Q6P5H6
Gene name |
Frmd5 |
Protein name |
FERM domain-containing protein 5 |
Names |
|
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:228564 |
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 Q6P5H6
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q6P5H6-F1 | Predicted | AlphaFoldDB |
24 variants for Q6P5H6
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3388584087 | 55 | K>* | No | EVA | |
| rs3388583735 | 69 | R>L | No | EVA | |
| rs3388587359 | 72 | L>* | No | EVA | |
| rs3388584695 | 119 | R>S | No | EVA | |
| rs3388581890 | 144 | E>V | No | EVA | |
| rs3388584151 | 145 | I>S | No | EVA | |
| rs3413117345 | 163 | F>Y | No | EVA | |
| rs3388580761 | 166 | K>N | No | EVA | |
| rs3388586117 | 184 | S>I | No | EVA | |
| rs3388586082 | 195 | F>I | No | EVA | |
| rs3388580783 | 207 | V>M | No | EVA | |
| rs3392076694 | 240 | F>L | No | EVA | |
| rs3392130330 | 241 | I>M | No | EVA | |
| rs3388584131 | 329 | E>K | No | EVA | |
| rs3388584741 | 332 | A>G | No | EVA | |
| rs3388580753 | 346 | M>V | No | EVA | |
| rs3388579264 | 377 | M>V | No | EVA | |
| rs27425158 | 417 | A>T | No | EVA | |
| rs3388579601 | 418 | V>M | No | EVA | |
| rs3388583769 | 457 | E>Q | No | EVA | |
| rs3412932138 | 469 | A>V | No | EVA | |
| rs3388581864 | 472 | A>* | No | EVA | |
| rs3388587318 | 472 | A>V | No | EVA | |
| rs3388584176 | 474 | A>D | No | EVA |
No associated diseases with Q6P5H6
7 regional properties for Q6P5H6
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | FERM domain | 17 - 298 | IPR000299 |
| domain | FERM adjacent | 308 - 354 | IPR014847 |
| domain | FERM, N-terminal | 21 - 83 | IPR018979 |
| domain | FERM, C-terminal PH-like domain | 214 - 302 | IPR018980 |
| conserved_site | FERM conserved site | 71 - 100 | IPR019747 |
| domain | FERM central domain | 103 - 210 | IPR019748 |
| domain | Band 4.1 domain | 13 - 210 | IPR019749 |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| adherens junction | A cell-cell junction composed of the epithelial cadherin-catenin complex. The epithelial cadherins, or E-cadherins, of each interacting cell extend through the plasma membrane into the extracellular space and bind to each other. The E-cadherins bind to catenins on the cytoplasmic side of the membrane, where the E-cadherin-catenin complex binds to cytoskeletal components and regulatory and signaling molecules. |
| cytoskeleton | A cellular structure that forms the internal framework of eukaryotic and prokaryotic cells. The cytoskeleton includes intermediate filaments, microfilaments, microtubules, the microtrabecular lattice, and other structures characterized by a polymeric filamentous nature and long-range order within the cell. The various elements of the cytoskeleton not only serve in the maintenance of cellular shape but also have roles in other cellular functions, including cellular movement, cell division, endocytosis, and movement of organelles. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| cytoskeletal protein binding | Binding to a protein component of a cytoskeleton (actin, microtubule, or intermediate filament cytoskeleton). |
| integrin binding | Binding to an integrin. |
| 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. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| actomyosin structure organization | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures containing both actin and myosin or paramyosin. The myosin may be organized into filaments. |
| negative regulation of cell motility | Any process that stops, prevents, or reduces the frequency, rate or extent of cell motility. |
| positive regulation of cell adhesion | Any process that activates or increases the frequency, rate or extent of cell adhesion. |
| regulation of cell migration | Any process that modulates the frequency, rate or extent of cell migration. |
14 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q58CU2 | EPB41L5 | Band 4.1-like protein 5 | Bos taurus (Bovine) | PR |
| Q9HCS5 | EPB41L4A | Band 4.1-like protein 4A | Homo sapiens (Human) | PR |
| Q9HCM4 | EPB41L5 | Band 4.1-like protein 5 | Homo sapiens (Human) | PR |
| A2A2Y4 | FRMD3 | FERM domain-containing protein 3 | Homo sapiens (Human) | PR |
| Q7Z6J6 | FRMD5 | FERM domain-containing protein 5 | Homo sapiens (Human) | PR |
| Q8BGS1 | Epb41l5 | Band 4.1-like protein 5 | Mus musculus (Mouse) | PR |
| P52963 | Epb41l4a | Band 4.1-like protein 4A | Mus musculus (Mouse) | PR |
| Q8BHD4 | Frmd3 | FERM domain-containing protein 3 | Mus musculus (Mouse) | PR |
| O70318 | Epb41l2 | Band 4.1-like protein 2 | Mus musculus (Mouse) | PR |
| Q9Z2H5 | Epb41l1 | Band 4.1-like protein 1 | Mus musculus (Mouse) | PR |
| P48193 | Epb41 | Protein 4.1 | Mus musculus (Mouse) | PR |
| Q9WV92 | Epb41l3 | Band 4.1-like protein 3 | Mus musculus (Mouse) | PR |
| Q0P4Q4 | frmd3 | FERM domain-containing protein 3 | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) | PR |
| O57457 | epb41l4a | Band 4.1-like protein 4 | Danio rerio (Zebrafish) (Brachydanio rerio) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MLSRLMSGSS | RSLEREYSCT | VRLLDDSEYT | CTIQRDAKGQ | YLFDLLCHHL | NLLEKDYFGI |
| 70 | 80 | 90 | 100 | 110 | 120 |
| RFVDPDKQRH | WLEFTKSVVK | QLRSQPPFTM | CFRVKFYPAD | PAALKEEITR | YLVFLQIKRD |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LYHGRLLCKT | SDAALLAAYI | LQAEIGDYDP | GKHPEGYSSK | FQFFPKHSEK | LEKKIAEIHK |
| 190 | 200 | 210 | 220 | 230 | 240 |
| TELSGQTPAT | SELNFLRKAQ | TLETYGVDPH | PCKDVSGNAA | FLAFTPFGFV | VLQGNKRVHF |
| 250 | 260 | 270 | 280 | 290 | 300 |
| IKWNEVTKLK | FEGKTFYLYV | SQKEEKKIIL | TYFAPTPEAC | KHLWKCGIEN | QAFYKLEKSS |
| 310 | 320 | 330 | 340 | 350 | 360 |
| QVRTVSSSNL | FFKGSRFRYS | GRVAKEVMES | SAKIKREPPE | IHRAGMVPSR | SCPSITHGPR |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LSSVPRTRRR | AVHISIMEGL | ESLRDSAHST | PVRSSSHGDT | FLPHVRSSRA | DSNERVAVIA |
| 430 | 440 | 450 | 460 | 470 | 480 |
| DEAYSPADSV | LPTPVAEHSL | ELMLLSRQIN | GATCSIEEEK | ESEASTPTAT | EAEALGGELR |
| 490 | 500 | 510 | |||
| ALCQGHGGSE | QEQRVHLKGP | QLQQQQWKGW | GKSVPLD |