
Compositional bias | 432-454 | Polar residues | ||||
Sequence: SISLQQHQQVPPWEQQHLAGRLS | ||||||
Region | 472-491 | Disordered | ||||
Sequence: RPLSRTQSSPAAPVSLLSPE | ||||||
Region | 505-852 | Histone deacetylase | ||||
Sequence: PATGLVYDSVMLKHQCSCGDNSKHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVLLYGTNPLSRLKLDNGKLTGLLAQRTFVMLPCGGVGVDTDTIWNELHSSNAARWAAGSVTDLAFKVASRELKNGFAVVRPPGHHADHSTAMGFCFFNSVAIACRQLQQHGKASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHDDGNFFPGSGAVDEVGTGSGEGFNVNVAWAGGLDPPMGDPEYLAAFRIVVMPIAREFAPDLVLVSAGFDAAEGHPAPLGGYHVSAKCFGYMTQQLMNLAGGAVVLALEGGHDLTAICDASEACVAALLGNKVD | ||||||
Region | 864-938 | Interaction with SIN3A | ||||
Sequence: NLSAIRSLEAVVRVHRKYWGCMQRLASCPDSWLPRVPGADAEVEAVTALASLSVGILAEDRPSERLVEEEEPMNL | ||||||
Motif | 904-938 | Nuclear export signal | ||||
Sequence: AEVEAVTALASLSVGILAEDRPSERLVEEEEPMNL |
Sequence similarities
Belongs to the histone deacetylase family. HD type 2 subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 6 isoforms produced by Alternative splicing.
Q8C2B3-1
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
- Length938
- Mass (Da)101,287
- Last updated2003-05-16 v2
- Checksum8D4B455CE6F95483
Q8C2B3-2
- Name2
Q8C2B3-3
- Name3
Q8C2B3-4
- Name4
Q8C2B3-5
- Name5
- Differences from canonical
- 1-22: Missing
Q8C2B3-6
- Name6
- Differences from canonical
- 138-161: Missing
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_007432 | 1-22 | in isoform 2, isoform 3 and isoform 5 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_007433 | 138-161 | in isoform 4 and isoform 6 | |||
Sequence: Missing | ||||||
Sequence conflict | 169 | in Ref. 2; BAC27161 | ||||
Sequence: E → G | ||||||
Sequence conflict | 183 | in Ref. 2; BAC29493 | ||||
Sequence: K → M | ||||||
Compositional bias | 217-241 | Polar residues | ||||
Sequence: LGDSSPSSSSTPASGCSSPNDSEHG | ||||||
Sequence conflict | 228 | in Ref. 2; BAC27161 | ||||
Sequence: P → T | ||||||
Alternative sequence | VSP_007434 | 249 | in isoform 2, isoform 3 and isoform 4 | |||
Sequence: E → EALLGQRLRLQETSLAPFALPTVSLLPAITLGLPAPAR | ||||||
Alternative sequence | VSP_007435 | 376-382 | in isoform 2 and isoform 4 | |||
Sequence: Missing | ||||||
Compositional bias | 432-454 | Polar residues | ||||
Sequence: SISLQQHQQVPPWEQQHLAGRLS | ||||||
Sequence conflict | 487 | in Ref. 1; AAF31419 and 2; BAC40598/BAC40666 | ||||
Sequence: L → M | ||||||
Sequence conflict | 645 | in Ref. 2; BAC29493 | ||||
Sequence: K → R | ||||||
Sequence conflict | 661 | in Ref. 2; BAC40598 | ||||
Sequence: S → P | ||||||
Sequence conflict | 737 | in Ref. 1; AAF31419 | ||||
Sequence: G → A |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF207749 EMBL· GenBank· DDBJ | AAF31419.1 EMBL· GenBank· DDBJ | mRNA | ||
AK030863 EMBL· GenBank· DDBJ | BAC27161.1 EMBL· GenBank· DDBJ | mRNA | ||
AK036586 EMBL· GenBank· DDBJ | BAC29493.1 EMBL· GenBank· DDBJ | mRNA | ||
AK044287 EMBL· GenBank· DDBJ | BAC31856.1 EMBL· GenBank· DDBJ | mRNA | ||
AK088828 EMBL· GenBank· DDBJ | BAC40598.1 EMBL· GenBank· DDBJ | mRNA | ||
AK088945 EMBL· GenBank· DDBJ | BAC40666.1 EMBL· GenBank· DDBJ | mRNA | ||
BC057332 EMBL· GenBank· DDBJ | AAH57332.1 EMBL· GenBank· DDBJ | mRNA |