Q3USJ8
Gene name |
Fchsd2 (Kiaa0769, Sh3md3) |
Protein name |
F-BAR and double SH3 domains protein 2 |
Names |
Protein nervous wreck 1, NWK1, SH3 multiple domains protein 3 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:207278 |
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
2 structures for Q3USJ8
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 7WEG | X-ray | 200 A | C/D | 728-740 | PDB |
| AF-Q3USJ8-F1 | Predicted | AlphaFoldDB |
28 variants for Q3USJ8
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3388902578 | 46 | K>E | No | EVA | |
| rs3388935068 | 50 | E>G | No | EVA | |
| rs223951513 | 51 | R>K | No | EVA | |
| rs1133158509 | 104 | I>V | No | EVA | |
| rs3388935099 | 286 | F>Y | No | EVA | |
| rs3388902646 | 292 | V>I | No | EVA | |
| rs3388931597 | 302 | Q>H | No | EVA | |
| rs3388931090 | 341 | N>I | No | EVA | |
| rs3388931418 | 371 | I>K | No | EVA | |
| rs3388931603 | 410 | M>I | No | EVA | |
| rs3388935058 | 419 | N>Y | No | EVA | |
| rs3388926473 | 473 | T>I | No | EVA | |
| rs3388912047 | 474 | C>F | No | EVA | |
| rs3388931366 | 480 | Y>* | No | EVA | |
| rs3413101006 | 498 | V>M | No | EVA | |
| rs3388907589 | 546 | R>Q | No | EVA | |
| rs3388935140 | 575 | L>I | No | EVA | |
| rs3388887388 | 582 | T>A | No | EVA | |
| rs3388902642 | 601 | N>K | No | EVA | |
| rs3388917118 | 602 | Q>H | No | EVA | |
| rs3397940166 | 604 | D>A | No | EVA | |
| rs3388923856 | 607 | F>I | No | EVA | |
| rs3388907618 | 672 | K>N | No | EVA | |
| rs3388926634 | 682 | P>L | No | EVA | |
| rs3388926621 | 684 | A>D | No | EVA | |
| rs244931940 | 726 | R>L | No | EVA | |
| rs3388935103 | 727 | R>Q | No | EVA | |
| rs3397940147 | 739 | L>P | No | EVA |
No associated diseases with Q3USJ8
Functions
6 GO annotations of cellular component
| Name | Definition |
|---|---|
| anchoring junction | A cell junction that mechanically attaches a cell (and its cytoskeleton) to neighboring cells or to the extracellular matrix. |
| clathrin-coated pit | A part of the endomembrane system in the form of an invagination of a membrane upon which a clathrin coat forms, and that can be converted by vesicle budding into a clathrin-coated vesicle. Coated pits form on the plasma membrane, where they are involved in receptor-mediated selective transport of many proteins and other macromolecules across the cell membrane, in the trans-Golgi network, and on some endosomes. |
| neuromuscular junction | The junction between the axon of a motor neuron and a muscle fiber. In response to the arrival of action potentials, the presynaptic button releases molecules of neurotransmitters into the synaptic cleft. These diffuse across the cleft and transmit the signal to the postsynaptic membrane of the muscle fiber, leading to a change in post-synaptic potential. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
| recycling endosome | An organelle consisting of a network of tubules that functions in targeting molecules, such as receptors transporters and lipids, to the plasma membrane. |
| stereocilium shaft | The shaft comprises the majority of the length of the stereocilium. This region is notable for the extreme stability of actin filaments, which are highly crosslinked into a parallel bundle. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| phosphatidylinositol-3,4,5-trisphosphate binding | Binding to phosphatidylinositol-3,4,5-trisphosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 3', 4' and 5' positions. |
| phosphatidylinositol-3,4-bisphosphate binding | Binding to phosphatidylinositol-3,4-bisphosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 3' and 4' positions. |
7 GO annotations of biological process
| Name | Definition |
|---|---|
| clathrin-dependent endocytosis | An endocytosis process that begins when material is taken up into clathrin-coated pits, which then pinch off to form clathrin-coated endocytic vesicles. |
| membrane organization | A process which results in the assembly, arrangement of constituent parts, or disassembly of a membrane. A membrane is a double layer of lipid molecules that encloses all cells, and, in eukaryotes, many organelles; may be a single or double lipid bilayer; also includes associated proteins. |
| neuromuscular synaptic transmission | The process of synaptic transmission from a neuron to a muscle, across a synapse. |
| positive regulation of actin filament polymerization | Any process that activates or increases the frequency, rate or extent of actin polymerization. |
| positive regulation of Arp2/3 complex-mediated actin nucleation | Any process that activates or increases the frequency, rate or extent of Arp2/3 complex-mediated actin nucleation. |
| protein transport | The directed movement of proteins into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. |
| regulation of actin filament polymerization | Any process that modulates the frequency, rate or extent of the assembly of actin filaments by the addition of actin monomers to a filament. |
15 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q5T0N5 | FNBP1L | Formin-binding protein 1-like | Homo sapiens (Human) | PR |
| Q7Z6B7 | SRGAP1 | SLIT-ROBO Rho GTPase-activating protein 1 | Homo sapiens (Human) | PR |
| Q96RU3 | FNBP1 | Formin-binding protein 1 | Homo sapiens (Human) | PR |
| O75044 | SRGAP2 | SLIT-ROBO Rho GTPase-activating protein 2 | Homo sapiens (Human) | PR |
| O94868 | FCHSD2 | F-BAR and double SH3 domains protein 2 | Homo sapiens (Human) | PR |
| Q91Z69 | Srgap1 | SLIT-ROBO Rho GTPase-activating protein 1 | Mus musculus (Mouse) | PR |
| Q812A2 | Srgap3 | SLIT-ROBO Rho GTPase-activating protein 3 | Mus musculus (Mouse) | PR |
| Q91Z67 | Srgap2 | SLIT-ROBO Rho GTPase-activating protein 2 | Mus musculus (Mouse) | PR |
| Q80TY0 | Fnbp1 | Formin-binding protein 1 | Mus musculus (Mouse) | PR |
| Q8CJ53 | Trip10 | Cdc42-interacting protein 4 | Mus musculus (Mouse) | PR |
| Q6PFY1 | Fchsd1 | F-BAR and double SH3 domains protein 1 | Mus musculus (Mouse) | PR |
| Q8K012 | Fnbp1l | Formin-binding protein 1-like | Mus musculus (Mouse) | PR |
| D4A208 | Srgap2 | SLIT-ROBO Rho GTPase-activating protein 2 | Rattus norvegicus (Rat) | PR |
| Q8R511 | Fnbp1 | Formin-binding protein 1 | Rattus norvegicus (Rat) | PR |
| Q2HWF0 | Fnbp1l | Formin-binding protein 1-like | Rattus norvegicus (Rat) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MQPPPRKVKV | TQELRNIQGE | QMTKLQAKHQ | AECDLLEDMR | TFSQKKAAIE | REYAQGIQKL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| ASQYLKRDWP | GIKTDDRNDY | RSMYPVWKSF | LEGTMQVAQS | RINICENYKN | FISEPARAVR |
| 130 | 140 | 150 | 160 | 170 | 180 |
| SLKEQQLKRC | VDQLTKIQTE | LQETVKDLVK | GKKKYFETEQ | MAHAVREKAD | IEAKSKLSLF |
| 190 | 200 | 210 | 220 | 230 | 240 |
| QSRISLQKAS | VKLKARRSEC | NTKATHARND | YLLTLAAANA | HQDRYYQTDL | VNIMKALDGN |
| 250 | 260 | 270 | 280 | 290 | 300 |
| VYDHLKDYLI | AFSRTELETC | QAIQNTFQFL | LENSSKVVRD | YNLQLFLQEN | AVFHKPQPFQ |
| 310 | 320 | 330 | 340 | 350 | 360 |
| FQPCDSDTSR | QLESETGTTE | EHSLNKEARK | WATRVAREHK | NIVHQQRVLN | ELECHGVALS |
| 370 | 380 | 390 | 400 | 410 | 420 |
| EQSRAELEQK | IDEARESIRK | AEIIKLKAEA | RLDLLKQIGV | SVDTWLKSAM | NQVMEELENE |
| 430 | 440 | 450 | 460 | 470 | 480 |
| RWARPPAVTS | NGTLHSLNAD | AEREEGEEFE | DNMDVFDDSS | SSPSGTLRNY | PLTCKVVYSY |
| 490 | 500 | 510 | 520 | 530 | 540 |
| KASQPDELTI | EEHEVLEVIE | DGDMEDWVKA | RNKVGQVGYV | PEKYLQFPTS | NSLLSMLQSL |
| 550 | 560 | 570 | 580 | 590 | 600 |
| AALDSRSHTS | SNSTEAELVS | GSLNGDASVC | FVKALYDYEG | QTDDELSFPE | GAIIRILNKE |
| 610 | 620 | 630 | 640 | 650 | 660 |
| NQDDDGFWEG | EFSGRIGVFP | SVLVEELSAS | ENGDTPWTRE | IQISPSPKPH | TSLPPLPLYD |
| 670 | 680 | 690 | 700 | 710 | 720 |
| QPPSSPYPSP | DKRSSQFFPR | SPSANENSLH | AESPGFSQAS | RQTPDTSYGK | LRPVRAAPPP |
| 730 | |||||
| PTQNHRRTTE | KMEDVEITLV |