Gene Report
Approved Symbol | HDAC2 |
---|---|
Approved Name | histone deacetylase 2 |
Symbol Alias | RPD3, YAF1 |
Location | 6q21 |
Position | chr6:114257320-114292359 (-) |
External Links |
Entrez Gene: 3066 Ensembl: ENSG00000196591 UCSC: uc003pwd.2 HGNC ID: 4853 |
No. of Studies (Positive/Negative) | 1(1/0) |
Type | Literature-origin |
Name in Literature | Reference | Research Type | Statistical Result | Relation Description | |
---|---|---|---|---|---|
histone deacetylase 2 | Hobara, 2010 | patients and normal controls | In MDD, the expression of HDAC2 and -5 mRNA was increased in...... In MDD, the expression of HDAC2 and -5 mRNA was increased in a depressive state, but not in a remissive state, compared to controls. More... |
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Note:
1. The different color of the nodes denotes the level of the nodes.
Genetic/Epigenetic Locus | Protein and Other Molecule | Cell and Molecular Pathway | Neural System | Cognition and Behavior | Symptoms and Signs | Environment | MDD |
2. User can drag the nodes to rearrange the layout of the network. Click the node will enter the report page of the node. Right-click will show also the menus to link to the report page of the node and remove the node and related edges. Hover the node will show the level of the node and hover the edge will show the evidence/description of the edge.
3. The network is generated using Cytoscape Web
Approved Name | UniportKB | No. of Studies (Positive/Negative) | Source | |
---|---|---|---|---|
Histone deacetylase 2 | Q92769 | 0(0/0) | Gene mapped |
Gene mapped GO terms | ||||
ID | Name | Type | Evidence | |
---|---|---|---|---|
GO:0043433 | negative regulation of sequence-specific DNA binding transcription factor activity | biological process | IMP[19041327] | |
GO:0000792 | heterochromatin | cellular component | IEA | |
GO:0000122 | negative regulation of transcription from RNA polymerase II promoter | biological process | IMP[19041327] | |
GO:0005657 | replication fork | cellular component | IEA | |
GO:0090311 | regulation of protein deacetylation | biological process | IEA | |
GO:0004407 | histone deacetylase activity | molecular function | IDA[16642021] | |
GO:0032041 | NAD-dependent histone deacetylase activity (H3-K14 specific) | molecular function | IEA | |
GO:0016358 | dendrite development | biological process | ISS | |
GO:0090090 | negative regulation of canonical Wnt receptor signaling pathway | biological process | IEA | |
GO:0046969 | NAD-dependent histone deacetylase activity (H3-K9 specific) | molecular function | IEA | |
GO:0001103 | RNA polymerase II repressing transcription factor binding | molecular function | IPI | |
GO:0035098 | ESC/E(Z) complex | cellular component | IDA | |
GO:0033558 | protein deacetylase activity | molecular function | IMP[19041327] | |
GO:0007596 | blood coagulation | biological process | TAS | |
GO:0016580 | Sin3 complex | cellular component | IDA[17827154] | |
GO:0045944 | positive regulation of transcription from RNA polymerase II promoter | biological process | IMP[19041327] | |
GO:0045893 | positive regulation of transcription, DNA-dependent | biological process | IC[19041327] | |
GO:0045862 | positive regulation of proteolysis | biological process | IMP[19041327] | |
GO:0042475 | odontogenesis of dentin-containing tooth | biological process | ISS | |
GO:0045347 | negative regulation of MHC class II biosynthetic process | biological process | IC[19041327] | |
GO:0031490 | chromatin DNA binding | molecular function | IEA | |
GO:0005515 | protein binding | molecular function | IPI[19497860] | |
GO:0005654 | nucleoplasm | cellular component | TAS | |
GO:0045786 | negative regulation of cell cycle | biological process | TAS | |
GO:0021766 | hippocampus development | biological process | IEA | |
GO:0009913 | epidermal cell differentiation | biological process | ISS | |
GO:0061198 | fungiform papilla formation | biological process | ISS | |
GO:0048714 | positive regulation of oligodendrocyte differentiation | biological process | IEA | |
GO:0016581 | NuRD complex | cellular component | IDA[17827154] | |
GO:0003682 | chromatin binding | molecular function | ISS | |
GO:0097372 | NAD-dependent histone deacetylase activity (H3-K18 specific) | molecular function | IEA | |
GO:0006338 | chromatin remodeling | biological process | IC[17827154] | |
GO:0042733 | embryonic digit morphogenesis | biological process | ISS | |
GO:0008284 | positive regulation of cell proliferation | biological process | IMP[18347167] | |
GO:0005737 | cytoplasm | cellular component | TAS[12711221] | |
GO:0016575 | histone deacetylation | biological process | IMP[19372552] | |
GO:0046970 | NAD-dependent histone deacetylase activity (H4-K16 specific) | molecular function | IEA | |
GO:0051091 | positive regulation of sequence-specific DNA binding transcription factor activity | biological process | IEA | |
GO:0010977 | negative regulation of neuron projection development | biological process | ISS[18754010] | |
GO:0006344 | maintenance of chromatin silencing | biological process | IMP[19372552] | |
GO:0006351 | transcription, DNA-dependent | biological process | IEA | |
GO:0005634 | nucleus | cellular component | IDA | |
GO:0061029 | eyelid development in camera-type eye | biological process | ISS | |
GO:0060789 | hair follicle placode formation | biological process | ISS | |
GO:0043565 | sequence-specific DNA binding | molecular function | IDA[19276356] | |
GO:0032967 | positive regulation of collagen biosynthetic process | biological process | IC[19041327] | |
GO:0005667 | transcription factor complex | cellular component | IEA | |
GO:0003700 | sequence-specific DNA binding transcription factor activity | molecular function | IEA | |
GO:0019899 | enzyme binding | molecular function | IPI[11641274] | |
GO:0010870 | positive regulation of receptor biosynthetic process | biological process | IMP[18316616] | |
GO:0008134 | transcription factor binding | molecular function | IPI[17827154] | |
GO:0043066 | negative regulation of apoptotic process | biological process | ISS | |
GO:0045892 | negative regulation of transcription, DNA-dependent | biological process | IC[19041327]; IMP[19276356] | |
GO:0048011 | nerve growth factor receptor signaling pathway | biological process | TAS |
Gene mapped KEGG pathways | ||||
ID | Name | Brief Description | Full Description | |
---|---|---|---|---|
hsa05200 | pathways in_cancer | Pathways in cancer | ||
hsa04110 | cell cycle | Cell cycle | Mitotic cell cycle progression is accomplished through a rep...... Mitotic cell cycle progression is accomplished through a reproducible sequence of events, DNA replication (S phase) and mitosis (M phase) separated temporally by gaps known as G1 and G2 phases. Cyclin-dependent kinases (CDKs) are key regulatory enzymes, each consisting of a catalytic CDK subunit and an activating cyclin subunit. CDKs regulate the cell's progression through the phases of the cell cycle by modulating the activity of key substrates. Downstream targets of CDKs include transcription factor E2F and its regulator Rb. Precise activation and inactivation of CDKs at specific points in the cell cycle are required for orderly cell division. Cyclin-CDK inhibitors (CKIs), such as p16Ink4a, p15Ink4b, p27Kip1, and p21Cip1, are involved in the negative regulation of CDK activities, thus providing a pathway through which the cell cycle is negatively regulated. Eukaryotic cells respond to DNA damage by activating signaling pathways that promote cell cycle arrest and DNA repair. In response to DNA damage, the checkpoint kinase ATM phosphorylates and activates Chk2, which in turn directly phosphorylates and activates p53 tumor suppressor protein. p53 and its transcriptional targets play an important role in both G1 and G2 checkpoints. ATR-Chk1-mediated protein degradation of Cdc25A protein phosphatase is also a mechanism conferring intra-S-phase checkpoint activation. More... | |
hsa05016 | huntingtons disease | Huntington's disease | Huntington disease (HD) is an autosomal-dominant neurodegene...... Huntington disease (HD) is an autosomal-dominant neurodegenerative disorder that primarily affects medium spiny striatal neurons (MSN). HD is caused by a CAG repeat expansion in the IT15 gene, which results in a long stretch of polyglutamine close to the amino-terminus of the HD protein huntingtin (Htt). Mutant Htt (mHtt) has effects both in the cytoplasm and in the nucleus. In the cytoplasm, full-length mHtt can interfere with BDNF vesicular transport on microtubules. This mutant protein also may lead to abnormal endocytosis and secretion in neurons, because normal Htt form a complex with the proteins Hip1, clathrin and AP2 that are involved in endocytosis. In addition, mHtt affects Ca2+ signaling by sensitizing InsP3R1 to activation by InsP3, stimulating NR2B/NR1 NMDAR activity, and destabilizing mitochondrial Ca2+ handling. As a result, stimulation of glutamate receptors leads to supranormal Ca2+ responses in HD MSN and mitochondrial Ca2+ overload. The mHtt translocates to the nucleus, where it forms intranuclear inclusions, though they are not primarily responsible for toxicity. Nuclear toxicity is believed to be caused by interference with gene transcription, leading to loss of transcription of neuroprotective molecules such as BDNF. While mHtt binds to p53 and upregulates levels of nuclear p53 as well as p53 transcriptional activity. Augmented p53 mediates mitochondrial dysfunction. More... | |
hsa04330 | notch signaling_pathway | Notch signaling pathway | The Notch signaling pathway is an evolutionarily conserved, ...... The Notch signaling pathway is an evolutionarily conserved, intercellular signaling mechanism essential for proper embryonic development in all metazoan organisms in the Animal kingdom. The Notch proteins (Notch1-Notch4 in vertebrates) are single-pass receptors that are activated by the Delta (or Delta-like) and Jagged/Serrate families of membrane-bound ligands. They are transported to the plasma membrane as cleaved, but otherwise intact polypeptides. Interaction with ligand leads to two additional proteolytic cleavages that liberate the Notch intracellular domain (NICD) from the plasma membrane. The NICD translocates to the nucleus, where it forms a complex with the DNA binding protein CSL, displacing a histone deacetylase (HDAc)-co-repressor (CoR) complex from CSL. Components of an activation complex, such as MAML1 and histone acetyltransferases (HATs), are recruited to the NICD-CSL complex, leading to the transcriptional activation of Notch target genes. More... | |
hsa05220 | chronic myeloid_leukemia | Chronic myeloid leukemia | Chronic myelogenous leukaemia (CML) is a biphasic disease, i...... Chronic myelogenous leukaemia (CML) is a biphasic disease, initiated by expression of the BCR/ABL fusion gene product in self-renewing, haematopoietic stem cells (HSCs). HSCs can differentiate into common myeloid progenitors (CMPs), which then differentiate into granulocyte/macrophage progenitors (GMPs). HSCs can also differentiate into common lymphoid progenitors (CLPs), which are the progenitors of lymphocytes such as T cells and B cells. The initial chronic phase of CML (CML-CP) is characterized by a massive expansion of the granulocytic-cell series. Acquisition of additional genetic mutations beyond expression of BCR/ABL causes the progression of CML from chronic phase to blast phase (CML-BP), characterized by an accumulation of myeloid or lymphoid blast cells. The BCR/ABL fusion gene encodes p210BCR/ABL, an oncoprotein, which, unlike the normal p145 c-Abl, has constitutive tyrosine kinase activity and is predominantly localized in the cytoplasm. The tyrosine kinase activity is essential for cell transformation and the cytoplasmic localization of BCR/ABL allows the assembly of phosphorylated substrates in multiprotein complexes that transmit mitogenic and antiapoptotic signals. Additional cytogenetic and molecular changes are frequently found in patients with CML during the progression of the disease from chronic to blast phase. Some of the genetic changes include mutations in TP53, RB, and CDKN2A (also known as p16INK4A), or overexpression of genes such as EVI1. Additional chromosome translocations are also observed, such as t(3;21)(q26;q22), which generates AML1/EVI1. AML1/EVI-1 represses TGF-beta-mediated growth inhibitory signal. More... |
Gene mapped BioCarta pathways | ||||
ID | Name | Brief Description | Full Description | |
---|---|---|---|---|
MEF2D_PATHWAY | mef2d pathway | Role of MEF2D in T-cell Apoptosis | Mef2 pathway. Mef2 pathway. | |
ETS_PATHWAY | ets pathway | METS affect on Macrophage Differentiation | Terminal differentiation of cells is often accompanied by re...... Terminal differentiation of cells is often accompanied by repression of cellular proliferation, suggesting that there is a mechanism by which these cellular functions are coordinated. Macrophage differentiation is one model system in which this occurs; as macrophages differentiate, they also stop proliferating. Transcriptional regulation plays a key role in cell cycle progression as well as many differentiation processes. Ras stimulates cell cycle progression in part through Ets transcription factors that bind to cell cycle regulatory genes to activate their expression. Ets transcription factors also help to induce early macrophage differentiation. The activation of Ras signaling by M-CSF activates transcription of genes involved in differentiation through the coordinate expression of both Ets factors and AP-1. Other genes involved in cell cycle regulation involved the coordinate action of E2F-1 and Ets transcription factors. Mets is a factor related in sequence to Ets2 that is upregulated during macrophage differentiation. Increased expression of the Mets protein during macrophage differentiation allows the creation of heterodimers with DP103 to act as transcriptional repressors of cell cycle progression genes, recruiting corepressor to promoters they interact with. DP103 is a gene previously identified as an RNA helicase involved in RNA processing that interacts with EBNA factors from Epstein Barr Virus. The transcriptional repression involving Mets with DP103 is selective, and does not involve all Ets regulated genes. While cell cycle genes are repressed by Mets, other gene activated by Ets factors such as those involved in differentiation are not repressed by Mets. The transcriptional repression by Mets also involved members of the Rb family of tumor suppressors, such as p107 and p130. This requirement for additional factors involved in regulating proliferation may allow for another level of control on cell proliferation and coordination with differentiation. More... | |
CARM_ER_PATHWAY | carm er_pathway | CARM1 and Regulation of the Estrogen Receptor | Several forms of post-translational modification regulate pr...... Several forms of post-translational modification regulate protein activities. Recently, protein methylation by CARM1 (coactivator-associated arginine methyltransferase 1) has been observed to play a key role in transcriptional regulation. CARM1 associates with the p160 class of transcriptional coactivators involved in gene activation by steroid hormone family receptors. CARM1 also interacts with CBP/p300 transcriptional coactivators involved in gene activation by a large variety of transcription factors, including steroid hormone receptors and CEBP. One target of CARM1 is the core histones H3 and H4, which are also targets of the histone acetylase activity of CBP/p300 coactivators. Recruitment of CARM1 to the promoter region by binding to coactivators increases histone methylation and makes promoter regions more accessible for transcription. Another target of CARM1 methylation is a coactivator it interacts with, CBP. Methylation of CBP by CARM1 blocks CBP from acting as a coactivator for CREB and redirects the limited CBP pool in the cell to be available for steroid hormone receptors. Other forms of post-translational protein modification such as phosphorylation are reversible in nature, but as of yet a protein demethylase is not known. The methylation activity of CARM1 modulates the activity of specific transcriptional regulators. CARM1 acts as a coactivator for the myogenic transcription factor Mef2c, and is necessary for normal muscle cell differentiation. The estrogen receptor is another transcription factor that uses CARM1 as one of several coactivators, acting synergistically with CBP through the Grip1 member of the p160 family of coactivators. The interaction of estrogen receptor with various ligand-dependent coactivators may produce the tissue selective response of some estrogen receptor ligands like tamoxifen. More... |
Gene mapped Reactome pathways | |||
ID | Name | Description | |
---|---|---|---|
REACT_13776 | p75 ntr_receptor_mediated_signalling | Besides signalling through the tyrosine kinase receptors TRK...... Besides signalling through the tyrosine kinase receptors TRK A, B, and C, the mature neurotrophins NGF, BDNF, and NT3/4 signal through their common receptor p75NTR. NGF binding to p75NTR activates a number of downstream signalling events controlling survival, death, proliferation, and axonogenesis, according to the cellular context. p75NTR is devoid of enzymatic activity, and signals by recruiting other proteins to its own intracellular domain. p75 interacting proteins include NRIF, TRAF2, 4, and 6, NRAGE, necdin, SC1, NADE, RhoA, Rac, ARMS, RIP2, FAP and PLAIDD. Here we annotate only the proteins for which a clear involvement in p75NTR signalling was demonstrated. A peculiarity of p75NTR is the ability to bind the pro-neurotrophins proNGF and proBDNF. Proneurotrophins do not associate with TRK receptors, whereas they efficiently signal cell death by apoptosis through p75NTR. The biological action of neurotrophins is thus regulated by proteolytic cleavage, with proforms preferentially activating p75NTR, mediating apoptosis, and mature forms activating TRK receptors, to promote survival. Moreover, the two receptors are utilised to differentially modulate neuronal plasticity. For instance, proBDNF-p75NTR signalling facilitates LTD, long term depression, in the hippocampus , while BDNF-TRKB signalling promotes LTP (long term potentiation). Many biological observations indicate a functional interaction between p75NTR and TRKA signaling pathways. More... | |
REACT_11061 | signalling by_ngf | Neurotrophins (NGF, BDNF, NT-3, NT-4/5) play pivotal roles i...... Neurotrophins (NGF, BDNF, NT-3, NT-4/5) play pivotal roles in survival, differentiation, and plasticity of neurons in the peripheral and central nervous system. They are produced, and secreted in minute amounts, by a variety of tissues. They signal through two types of receptors: TRK tyrosine kinase receptors (TRKA, TRKB, TRKC), which specifically interact with the different neurotrophins, and p75NTR, which interacts with all neurotrophins. TRK receptors are reported in a variety of tissues in addition to neurons. p75NTRs are also widespread. Neurotrophins and their receptors are synthesized as several different splice variants, which differ in terms of their biological activities. The nerve growth factor (NGF) was the first growth factor to be identified and has served as a model for studying the mechanisms of action of neurotrophins and growth factors. The mechanisms by which NGF generates diverse cellular responses have been studied extensively in the rat pheochromocytoma cell line PC12. When exposed to NGF, PC12 cells exit the cell cycle and differentiate into sympathetic neuron-like cells. Current data show that signalling by the other neurotrophins is similar to NGF signalling. More... |
HDAC2 related interactors from protein-protein interaction data in HPRD (count: 65)
Gene | Interactor | Interactor in MK4MDD? | Experiment Type | PMID | |
---|---|---|---|---|---|
HDAC2 | CDYL | No | in vitro;in vivo | 12947414 | |
HDAC2 | TOP2A | No | in vivo | 11062478 | |
HDAC2 | PML | No | in vitro | 11259576 | |
HDAC2 | CTBP1 | No | in vitro;in vivo | 10766745 , 11022042 | |
HDAC2 | THRB | No | in vitro | 10508171 | |
HDAC2 | RELA | No | in vitro;in vivo | 12138131 , 12419806 | |
HDAC2 | SP3 | No | in vivo | 12151407 | |
HDAC2 | HDAC1 | No | in vitro;in vivo | 15451426 , 9520398 , 11287668 | |
HDAC2 | DNMT1 | Yes | in vitro;in vivo;yeast 2-hybrid | 10888872 | |
HDAC2 | RBBP7 | No | in vivo | 15451426 | |
HDAC2 | SNW1 | No | in vitro;in vivo;yeast 2-hybrid | 10644367 | |
HDAC2 | DAXX | No | in vitro | 10669754 | |
HDAC2 | CIR1 | No | yeast 2-hybrid | 9874765 | |
HDAC2 | TP53 | No | in vitro;in vivo | 10777477 | |
HDAC2 | SUV39H1 | No | in vitro;in vivo | 11788710 | |
HDAC2 | EED | No | in vitro;in vivo;yeast 2-hybrid | 10581039 | |
HDAC2 | MAD1L1 | No | in vitro | 15388328 | |
HDAC2 | IKZF4 | No | in vivo | 12015313 | |
HDAC2 | EID2 | No | in vivo | 12586827 | |
HDAC2 | BRMS1L | No | in vivo | 15451426 | |
HDAC2 | PPP1R8 | No | in vitro;in vivo | 12788942 | |
HDAC2 | RBP1 | No | in vivo | 15451426 | |
HDAC2 | SALL1 | No | in vitro | 11836251 | |
HDAC2 | SMYD1 | No | in vivo | 11923873 | |
HDAC2 | CDC20 | No | in vitro | 15388328 | |
HDAC2 | FKBP3 | No | in vitro;in vivo | 11532945 | |
HDAC2 | THRA | Yes | in vitro | 10508171 | |
HDAC2 | ARID4A | No | in vivo | 10490602 | |
HDAC2 | PHF21A | No | in vitro | 15325272 | |
HDAC2 | SPEN | No | in vitro;in vivo | 11331609 | |
HDAC2 | CSNK2A1 | No | in vitro;in vivo | 12176973 , 12082111 | |
HDAC2 | SP1 | No | in vivo | 12151407 | |
HDAC2 | RCOR1 | No | in vitro;in vivo | 11171972 | |
HDAC2 | HDAC10 | No | in vivo | 11739383 | |
HDAC2 | BRCA1 | No | in vitro;in vivo | 10220405 | |
HDAC2 | RFX5 | No | in vivo | 16464847 | |
HDAC2 | DNMT3B | Yes | in vitro;in vivo | 15120635 | |
HDAC2 | MBD2 | No | in vitro;in vivo | 10471499 | |
HDAC2 | SAP30 | No | in vivo | 15451426 | |
HDAC2 | RBBP4 | No | in vitro;in vivo | 15451426 , 12943729 , 12091390 , 11302704 | |
HDAC2 | PTMA | No | in vitro | 12634383 | |
HDAC2 | MXD1 | No | in vivo | 9150134 | |
HDAC2 | ANTXR1 | No | in vivo | 10545197 | |
HDAC2 | BUB3 | No | in vitro | 15388328 | |
HDAC2 | SMARCA5 | No | in vivo | 15775975 | |
HDAC2 | NRIP1 | No | in vitro | 15060175 | |
HDAC2 | STAT3 | No | in vivo | 15653507 | |
HDAC2 | HOPX | No | in vivo | 12975471 | |
HDAC2 | MTA1 | No | in vitro;in vivo | 11146623 | |
HDAC2 | PA2G4 | No | in vitro | 12682367 | |
HDAC2 | PPARD | No | in vivo | 11867749 | |
HDAC2 | PHB2 | No | in vitro | 15140878 | |
HDAC2 | DMAP1 | No | in vivo;yeast 2-hybrid | 10888872 | |
HDAC2 | SETDB1 | Yes | in vitro;in vivo | 12398767 | |
HDAC2 | YY1 | No | in vitro;in vivo | 11486036 | |
HDAC2 | BRMS1 | No | in vivo | 15451426 | |
HDAC2 | IKZF1 | No | in vitro;in vivo | 10357820 | |
HDAC2 | SIN3A | No | in vitro;in vivo | 9150134 , 15451426 , 16254079 | |
HDAC2 | IFRD1 | No | in vitro;in vivo | 12198164 | |
HDAC2 | CSNK2A2 | No | in vitro | 12082111 | |
HDAC2 | HIF1AN | No | in vitro | 11641274 | |
HDAC2 | CDH1 | No | in vitro | 15388328 | |
HDAC2 | ING1 | No | in vivo | 15451426 | |
HDAC2 | RUNX3 | No | in vitro;in vivo | 15138260 | |
HDAC2 | DDX20 | No | in vivo | 12007404 |