Q8C2B3 · HDAC7_MOUSE

  • Protein
    Histone deacetylase 7
  • Gene
    Hdac7
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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).

Catalytic activity

Activity regulation

Its activity is inhibited by Trichostatin A (TSA), a known histone deacetylase inhibitor.

Features

Showing features for binding site, active site, site.

TypeIDPosition(s)Description
Binding site520Zn2+ (UniProtKB | ChEBI)
Binding site522Zn2+ (UniProtKB | ChEBI)
Binding site528Zn2+ (UniProtKB | ChEBI)
Binding site605Zn2+ (UniProtKB | ChEBI)
Active site657
Site830Contributes to catalysis

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentcytosol
Cellular Componenthistone deacetylase complex
Cellular Componentnucleus
Molecular Function14-3-3 protein binding
Molecular Functionchromatin binding
Molecular FunctionDNA-binding transcription factor binding
Molecular Functionhistone deacetylase activity
Molecular Functionmetal ion binding
Molecular Functionprotein kinase C binding
Molecular Functionprotein lysine deacetylase activity
Molecular Functiontranscription corepressor activity
Biological ProcessB cell activation
Biological ProcessB cell differentiation
Biological Processcell-cell junction assembly
Biological Processchromatin organization
Biological Processinflammatory response
Biological Processnegative regulation of DNA-templated transcription
Biological Processnegative regulation of interleukin-2 production
Biological Processnegative regulation of non-canonical NF-kappaB signal transduction
Biological Processnegative regulation of osteoblast differentiation
Biological Processnegative regulation of striated muscle tissue development
Biological Processnegative regulation of transcription by RNA polymerase II
Biological Processnervous system development
Biological Processpositive regulation of cell migration involved in sprouting angiogenesis
Biological Processregulation of mRNA processing
Biological Processvasculogenesis

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Histone deacetylase 7
  • EC number
  • Short names
    HD7
  • Alternative names
    • Histone deacetylase 7A (HD7a)
    • Protein deacetylase HDAC7
      (EC:3.5.1.-
      ) . EC:3.5.1.- (UniProtKB | ENZYME | Rhea)

Gene names

    • Name
      Hdac7
    • Synonyms
      Hdac7a

Organism names

  • Taxonomic identifier
  • Strains
    • C57BL/6J
    • NOD
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q8C2B3
  • Secondary accessions
    • Q8C2C9
    • Q8C8X4
    • Q8CB80
    • Q8CDA3
    • Q9JL72

Proteomes

Organism-specific databases

Subcellular Location

Nucleus
Cytoplasm
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).

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis178Strong reduction of CaMK1-dependent nuclear export. Reduces interaction with YWHAE.
Mutagenesis344Strong reduction of CaMK1-dependent nuclear export. Reduces interaction with YWHAE.
Mutagenesis479Strong reduction of CaMK1-dependent nuclear export. Reduces interaction with YWHAE.
Mutagenesis657Abolishes deacetylase activity, but not the interaction with HDAC2 and HDAC3.
Mutagenesis692Disrupts the dot-like nuclear pattern.
Mutagenesis694Disrupts the dot-like nuclear pattern. Abolishes deacetylase activity, but not the interaction with HDAC2 and HDAC3.
Mutagenesis717Abolishes deacetylase activity, but not the interaction with HDAC2 and HDAC3.

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.

Go to variant viewer

Chemistry

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00001147061-938Histone deacetylase 7
Modified residue132Phosphoserine
Modified residue178Phosphoserine; by MARK2, MARK3 and PKD/PRKD1
Modified residue204Phosphoserine; by PKD/PRKD2
Modified residue344Phosphoserine; by PKD/PRKD1
Modified residue350Phosphoserine
Modified residue398Phosphoserine
Modified residue479Phosphoserine; by PKD/PRKD1
Modified residue480Phosphoserine
Modified residue582Phosphoserine

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

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).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q8C2B3Ywhae P622595EBI-643830, EBI-356480
XENO Q8C2B3-1PRKD1 Q151393EBI-15705168, EBI-1181072

Protein-protein interaction databases

Chemistry

Miscellaneous

Structure

Family & Domains

Features

Showing features for region, compositional bias, motif.

TypeIDPosition(s)Description
Region1-40Disordered
Region1-121Interaction with MEF2C
Region2-254Transcription repression 1
Region72-172Interaction with MEF2A
Region155-280Disordered
Compositional bias217-241Polar residues
Region241-533Transcription repression 2
Region331-361Disordered
Region373-463Disordered
Compositional bias432-454Polar residues
Region472-491Disordered
Region505-852Histone deacetylase
Region864-938Interaction with SIN3A
Motif904-938Nuclear export signal

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (6)
  • Sequence status
    Complete

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.

  • Length
    938
  • Mass (Da)
    101,287
  • Last updated
    2003-05-16 v2
  • Checksum
    8D4B455CE6F95483
MHSPGAGCPALQPDTPGSQPQPMDLRVGQRPTVEPPPEPALLTLQHPQRLHRHLFLAGLHQQQRSAEPMRLSMDPPMPELQGGQQEQELRQLLNKDKSKRSAVASSVVKQKLAEVILKKQQAALERTVHPSSPSIPYRTLEPLDTEGAARSVLSSFLPPVPSLPTEPPEHFPLRKTVSEPNLKLRYKPKKSLERRKNPLLRKESAPPSLRRRPAETLGDSSPSSSSTPASGCSSPNDSEHGPNPALGSEADGDRRTHSTLGPRGPVLGNPHAPLFLHHGLEPEAGGTLPSRLQPILLLDPSVSHAPLWTVPGLGPLPFHFAQPLLTTERLSGSGLHRPLNRTRSEPLPPSATASPLLAPLQPRQDRLKPHVQLIKPAISPPQRPAKPSEKPRLRQIPSAEDLETDGGGVGPMANDGLEHRESGRGPPEGRGSISLQQHQQVPPWEQQHLAGRLSQGSPGDSVLIPLAQVGHRPLSRTQSSPAAPVSLLSPEPTCQTQVLNSSETPATGLVYDSVMLKHQCSCGDNSKHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVLLYGTNPLSRLKLDNGKLTGLLAQRTFVMLPCGGVGVDTDTIWNELHSSNAARWAAGSVTDLAFKVASRELKNGFAVVRPPGHHADHSTAMGFCFFNSVAIACRQLQQHGKASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHDDGNFFPGSGAVDEVGTGSGEGFNVNVAWAGGLDPPMGDPEYLAAFRIVVMPIAREFAPDLVLVSAGFDAAEGHPAPLGGYHVSAKCFGYMTQQLMNLAGGAVVLALEGGHDLTAICDASEACVAALLGNKVDPLSEESWKQKPNLSAIRSLEAVVRVHRKYWGCMQRLASCPDSWLPRVPGADAEVEAVTALASLSVGILAEDRPSERLVEEEEPMNL

Q8C2B3-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 1-22: Missing
    • 249-249: E → EALLGQRLRLQETSLAPFALPTVSLLPAITLGLPAPAR
    • 376-382: Missing

Q8C2B3-3

  • Name
    3
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 1-22: Missing
    • 249-249: E → EALLGQRLRLQETSLAPFALPTVSLLPAITLGLPAPAR

Q8C2B3-4

  • Name
    4
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q8C2B3-5

  • Name
    5
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q8C2B3-6

  • Name
    6
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There are 6 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
F6VIB5F6VIB5_MOUSEHdac7257
E9PXW1E9PXW1_MOUSEHdac7892
E9PXW8E9PXW8_MOUSEHdac7868
E9PZG4E9PZG4_MOUSEHdac7636
E9PX62E9PX62_MOUSEHdac7851
F6RY11F6RY11_MOUSEHdac7213

Features

Showing features for alternative sequence, sequence conflict, compositional bias.

TypeIDPosition(s)Description
Alternative sequenceVSP_0074321-22in isoform 2, isoform 3 and isoform 5
Alternative sequenceVSP_007433138-161in isoform 4 and isoform 6
Sequence conflict169in Ref. 2; BAC27161
Sequence conflict183in Ref. 2; BAC29493
Compositional bias217-241Polar residues
Sequence conflict228in Ref. 2; BAC27161
Alternative sequenceVSP_007434249in isoform 2, isoform 3 and isoform 4
Alternative sequenceVSP_007435376-382in isoform 2 and isoform 4
Compositional bias432-454Polar residues
Sequence conflict487in Ref. 1; AAF31419 and 2; BAC40598/BAC40666
Sequence conflict645in Ref. 2; BAC29493
Sequence conflict661in Ref. 2; BAC40598
Sequence conflict737in Ref. 1; AAF31419

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

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