Q5R902 (HDAC5_PONAB) Reviewed, UniProtKB/Swiss-Prot
Last modified
March 6, 2013.
Version 52.
History...
Clusters with 
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Histone deacetylase 5 Short name=HD5 EC=3.5.1.98 | ||
| Gene names |
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| Organism | Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome] | ||
| Taxonomic identifier | 9601 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo |
Protein attributes
| Sequence length | 1122 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence 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 By similarity. Interacts with BAHD1, BCOR, HDAC7, HDAC9, CTBP1, MEF2C, NCOR2, NRIP1, PHB2 and a 14-3-3 chaperone protein. Interacts with KDM5B By similarity. Interacts with MYOCD By similarity. Interacts with GRK5 By similarity. Interacts with DDIT3/CHOP 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. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1122 | 1122 | Histone deacetylase 5 | PRO_0000357051 | |||||
Regions | |||||||||
| Region | 684 – 1028 | 345 | Histone deacetylase | ||||||
| Motif | 1081 – 1122 | 42 | Nuclear export signal By similarity | ||||||
| Compositional bias | 47 – 52 | 6 | Poly-Gly | ||||||
| Compositional bias | 85 – 92 | 8 | Poly-Gln | ||||||
| Compositional bias | 596 – 599 | 4 | Poly-Glu | ||||||
| Compositional bias | 1099 – 1104 | 6 | Poly-Ala | ||||||
Sites | |||||||||
| Active site | 833 | 1 | By similarity | ||||||
| Metal binding | 696 | 1 | Zinc By similarity | ||||||
| Metal binding | 698 | 1 | Zinc By similarity | ||||||
| Metal binding | 704 | 1 | Zinc By similarity | ||||||
| Metal binding | 781 | 1 | Zinc By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 259 | 1 | Phosphoserine; by AMPK, CaMK1, SIK1 and PKD/PRKD1 By similarity | ||||||
| Modified residue | 292 | 1 | Phosphothreonine; by PKC By similarity | ||||||
| Modified residue | 498 | 1 | Phosphoserine; by AMPK, CaMK1, SIK1 and PKD/PRKD1 By similarity | ||||||
| Modified residue | 533 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 661 | 1 | Phosphoserine By similarity | ||||||
Sequences
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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. |
| UniGene | Pab.17810. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1ZZ0 based on UniProtKB Q70I53. |
| ProteinModelPortal | Q5R902. |
| SMR | Q5R902. Positions 67-133, 681-1063. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Phylogenomic databases | |
| HOGENOM | HOG000232065. |
| HOVERGEN | HBG057100. |
| InParanoid | Q5R902. |
Family and domain databases | |
| Gene3D | 3.40.800.20. 1 hit. |
| InterPro | IPR000286. His_deacetylse. IPR023801. His_deacetylse_dom. IPR024643. Hist_deacetylase_Gln_rich_N. IPR017320. Histone_deAcase_II_euk. [Graphical view] |
| PANTHER | PTHR10625. PTHR10625. 1 hit. |
| Pfam | PF12203. HDAC4_Gln. 1 hit. PF00850. Hist_deacetyl. 1 hit. [Graphical view] |
| PIRSF | PIRSF037911. HDAC_II_euk. 1 hit. |
| PRINTS | PR01270. HDASUPER. |
| ProtoNet | Search... |
Entry information
| Entry name | HDAC5_PONAB | ||||||||
| Accession | Primary (citable) accession number: Q5R902 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |