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Q80ZH1 (HDAC5_CRIGR) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Histone deacetylase 5

Short name=HD5
EC=3.5.1.98
Gene names
Name:HDAC5
OrganismCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Taxonomic identifier10029 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus

Protein attributes

Sequence length1111 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. Interacts with GRK5 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-250 and Ser-489 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-250 and Ser-489. 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 – 11111111Histone deacetylase 5
PRO_0000357050

Regions

Region671 – 1017347Histone deacetylase
Motif1070 – 110940Nuclear export signal By similarity
Compositional bias47 – 526Poly-Gly
Compositional bias85 – 928Poly-Gln
Compositional bias578 – 58811Poly-Glu

Sites

Active site8221 By similarity
Metal binding6851Zinc By similarity
Metal binding6871Zinc By similarity
Metal binding6931Zinc By similarity
Metal binding7701Zinc By similarity

Amino acid modifications

Modified residue2501Phosphoserine; by AMPK, CaMK1, SIK1 and PKD/PRKD1 By similarity
Modified residue2831Phosphothreonine; by PKC By similarity
Modified residue4891Phosphoserine; by AMPK, CaMK1, SIK1 and PKD/PRKD1 By similarity
Modified residue5241N6-acetyllysine By similarity
Modified residue6501Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q80ZH1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 52559AE959E190E6

FASTA1,111120,988
        10         20         30         40         50         60 
MNSPNESDGM PGREPSLEIL PRTPLHSIPV AVEVKPVLPG AMPSSMGGGG GGSPSPVELR 

        70         80         90        100        110        120 
GALAGPMDPA LREQQLQQEL LVLKQQQQLQ KQLLFAEFQK QHDHLTRQHE VQLQKHLKQQ 

       130        140        150        160        170        180 
QEMLAAKRQQ ELEQQRQREQ QRQEELEKQR LEQQLLILRN KEKSKESAIA STEVKLRLQE 

       190        200        210        220        230        240 
FLLSKSKEPT PGSLNHSLPQ HPKCWGAHHA SLDQSSPPQS GPPGTPPSYK LPLLGPYDSR 

       250        260        270        280        290        300 
DDFPLRKTAS EPNLKVRSRL KQKVAERRSS PLLRRKDGTV ISTFKKRAVE ITGTGPGVSS 

       310        320        330        340        350        360 
VCNSAPGSGP SSPNSSHSAI AENGFTGSVP NIPTEMLPQH RALPLDSSPN QFSLYTSPSL 

       370        380        390        400        410        420 
PNISLGLQAT VTVTNSHLTA SPKLSTQQEA ERQALQSLRQ GGTLTGKFMS TSSIPGCLLG 

       430        440        450        460        470        480 
VTLEGDTSPH GHASLLQHVL LLEQARQQST LIAVPLHGQS PLVTGERVAT SMRTVGKLPR 

       490        500        510        520        530        540 
HRPLSRTQSS PLPQSPQALQ QLVMQQQHQQ FLEKQKQQQM QLGKILTKTG ELPRQPTTHP 

       550        560        570        580        590        600 
EETEEELTEQ QEALLGEGAL TMPREGSTES ESTQEDLEEE EDEEEEDEDC IQVKDEEGES 

       610        620        630        640        650        660 
GPDEGPDLEE SSAGYKKLFT DAQQLQPLQV YQAPLSLATV PHQALGRTQS SPAAPGSMKS 

       670        680        690        700        710        720 
PPDQPTKHLF TTGVVYDTFM LKHQCMCGNT HVHPEHAGRI QSIWSRLQET GLLSKCERIR 

       730        740        750        760        770        780 
GRKATLDEIQ TVHSEYHTLL YGTSPLNRQK LDSKKLLGPI SQKMYAMLPC GGIGVDSDTV 

       790        800        810        820        830        840 
WNEMHSSSAV RMAVGCLVEL AFKVAAGELK NGFAIIRPPG HHAEESTAMG FCFFNSVAIT 

       850        860        870        880        890        900 
AKLLQQKLNV GKVLIVDWDI HHGNGTQQAF YDDPSVLYIS LHRYDNGNFF PGSGAPEEVG 

       910        920        930        940        950        960 
GGPGMGYNVN VAWTGGVDPP IGDVEYLTAF RTVVMPIAHE FSPDVVLVSA GFDAVEGHLS 

       970        980        990       1000       1010       1020 
PLGGYSVTAR CFGHLTRQLM TLAGGRVVLA LEGGHDLTAI CDASEACVSA LLSVELQPLD 

      1030       1040       1050       1060       1070       1080 
EAVLQQKPSI NAVATLEKVI EIQSKHWSCV QRFATGLGCS LQEAQAGETE EAETVSAMAL 

      1090       1100       1110 
LSVGAEQAQA VATQEHSPRP AEEPMEQEPT L 

« Hide

References

[1]"Suppressors of alpha(1,3)fucosylation identified by expression cloning in the LEC11B gain-of-function CHO mutant."
Chen W., Tang J., Stanley P.
Glycobiology 15:259-269(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Ovary.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY145846 mRNA. Translation: AAN46420.1.
RefSeqNP_001233710.1. NM_001246781.1.

3D structure databases

ProteinModelPortalQ80ZH1.
SMRQ80ZH1. Positions 68-132, 670-1052.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100689350.
KEGGcge:100689350.

Organism-specific databases

CTD10014.

Phylogenomic databases

HOVERGENHBG057100.
KOK11406.

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_CRIGR
AccessionPrimary (citable) accession number: Q80ZH1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: June 1, 2003
Last modified: April 16, 2014
This is version 62 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