Q7TMV1
Gene name |
Rnf139 |
Protein name |
E3 ubiquitin-protein ligase RNF139 |
Names |
ATP-binding cassette sub-family G member 2, Breast cancer resistance protein 1 homolog, Urate exporter, RING finger protein 139, RING-type E3 ubiquitin transferase RNF139, Translocation in renal carcinoma on chromosome 8 protein |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:75841 |
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 Q7TMV1
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q7TMV1-F1 | Predicted | AlphaFoldDB |
No variants for Q7TMV1
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q7TMV1 | |||||
No associated diseases with Q7TMV1
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 | |
4 GO annotations of cellular component
| Name | Definition |
|---|---|
| Derlin-1 retrotranslocation complex | A protein complex that functions in the retrotranslocation step of ERAD (ER-associated protein degradation), and includes at its core Derlin-1 oligomers forming a retrotranslocation channel. |
| endomembrane system | A collection of membranous structures involved in transport within the cell. The main components of the endomembrane system are endoplasmic reticulum, Golgi bodies, vesicles, cell membrane and nuclear envelope. Members of the endomembrane system pass materials through each other or though the use of vesicles. |
| 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. |
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| protease binding | Binding to a protease or a peptidase. |
| 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. |
| ubiquitin-like protein transferase activity | Catalysis of the transfer of a ubiquitin-like from one protein to another via the reaction X-ULP + Y --> Y-ULP + X, where both X-ULP and Y-ULP are covalent linkages. ULP represents a ubiquitin-like protein. |
| ubiquitin-protein transferase activity | Catalysis of the transfer of ubiquitin from one protein to another via the reaction X-Ub + Y --> Y-Ub + X, where both X-Ub and Y-Ub are covalent linkages. |
| zinc ion binding | Binding to a zinc ion (Zn). |
8 GO annotations of biological process
| Name | Definition |
|---|---|
| ERAD pathway | The protein catabolic pathway which targets endoplasmic reticulum (ER)-resident proteins for degradation by the cytoplasmic proteasome. It begins with recognition of the ER-resident protein, includes retrotranslocation (dislocation) of the protein from the ER to the cytosol, protein modifications necessary for correct substrate transfer (e.g. ubiquitination), transport of the protein to the proteasome, and ends with degradation of the protein by the cytoplasmic proteasome. |
| negative regulation of cell population proliferation | Any process that stops, prevents or reduces the rate or extent of cell proliferation. |
| negative regulation of translation | Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of proteins by the translation of mRNA or circRNA. |
| positive regulation of ubiquitin-dependent protein catabolic process | Any process that activates or increases the frequency, rate or extent of ubiquitin-dependent protein catabolic process. |
| protein destabilization | Any process that decreases the stability of a protein, making it more vulnerable to degradative processes or aggregation. |
| protein ubiquitination | The process in which one or more ubiquitin groups are added to a protein. |
| regulation of ER to Golgi vesicle-mediated transport | Any process that modulates the rate, frequency, or extent of ER to Golgi vesicle-mediated transport, the directed movement of substances from the endoplasmic reticulum (ER) to the Golgi, mediated by COP II vesicles. Small COP II coated vesicles form from the ER and then fuse directly with the cis-Golgi. Larger structures are transported along microtubules to the cis-Golgi. |
| regulation of protein processing | Any process that modulates the frequency, rate or extent of protein processing, a protein maturation process achieved by the cleavage of a peptide bond or bonds within a protein. |
8 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q9UKV5 | AMFR | E3 ubiquitin-protein ligase AMFR | Homo sapiens (Human) | PR |
| Q5M7Z0 | RNFT1 | E3 ubiquitin-protein ligase RNFT1 | Homo sapiens (Human) | PR |
| Q8WU17 | RNF139 | E3 ubiquitin-protein ligase RNF139 | Homo sapiens (Human) | PR |
| Q9DCN7 | Rnft1 | E3 ubiquitin-protein ligase RNFT1 | 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 |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAAVGPPQQQ | VRMAQQQVWA | ALEVALRVPC | LYIIDAIFNS | YYDSSQSRFC | IGLQIFLRLL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| GIVVSSIVLI | LSQRSLFKFY | MYSSAFLLAA | TSVLVNYYAA | LHIDFYGAYN | TSAFGIELLP |
| 130 | 140 | 150 | 160 | 170 | 180 |
| RKGPSLWMAL | IVLQLTFGIG | YVTLLQIQSI | YSQLMILNIL | VPIIGLITEL | PLHIRETVVL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| MSSLILIFNT | VLVLAVKLKW | FYYSTRYVYL | LVRHMYRIYG | LQLLMEDTWK | RIRFPDILRV |
| 250 | 260 | 270 | 280 | 290 | 300 |
| FWLTRITTQA | TVLMYILRMA | NETESFFISW | DDFWDVICNL | IISGCDSTLT | VLGMSAVISS |
| 310 | 320 | 330 | 340 | 350 | 360 |
| IAHYLGLGIL | AFIGSTEEDD | RRLGFVAPVL | FFILALQTGL | SGLRPEERLI | RLSRNMCLLL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| TAVLHFIHGM | TDPVLMSLSA | SHVSSFHRHF | PVLFVSACLF | ILPVLLSYVL | WHHYALNTWL |
| 430 | 440 | 450 | 460 | 470 | 480 |
| FAVTAFCVEL | CLKVIVSLTV | YTLFMIDGYY | NVLWEKLDDY | VYFVRSTGNI | IEFIFGVVMF |
| 490 | 500 | 510 | 520 | 530 | 540 |
| GNGAYTMMFE | SGSKIRACMM | CLHAYFNIYL | QVKNGWKTFM | NRRTAVKKIN | SLPEIKGSHL |
| 550 | 560 | 570 | 580 | 590 | 600 |
| QEIDDVCAIC | YHEFTTSARI | TPCNHYFHAL | CLRKWLYIQD | TCPMCHQKVY | IEDEIKDNSN |
| 610 | 620 | 630 | 640 | 650 | 660 |
| ASNNNGFIAP | NENPNPEEAL | REDAAGSDRE | LNEDDSTDCD | DDAQRERNGG | IQHTGAAAAA |
| AEFNDDTD |