Gene Report
Basic Info
Approved Symbol |
SYVN1
|
Symbol Alias |
HRD1 |
Approved Name |
synovial apoptosis inhibitor 1, synoviolin |
Location |
11q13 |
Position |
chr11:64889252-64902004, - |
External Links |
HGNC: 20738
Entrez Gene: 84447
Ensembl: ENSG00000162298
UCSC: uc001odb.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)
Gene related GO terms (count: 15)
Gene related KEGG pathways (count: 2)
ID |
Name |
No. of Genes in ADHDgene |
Brief Description |
hsa04120 |
Ubiquitin mediated proteolysis |
29 |
Protein ubiquitination plays an important role in eukaryotic......
Protein ubiquitination plays an important role in eukaryotic cellular processes. It mainly functions as a signal for 26S proteasome dependent protein degradation. The addition of ubiquitin to proteins being degraded is performed by a reaction cascade consisting of three enzymes, named E1 (ubiquitin activating enzyme), E2 (ubiquitin conjugating enzyme), and E3 (ubiquitin ligase). Each E3 has specificity to its substrate, or proteins to be targeted by ubiquitination. Many E3s are discovered in eukaryotes and they are classified into four types: HECT type, U-box type, single RING-finger type, and multi-subunit RING-finger type. Multi-subunit RING-finger E3s are exemplified by cullin-Rbx E3s and APC/C. They consist of a RING-finger-containing subunit (RBX1 or RBX2) that functions to bind E2s, a scaffold-like cullin molecule, adaptor proteins, and a target recognizing subunit that binds substrates.
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|
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.
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|
Genes shared at least 5 GO terms with SYVN1 (count: 17)
Genes shared at least 2 KEGG pathways with SYVN1 (count: 1)
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