P55194
PR
Gene name |
Sh3bp1 |
Protein name |
SH3 domain-binding protein 1 |
Names |
3BP-1 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:20401 |
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 P55194
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 1ABO | X-ray | 200 A | C/D | 607-616 | PDB |
| AF-P55194-F1 | Predicted | AlphaFoldDB |
39 variants for P55194
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3389369638 | 34 | Q>L | No | EVA | |
| rs253729046 | 101 | T>S | No | EVA | |
| rs3389382923 | 109 | A>D | No | EVA | |
| rs1134421694 | 129 | R>M | No | EVA | |
| rs3389382941 | 180 | T>S | No | EVA | |
| rs3389374550 | 198 | L>I | No | EVA | |
| rs3406328941 | 209 | Y>D | No | EVA | |
| rs3389379141 | 216 | F>L | No | EVA | |
| rs3389369588 | 227 | F>L | No | EVA | |
| rs3389382915 | 228 | I>F | No | EVA | |
| rs3389388591 | 231 | L>S | No | EVA | |
| rs3389341839 | 237 | Y>H | No | EVA | |
| rs3405773042 | 246 | D>E | No | EVA | |
| rs248318848 | 250 | A>T | No | EVA | |
| rs33865795 | 257 | S>N | No | EVA | |
| rs3389382943 | 263 | P>L | No | EVA | |
| rs3389382926 | 276 | V>L | No | EVA | |
| rs3389293302 | 315 | A>G | No | EVA | |
| rs3389379219 | 318 | S>P | No | EVA | |
| rs3389370822 | 327 | M>I | No | EVA | |
| rs3389366841 | 352 | L>I | No | EVA | |
| rs254480431 | 389 | S>R | No | EVA | |
| rs225268457 | 390 | R>H | No | EVA | |
| rs3389369567 | 391 | L>I | No | EVA | |
| rs3389361790 | 405 | F>Y | No | EVA | |
| rs3389388633 | 414 | D>A | No | EVA | |
| rs236001458 | 415 | V>I | No | EVA | |
| rs3389366469 | 428 | G>V | No | EVA | |
| rs3389388594 | 442 | A>T | No | EVA | |
| rs3389534483 | 491 | S>N | No | EVA | |
| rs3389370796 | 501 | P>H | No | EVA | |
| rs13463449 | 515 | P>L | No | EVA | |
| rs3406275462 | 524 | E>A | No | EVA | |
| rs3405773040 | 542 | P>S | No | EVA | |
| rs3389369651 | 564 | P>L | No | EVA | |
| rs3389388662 | 575 | R>H | No | EVA | |
| rs215935449 | 587 | S>F | No | EVA | |
| rs228683907 | 604 | S>N | No | EVA | |
| rs108454243 | 652 | G>E | No | EVA |
No associated diseases with P55194
Functions
8 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. |
| bicellular tight junction | An occluding cell-cell junction that is composed of a branching network of sealing strands that completely encircles the apical end of each cell in an epithelial sheet; the outer leaflets of the two interacting plasma membranes are seen to be tightly apposed where sealing strands are present. Each sealing strand is composed of a long row of transmembrane adhesion proteins embedded in each of the two interacting plasma membranes. |
| cell leading edge | The area of a motile cell closest to the direction of movement. |
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| exocyst | A protein complex peripherally associated with the plasma membrane that determines where vesicles dock and fuse. At least eight complex components are conserved between yeast and mammals. |
| lamellipodium | A thin sheetlike process extended by the leading edge of a migrating cell or extending cell process; contains a dense meshwork of actin filaments. |
| nucleus | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. |
| phagocytic cup | An invagination of the cell membrane formed by an actin dependent process during phagocytosis. Following internalization it is converted into a phagosome. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| GTPase activator activity | Binds to and increases the activity of a GTPase, an enzyme that catalyzes the hydrolysis of GTP. |
| semaphorin receptor binding | Binding to a semaphorin receptor. |
| SH3 domain binding | Binding to a SH3 domain (Src homology 3) of a protein, small protein modules containing approximately 50 amino acid residues found in a great variety of intracellular or membrane-associated proteins. |
14 GO annotations of biological process
| Name | Definition |
|---|---|
| actin filament 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 comprising actin filaments. Includes processes that control the spatial distribution of actin filaments, such as organizing filaments into meshworks, bundles, or other structures, as by cross-linking. |
| cell junction assembly | A cellular process that results in the aggregation, arrangement and bonding together of a set of components to form a cell junction. |
| cell migration | The controlled self-propelled movement of a cell from one site to a destination guided by molecular cues. Cell migration is a central process in the development and maintenance of multicellular organisms. |
| establishment of epithelial cell apical/basal polarity | The specification and formation of the apicobasal polarity of an epithelial cell. |
| filopodium assembly | The assembly of a filopodium, a thin, stiff protrusion extended by the leading edge of a motile cell such as a crawling fibroblast or amoeba, or an axonal growth cone. |
| negative regulation of small GTPase mediated signal transduction | Any process that stops, prevents, or reduces the frequency, rate or extent of small GTPase mediated signal transduction. |
| phagocytosis, engulfment | The internalization of bacteria, immune complexes and other particulate matter or of an apoptotic cell by phagocytosis, including the membrane and cytoskeletal processes required, which involves one of three mechanisms: zippering of pseudopods around a target via repeated receptor-ligand interactions, sinking of the target directly into plasma membrane of the phagocytosing cell, or induced uptake via an enhanced membrane ruffling of the phagocytosing cell similar to macropinocytosis. |
| positive regulation of GTPase activity | Any process that activates or increases the activity of a GTPase. |
| regulation of actin cytoskeleton organization | Any process that modulates the frequency, rate or extent of the formation, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising actin filaments and their associated proteins. |
| regulation of actin filament depolymerization | Any process that modulates the frequency, rate or extent of the disassembly of actin filaments by the removal of actin monomers from a filament. |
| regulation of blood vessel endothelial cell migration | Any process that modulates the frequency, rate or extent of the migration of the endothelial cells of blood vessels. |
| regulation of Rac protein signal transduction | Any process that modulates the frequency, rate or extent of Rac protein signal transduction. |
| ruffle assembly | The aggregation, arrangement and bonding together of a set of components to form a ruffle, a projection at the leading edge of a crawling cell; the protrusions are supported by a microfilament meshwork. The formation of ruffles (also called membrane ruffling) is thought to be controlled by a group of enzymes known as Rho GTPases, specifically RhoA, Rac1 and cdc42. |
| semaphorin-plexin signaling pathway | The series of molecular signals generated as a consequence of a semaphorin receptor (composed of a plexin and a neurophilin) binding to a semaphorin ligand. |
6 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q9VDS5 | RhoGAP92B | Rho GTPase-activating protein 92B | Drosophila melanogaster (Fruit fly) | PR |
| P32019 | INPP5B | Type II inositol 1,4,5-trisphosphate 5-phosphatase | Homo sapiens (Human) | PR |
| Q9Y3L3 | SH3BP1 | SH3 domain-binding protein 1 | Homo sapiens (Human) | PR |
| Q8K2H3 | Fam13b | Protein FAM13B | Mus musculus (Mouse) | PR |
| Q8K337 | Inpp5b | Type II inositol 1,4,5-trisphosphate 5-phosphatase | Mus musculus (Mouse) | PR |
| Q8BYW1 | Arhgap25 | Rho GTPase-activating protein 25 | Mus musculus (Mouse) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MMKRQLHRMR | QLAHTGSSGR | TPETAEFLGE | DLLQVEQRLE | PAKRAAHNVH | KRLQACLQGQ |
| 70 | 80 | 90 | 100 | 110 | 120 |
| SGADMDKRVK | KLPLMALSTT | MAESFKELDP | DSSMGKALEM | TCAIQNQLAR | ILAEFEMTLE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| RDVLQPLSRL | SEEELPAILK | HKKSLQKLVS | DWNTLKSRLS | QAAKNSGSNQ | GLGGASGSHT |
| 190 | 200 | 210 | 220 | 230 | 240 |
| HTTTANKVEM | LKEEEEELKK | KVEQCKDEYL | ADLYHFSTKE | DSYANYFIHL | LEIQADYHRK |
| 250 | 260 | 270 | 280 | 290 | 300 |
| SLTSLDTALA | ELRDNHSQAD | HSPLTTAAPF | SRVYGVSLRT | HLQDLGRDIA | LPIEACVLLL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LSEGMQEEGL | FRLAAGASVL | KRLKQTMASD | PHSLEEFCSD | PHAVAGALKS | YLRELPEPLM |
| 370 | 380 | 390 | 400 | 410 | 420 |
| TSDLYDDWMR | AASLKEPGAR | LEALHDVCSR | LPQENFNNLR | YLMKFLALLA | EEQDVNKMTP |
| 430 | 440 | 450 | 460 | 470 | 480 |
| SNIAIVLGPN | LLWPPEKEGD | QAQLDAASVS | SIQVVGVVEA | LIQNADTLFP | GDINFNVSGI |
| 490 | 500 | 510 | 520 | 530 | 540 |
| FPGLAPQEKV | SSQQVSEELP | PVTVPAPATT | PAPTPAPASM | AVRERTEADL | PKPTSPKVSR |
| 550 | 560 | 570 | 580 | 590 | 600 |
| NPTETAASAE | DMTRKTKRPA | PARPTMPPPQ | PSSTRSSPPA | PSLPPGSVSP | GTPQALPRRL |
| 610 | 620 | 630 | 640 | 650 | 660 |
| VGTSLRAPTM | PPPLPPVPPQ | PARRQSRRLP | ASPVISNMPA | QVDQGVATED | RGGPEAVGGH |
| 670 | |||||
| PPPPALPPQP | RPRGLISETE |