P87139
Gene name |
SPAC57A7.07c |
Protein name |
Uncharacterized RING finger protein C57A7.09 |
Names |
|
Species |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
KEGG Pathway |
spo:SPAC57A7.09 |
EC number |
|
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 P87139
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P87139-F1 | Predicted | AlphaFoldDB |
5 variants for P87139
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| I_1526031_G_A | 40 | A>V | No | Jeffares_SNPs | |
| I_1525851_G_C | 100 | S>C | No | Jeffares_SNPs | |
| I_1525552_A_C | 200 | S>A | No | Jeffares_SNPs | |
| I_1525271_T_A | 293 | E>D | No | Jeffares_SNPs | |
| I_1525245_C_T | 302 | G>E | No | Jeffares_SNPs |
No associated diseases with P87139
1 regional properties for P87139
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Zinc finger, RING-type | 320 - 363 | IPR001841 |
7 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| fungal-type vacuole | A vacuole that has both lytic and storage functions. The fungal vacuole is a large, membrane-bounded organelle that functions as a reservoir for the storage of small molecules (including polyphosphate, amino acids, several divalent cations (e.g. calcium), other ions, and other small molecules) as well as being the primary compartment for degradation. It is an acidic compartment, containing an ensemble of acid hydrolases. At least in S. cerevisiae, there are indications that the morphology of the vacuole is variable and correlated with the cell cycle, with logarithmically growing cells having a multilobed, reticulated vacuole, while stationary phase cells contain a single large structure. |
| Golgi apparatus | A membrane-bound cytoplasmic organelle of the endomembrane system that further processes the core oligosaccharides (e.g. N-glycans) added to proteins in the endoplasmic reticulum and packages them into membrane-bound vesicles. The Golgi apparatus operates at the intersection of the secretory, lysosomal, and endocytic pathways. |
| Golgi membrane | The lipid bilayer surrounding any of the compartments of the Golgi apparatus. |
| 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. |
| late endosome | A prelysosomal endocytic organelle differentiated from early endosomes by lower lumenal pH and different protein composition. Late endosomes are more spherical than early endosomes and are mostly juxtanuclear, being concentrated near the microtubule organizing center. |
| vacuolar membrane | The lipid bilayer surrounding the vacuole and separating its contents from the cytoplasm of the cell. |
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. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| protein modification by small protein conjugation or removal | A protein modification process in which one or more groups of a small protein, such as ubiquitin or a ubiquitin-like protein, are covalently attached to or removed from a target protein. |
| 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 a ubiquitin group, or multiple ubiquitin groups, to the protein. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSYYQIIVCI | LASISYIILL | EVIALDLGVL | DNIFIPKRFA | ASTDVAIQLP | DRNVTLWSRQ |
| 70 | 80 | 90 | 100 | 110 | 120 |
| AVFGKHFTNA | SATTVINLYL | PSNFQEDMSG | CPNRNDTDAS | YFYENDIIDY | DIEYIEQKSY |
| 130 | 140 | 150 | 160 | 170 | 180 |
| SSKPSARVQK | DDGGESKDEA | ILDFLLVQRG | KCTYFDKALE | AQRLGFKGVI | VGDNRSPSSF |
| 190 | 200 | 210 | 220 | 230 | 240 |
| RLHYMVAPDK | VDESKVHIPS | LFVSTSSYNL | LWSDLLHSYR | QPLKLYAKPE | ELGDMFWPFL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LCFSPSIIML | ITVQALAIRK | FIRTYRTKSK | TRRFIEDLPS | RTISREGFYS | EEEEIENSTQ |
| 310 | 320 | 330 | 340 | 350 | 360 |
| NGELVPLMDE | STRRATFGVE | CVICLESFTK | GDKVVALPCK | HEFHRPCIAK | WIVDYRHACP |
| 370 | |||||
| TCNTEVPPPK | PF |