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Q99P96 (HDAC7_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone deacetylase 7

Short name=HD7
EC=3.5.1.98
Alternative name(s):
Histone deacetylase 7A
Short name=HD7a
Gene names
Name:Hdac7
Synonyms:Hdac7a
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length238 AA.
Sequence statusFragment.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Catalytic activity

Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone.

Subunit structure

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.

Subcellular location

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.

Domain

The nuclear export sequence mediates the shuttling between the nucleus and the cytoplasm By similarity.

Post-translational modification

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.

Miscellaneous

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

Sequence similarities

Belongs to the histone deacetylase family. HD type 2 subfamily.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   DomainRepeat
   Molecular functionChromatin regulator
Hydrolase
Repressor
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processB cell activation

Traceable author statement PubMed 12711221. Source: UniProtKB

B cell differentiation

Traceable author statement PubMed 12711221. Source: UniProtKB

chromatin modification

Traceable author statement PubMed 12711221. Source: UniProtKB

chromatin organization

Traceable author statement PubMed 12711221. Source: UniProtKB

histone deacetylation

Traceable author statement PubMed 12711221. Source: GOC

inflammatory response

Traceable author statement PubMed 12711221. Source: UniProtKB

negative regulation of striated muscle tissue development

Traceable author statement PubMed 12711221. Source: UniProtKB

negative regulation of transcription, DNA-templated

Traceable author statement PubMed 12711221. Source: UniProtKB

nervous system development

Traceable author statement PubMed 12711221. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

histone deacetylase complex

Traceable author statement PubMed 12711221. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_function14-3-3 protein binding

Inferred from sequence or structural similarity. Source: UniProtKB

NAD-dependent histone deacetylase activity (H3-K14 specific)

Inferred from electronic annotation. Source: UniProtKB-EC

NAD-dependent histone deacetylase activity (H3-K18 specific)

Inferred from electronic annotation. Source: UniProtKB-EC

NAD-dependent histone deacetylase activity (H3-K9 specific)

Inferred from electronic annotation. Source: UniProtKB-EC

NAD-dependent histone deacetylase activity (H4-K16 specific)

Inferred from electronic annotation. Source: UniProtKB-EC

histone deacetylase activity

Traceable author statement PubMed 12711221. Source: UniProtKB

transcription factor binding

Traceable author statement PubMed 12711221. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – ›238›238Histone deacetylase 7
PRO_0000114707

Amino acid modifications

Modified residue1181Phosphoserine By similarity
Modified residue1641Phosphoserine; by MARK2, MARK3 and PKD/PRKD1 By similarity
Modified residue1901Phosphoserine; by PKD/PRKD2 By similarity

Experimental info

Non-terminal residue11
Non-terminal residue2381

Sequences

Sequence LengthMass (Da)Tools
Q99P96 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: B8869B96FBD040C5

FASTA23826,101
        10         20         30         40         50         60 
TPGSQPQPMD LRVGQRPTVE PPPEPALLTL QHPQRLHRHL FLAGLQQQQR SAEPMRLSMD 

        70         80         90        100        110        120 
PPLPELQGGQ QEQELRQLLN KDKSKRSAVA SSVVKQKLAE VILKKQQAAL ERTVHPSSPS 

       130        140        150        160        170        180 
IPYRTLEPLD TEGAARSVLS SFLPPVPSLP TEPPEHFPLR KTVSEPNLKL RYKPKKSLER 

       190        200        210        220        230 
RKNPLLRKES APPSLRRRPA ETLGDSSPSS SSTPASGCSS PNDSEHGPNP ALGSEADG 

« Hide

References

[1]"Expression pattern of rat histone deacetylases."
Wilquet V., Chavez M., Korbers R., Geerts A.
Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Wistar.
Tissue: Testis.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF321135 mRNA. Translation: AAK11188.1.
UniGeneRn.203327.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000011322.

Chemistry

ChEMBLCHEMBL2095943.

Proteomic databases

PaxDbQ99P96.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCRGD:619982. rat.

Organism-specific databases

RGD619982. Hdac7.

Phylogenomic databases

eggNOGCOG0123.
HOGENOMHOG000232065.

Gene expression databases

GenevestigatorQ99P96.

Family and domain databases

InterProIPR000286. His_deacetylse.
[Graphical view]
PANTHERPTHR10625. PTHR10625. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHDAC7_RAT
AccessionPrimary (citable) accession number: Q99P96
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2003
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families