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Q5R902 (HDAC5_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 57. 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 5

Short name=HD5
EC=3.5.1.98
Gene names
Name:HDAC5
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length1122 AA.
Sequence statusComplete.
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 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 AHRR, BAHD1, BCOR, HDAC7, HDAC9, CTBP1, MEF2C, NCOR2, NRIP1, PHB2 and a 14-3-3 chaperone protein. Interacts with BCL6, DDIT3/CHOP, GRK5, KDM5B and MYOCD By similarity.

Subcellular location

Nucleus By similarity. Cytoplasm By similarity. Note: 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 a 14-3-3 chaperone protein and is due to its phosphorylation at Ser-259 and Ser-498 by AMPK, CaMK1 and SIK1 By similarity.

Domain

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

Post-translational modification

Phosphorylated by AMPK, CaMK1, SIK1 and PRKD1 at Ser-259 and Ser-498. The phosphorylation is required for the export to the cytoplasm and inhibition. Phosphorylated by the PKC kinases PKN1 and PKN2, impairing nuclear import By similarity. Phosphorylated by GRK5, leading to nuclear export of HDAC5 and allowing MEF2-mediated transcription By similarity.

Ubiquitinated. Polyubiquitination however does not lead to its degradation By similarity.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11221122Histone deacetylase 5
PRO_0000357051

Regions

Region684 – 1028345Histone deacetylase
Motif1081 – 112242Nuclear export signal By similarity
Compositional bias47 – 526Poly-Gly
Compositional bias85 – 928Poly-Gln
Compositional bias596 – 5994Poly-Glu
Compositional bias1099 – 11046Poly-Ala

Sites

Active site8331 By similarity
Metal binding6961Zinc By similarity
Metal binding6981Zinc By similarity
Metal binding7041Zinc By similarity
Metal binding7811Zinc By similarity

Amino acid modifications

Modified residue2591Phosphoserine; by AMPK, CaMK1, SIK1 and PKD/PRKD1 By similarity
Modified residue2921Phosphothreonine; by PKC By similarity
Modified residue4981Phosphoserine; by AMPK, CaMK1, SIK1 and PKD/PRKD1 By similarity
Modified residue5331N6-acetyllysine By similarity
Modified residue6611Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5R902 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 7143C2F3B508D37C

FASTA1,122121,925
        10         20         30         40         50         60 
MNSPNESDGM SGREPSLEIL PRTSLHSIPV TVEVKPVLPR AMPSSMGGGG GGSPSPVELR 

        70         80         90        100        110        120 
GALVGSVDPT LREQLLQQEL LALKQQQQLQ KQLLFAEFQK QHDHLTRQHE VQLQKHLKQQ 

       130        140        150        160        170        180 
QEMLAAKQQQ EMLAAKRQQE LEQQRQREQQ RQEELEKQRL EQQLLILRNK EKSKESAIAS 

       190        200        210        220        230        240 
TEVKLRLQEF LLSKSKEPTP GGLNHSLPQH PKCWGAHHAS LDQSSPPQSG PPGTPPSYKL 

       250        260        270        280        290        300 
PLPGPYDSRD DFPLRKTASE PNLKVRSRLK QKVAERRSSP LLRRKDGTVI STFKKRAVEI 

       310        320        330        340        350        360 
TGAGPGASSV CNSAPGSGPS SPNSSHSTIA ENGFTGSVPN IPTEMLPQHR ALPLDSSSNQ 

       370        380        390        400        410        420 
FSLYTSPSLP NISLGLQATV TVTNSHLTAS PKLSTQQEAE RQALQSLRQG GTLTGKFMST 

       430        440        450        460        470        480 
SSIPGCLLGV ALEGDGSPHG HASLLQHVLL LEQARQQSTL IAVPLHGQSP LVTGERVATS 

       490        500        510        520        530        540 
MRTVGKLPRH RPLSRTQSSP LPQSPQALQQ LVMQQQHQQF LEKQKQQQLQ LGKILTKTGE 

       550        560        570        580        590        600 
LPRQPTTHPE ETEEELTEQQ EALLGEGALT MPREGSTESE STQEDLEEED EEEDGEEEED 

       610        620        630        640        650        660 
CIQVKDEEGE SGAEEGPDLE EPGAGYKKLF SDAQPLQPLQ VYQAPLSLAT VPHQALGRTQ 

       670        680        690        700        710        720 
SSPAAPGGMK SPPDQPVKHL FTTGVVYDTF MLKHQCMCGN THVHPEHAGR IQSTWSRLQE 

       730        740        750        760        770        780 
TGLLSKCERI RGRKATLDEI QTVHSEYHTL LYGTSPLNRQ KVDSKKLLGP ISQKMYAVLP 

       790        800        810        820        830        840 
CGGIGVDSDT VWNEMHSSSA VRMAVGCLLE LAFKVAAGEL KNGFAIIRPP GHHAEESTAM 

       850        860        870        880        890        900 
GFCFFNSVAI TAKLLQQKLN VGKVLIVDWD IHHGNGTQQA FYNDPSVLYI SLHRYDNGNF 

       910        920        930        940        950        960 
FPGSGAPEEV GGGPGVGYNV NVAWIGGVDP PIGDVEYLTA FRTVVMPIAH EFSPDVVLVS 

       970        980        990       1000       1010       1020 
AGFDAVEGHL SPLGGYSVTA RCFGHLTRQL MTLAGGRVVL ALEGGHDLTA ICDASEACVS 

      1030       1040       1050       1060       1070       1080 
ALLSVELQPL DEAVLQQKPN INAVATLEKV IEIQSKHWSC VQKFAAGLGR SLREAQAGET 

      1090       1100       1110       1120 
EEAETVSAMA LLSVGAEQAQ AAAAREHSPR PAEEPMEQEP AL 

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain cortex.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR859595 mRNA. Translation: CAH91758.1.
UniGenePab.17810.

3D structure databases

ProteinModelPortalQ5R902.
SMRQ5R902. Positions 67-133, 681-1063.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOGENOMHOG000232065.
HOVERGENHBG057100.
InParanoidQ5R902.

Family and domain databases

Gene3D3.40.800.20. 1 hit.
InterProIPR000286. His_deacetylse.
IPR023801. His_deacetylse_dom.
IPR024643. Hist_deacetylase_Gln_rich_N.
IPR017320. Histone_deAcase_II_euk.
[Graphical view]
PANTHERPTHR10625. PTHR10625. 1 hit.
PfamPF12203. HDAC4_Gln. 1 hit.
PF00850. Hist_deacetyl. 1 hit.
[Graphical view]
PIRSFPIRSF037911. HDAC_II_euk. 1 hit.
PRINTSPR01270. HDASUPER.
ProtoNetSearch...

Entry information

Entry nameHDAC5_PONAB
AccessionPrimary (citable) accession number: Q5R902
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: December 21, 2004
Last modified: April 16, 2014
This is version 57 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