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Q5R902

- HDAC5_PONAB

UniProt

Q5R902 - HDAC5_PONAB

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Protein

Histone deacetylase 5

Gene

HDAC5

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
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 bindingi696 – 6961ZincBy similarity
Metal bindingi698 – 6981ZincBy similarity
Metal bindingi704 – 7041ZincBy similarity
Metal bindingi781 – 7811ZincBy similarity
Active sitei833 – 8331By 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
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
ProteomesiUP000001595: Unplaced

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-259 and Ser-498 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 – 11221122Histone deacetylase 5PRO_0000357051Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei259 – 2591Phosphoserine; by AMPK, CaMK1, SIK1 and PKD/PRKD1By similarity
Modified residuei292 – 2921Phosphothreonine; by PKCBy similarity
Modified residuei498 – 4981Phosphoserine; by AMPK, CaMK1, SIK1 and PKD/PRKD1By similarity
Modified residuei533 – 5331N6-acetyllysineBy similarity
Modified residuei661 – 6611PhosphoserineBy similarity

Post-translational modificationi

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).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

ProteinModelPortaliQ5R902.
SMRiQ5R902. Positions 67-133, 681-1063.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni684 – 1028345Histone deacetylaseAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1081 – 112242Nuclear export signalBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi47 – 526Poly-Gly
Compositional biasi85 – 928Poly-Gln
Compositional biasi596 – 5994Poly-Glu
Compositional biasi1099 – 11046Poly-Ala

Domaini

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

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000232065.
HOVERGENiHBG057100.
InParanoidiQ5R902.

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.

Q5R902-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNSPNESDGM SGREPSLEIL PRTSLHSIPV TVEVKPVLPR AMPSSMGGGG
60 70 80 90 100
GGSPSPVELR GALVGSVDPT LREQLLQQEL LALKQQQQLQ KQLLFAEFQK
110 120 130 140 150
QHDHLTRQHE VQLQKHLKQQ QEMLAAKQQQ EMLAAKRQQE LEQQRQREQQ
160 170 180 190 200
RQEELEKQRL EQQLLILRNK EKSKESAIAS TEVKLRLQEF LLSKSKEPTP
210 220 230 240 250
GGLNHSLPQH PKCWGAHHAS LDQSSPPQSG PPGTPPSYKL PLPGPYDSRD
260 270 280 290 300
DFPLRKTASE PNLKVRSRLK QKVAERRSSP LLRRKDGTVI STFKKRAVEI
310 320 330 340 350
TGAGPGASSV CNSAPGSGPS SPNSSHSTIA ENGFTGSVPN IPTEMLPQHR
360 370 380 390 400
ALPLDSSSNQ FSLYTSPSLP NISLGLQATV TVTNSHLTAS PKLSTQQEAE
410 420 430 440 450
RQALQSLRQG GTLTGKFMST SSIPGCLLGV ALEGDGSPHG HASLLQHVLL
460 470 480 490 500
LEQARQQSTL IAVPLHGQSP LVTGERVATS MRTVGKLPRH RPLSRTQSSP
510 520 530 540 550
LPQSPQALQQ LVMQQQHQQF LEKQKQQQLQ LGKILTKTGE LPRQPTTHPE
560 570 580 590 600
ETEEELTEQQ EALLGEGALT MPREGSTESE STQEDLEEED EEEDGEEEED
610 620 630 640 650
CIQVKDEEGE SGAEEGPDLE EPGAGYKKLF SDAQPLQPLQ VYQAPLSLAT
660 670 680 690 700
VPHQALGRTQ SSPAAPGGMK SPPDQPVKHL FTTGVVYDTF MLKHQCMCGN
710 720 730 740 750
THVHPEHAGR IQSTWSRLQE TGLLSKCERI RGRKATLDEI QTVHSEYHTL
760 770 780 790 800
LYGTSPLNRQ KVDSKKLLGP ISQKMYAVLP CGGIGVDSDT VWNEMHSSSA
810 820 830 840 850
VRMAVGCLLE LAFKVAAGEL KNGFAIIRPP GHHAEESTAM GFCFFNSVAI
860 870 880 890 900
TAKLLQQKLN VGKVLIVDWD IHHGNGTQQA FYNDPSVLYI SLHRYDNGNF
910 920 930 940 950
FPGSGAPEEV GGGPGVGYNV NVAWIGGVDP PIGDVEYLTA FRTVVMPIAH
960 970 980 990 1000
EFSPDVVLVS AGFDAVEGHL SPLGGYSVTA RCFGHLTRQL MTLAGGRVVL
1010 1020 1030 1040 1050
ALEGGHDLTA ICDASEACVS ALLSVELQPL DEAVLQQKPN INAVATLEKV
1060 1070 1080 1090 1100
IEIQSKHWSC VQKFAAGLGR SLREAQAGET EEAETVSAMA LLSVGAEQAQ
1110 1120
AAAAREHSPR PAEEPMEQEP AL
Length:1,122
Mass (Da):121,925
Last modified:December 21, 2004 - v1
Checksum:i7143C2F3B508D37C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR859595 mRNA. Translation: CAH91758.1.
UniGeneiPab.17810.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR859595 mRNA. Translation: CAH91758.1 .
UniGenei Pab.17810.

3D structure databases

ProteinModelPortali Q5R902.
SMRi Q5R902. Positions 67-133, 681-1063.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOGENOMi HOG000232065.
HOVERGENi HBG057100.
InParanoidi Q5R902.

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

Entry informationi

Entry nameiHDAC5_PONAB
AccessioniPrimary (citable) accession number: Q5R902
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: December 21, 2004
Last modified: October 1, 2014
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3