Q9JID9
PR
Gene name |
Sh2b2 (Aps) |
Protein name |
SH2B adapter protein 2 |
Names |
Adapter protein with pleckstrin homology and Src homology 2 domains, SH2 and PH domain-containing adapter protein APS |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:23921 |
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 Q9JID9
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 1V5M | NMR | - | A | 177-299 | PDB |
| AF-Q9JID9-F1 | Predicted | AlphaFoldDB |
30 variants for Q9JID9
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3388797096 | 17 | D>E | No | EVA | |
| rs226313873 | 25 | H>R | No | EVA | |
| rs3388784826 | 57 | S>T | No | EVA | |
| rs3388803524 | 64 | F>V | No | EVA | |
| rs242349341 | 78 | S>A | No | EVA | |
| rs3388804729 | 132 | C>Y | No | EVA | |
| rs3388790287 | 146 | S>F | No | EVA | |
| rs225725065 | 159 | E>D | No | EVA | |
| rs3388797049 | 165 | R>L | No | EVA | |
| rs3388780293 | 171 | R>L | No | EVA | |
| rs3388804724 | 196 | M>I | No | EVA | |
| rs3388780297 | 198 | A>T | No | EVA | |
| rs3388801197 | 263 | K>* | No | EVA | |
| rs3406005408 | 269 | L>F | No | EVA | |
| rs218471900 | 307 | T>I | No | EVA | |
| rs3388800241 | 318 | A>V | No | EVA | |
| rs3388768666 | 345 | G>V | No | EVA | |
| rs3388803499 | 351 | P>S | No | EVA | |
| rs253525295 | 359 | V>M | No | EVA | |
| rs3396315610 | 411 | H>P | No | EVA | |
| rs3396018971 | 414 | L>M | No | EVA | |
| rs3388794080 | 416 | R>W | No | EVA | |
| rs3388784897 | 432 | G>V | No | EVA | |
| rs3396178054 | 457 | K>M | No | EVA | |
| rs3388794069 | 486 | F>L | No | EVA | |
| rs3395559855 | 492 | P>L | No | EVA | |
| rs3396315705 | 494 | E>D | No | EVA | |
| rs3388798874 | 509 | A>V | No | EVA | |
| rs3395883052 | 510 | Q>L | No | EVA | |
| rs3396246650 | 512 | P>T | No | EVA |
No associated diseases with Q9JID9
Functions
6 GO annotations of cellular component
| Name | Definition |
|---|---|
| actin filament | A filamentous structure formed of a two-stranded helical polymer of the protein actin and associated proteins. Actin filaments are a major component of the contractile apparatus of skeletal muscle and the microfilaments of the cytoskeleton of eukaryotic cells. The filaments, comprising polymerized globular actin molecules, appear as flexible structures with a diameter of 5-9 nm. They are organized into a variety of linear bundles, two-dimensional networks, and three dimensional gels. In the cytoskeleton they are most highly concentrated in the cortex of the cell just beneath the plasma membrane. |
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
| ruffle | Projection at the leading edge of a crawling cell; the protrusions are supported by a microfilament meshwork. |
| stress fiber | A contractile actin filament bundle that consists of short actin filaments with alternating polarity, cross-linked by alpha-actinin and possibly other actin bundling proteins, and with myosin present in a periodic distribution along the fiber. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| identical protein binding | Binding to an identical protein or proteins. |
| SH2 domain binding | Binding to a SH2 domain (Src homology 2) of a protein, a protein domain of about 100 amino-acid residues and belonging to the alpha + beta domain class. |
| signaling adaptor activity | The binding activity of a molecule that brings together two or more molecules in a signaling pathway, permitting those molecules to function in a coordinated way. Adaptor molecules themselves do not have catalytic activity. |
| transmembrane receptor protein tyrosine kinase adaptor activity | The binding activity of a molecule that brings together a transmembrane receptor protein tyrosine kinase and one or more other molecules, permitting them to function in a coordinated way. |
16 GO annotations of biological process
| Name | Definition |
|---|---|
| actin cytoskeleton 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 and their associated proteins. |
| antigen receptor-mediated signaling pathway | The series of molecular signals initiated by the cross-linking of an antigen receptor on a B or T cell. |
| B cell receptor signaling pathway | The series of molecular signals initiated by the cross-linking of an antigen receptor on a B cell. |
| B-1 B cell homeostasis | The process of regulating the proliferation and elimination of B cells of the B-1 subset such that the total number of B-1 B cells within a whole or part of an organism is stable over time in the absence of an outside stimulus. B-1 B cells are a distinct subset of B cells characterized as being CD5 positive, found predominantly in the peritoneum, pleural cavities, and spleen, and enriched for self-reactivity. |
| brown fat cell differentiation | The process in which a relatively unspecialized cell acquires specialized features of a brown adipocyte, an animal connective tissue cell involved in adaptive thermogenesis. Brown adipocytes contain multiple small droplets of triglycerides and a high number of mitochondria. |
| cytokine-mediated signaling pathway | The series of molecular signals initiated by the binding of a cytokine to a receptor on the surface of a cell, and ending with the regulation of a downstream cellular process, e.g. transcription. |
| establishment of localization in cell | Any process, occuring in a cell, that localizes a substance or cellular component. This may occur via movement, tethering or selective degradation. |
| glucose homeostasis | Any process involved in the maintenance of an internal steady state of glucose within an organism or cell. |
| glucose import | The directed movement of the hexose monosaccharide glucose into a cell or organelle. |
| insulin receptor signaling pathway | The series of molecular signals generated as a consequence of the insulin receptor binding to insulin. |
| intracellular signal transduction | The process in which a signal is passed on to downstream components within the cell, which become activated themselves to further propagate the signal and finally trigger a change in the function or state of the cell. |
| negative regulation of glucose import | Any process that stops, prevents, or reduces the frequency, rate or extent of the import of the hexose monosaccharide glucose into a cell or organelle. |
| nervous system development | The process whose specific outcome is the progression of nervous tissue over time, from its formation to its mature state. |
| regulation of immune response | Any process that modulates the frequency, rate or extent of the immune response, the immunological reaction of an organism to an immunogenic stimulus. |
| regulation of metabolic process | Any process that modulates the frequency, rate or extent of the chemical reactions and pathways within a cell or an organism. |
| regulation of Ras protein signal transduction | Any process that modulates the frequency, rate or extent of Ras protein signal transduction. |
1 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q9Z200 | Sh2b2 | SH2B adapter protein 2 | Rattus norvegicus (Rat) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MNGATPSSAA | APAPVPDWRQ | FCELHAQVAA | VDFAHKFCRF | LRDNPTYDTP | DAGTSFSRHF |
| 70 | 80 | 90 | 100 | 110 | 120 |
| AANFLAVFSE | EVRRVLGSAA | DTMEPEPAVT | SVTSALKTAT | YGHSRSSEDV | SAHAATKARV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| RKGFSLRNMS | LCVVDGVRDL | WHRRSSPEPD | GGATPKAAEP | ASEPRDKWTR | RLRLARTLAA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KVELVDIQRE | GALRFMVADD | AASGPGGTAQ | WQKCRLLLRR | AVAGERFRLE | FFVPPKASRP |
| 250 | 260 | 270 | 280 | 290 | 300 |
| KVSIPLSAII | EVRTTMPLEM | PEKDNTFVLK | VENGAEYILE | TIDSLQKHSW | VADIQGCVDP |
| 310 | 320 | 330 | 340 | 350 | 360 |
| GDSEEDTGLS | CARGGCLASR | VASCSCELLT | DADMPRPPET | TTAVGAVVTA | PHGRARDTVG |
| 370 | 380 | 390 | 400 | 410 | 420 |
| ESLAHVPLET | FLQTLESSGG | VSENNNPGDE | GAELDTDAEA | ELELSDYPWF | HGTLSRVKAA |
| 430 | 440 | 450 | 460 | 470 | 480 |
| QLVLAGGPRS | HGLFVIRQSE | TRPGECVLTF | NFQGKAKHLR | LSLNGHGQCH | VQHLWFQSVF |
| 490 | 500 | 510 | 520 | 530 | 540 |
| DMLRHFHTHP | IPLESGGSAD | ITLRSYVRAQ | GPPPDPGPAP | NTAAPVPACW | TEPAGQHYFS |
| 550 | 560 | 570 | 580 | 590 | 600 |
| SLATATCPPA | SPSNGAGASS | SSGSSSSATS | LPPRPAEGPL | SAHSRSNSTE | HLLDAASGAT |
| 610 | 620 | ||||
| EEPTEATLGR | ARAVENQYSF | Y |