Q8BU04
Gene name |
Ubr7 |
Protein name |
Putative E3 ubiquitin-protein ligase UBR7 |
Names |
N-recognin-7, RING-type E3 ubiquitin transferase UBR7 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:66622 |
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 Q8BU04
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q8BU04-F1 | Predicted | AlphaFoldDB |
22 variants for Q8BU04
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs256564306 | 9 | E>G | No | EVA | |
| rs260465345 | 54 | G>E | No | EVA | |
| rs228709210 | 54 | G>R | No | EVA | |
| rs247377049 | 79 | S>T | No | EVA | |
| rs3410927760 | 107 | K>* | No | EVA | |
| rs3403640684 | 107 | K>I | No | EVA | |
| rs47160510 | 136 | V>I | No | EVA | |
| rs264357926 | 198 | Q>R | No | EVA | |
| rs3389248955 | 216 | T>I | No | EVA | |
| rs46431462 | 226 | P>L | No | EVA | |
| rs3389254327 | 230 | A>T | No | EVA | |
| rs239922346 | 240 | A>V | No | EVA | |
| rs260278377 | 261 | S>T | No | EVA | |
| rs212301497 | 284 | S>Y | No | EVA | |
| rs3389251952 | 298 | K>N | No | EVA | |
| rs3389271365 | 314 | C>Y | No | EVA | |
| rs255491595 | 347 | N>S | No | EVA | |
| rs3389256919 | 379 | L>F | No | EVA | |
| rs3389252956 | 395 | T>R | No | EVA | |
| rs3389249029 | 404 | Q>* | No | EVA | |
| rs3389241954 | 406 | F>I | No | EVA | |
| rs257061369 | 419 | G>A | No | EVA |
No associated diseases with Q8BU04
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 | |
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| 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. |
| zinc ion binding | Binding to a zinc ion (Zn). |
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 |
|---|---|---|---|---|
| Q8N806 | UBR7 | Putative E3 ubiquitin-protein ligase UBR7 | Homo sapiens (Human) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAGAESPTEC | QAELEPVVSL | VDVLEEDEEL | ENEACAVLGG | SDSEKCSYSQ | GSVGRQALYA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| CSTCTPEGEE | PAGICLACSY | ECHGSHKLFE | LYTKRNFRCD | CGNSKFKNLE | CKLFPDKSKV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| NSCNKYNDNF | FGLYCVCKRP | YPDPEDEVPD | EMIQCVVCED | WFHGRHLGAI | PPESGDFQEM |
| 190 | 200 | 210 | 220 | 230 | 240 |
| VCQACMRRCS | FLWAYAAQLA | VTRISAEDDG | LLPNATGMGD | EDVSKPENGA | PQDNGLKEDA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| PEHGRDSVNE | VKAEQKNEPC | SSSSSESDLQ | TVFKKENIKT | EPQSSCRLQE | LQAKQFVKKD |
| 310 | 320 | 330 | 340 | 350 | 360 |
| AATYWPLNWR | SKLCTCQDCM | KMYGELDVLF | LTDECDTVLA | YENKGKNDQA | TDRRDPLMDT |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LSSMNRVQQV | ELICEYNDLK | TELKDYLKRF | ADEGTVVKRE | DIQQFFEEFQ | SKKRRRVDGL |
| QYYCS |