Q8CBG9
Gene name |
Rnf170 |
Protein name |
E3 ubiquitin-protein ligase RNF170 |
Names |
RING finger protein 170, RING-type E3 ubiquitin transferase RNF170 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:77733 |
EC number |
2.3.2.27: Aminoacyltransferases |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q8CBG9
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q8CBG9-F1 | Predicted | AlphaFoldDB |
15 variants for Q8CBG9
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs215483036 | 11 | K>E | No | EVA | |
| rs230642495 | 36 | E>D | No | EVA | |
| rs3388949498 | 46 | F>C | No | EVA | |
| rs244686958 | 52 | D>N | No | EVA | |
| rs3388932111 | 54 | V>F | No | EVA | |
| rs264668705 | 62 | L>F | No | EVA | |
| rs224479775 | 65 | T>I | No | EVA | |
| rs236714132 | 105 | A>T | No | EVA | |
| rs3388974542 | 109 | F>L | No | EVA | |
| rs3388977743 | 134 | F>L | No | EVA | |
| rs3388977515 | 142 | Y>* | No | EVA | |
| rs3388970969 | 146 | G>W | No | EVA | |
| rs3398767959 | 150 | G>A | No | EVA | |
| rs3388964994 | 151 | A>V | No | EVA | |
| rs3388970911 | 208 | L>M | No | EVA |
No associated diseases with Q8CBG9
4 regional properties for Q8CBG9
Functions
| Description | ||
|---|---|---|
| EC Number | 2.3.2.27 | Aminoacyltransferases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| endoplasmic reticulum membrane | The lipid bilayer surrounding the endoplasmic reticulum. |
| integral component of membrane | The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| metal ion binding | Binding to a metal ion. |
| ubiquitin protein ligase activity | Catalysis of the transfer of ubiquitin to a substrate protein via the reaction X-ubiquitin + S -> X + S-ubiquitin, where X is either an E2 or E3 enzyme, the X-ubiquitin linkage is a thioester bond, and the S-ubiquitin linkage is an amide bond: an isopeptide bond between the C-terminal glycine of ubiquitin and the epsilon-amino group of lysine residues in the substrate or, in the linear extension of ubiquitin chains, a peptide bond the between the C-terminal glycine and N-terminal methionine of ubiquitin residues. |
No GO annotations of biological process
| Name | Definition |
|---|---|
| No GO annotations for biological process |
1 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| F1MK05 | RNF170 | E3 ubiquitin-protein ligase RNF170 | Bos taurus (Bovine) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MQRYWRFQDN | KIQDICFGVL | GESWIQRPVM | ARYYSEGQSL | QQDDSFIEGV | SDQVLVAVVV |
| 70 | 80 | 90 | 100 | 110 | 120 |
| SLALTATLLY | ALLRNVQQNI | HPENQELVRV | LREQFQTEQD | VPAPARQQFY | TEMYCPICLH |
| 130 | 140 | 150 | 160 | 170 | 180 |
| QASFPVETNC | GHLFCGSCII | AYWRYGSWLG | AISCPICRQT | VTLLLTVFGE | DDQSQDVIRL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| RQDVNDYNRR | FSGQPRSIME | RIMDLPTLLR | HAFREVFSVG | GLFWMFRIRI | MLCLMGAFFY |
| 250 | 260 | 270 | 280 | ||
| LISPLDFVPE | ALFGILGFLD | DFFVIFLLLI | YISIMYREVI | TQRLTR |