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Q9YGY4

- HDAC9_XENLA

UniProt

Q9YGY4 - HDAC9_XENLA

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Protein

Histone deacetylase 9

Gene

hdac9

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

GO - Molecular functioni

  1. NAD-dependent histone deacetylase activity (H3-K14 specific) Source: UniProtKB-EC
  2. NAD-dependent histone deacetylase activity (H3-K18 specific) Source: UniProtKB-EC
  3. NAD-dependent histone deacetylase activity (H3-K9 specific) Source: UniProtKB-EC
  4. NAD-dependent histone deacetylase activity (H4-K16 specific) Source: UniProtKB-EC

GO - Biological processi

  1. regulation of transcription, DNA-templated Source: UniProtKB-KW
  2. 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 9 (EC:3.5.1.98)
Alternative name(s):
Histone deacetylase-related protein
MEF2-interacting transcription repressor MITR
Gene namesi
Name:hdac9
Synonyms:hdrp, mitr
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-865808. hdac9.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 596596Histone deacetylase 9PRO_0000280538Add
BLAST

Expressioni

Tissue specificityi

Broadly expressed.1 Publication

Developmental stagei

Broadly expressed at low levels at all stages.1 Publication

Interactioni

Subunit structurei

Homodimer (By similarity). Interacts with mef2.By similarity1 Publication

Protein-protein interaction databases

BioGridi97196. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ9YGY4.
SMRiQ9YGY4. Positions 64-131.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni172 – 22251Interaction with mef2Add
BLAST

Sequence similaritiesi

Phylogenomic databases

HOVERGENiHBG057100.
KOiK11409.

Family and domain databases

InterProiIPR000286. His_deacetylse.
IPR024643. Hist_deacetylase_Gln_rich_N.
[Graphical view]
PANTHERiPTHR10625. PTHR10625. 1 hit.
PfamiPF12203. HDAC4_Gln. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9YGY4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLQTIYESES YFSSDGVAGR EQLLAEQRMH AMIGKDIKSE FPIGLESISP
60 70 80 90 100
LDLRTDLRTA VPVGDPGLRE KQLQQELLII KQQQQIQKQL LIAEFQKQHE
110 120 130 140 150
NLTRQHQVQL QEHLKLQQEL LAMKQQQELL EREKEQKMEQ QRKEQEAERH
160 170 180 190 200
RQEQQLCHPR SKDRVKERAV ASTEVKQKLQ EFILSKSATK EPLTNGTSHS
210 220 230 240 250
MGRHPKLWYT AAHHTSLDQS SPPPSGTSPT YKCPPPGNQD DFPLRKTASE
260 270 280 290 300
PNLKVRSRLK QKVVERRSSP LLRRKDSIVS SSYKKRIFEV AESSVSSSSP
310 320 330 340 350
VSGPSSPNNG PVAMEAEHET PVLSVNSRIE NLVSHHHLVH HERSLSLLNL
360 370 380 390 400
YTSPSLPNIT LGLHATATQL NTSSSLKEQQ KYDPQAPRQG VSMAGQYAGG
410 420 430 440 450
IPTSSNHVSL EGKANSHQAI LQHLLLKEQM RQQKILASGG TPVLHQSPLA
460 470 480 490 500
AKDRVSPAGR VAHKLPRHRP LHRTQSAPLP QSTLAQLVIQ QQHQQFLEKQ
510 520 530 540 550
KQYQQQIHMN KILSKSIEQL RQPEGHLEEA EEDLHGDNLM QEKSSSIDNT
560 570 580 590
RSYSSTDLRT GPFGSVKVKE EPPDSENEIK THLQSEQKSV FAQQVT
Length:596
Mass (Da):67,307
Last modified:March 20, 2007 - v2
Checksum:i4E4BD92BAC605E84
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z97214 mRNA. Translation: CAB10167.1. Different initiation.
RefSeqiNP_001079307.1. NM_001085838.1.
UniGeneiXl.227.

Genome annotation databases

GeneIDi378615.
KEGGixla:378615.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z97214 mRNA. Translation: CAB10167.1 . Different initiation.
RefSeqi NP_001079307.1. NM_001085838.1.
UniGenei Xl.227.

3D structure databases

ProteinModelPortali Q9YGY4.
SMRi Q9YGY4. Positions 64-131.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 97196. 1 interaction.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 378615.
KEGGi xla:378615.

Organism-specific databases

CTDi 9734.
Xenbasei XB-GENE-865808. hdac9.

Phylogenomic databases

HOVERGENi HBG057100.
KOi K11409.

Family and domain databases

InterProi IPR000286. His_deacetylse.
IPR024643. Hist_deacetylase_Gln_rich_N.
[Graphical view ]
PANTHERi PTHR10625. PTHR10625. 1 hit.
Pfami PF12203. HDAC4_Gln. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. 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.

Entry informationi

Entry nameiHDAC9_XENLA
AccessioniPrimary (citable) accession number: Q9YGY4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: March 20, 2007
Last modified: October 29, 2014
This is version 56 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3