| IED ID | IndEnz0005000119 |
| Enzyme Type ID | lipase000119 |
| Protein Name |
Histone deacetylase 9 HD9 EC 3.5.1.98 Histone deacetylase 7B HD7b Histone deacetylase-related protein MEF2-interacting transcription repressor MITR |
| Gene Name | Hdac9 Hdac7b Hdrp Mitr |
| Organism | Mus musculus (Mouse) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MHSMISSVDVKSEVPMGLEPISPLDLRTDLRMMMPVVDPVVREKQLQQELLLIQQQQQIQKQLLIAEFQKQHENLTRQHQAQLQEHIKELLAIKQQQELLEKEQKLEQQRQEQEVERHRREQQLPPLRGKDRGRERAVASTEVKQKLQEFLLSKSATKDTPTNGKNHSVGRHPKLWYTAAHHTSLDQSSPPLSGTSPSYKYTLPGAQDSKDDFPLRKTASEPNLKVRSRLKQKVAERRSSPLLRRKDGNLVTSFKKRVFEVAESSVSSSSPGSGPSSPNNGPAGNVTENEASALPPTPHPEQLVPQQRILIHEDSMNLLSLYTSPSLPNITLGLPAVPSPLNASNSLKDKQKCETQMLRQGVPLPSQYGSSIAASSSHVHVAMEGKPNSSHQALLQHLLLKEQMRQQKLLVAGGVPLHPQSPLATKERISPGIRGTHKLPRHRPLNRTQSAPLPQSTLAQLVIQQQHQQFLEKQKQYQQQIHMNKLLSKSIEQLKQPGSHLEEAEEELQGDQSMEDRAASKDNSARSDSSACVEDTLGQVGAVKVKEEPVDSDEDAQIQEMECGEQAAFMQQVIGKDLAPGFVIKVII |
| Enzyme Length | 588 |
| Uniprot Accession Number | Q99N13 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-[histone]; Xref=Rhea:RHEA:58196, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089, ChEBI:CHEBI:61930; EC=3.5.1.98; |
| DNA Binding | |
| EC Number | 3.5.1.98 |
| Enzyme Function | FUNCTION: Devoided of intrinsic deacetylase activity, promotes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4) by recruiting HDAC1 and HDAC3. Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Represses MEF2-dependent transcription, inhibits skeletal myogenesis and may be involved in heart development. Protects neurons from apoptosis, both by inhibiting JUN phosphorylation by MAPK10 and by repressing JUN transcription via HDAC1 recruitment to JUN promoter. {ECO:0000269|PubMed:11390982, ECO:0000269|PubMed:12202037, ECO:0000269|PubMed:15711539, ECO:0000269|PubMed:16611996}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (2); Chain (1); Compositional bias (6); Helix (1); Modified residue (5); Mutagenesis (1); Region (8); Sequence conflict (6) |
| Keywords | 3D-structure;Alternative splicing;Chromatin regulator;Hydrolase;Nucleus;Phosphoprotein;Reference proteome;Repressor;Transcription;Transcription regulation;Ubl conjugation |
| Interact With | Q9Z2V5; P60335; Q3TKT4 |
| Induction | INDUCTION: By MEF2 during muscle differentiation. Down-regulated by muscle denervation. Down-regulated by trichostatin A or sodium butyrate, and during neuronal apoptosis (at protein level). {ECO:0000269|PubMed:17101791}. |
| Subcellular Location | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11390982, ECO:0000269|PubMed:15546868, ECO:0000269|PubMed:15711539}. |
| Modified Residue | MOD_RES 22; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q9UKV0"; MOD_RES 220; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:11390982, ECO:0000269|PubMed:12202037"; MOD_RES 240; /note="Phosphoserine; by DYRK1B"; /evidence="ECO:0000269|PubMed:15546868"; MOD_RES 450; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:11390982, ECO:0000269|PubMed:12202037"; MOD_RES 552; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079" |
| Post Translational Modification | PTM: Sumoylated. {ECO:0000250}.; PTM: Phosphorylated on Ser-220 and Ser-450; which promotes 14-3-3-binding, impairs interaction with MEF2, and antagonizes antimyogenic activity. Phosphorylated on Ser-240 by DYRK1B; which impairs nuclear accumulation. Phosphorylated by the PKC kinases PKN1 and PKN2, impairing nuclear import. {ECO:0000269|PubMed:11390982, ECO:0000269|PubMed:12202037, ECO:0000269|PubMed:15546868}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1TQE; |
| Mapped Pubmed ID | 10655483; 12242305; 12590135; 12711221; 15102471; 15367668; 15537544; 15601857; 15737621; 16141072; 16260608; 16280321; 16602821; 16873063; 17786239; 17922010; 17988634; 18480421; 18824292; 18926829; 19412888; 19879272; 19893013; 20525066; 20596014; 20947501; 21267068; 21421818; 21518438; 21680747; 21708950; 21731673; 21746928; 21953612; 21985497; 22226696; 22442009; 22715468; 23288173; 23297420; 24101673; 24105743; 25011550; 25035344; 25388417; 25681462; 25793404; 25873389; 26483211; 27033599; 27250566; 27633396; 28028172; 29520069; 30031609; 30186101; 30372441; 30679521; 31202927; 31223056; 31320610; 31659325; 32546048; 32554611; 32620134; 32702412; 34119632; 34290714; 34338228; |
| Motif | |
| Gene Encoded By | |
| Mass | 65,687 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:58196 |
| Cross Reference Brenda |