| IED ID | IndEnz0005000118 |
| Enzyme Type ID | lipase000118 |
| Protein Name |
Histone deacetylase 9 HD9 EC 3.5.1.98 Histone deacetylase 7B HD7 HD7b Histone deacetylase-related protein MEF2-interacting transcription repressor MITR |
| Gene Name | HDAC9 HDAC7 HDAC7B HDRP KIAA0744 MITR |
| Organism | Homo sapiens (Human) |
| 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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MHSMISSVDVKSEVPVGLEPISPLDLRTDLRMMMPVVDPVVREKQLQQELLLIQQQQQIQKQLLIAEFQKQHENLTRQHQAQLQEHIKELLAIKQQQELLEKEQKLEQQRQEQEVERHRREQQLPPLRGKDRGRERAVASTEVKQKLQEFLLSKSATKDTPTNGKNHSVSRHPKLWYTAAHHTSLDQSSPPLSGTSPSYKYTLPGAQDAKDDFPLRKTASEPNLKVRSRLKQKVAERRSSPLLRRKDGNVVTSFKKRMFEVTESSVSSSSPGSGPSSPNNGPTGSVTENETSVLPPTPHAEQMVSQQRILIHEDSMNLLSLYTSPSLPNITLGLPAVPSQLNASNSLKEKQKCETQTLRQGVPLPGQYGGSIPASSSHPHVTLEGKPPNSSHQALLQHLLLKEQMRQQKLLVAGGVPLHPQSPLATKERISPGIRGTHKLPRHRPLNRTQSAPLPQSTLAQLVIQQQHQQFLEKQKQYQQQIHMNKLLSKSIEQLKQPGSHLEEAEEELQGDQAMQEDRAPSSGNSTRSDSSACVDDTLGQVGAVKVKEEPVDSDEDAQIQEMESGEQAAFMQQPFLEPTHTRALSVRQAPLAAVGMDGLEKHRLVSRTHSSPAASVLPHPAMDRPLQPGSATGIAYDPLMLKHQCVCGNSTTHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHSLLYGTNPLDGQKLDPRILLGDDSQKFFSSLPCGGLGVDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAMGFCFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGSGAPNEVGTGLGEGYNINIAWTGGLDPPMGDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHTPPLGGYKVTAKCFGHLTKQLMTLADGRVVLALEGGHDLTAICDASEACVNALLGNELEPLAEDILHQSPNMNAVISLQKIIEIQSMSLKFS |
| Enzyme Length | 1011 |
| Uniprot Accession Number | Q9UKV0 |
| Absorption | |
| Active Site | ACT_SITE 783; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by Trichostatin A (TSA) and suberoylanilide hydroxamic acid. {ECO:0000269|PubMed:11535832}. |
| 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; Evidence={ECO:0000269|PubMed:11535832}; |
| DNA Binding | |
| EC Number | 3.5.1.98 |
| Enzyme Function | 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. Represses MEF2-dependent transcription. {ECO:0000269|PubMed:11535832}.; FUNCTION: Isoform 3 lacks active site residues and therefore is catalytically inactive. Represses MEF2-dependent transcription by recruiting HDAC1 and/or HDAC3. Seems to inhibit skeletal myogenesis and to 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. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Alternative sequence (11); Chain (1); Compositional bias (4); Erroneous initiation (1); Frameshift (1); Metal binding (4); Modified residue (5); Natural variant (1); Region (9); Sequence conflict (9) |
| Keywords | Alternative splicing;Chromatin regulator;Chromosomal rearrangement;Hydrolase;Metal-binding;Nucleus;Phosphoprotein;Reference proteome;Repressor;Transcription;Transcription regulation;Ubl conjugation;Zinc |
| Interact With | P41182; Q06413; P41212; Q60974; Q60974 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. |
| Modified Residue | MOD_RES 22; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:19690332; MOD_RES 220; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q99N13; MOD_RES 240; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q99N13; MOD_RES 451; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q99N13; MOD_RES 554; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q99N13 |
| Post Translational Modification | 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; which impairs nuclear accumulation (By similarity). Isoform 7 is phosphorylated on Tyr-1010. Phosphorylated by the PKC kinases PKN1 and PKN2, impairing nuclear import. {ECO:0000250, ECO:0000269|PubMed:20188095}.; PTM: Sumoylated. {ECO:0000269|PubMed:12032081, ECO:0000269|PubMed:12590135}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10713164; 11112321; 12374742; 14980219; 16147992; 16530045; 16751179; 18374649; 18549475; 19303849; 20711500; 20936779; 23752268; 33326746; 7588063; 9694793; |
| Motif | |
| Gene Encoded By | |
| Mass | 111,297 |
| Kinetics | |
| Metal Binding | METAL 646; /note=Zinc; /evidence=ECO:0000250; METAL 648; /note=Zinc; /evidence=ECO:0000250; METAL 654; /note=Zinc; /evidence=ECO:0000250; METAL 731; /note=Zinc; /evidence=ECO:0000250 |
| Rhea ID | RHEA:58196 |
| Cross Reference Brenda | 3.5.1.98; |