Q9DCN7
Gene name |
Rnft1 |
Protein name |
E3 ubiquitin-protein ligase RNFT1 |
Names |
RING finger and transmembrane domain-containing protein 1 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:76892 |
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 Q9DCN7
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9DCN7-F1 | Predicted | AlphaFoldDB |
20 variants for Q9DCN7
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3389158950 | 68 | H>P | No | EVA | |
| rs3389153710 | 118 | I>N | No | EVA | |
| rs3389198229 | 148 | K>N | No | EVA | |
| rs3389198259 | 150 | I>V | No | EVA | |
| rs3389187987 | 184 | H>L | No | EVA | |
| rs3389198217 | 194 | F>I | No | EVA | |
| rs3389189957 | 196 | N>K | No | EVA | |
| rs3389198194 | 205 | W>* | No | EVA | |
| rs3389153667 | 211 | V>A | No | EVA | |
| rs3389126216 | 263 | P>A | No | EVA | |
| rs3389187986 | 270 | I>V | No | EVA | |
| rs3389158990 | 274 | E>D | No | EVA | |
| rs3389191237 | 274 | E>K | No | EVA | |
| rs3389159015 | 276 | G>D | No | EVA | |
| rs3389164622 | 294 | L>V | No | EVA | |
| rs3389164575 | 332 | D>G | No | EVA | |
| rs3401943791 | 356 | E>Q | No | EVA | |
| rs3402715294 | 358 | C>Y | No | EVA | |
| rs3389164579 | 379 | C>Y | No | EVA | |
| rs3389158980 | 383 | W>R | No | EVA |
No associated diseases with Q9DCN7
4 regional properties for Q9DCN7
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Ribosome maturation protein SBDS, conserved site | 36 - 55 | IPR018023 |
| domain | Ribosome maturation protein SDO1/SBDS, central domain | 101 - 164 | IPR018978 |
| domain | Ribosome maturation protein SDO1/SBDS, N-terminal | 10 - 93 | IPR019783 |
| domain | Ribosome maturation protein SDO1/SBDS, C-terminal domain | 165 - 230 | IPR046928 |
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 | |
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| early endosome membrane | The lipid bilayer surrounding an early endosome. |
| endoplasmic reticulum | The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached). |
| 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. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| metal ion binding | Binding to a metal ion. |
| ubiquitin binding | Binding to ubiquitin, a protein that when covalently bound to other cellular proteins marks them for proteolytic degradation. |
| 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. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| positive regulation of ERAD pathway | Any process that activates or increases the frequency, rate or extent of ERAD pathway. |
| protein autoubiquitination | The ubiquitination by a protein of one or more of its own amino acid residues, or residues on an identical protein. Ubiquitination occurs on the lysine residue by formation of an isopeptide crosslink. |
9 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q9UKV5 | AMFR | E3 ubiquitin-protein ligase AMFR | Homo sapiens (Human) | PR |
| Q8WU17 | RNF139 | E3 ubiquitin-protein ligase RNF139 | Homo sapiens (Human) | PR |
| Q5M7Z0 | RNFT1 | E3 ubiquitin-protein ligase RNFT1 | Homo sapiens (Human) | PR |
| Q7TMV1 | Rnf139 | E3 ubiquitin-protein ligase RNF139 | Mus musculus (Mouse) | PR |
| Q9R049 | Amfr | E3 ubiquitin-protein ligase AMFR | Mus musculus (Mouse) | PR |
| P90859 | F26E4.3 | E3 ubiquitin-protein ligase hrd-like protein 1 | Caenorhabditis elegans | PR |
| Q7ZWF4 | rnf145 | RING finger protein 145 | Danio rerio (Zebrafish) (Brachydanio rerio) | PR |
| A5WW08 | chfr | E3 ubiquitin-protein ligase CHFR | Danio rerio (Zebrafish) (Brachydanio rerio) | PR |
| Q6NZ21 | rnft1 | E3 ubiquitin-protein ligase RNFT1 | Danio rerio (Zebrafish) (Brachydanio rerio) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MQASCNQLHD | PPGTAHEDAA | ASPCGHSRST | EGSLHPGDVH | IQINSGPKEY | SENPSSRNPR |
| 70 | 80 | 90 | 100 | 110 | 120 |
| SGVCTCAHGC | VHGRFRSYSH | SEARPPDDFA | TESGEHGSGS | FSEFRYLFKW | LQKSLPYILI |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LGIKLVMQHI | TGISLGIGLL | TTFMYANKSI | VNQVFLRERS | SKLRCAWLLV | FLAGSSVLLY |
| 190 | 200 | 210 | 220 | 230 | 240 |
| YTFHSQSLHY | SLIFLNPTLE | QLSFWEVLWI | VGITDFILKF | FFMGLKCLIL | LVPSFIMPFK |
| 250 | 260 | 270 | 280 | 290 | 300 |
| SKGYWYMLLE | ELCQYYRIFV | PIPVWFRYLI | SYGEFGNVTT | WSLGILLALL | YLILKLLDFF |
| 310 | 320 | 330 | 340 | 350 | 360 |
| GHLRTFRQVL | RVFFTRPSYG | VPASKRQCSD | MDGICTICQA | EFQKPVLLFC | QHIFCEECIT |
| 370 | 380 | 390 | |||
| LWFNREKTCP | LCRTVISECI | NKWKDGATSS | HLQMY |