SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q99P96

- HDAC7_RAT

UniProt

Q99P96 - HDAC7_RAT

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Histone deacetylase 7
Gene
Hdac7, Hdac7a
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

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 activityi

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

GO - Molecular functioni

  1. 14-3-3 protein binding Source: UniProtKB
  2. NAD-dependent histone deacetylase activity (H3-K14 specific) Source: UniProtKB-EC
  3. NAD-dependent histone deacetylase activity (H3-K18 specific) Source: UniProtKB-EC
  4. NAD-dependent histone deacetylase activity (H3-K9 specific) Source: UniProtKB-EC
  5. NAD-dependent histone deacetylase activity (H4-K16 specific) Source: UniProtKB-EC
  6. histone deacetylase activity Source: UniProtKB
  7. transcription factor binding Source: UniProtKB

GO - Biological processi

  1. B cell activation Source: UniProtKB
  2. B cell differentiation Source: UniProtKB
  3. chromatin modification Source: UniProtKB
  4. chromatin organization Source: UniProtKB
  5. histone deacetylation Source: GOC
  6. inflammatory response Source: UniProtKB
  7. negative regulation of striated muscle tissue development Source: UniProtKB
  8. negative regulation of transcription, DNA-templated Source: UniProtKB
  9. nervous system development Source: UniProtKB
  10. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Hydrolase, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Histone deacetylase 7 (EC:3.5.1.98)
Short name:
HD7
Alternative name(s):
Histone deacetylase 7A
Short name:
HD7a
Gene namesi
Name:Hdac7
Synonyms:Hdac7a
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi619982. Hdac7.

Subcellular locationi

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.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. histone deacetylase complex Source: UniProtKB
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – ›238›238Histone deacetylase 7
PRO_0000114707Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei118 – 1181Phosphoserine By similarity
Modified residuei164 – 1641Phosphoserine; by MARK2, MARK3 and PKD/PRKD1 By similarity
Modified residuei190 – 1901Phosphoserine; by PKD/PRKD2 By similarity

Post-translational modificationi

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.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ99P96.

Expressioni

Gene expression databases

GenevestigatoriQ99P96.

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000011322.

Family & Domainsi

Domaini

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

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0123.
HOGENOMiHOG000232065.

Family and domain databases

InterProiIPR000286. His_deacetylse.
[Graphical view]
PANTHERiPTHR10625. PTHR10625. 1 hit.

Sequencei

Sequence statusi: Fragment.

Q99P96-1 [UniParc]FASTAAdd to Basket

« Hide

TPGSQPQPMD LRVGQRPTVE PPPEPALLTL QHPQRLHRHL FLAGLQQQQR    50
SAEPMRLSMD PPLPELQGGQ QEQELRQLLN KDKSKRSAVA SSVVKQKLAE 100
VILKKQQAAL ERTVHPSSPS IPYRTLEPLD TEGAARSVLS SFLPPVPSLP 150
TEPPEHFPLR KTVSEPNLKL RYKPKKSLER RKNPLLRKES APPSLRRRPA 200
ETLGDSSPSS SSTPASGCSS PNDSEHGPNP ALGSEADG 238
Length:238
Mass (Da):26,101
Last modified:June 1, 2001 - v1
Checksum:iB8869B96FBD040C5
GO

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Non-terminal residuei238 – 2381

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF321135 mRNA. Translation: AAK11188.1.
UniGeneiRn.203327.

Genome annotation databases

UCSCiRGD:619982. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF321135 mRNA. Translation: AAK11188.1 .
UniGenei Rn.203327.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000011322.

Chemistry

ChEMBLi CHEMBL2095943.

Proteomic databases

PaxDbi Q99P96.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

UCSCi RGD:619982. rat.

Organism-specific databases

RGDi 619982. Hdac7.

Phylogenomic databases

eggNOGi COG0123.
HOGENOMi HOG000232065.

Gene expression databases

Genevestigatori Q99P96.

Family and domain databases

InterProi IPR000286. His_deacetylse.
[Graphical view ]
PANTHERi PTHR10625. PTHR10625. 1 hit.
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiHDAC7_RAT
AccessioniPrimary (citable) accession number: Q99P96
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi