Q6ZQ89
Gene name |
Marchf6 (Kiaa0597, March6) |
Protein name |
E3 ubiquitin-protein ligase MARCHF6 |
Names |
Membrane-associated RING finger protein 6, Membrane-associated RING-CH protein VI, MARCH-VI, RING-type E3 ubiquitin transferase MARCHF6 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:223455 |
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 Q6ZQ89
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q6ZQ89-F1 | Predicted | AlphaFoldDB |
26 variants for Q6ZQ89
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3389357171 | 79 | F>Y | No | EVA | |
| rs3389346647 | 88 | T>N | No | EVA | |
| rs3389352504 | 89 | A>T | No | EVA | |
| rs3404451367 | 176 | L>V | No | EVA | |
| rs3389318359 | 206 | D>Y | No | EVA | |
| rs3389346580 | 227 | G>D | No | EVA | |
| rs3389353799 | 235 | D>N | No | EVA | |
| rs3389353728 | 236 | N>K | No | EVA | |
| rs3389318292 | 249 | D>G | No | EVA | |
| rs3389346663 | 289 | H>Y | No | EVA | |
| rs3389355435 | 405 | T>I | No | EVA | |
| rs3389359964 | 425 | W>C | No | EVA | |
| rs3405666740 | 491 | V>A | No | EVA | |
| rs3389352532 | 536 | L>S | No | EVA | |
| rs3389327929 | 545 | T>M | No | EVA | |
| rs3389327883 | 605 | A>V | No | EVA | |
| rs218931727 | 822 | V>I | No | EVA | |
| rs229784733 | 830 | A>V | No | EVA | |
| rs3389346618 | 835 | G>A | No | EVA | |
| rs3389350838 | 845 | H>Y | No | EVA | |
| rs3389327905 | 847 | R>E | No | EVA | |
| rs3389357103 | 848 | I>F | No | EVA | |
| rs3389366958 | 857 | V>A | No | EVA | |
| rs3389276014 | 875 | H>Y | No | EVA | |
| rs3389370882 | 877 | K>* | No | EVA | |
| rs3389370893 | 884 | G>E | No | EVA |
No associated diseases with Q6ZQ89
1 regional properties for Q6ZQ89
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | MAGE homology domain | 85 - 285 | IPR002190 |
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 |
|---|---|
| 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 endoplasmic reticulum membrane | The component of the endoplasmic reticulum 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. |
| 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. |
6 GO annotations of molecular function
| Name | Definition |
|---|---|
| enzyme binding | Binding to an enzyme, a protein with catalytic activity. |
| ubiquitin conjugating enzyme binding | Binding to a ubiquitin conjugating enzyme, any of the E2 proteins. |
| 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-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. |
| ubiquitin-specific protease binding | Binding to a ubiquitin-specific protease. |
| zinc ion binding | Binding to a zinc ion (Zn). |
5 GO annotations of biological process
| Name | Definition |
|---|---|
| proteasomal protein catabolic process | The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds that is mediated by the proteasome. |
| proteasome-mediated ubiquitin-dependent protein catabolic process | The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, and mediated by the proteasome. |
| protein K48-linked ubiquitination | A protein ubiquitination process in which a polymer of ubiquitin, formed by linkages between lysine residues at position 48 of the ubiquitin monomers, is added to a protein. K48-linked ubiquitination targets the substrate protein for degradation. |
| protein ubiquitination | The process in which one or more ubiquitin groups are added to a protein. |
| ubiquitin-dependent ERAD pathway | The series of steps necessary to target endoplasmic reticulum (ER)-resident proteins for degradation by the cytoplasmic proteasome. Begins with recognition of the ER-resident protein, includes retrotranslocation (dislocation) of the protein from the ER to the cytosol, protein ubiquitination necessary for correct substrate transfer, transport of the protein to the proteasome, and ends with degradation of the protein by the cytoplasmic proteasome. |
3 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| O60337 | MARCHF6 | E3 ubiquitin-protein ligase MARCHF6 | Homo sapiens (Human) | PR |
| Q6NZQ8 | Marchf1 | E3 ubiquitin-protein ligase MARCHF1 | Mus musculus (Mouse) | PR |
| Q28IK8 | marchf8 | E3 ubiquitin-protein ligase MARCHF8 | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MDTAEEDICR | VCRSEGTPEK | PLYHPCVCTG | SIKFIHQECL | VQWLKHSRKE | YCELCKHRFA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| FTPIYSPDMP | SRLPIQDIFA | GLVTSIGTAI | RYWFHYTLVA | FAWLGVVPLT | ACRIYKCLFT |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GSVSSLLTLP | LDMLSTENLL | ADCLQGCFVV | TCTLCAFISL | VWLREQIVHG | GAPIWLEHAA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| PPFNAAGHHQ | NEAPVGGNGA | ENPAADQPAN | PAGENAVLGE | NPDAQDGQAE | EEEEDNEEED |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DAGVEDAADA | NNGAQDDMNW | NALEWDRAAE | ELTWERMLGL | DGSLVFLEHV | FWVVSLNTLF |
| 310 | 320 | 330 | 340 | 350 | 360 |
| ILVFAFCPYH | IGHFSLVGLG | FEEHVQASHF | EGLITTIVGY | ILLAITLIIC | HALATLVKFH |
| 370 | 380 | 390 | 400 | 410 | 420 |
| RSRRLLGVCY | IVVKVSLLVV | VEIGVFPLIC | GWWLDICSLE | MFDATLKDRE | LSFQSAPGTT |
| 430 | 440 | 450 | 460 | 470 | 480 |
| MFLHWLVGMV | YVFYFASFIL | LLREVLRPGV | LWFLRNLNDP | DFNPVQEMIH | LPIYRHLRRF |
| 490 | 500 | 510 | 520 | 530 | 540 |
| ILSVIVFGSI | VLLMLWLPIR | IIKSLLPNFL | PYNVMLYSDA | PVSELSLELL | LLQVVLPALL |
| 550 | 560 | 570 | 580 | 590 | 600 |
| EQGHTRQWLK | GLVRAWTVTA | GYLLDLHSYL | LGDQEENENS | ANQQVNNNQP | ARNNNAVPAG |
| 610 | 620 | 630 | 640 | 650 | 660 |
| EGLHAAHQAI | LQQGGPVGFQ | PYRRPLNFPL | RIFLLIVFMC | ITLLIASLIC | LTLPVFAGRW |
| 670 | 680 | 690 | 700 | 710 | 720 |
| LMSFWTGTAK | IHELYTAACG | LYVCWLTIRA | VTVLVAWMPQ | GRRVIFQKVK | EWSLMIMKTL |
| 730 | 740 | 750 | 760 | 770 | 780 |
| IVAVLLAGVV | PLLLGLLFEL | VIVAPLRVPL | DQTPLFYPWQ | DWALGVLHAK | IIAAITLMGP |
| 790 | 800 | 810 | 820 | 830 | 840 |
| QWWLKTVIEQ | VYANGIRNID | LHYIIRKLAA | PVISVLLLSL | CVPYVIASGA | VPLLGVTAEM |
| 850 | 860 | 870 | 880 | 890 | 900 |
| QNLVHRRIYP | FLLMVVVLMG | ILSFQVRQFK | RLYEHIKNDK | YLVGQRLVNY | ERKSGKQGPS |
| TPPPVSSQE |