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Q80ZH1

- HDAC5_CRIGR

UniProt

Q80ZH1 - HDAC5_CRIGR

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Protein

Histone deacetylase 5

Gene

HDAC5

Organism
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Status
Reviewed - Annotation score: 4 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 MEF2C. During muscle differentiation, it shuttles into the cytoplasm, allowing the expression of myocyte enhancer factors (By similarity).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi685 – 6851ZincBy similarity
Metal bindingi687 – 6871ZincBy similarity
Metal bindingi693 – 6931ZincBy similarity
Metal bindingi770 – 7701ZincBy similarity
Active sitei822 – 8221By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  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

GO - Biological processi

  1. regulation of myotube differentiation Source: UniProtKB
  2. regulation of transcription, DNA-templated Source: UniProtKB-KW
  3. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Hydrolase, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Histone deacetylase 5 (EC:3.5.1.98)
Short name:
HD5
Gene namesi
Name:HDAC5
OrganismiCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Taxonomic identifieri10029 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus

Subcellular locationi

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).By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11111111Histone deacetylase 5PRO_0000357050Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei250 – 2501Phosphoserine; by AMPK, CaMK1, SIK1 and PKD/PRKD1By similarity
Modified residuei283 – 2831Phosphothreonine; by PKCBy similarity
Modified residuei489 – 4891Phosphoserine; by AMPK, CaMK1, SIK1 and PKD/PRKD1By similarity
Modified residuei524 – 5241N6-acetyllysineBy similarity
Modified residuei650 – 6501PhosphoserineBy similarity

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Interactioni

Subunit structurei

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. Interacts with EP300 in the presence of TFAP2C (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliQ80ZH1.
SMRiQ80ZH1. Positions 68-132, 670-1052.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni671 – 1017347Histone deacetylaseAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1070 – 110940Nuclear export signalBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi47 – 526Poly-Gly
Compositional biasi85 – 928Poly-Gln
Compositional biasi578 – 58811Poly-GluAdd
BLAST

Domaini

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

Sequence similaritiesi

Phylogenomic databases

HOVERGENiHBG057100.
KOiK11406.

Family and domain databases

Gene3Di3.40.800.20. 1 hit.
InterProiIPR000286. His_deacetylse.
IPR023801. His_deacetylse_dom.
IPR024643. Hist_deacetylase_Gln_rich_N.
IPR017320. Histone_deAcase_II_euk.
[Graphical view]
PANTHERiPTHR10625. PTHR10625. 1 hit.
PfamiPF12203. HDAC4_Gln. 1 hit.
PF00850. Hist_deacetyl. 1 hit.
[Graphical view]
PIRSFiPIRSF037911. HDAC_II_euk. 1 hit.
PRINTSiPR01270. HDASUPER.

Sequencei

Sequence statusi: Complete.

Q80ZH1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNSPNESDGM PGREPSLEIL PRTPLHSIPV AVEVKPVLPG AMPSSMGGGG
60 70 80 90 100
GGSPSPVELR GALAGPMDPA LREQQLQQEL LVLKQQQQLQ KQLLFAEFQK
110 120 130 140 150
QHDHLTRQHE VQLQKHLKQQ QEMLAAKRQQ ELEQQRQREQ QRQEELEKQR
160 170 180 190 200
LEQQLLILRN KEKSKESAIA STEVKLRLQE FLLSKSKEPT PGSLNHSLPQ
210 220 230 240 250
HPKCWGAHHA SLDQSSPPQS GPPGTPPSYK LPLLGPYDSR DDFPLRKTAS
260 270 280 290 300
EPNLKVRSRL KQKVAERRSS PLLRRKDGTV ISTFKKRAVE ITGTGPGVSS
310 320 330 340 350
VCNSAPGSGP SSPNSSHSAI AENGFTGSVP NIPTEMLPQH RALPLDSSPN
360 370 380 390 400
QFSLYTSPSL PNISLGLQAT VTVTNSHLTA SPKLSTQQEA ERQALQSLRQ
410 420 430 440 450
GGTLTGKFMS TSSIPGCLLG VTLEGDTSPH GHASLLQHVL LLEQARQQST
460 470 480 490 500
LIAVPLHGQS PLVTGERVAT SMRTVGKLPR HRPLSRTQSS PLPQSPQALQ
510 520 530 540 550
QLVMQQQHQQ FLEKQKQQQM QLGKILTKTG ELPRQPTTHP EETEEELTEQ
560 570 580 590 600
QEALLGEGAL TMPREGSTES ESTQEDLEEE EDEEEEDEDC IQVKDEEGES
610 620 630 640 650
GPDEGPDLEE SSAGYKKLFT DAQQLQPLQV YQAPLSLATV PHQALGRTQS
660 670 680 690 700
SPAAPGSMKS PPDQPTKHLF TTGVVYDTFM LKHQCMCGNT HVHPEHAGRI
710 720 730 740 750
QSIWSRLQET GLLSKCERIR GRKATLDEIQ TVHSEYHTLL YGTSPLNRQK
760 770 780 790 800
LDSKKLLGPI SQKMYAMLPC GGIGVDSDTV WNEMHSSSAV RMAVGCLVEL
810 820 830 840 850
AFKVAAGELK NGFAIIRPPG HHAEESTAMG FCFFNSVAIT AKLLQQKLNV
860 870 880 890 900
GKVLIVDWDI HHGNGTQQAF YDDPSVLYIS LHRYDNGNFF PGSGAPEEVG
910 920 930 940 950
GGPGMGYNVN VAWTGGVDPP IGDVEYLTAF RTVVMPIAHE FSPDVVLVSA
960 970 980 990 1000
GFDAVEGHLS PLGGYSVTAR CFGHLTRQLM TLAGGRVVLA LEGGHDLTAI
1010 1020 1030 1040 1050
CDASEACVSA LLSVELQPLD EAVLQQKPSI NAVATLEKVI EIQSKHWSCV
1060 1070 1080 1090 1100
QRFATGLGCS LQEAQAGETE EAETVSAMAL LSVGAEQAQA VATQEHSPRP
1110
AEEPMEQEPT L
Length:1,111
Mass (Da):120,988
Last modified:June 1, 2003 - v1
Checksum:i52559AE959E190E6
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY145846 mRNA. Translation: AAN46420.1.
RefSeqiNP_001233710.1. NM_001246781.1.
XP_007643219.1. XM_007645029.1.

Genome annotation databases

GeneIDi100689350.
KEGGicge:100689350.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY145846 mRNA. Translation: AAN46420.1 .
RefSeqi NP_001233710.1. NM_001246781.1.
XP_007643219.1. XM_007645029.1.

3D structure databases

ProteinModelPortali Q80ZH1.
SMRi Q80ZH1. Positions 68-132, 670-1052.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100689350.
KEGGi cge:100689350.

Organism-specific databases

CTDi 10014.

Phylogenomic databases

HOVERGENi HBG057100.
KOi K11406.

Family and domain databases

Gene3Di 3.40.800.20. 1 hit.
InterProi IPR000286. His_deacetylse.
IPR023801. His_deacetylse_dom.
IPR024643. Hist_deacetylase_Gln_rich_N.
IPR017320. Histone_deAcase_II_euk.
[Graphical view ]
PANTHERi PTHR10625. PTHR10625. 1 hit.
Pfami PF12203. HDAC4_Gln. 1 hit.
PF00850. Hist_deacetyl. 1 hit.
[Graphical view ]
PIRSFi PIRSF037911. HDAC_II_euk. 1 hit.
PRINTSi PR01270. HDASUPER.
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiHDAC5_CRIGR
AccessioniPrimary (citable) accession number: Q80ZH1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: June 1, 2003
Last modified: October 1, 2014
This is version 64 of the entry and version 1 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