Q6PER3
SS
Gene name |
Mapre3 |
Protein name |
Microtubule-associated protein RP/EB family member 3 |
Names |
EB1 protein family member 3 , EBF3 , End-binding protein 3 , EB3 , RP3 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:100732 |
EC number |
|
Protein Class |
|
Descriptions
EB1 including a Calponin homology (CH) domain and the C-terminal dimerization domain is a plus-end tracking protein that binds to the plus-end of microtubules (MT) and regulates the dynamics of the microtubule cytoskeleton. The CH domain is responsible for MT-binding and inhibited by the binding of the CH domain and the central region of the C-terminal domain including the FYF motif. SxIP competes with the CH domain and binds on the FYF motif of the C-terminal domain, and activates the CH domain.
Autoinhibitory domains (AIDs)
Target domain |
1-130 (CH domain) |
Relief mechanism |
Partner binding |
Assay |
|
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q6PER3
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q6PER3-F1 | Predicted | AlphaFoldDB |
14 variants for Q6PER3
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3543331708 | 2 | A>V | No | EVA | |
| rs3388746944 | 24 | V>A | No | EVA | |
| rs3388752109 | 33 | T>S | No | EVA | |
| rs3388745166 | 75 | F>L | No | EVA | |
| rs3388751566 | 85 | M>T | No | EVA | |
| rs3543317349 | 93 | V>I | No | EVA | |
| rs3388737161 | 107 | F>S | No | EVA | |
| rs3543332857 | 132 | G>S | No | EVA | |
| rs3388754353 | 145 | I>N | No | EVA | |
| rs3388751842 | 148 | K>I | No | EVA | |
| rs3388751595 | 213 | K>* | No | EVA | |
| rs3388746828 | 230 | L>F | No | EVA | |
| rs3388756521 | 231 | R>* | No | EVA | |
| rs3388751832 | 268 | D>N | No | EVA |
No associated diseases with Q6PER3
14 regional properties for Q6PER3
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | C2 domain | 1071 - 1194 | IPR000008 |
| domain | Phosphatidylinositol-specific phospholipase C, X domain | 320 - 465 | IPR000909 |
| domain | SH2 domain | 548 - 657 | IPR000980-1 |
| domain | SH2 domain | 666 - 756 | IPR000980-2 |
| domain | SH3 domain | 791 - 851 | IPR001452 |
| domain | Phospholipase C, phosphatidylinositol-specific, Y domain | 953 - 1070 | IPR001711 |
| domain | Pleckstrin homology domain | 27 - 144 | IPR001849-1 |
| domain | Pleckstrin homology domain | 489 - 680 | IPR001849-2 |
| domain | Pleckstrin homology domain | 804 - 933 | IPR001849-3 |
| domain | EF-hand domain | 152 - 187 | IPR002048 |
| binding_site | EF-Hand 1, calcium-binding site | 165 - 177 | IPR018247 |
| domain | PLC-gamma, C-terminal SH2 domain | 663 - 765 | IPR035023 |
| domain | PLC-gamma, N-terminal SH2 domain | 545 - 649 | IPR035024 |
| domain | 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1, SH3 domain | 791 - 850 | IPR035724 |
8 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| cytoplasmic microtubule | Any microtubule in the cytoplasm of a cell. |
| microtubule cytoskeleton | The part of the cytoskeleton (the internal framework of a cell) composed of microtubules and associated proteins. |
| microtubule organizing center | An intracellular structure that can catalyze gamma-tubulin-dependent microtubule nucleation and that can anchor microtubules by interacting with their minus ends, plus ends or sides. |
| microtubule plus-end | The growing (plus) end of a microtubule. In vitro, microtubules polymerize more quickly at the plus end than at the minus end. In vivo, microtubule growth occurs only at the plus end, and the plus end switches between periods of growth and shortening, a behavior known as dynamic instability. |
| midbody | A thin cytoplasmic bridge formed between daughter cells at the end of cytokinesis. The midbody forms where the contractile ring constricts, and may persist for some time before finally breaking to complete cytokinesis. |
| mitotic spindle astral microtubule end | Any microtubule end that is part of a mitotic spindle astral microtubule. |
| spindle midzone | The area in the center of the spindle where the spindle microtubules from opposite poles overlap. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| identical protein binding | Binding to an identical protein or proteins. |
| microtubule binding | Binding to a microtubule, a filament composed of tubulin monomers. |
| microtubule plus-end binding | Binding to the plus end of a microtubule. |
| protein kinase binding | Binding to a protein kinase, any enzyme that catalyzes the transfer of a phosphate group, usually from ATP, to a protein substrate. |
7 GO annotations of biological process
| Name | Definition |
|---|---|
| cell division | The process resulting in division and partitioning of components of a cell to form more cells; may or may not be accompanied by the physical separation of a cell into distinct, individually membrane-bounded daughter cells. |
| positive regulation of cyclin-dependent protein serine/threonine kinase activity | Any process that activates or increases the frequency, rate or extent of CDK activity. |
| positive regulation of DNA-templated transcription | Any process that activates or increases the frequency, rate or extent of cellular DNA-templated transcription. |
| protein localization to microtubule | A process in which a protein is transported to, or maintained at, a microtubule. |
| regulation of microtubule polymerization | Any process that modulates the frequency, rate or extent of microtubule polymerization. |
| regulation of microtubule polymerization or depolymerization | Any process that modulates the frequency, rate or extent of microtubule polymerization or depolymerization by the addition or removal of tubulin heterodimers from a microtubule. |
| spindle assembly | The aggregation, arrangement and bonding together of a set of components to form the spindle, the array of microtubules and associated molecules that serves to move duplicated chromosomes apart. |
12 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q3ZBD9 | MAPRE1 | Microtubule-associated protein RP/EB family member 1 | Bos taurus (Bovine) | SS |
| Q5ZLC7 | MAPRE1 | Microtubule-associated protein RP/EB family member 1 | Gallus gallus (Chicken) | SS |
| Q15555 | MAPRE2 | Microtubule-associated protein RP/EB family member 2 | Homo sapiens (Human) | PR |
| Q15691 | MAPRE1 | Microtubule-associated protein RP/EB family member 1 | Homo sapiens (Human) | EV |
| Q9UPY8 | MAPRE3 | Microtubule-associated protein RP/EB family member 3 | Homo sapiens (Human) | SS |
| Q61166 | Mapre1 | Microtubule-associated protein RP/EB family member 1 | Mus musculus (Mouse) | SS |
| Q8R001 | Mapre2 | Microtubule-associated protein RP/EB family member 2 | Mus musculus (Mouse) | PR |
| Q5XIT1 | Mapre3 | Microtubule-associated protein RP/EB family member 3 | Rattus norvegicus (Rat) | SS |
| Q66HR2 | Mapre1 | Microtubule-associated protein RP/EB family member 1 | Rattus norvegicus (Rat) | SS |
| Q7XJ60 | EB1A | Microtubule-associated protein RP/EB family member 1A | Arabidopsis thaliana (Mouse-ear cress) | SS |
| Q9FJJ5 | EB1B | Microtubule-associated protein RP/EB family member 1B | Arabidopsis thaliana (Mouse-ear cress) | EV |
| Q6P848 | mapre1 | Microtubule-associated protein RP/EB family member 1 | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) | SS |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAVNVYSTSV | TSENLSRHDM | LAWVNDSLHL | NYTKIEQLCS | GAAYCQFMDM | LFPGCVHLRK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VKFQAKLEHE | YIHNFKVLQA | AFKKMGVDKI | IPVEKLVKGK | FQDNFEFIQW | FKKFFDANYD |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GKDYNPLLAR | QGQDVAPPPN | PGDQIFNKSK | KLIGTAVPQR | TSPTGPKNMQ | TSGRLSNVAP |
| 190 | 200 | 210 | 220 | 230 | 240 |
| PCILRKNPPS | ARNGGHEADA | QILELNQQLL | DLKLTVDGLE | KERDFYFSKL | RDIELICQEH |
| 250 | 260 | 270 | 280 | ||
| ESENSPVISG | IIGILYATEE | GFAPPEDDEI | EEHQQEDQDE | Y |