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Q9YGY4 (HDAC9_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 54. 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 9

EC=3.5.1.98
Alternative name(s):
Histone deacetylase-related protein
MEF2-interacting transcription repressor MITR
Gene names
Name:hdac9
Synonyms:hdrp, mitr
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Protein attributes

Sequence length596 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Devoided of intrinsic deacetylase activity, promotes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4) by recruiting other histone deacetylases. Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Represses MEF2-dependent transcription. Ref.1

Catalytic activity

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

Subunit structure

Homodimer By similarity. Interacts with mef2. Ref.1

Subcellular location

Nucleus By similarity.

Tissue specificity

Broadly expressed. Ref.1

Developmental stage

Broadly expressed at low levels at all stages. Ref.1

Sequence similarities

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

Sequence caution

The sequence CAB10167.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 596596Histone deacetylase 9
PRO_0000280538

Regions

Region172 – 22251Interaction with mef2

Sequences

Sequence LengthMass (Da)Tools
Q9YGY4 [UniParc].

Last modified March 20, 2007. Version 2.
Checksum: 4E4BD92BAC605E84

FASTA59667,307
        10         20         30         40         50         60 
MLQTIYESES YFSSDGVAGR EQLLAEQRMH AMIGKDIKSE FPIGLESISP LDLRTDLRTA 

        70         80         90        100        110        120 
VPVGDPGLRE KQLQQELLII KQQQQIQKQL LIAEFQKQHE NLTRQHQVQL QEHLKLQQEL 

       130        140        150        160        170        180 
LAMKQQQELL EREKEQKMEQ QRKEQEAERH RQEQQLCHPR SKDRVKERAV ASTEVKQKLQ 

       190        200        210        220        230        240 
EFILSKSATK EPLTNGTSHS MGRHPKLWYT AAHHTSLDQS SPPPSGTSPT YKCPPPGNQD 

       250        260        270        280        290        300 
DFPLRKTASE PNLKVRSRLK QKVVERRSSP LLRRKDSIVS SSYKKRIFEV AESSVSSSSP 

       310        320        330        340        350        360 
VSGPSSPNNG PVAMEAEHET PVLSVNSRIE NLVSHHHLVH HERSLSLLNL YTSPSLPNIT 

       370        380        390        400        410        420 
LGLHATATQL NTSSSLKEQQ KYDPQAPRQG VSMAGQYAGG IPTSSNHVSL EGKANSHQAI 

       430        440        450        460        470        480 
LQHLLLKEQM RQQKILASGG TPVLHQSPLA AKDRVSPAGR VAHKLPRHRP LHRTQSAPLP 

       490        500        510        520        530        540 
QSTLAQLVIQ QQHQQFLEKQ KQYQQQIHMN KILSKSIEQL RQPEGHLEEA EEDLHGDNLM 

       550        560        570        580        590 
QEKSSSIDNT RSYSSTDLRT GPFGSVKVKE EPPDSENEIK THLQSEQKSV FAQQVT 

« Hide

References

[1]"MEF-2 function is modified by a novel co-repressor, MITR."
Sparrow D.B., Miska E.A., Langley E., Reynaud-Deonauth S., Kotecha S., Towers N., Spohr G., Kouzarides T., Mohun T.J.
EMBO J. 18:5085-5098(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH MEF2, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, FUNCTION.
[2]"Identification of a transcriptional repressor related to the noncatalytic domain of histone deacetylases 4 and 5."
Zhou X., Richon V.M., Rifkind R.A., Marks P.A.
Proc. Natl. Acad. Sci. U.S.A. 97:1056-1061(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z97214 mRNA. Translation: CAB10167.1. Different initiation.
RefSeqNP_001079307.1. NM_001085838.1.
UniGeneXl.227.

3D structure databases

ProteinModelPortalQ9YGY4.
SMRQ9YGY4. Positions 64-131.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid97196. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID378615.
KEGGxla:378615.

Organism-specific databases

CTD9734.
XenbaseXB-GENE-865808. hdac9.

Phylogenomic databases

HOVERGENHBG057100.
KOK11409.

Family and domain databases

InterProIPR000286. His_deacetylse.
IPR024643. Hist_deacetylase_Gln_rich_N.
[Graphical view]
PANTHERPTHR10625. PTHR10625. 1 hit.
PfamPF12203. HDAC4_Gln. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHDAC9_XENLA
AccessionPrimary (citable) accession number: Q9YGY4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: March 20, 2007
Last modified: April 16, 2014
This is version 54 of the entry and version 2 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