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Gene Report
Basic Info
| Approved Symbol | HSPA8 |
|---|---|
| Previous Symbol | HSPA10 |
| Symbol Alias | HSC71, HSC70, HSP73 |
| Approved Name | heat shock 70kDa protein 8 |
| Previous Name | heat shock 70kD protein 8 |
| Location | 11q24.1 |
| Position | chr11:122928197-122933938, - |
| External Links |
HGNC: 5241 Entrez Gene: 3312 Ensembl: ENSG00000109971 UCSC: uc001pyo.2 |
| No. of Studies | 0 (significant: 0; non-significant: 0; trend: 0) |
| Source | Mapped by significant region |
Gene related studies (count: 0)
Gene related SNPs (count: 0)
Gene related CNVs (count: 0)
Gene related other variant (count: 0)
Gene related regions (count: 1)
| Region Name | Position | No. of Studies (significant/non-significant/trend)  |
|---|---|---|
| 11q | chr11:53700000-135006516 | 2 (1/1/0) |
Gene related GO terms (count: 32)
GO terms by PBA (with statistical significance of FDR<0.05) (count: 1)
| ID | Name | Type | Evidence[PMID] | No. of Genes in ADHDgene |
|---|---|---|---|---|
| GO:0005681 | spliceosomal complex | Cellular Component | 51 |
GO terms by database search (count: 31)
Gene related KEGG pathways (count: 7)
| ID | Name | No. of Genes in ADHDgene | Brief Description |
|---|---|---|---|
| hsa03040 | Spliceosome | 47 | After transcription, eukaryotic mRNA precursors contain prot...... After transcription, eukaryotic mRNA precursors contain protein-coding exons and noncoding introns. In the following splicing, introns are excised and exons are joined by a macromolecular complex, the spliceosome. The standard spliceosome is made up of five small nuclear ribonucleoproteins (snRNPs), U1, U2, U4, U5, and U6 snRNPs, and several spliceosome-associated proteins (SAPs). Spliceosomes are not a simple stable complex, but a dynamic family of particles that assemble on the mRNA precursor and help fold it into a conformation that allows transesterification to proceed. Various spliceosome forms (e.g. A-, B- and C-complexes) have been identified. More... |
| hsa04144 | Endocytosis | 39 | Endocytosis is a mechanism for cells to remove ligands, nutr...... Endocytosis is a mechanism for cells to remove ligands, nutrients, and plasma membrane (PM) proteins, and lipids from the cell surface, bringing them into the cell interior. Transmembrane proteins entering through clathrin-dependent endocytosis (CDE) have sequences in their cytoplasmic domains that bind to the APs (adaptor-related protein complexes) and enable their rapid removal from the PM. In addition to APs and clathrin, there are numerous accessory proteins including dynamin. Depending on the various proteins that enter the endosome membrane, these cargoes are sorted to distinct destinations. Some cargoes, such as nutrient receptors, are recycled back to the PM. Ubiquitylated membrane proteins, such as activated growth-factor receptors, are sorted into intraluminal vesicles and eventually end up in the lysosome lumen via multivesicular endosomes (MVEs). There are distinct mechanisms of clathrin-independent endocytosis (CIE) depending upon the cargo and the cell type. More... |
| hsa04612 | Antigen processing and presentation | 9 | |
| hsa05145 | Toxoplasmosis | 33 | Toxoplasma gondii is an obligate intracellular parasite that...... Toxoplasma gondii is an obligate intracellular parasite that is prevalent worldwide. The tachyzoite form acquired by oral ingestion downmodulates proinflammatory signaling pathways via various mechanisms. During early infection, nuclear translocation of NFkB is temporally blocked and p38 MAPK phosphorylation is prevented, suppressing IL-12 production. Another pathway for IL-12 induction occurs through CCR5 dependent pathway, but parasitic induction of an eicosanoid LXA4 contributes to the downregulation of IL-12. Direct activation of STAT3 by the parasite enhance anti-inflammatory function of IL-10 and TGF beta. T. gondii can cause lifelong chronic infection by establishing an anti-apoptotic environment through induction of bcl-2 or IAPs and by redirecting LDL-mediated cholesterol transport to scavenge nutrients from the host. More... |
| hsa04010 | MAPK signaling pathway | 69 | The mitogen-activated protein kinase (MAPK) cascade is a hig...... The mitogen-activated protein kinase (MAPK) cascade is a highly conserved module that is involved in various cellular functions, including cell proliferation, differentiation and migration. Mammals express at least four distinctly regulated groups of MAPKs, extracellular signal-related kinases (ERK)-1/2, Jun amino-terminal kinases (JNK1/2/3), p38 proteins (p38alpha/beta/gamma/delta) and ERK5, that are activated by specific MAPKKs: MEK1/2 for ERK1/2, MKK3/6 for the p38, MKK4/7 (JNKK1/2) for the JNKs, and MEK5 for ERK5. Each MAPKK, however, can be activated by more than one MAPKKK, increasing the complexity and diversity of MAPK signalling. Presumably each MAPKKK confers responsiveness to distinct stimuli. For example, activation of ERK1/2 by growth factors depends on the MAPKKK c-Raf, but other MAPKKKs may activate ERK1/2 in response to pro-inflammatory stimuli. More... |
| hsa05162 | Measles | 20 | Measles virus (MV) is highly contagious virus that leads inf...... Measles virus (MV) is highly contagious virus that leads infant death worldwide. Humans are the unique natural reservoir for this virus. It causes severe immunosuppression favouring secondary bacterial infections. Several MV proteins have been suggested to disturb host immunity. After infection of host lymphoid cells via SLAM, MV inhibits cytokine response by direct interference with host signaling systems. Three proteins (P, V, and C) associate with Jak/STAT proteins in interferon-triggered pathway and other important proteins related to apoptosis. Interaction between MV and host brings about the shift towards a Th2 response by decreasing IL-12 production and induces lymphopenia by suppressing cell proliferation. More... |
| hsa04141 | Protein processing in endoplasmic reticulum | 26 | The endoplasmic reticulum (ER) is a subcellular organelle wh...... The endoplasmic reticulum (ER) is a subcellular organelle where proteins are folded with the help of lumenal chaperones. Newly synthesized peptides enter the ER via the sec61 pore and are glycosylated. Correctly folded proteins are packaged into transport vesicles that shuttle them to the Golgi complex. Misfolded proteins are retained within the ER lumen in complex with molecular chaperones. Proteins that are terminally misfolded bind to BiP and are directed toward degradation through the proteasome in a process called ER-associated degradation (ERAD). Accumulation of misfolded proteins in the ER causes ER stress and activates a signaling pathway called the unfolded protein response (UPR). In certain severe situations, however, the protective mechanisms activated by the UPR are not sufficient to restore normal ER function and cells die by apoptosis. More... |
Genes shared at least 5 GO terms with HSPA8 (count: 126)
Genes shared at least 2 KEGG pathways with HSPA8 (count: 29)
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Region: chr11:122928197..122933938 View in gBrowse
Copyright: Bioinformatics Lab, Institute of Psychology, Chinese Academy of Sciences Feedback
Last update: Feb 26, 2014