Q99P96 (HDAC7_RAT) Reviewed, UniProtKB/Swiss-Prot
Last modified May 1, 2013. Version 79. History...
Names and origin
|Protein names||Recommended name:|
Histone deacetylase 7
Histone deacetylase 7A
|Organism||Rattus norvegicus (Rat) [Reference proteome]|
|Taxonomic identifier||10116 [NCBI]|
|Taxonomic lineage||Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus|
|Sequence length||238 AA.|
|Protein existence||Evidence at transcript level|
General annotation (Comments)
Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Involved in muscle maturation by repressing transcription of myocyte enhancer factors such as MEF2A, MEF2B and MEF2C. During muscle differentiation, it shuttles into the cytoplasm, allowing the expression of myocyte enhancer factors By similarity.
Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone.
Interacts with KAT5 and EDNRA. Interacts with HDAC1, HDAC2, HDAC3, HDAC4, HDAC5, NCOR1, NCOR2, SIN3A, SIN3B, RBBP4, RBBP7, MTA1L1, SAP30 and MBD3. Interacts with the 14-3-3 protein YWHAE, MEF2A, MEF2B and MEF2C. Interacts with KDM5B By similarity. Interacts with ZMYND15 By similarity. Interacts with PML By similarity.
Nucleus By similarity. Cytoplasm By similarity. Note: In the nucleus, it associates with distinct subnuclear dot-like structures. Shuttles between the nucleus and the cytoplasm. In muscle cells, it shuttles into the cytoplasm during myocyte differentiation. The export to cytoplasm depends on the interaction with the 14-3-3 protein YWHAE and is due to its phosphorylation By similarity.
The nuclear export sequence mediates the shuttling between the nucleus and the cytoplasm By similarity.
May be phosphorylated by CaMK1. Phosphorylated by the PKC kinases PKN1 and PKN2, impairing nuclear import. Phosphorylation at Ser-164 by MARK2, MARK3 and PRKD1 promotes interaction with 14-3-3 proteins and export from the nucleus. Phosphorylation at Ser-164 is a prerequisite for phosphorylation at Ser-190 By similarity.
Its activity is inhibited by Trichostatin A (TSA), a known histone deacetylase inhibitor By similarity.
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Chain||‹1 – ›238||›238||Histone deacetylase 7||PRO_0000114707|
Amino acid modifications
|Modified residue||118||1||Phosphoserine By similarity|
|Modified residue||164||1||Phosphoserine; by MARK2, MARK3 and PKD/PRKD1 By similarity|
|Modified residue||190||1||Phosphoserine; by PKD/PRKD2 By similarity|
|AF321135 mRNA. Translation: AAK11188.1.|
3D structure databases
Protein-protein interaction databases
Protocols and materials databases
Genome annotation databases
|UCSC||RGD:619982. rat. |
|RGD||619982. Hdac7. |
Gene expression databases
|GermOnline||ENSRNOG00000008308. Rattus norvegicus. |
Family and domain databases
|Accession||Primary (citable) accession number: Q99P96|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Chordata Protein Annotation Program|
Index of protein domains and families