Q6PFY1
PR
Gene name |
Fchsd1 |
Protein name |
F-BAR and double SH3 domains protein 1 |
Names |
Protein nervous wreck 2, NWK2 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:319262 |
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 Q6PFY1
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q6PFY1-F1 | Predicted | AlphaFoldDB |
33 variants for Q6PFY1
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3389408638 | 27 | T>P | No | EVA | |
| rs3389498828 | 51 | R>Q | No | EVA | |
| rs3389502703 | 145 | S>R | No | EVA | |
| rs3407387805 | 158 | L>* | No | EVA | |
| rs3407458590 | 158 | L>M | No | EVA | |
| rs31752257 | 230 | A>T | No | EVA | |
| rs3389498820 | 253 | T>I | No | EVA | |
| rs3389457512 | 281 | V>M | No | EVA | |
| rs3413135161 | 288 | P>L | No | EVA | |
| rs3389514612 | 291 | F>L | No | EVA | |
| rs3389457582 | 300 | Q>R | No | EVA | |
| rs3389408635 | 312 | W>* | No | EVA | |
| rs3407458547 | 343 | H>P | No | EVA | |
| rs3408439581 | 345 | H>Q | No | EVA | |
| rs3389500118 | 355 | R>C | No | EVA | |
| rs3389514584 | 377 | I>T | No | EVA | |
| rs3389498842 | 398 | G>C | No | EVA | |
| rs3389496016 | 440 | E>V | No | EVA | |
| rs3389490956 | 473 | V>L | No | EVA | |
| rs241471047 | 476 | G>S | No | EVA | |
| rs3389508558 | 480 | G>* | No | EVA | |
| rs3389514572 | 489 | E>* | No | EVA | |
| rs3389500132 | 494 | E>* | No | EVA | |
| rs3389477983 | 498 | E>D | No | EVA | |
| rs3389457493 | 580 | G>E | No | EVA | |
| rs3389465683 | 581 | V>L | No | EVA | |
| rs3389498792 | 593 | H>R | No | EVA | |
| rs3389494582 | 659 | D>Y | No | EVA | |
| rs3389447911 | 666 | R>K | No | EVA | |
| rs3389494603 | 670 | P>T | No | EVA | |
| rs3389497810 | 673 | P>S | No | EVA | |
| rs3389508524 | 677 | K>R | No | EVA | |
| rs261001244 | 685 | D>N | No | EVA |
No associated diseases with Q6PFY1
5 regional properties for Q6PFY1
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | FCH domain | 16 - 105 | IPR001060 |
| domain | SH3 domain | 466 - 527 | IPR001452-1 |
| domain | SH3 domain | 544 - 607 | IPR001452-2 |
| domain | F-BAR domain | 12 - 280 | IPR031160 |
| domain | FCHSD, SH3 domain 1 | 468 - 524 | IPR035460 |
Functions
4 GO annotations of cellular component
| Name | Definition |
|---|---|
| cell projection | A prolongation or process extending from a cell, e.g. a flagellum or axon. |
| 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. |
| perikaryon | The portion of the cell soma (neuronal cell body) that excludes the nucleus. |
| 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. |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| lipid binding | Binding to a lipid. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| 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. |
| 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 |
| Q3USJ8 | Fchsd2 | F-BAR and double SH3 domains protein 2 | 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 |
| MQPPPRKVKP | AQEVKLRFLE | QLSILQTRQQ | READLLEDIR | SYSKQRAAIE | REYGQALQKL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| AGPFLKREGQ | RSGEADSRTV | FGAWRCLLDA | TVAGGQTRLQ | ASDRYRDLAG | GTGRSAKEQV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LRKGTESLQQ | AQAEVLQSVR | ELSRSRKLYG | QRQRVWALAQ | EKAADVQARL | NRSDHGIFHS |
| 190 | 200 | 210 | 220 | 230 | 240 |
| RTSLQKLSTK | LSAQSAQYSQ | QLRAARNEYL | LNLVATNAHL | AHYYQEELPA | LLKVLVSELS |
| 250 | 260 | 270 | 280 | 290 | 300 |
| EYLRDPLTLL | GHTELEAAEM | ILEHARHGGK | ATSQVNWEQD | VKLFLQGPGV | FSPTPPQQFQ |
| 310 | 320 | 330 | 340 | 350 | 360 |
| PAGADQVCGL | EWGAGGMAGE | SGLEKEVQRW | TSRAARDYKI | QHHGHRVLQR | LEQRRQQAPG |
| 370 | 380 | 390 | 400 | 410 | 420 |
| REAPGVEQRL | QEVRENIRRA | QVSQVKGAAR | LALLQEAGLD | VQRWLKPAMT | QAQDEVEQER |
| 430 | 440 | 450 | 460 | 470 | 480 |
| RLSEARLSQR | DLSPTAEDAE | LSDFDECEEA | GELFEEPAPP | ALATRPLPCP | AHVVFGYQAG |
| 490 | 500 | 510 | 520 | 530 | 540 |
| REDELTITEG | EWLEVIEEGD | ADEWVKARNQ | HGEAGFVPER | YLNFPDLSLP | ESCHGIDNPS |
| 550 | 560 | 570 | 580 | 590 | 600 |
| GGEPTAFLAR | ALYSYTGQSE | EELSFPEGAL | IRLLPRAQDG | VDDGFWRGEF | GGHVGVFPSL |
| 610 | 620 | 630 | 640 | 650 | 660 |
| LVEELLGPPG | PPELSDPEQM | LPSPSPPSFS | PPAPTCALDG | STAPALPSDK | VLDCPGPLDM |
| 670 | 680 | ||||
| MVPRLRPMRP | PPPPPAKAPD | PGHPDPLT |