Q925Q9
SS
Gene name |
Sh3kbp1 (Ruk, Seta) |
Protein name |
SH3 domain-containing kinase-binding protein 1 |
Names |
Regulator of ubiquitous kinase, Ruk, SH3-containing, expressed in tumorigenic astrocytes |
Species |
Rattus norvegicus (Rat) |
KEGG Pathway |
rno:84357 |
EC number |
|
Protein Class |
|
Descriptions
The CIN85 (Cbl-interacting protein of 85 kDa) is a multifunction adapter or scaffolding protein consisting of three SH3 domains in the N-terminal half of the protein connected by unstructured linkers followed by a proline rich region, a serine rich region, and a coiled coil domain at the C-terminus and plays important roles in both receptor tyrosine kinase downregulation and phosphatidylinositol 3 kinase inhibition. Prevention of the intramolecular interaction of domain C with the proline-rich motif P1 results in the complex formation of CIN85 with specific targets such as Cbl or p85 proteins.
Autoinhibitory domains (AIDs)
Target domain |
315-370 (SH3 domain-containing kinase-binding protein 1, third SH3 domain) |
Relief mechanism |
|
Assay |
|
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q925Q9
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q925Q9-F1 | Predicted | AlphaFoldDB |
No variants for Q925Q9
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q925Q9 | |||||
No associated diseases with Q925Q9
6 regional properties for Q925Q9
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | SH3 domain | 1 - 58 | IPR001452-1 |
| domain | SH3 domain | 98 - 157 | IPR001452-2 |
| domain | SH3 domain | 311 - 372 | IPR001452-3 |
| domain | SH3 domain-containing kinase-binding protein 1, first SH3 domain | 3 - 55 | IPR035770 |
| domain | SH3 domain-containing kinase-binding protein 1, second SH3 domain | 102 - 154 | IPR035771 |
| domain | SH3 domain-containing kinase-binding protein 1, third SH3 domain | 315 - 370 | IPR035772 |
Functions
8 GO annotations of cellular component
| Name | Definition |
|---|---|
| cell-cell junction | A cell junction that forms a connection between two or more cells of an organism; excludes direct cytoplasmic intercellular bridges, such as ring canals in insects. |
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| cytoplasmic vesicle membrane | The lipid bilayer surrounding a cytoplasmic vesicle. |
| 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. |
| endocytic vesicle | A membrane-bounded intracellular vesicle formed by invagination of the plasma membrane around an extracellular substance. Endocytic vesicles fuse with early endosomes to deliver the cargo for further sorting. |
| focal adhesion | A cell-substrate junction that anchors the cell to the extracellular matrix and that forms a point of termination of actin filaments. In insects focal adhesion has also been referred to as hemi-adherens junction (HAJ). |
| neuron projection | A prolongation or process extending from a nerve cell, e.g. an axon or dendrite. |
| synapse | The junction between an axon of one neuron and a dendrite of another neuron, a muscle fiber or a glial cell. As the axon approaches the synapse it enlarges into a specialized structure, the presynaptic terminal bouton, which contains mitochondria and synaptic vesicles. At the tip of the terminal bouton is the presynaptic membrane; facing it, and separated from it by a minute cleft (the synaptic cleft) is a specialized area of membrane on the receiving cell, known as the postsynaptic membrane. In response to the arrival of nerve impulses, the presynaptic terminal bouton secretes molecules of neurotransmitters into the synaptic cleft. These diffuse across the cleft and transmit the signal to the postsynaptic membrane. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| 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. |
| ubiquitin protein ligase binding | Binding to a ubiquitin protein ligase enzyme, any of the E3 proteins. |
8 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. |
| apoptotic process | A programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died. |
| 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. |
| 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. |
| endocytosis | A vesicle-mediated transport process in which cells take up external materials or membrane constituents by the invagination of a small region of the plasma membrane to form a new membrane-bounded vesicle. |
| positive regulation of B cell activation | Any process that activates or increases the frequency, rate or extent of B cell activation. |
| regulation of apoptotic process | Any process that modulates the occurrence or rate of cell death by apoptotic process. |
| regulation of cell shape | Any process that modulates the surface configuration of a cell. |
6 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q96B97 | SH3KBP1 | SH3 domain-containing kinase-binding protein 1 | Homo sapiens (Human) | EV |
| Q8R550 | Sh3kbp1 | SH3 domain-containing kinase-binding protein 1 | Mus musculus (Mouse) | SS |
| Q6AYE2 | Sh3glb1 | Endophilin-B1 | Rattus norvegicus (Rat) | PR |
| O35179 | Sh3gl2 | Endophilin-A1 | Rattus norvegicus (Rat) | PR |
| O35180 | Sh3gl3 | Endophilin-A3 | Rattus norvegicus (Rat) | PR |
| F1LRS8 | Cd2ap | CD2-associated protein | Rattus norvegicus (Rat) | SS |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MVEAIVEFDY | QAQHDDELTI | SVGEVITNIR | KEDGGWWEGQ | INGRRGLFPD | NFVREIKKDV |
| 70 | 80 | 90 | 100 | 110 | 120 |
| KKDLLSNKAP | EKPMHDVSSG | NSLLSSETIL | RTNKRGERRR | RRCQVAFSYL | PQNDDELELK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VGDIIEVVGE | VEEGWWEGVL | NGKTGMFPSN | FIKELSGESD | ELGISQDEQL | SKSRPEGFLP |
| 190 | 200 | 210 | 220 | 230 | 240 |
| ASLLPFPAHG | AKGKTTFEGT | ILYRAAPGKT | EGHRRYYSLR | ETTGSESDGG | DSSSTKSEGA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| NGTVATAAIQ | PKKVKGVGFG | DIFKDKPIKL | RPRSIEVEND | FLPVEKTIGK | KLPPATSTPD |
| 310 | 320 | 330 | 340 | 350 | 360 |
| PSKTEMDSRT | KTKDYCKVIF | PYEAQNDDEL | TIKEGDIVTL | INKDCIDVGW | WEGELNGRRG |
| 370 | 380 | 390 | 400 | 410 | 420 |
| VFPDNFVKLL | PSDFDKEGNR | PKKPPPPSAP | VIKQGAGTTE | RKHEIKKIPP | ERPETLPNRT |
| 430 | 440 | 450 | 460 | 470 | 480 |
| EEKERPEREP | KLDLQKPSVP | AIPPKKPRPP | KTNSLNRPGV | LPPRRPERPV | GPLTHTRGDS |
| 490 | 500 | 510 | 520 | 530 | 540 |
| SKIDLAGSTL | SGILDKDLSD | RSNDIDLEGF | DSVISSTEKL | SHPTTSRPKA | TGRRPPSQSL |
| 550 | 560 | 570 | 580 | 590 | 600 |
| TSSSLSSPDI | FDSPSPEEDK | EEHISLAHRG | IDVSKKTSRT | VTISQVSDNK | ASLPPKPGTM |
| 610 | 620 | 630 | 640 | 650 | 660 |
| AAASSGPASL | SSVASSPMSS | SLGTAGQRAS | SPSLFSAEGK | AKTESAVSSQ | AAIEELKMQV |
| 670 | 680 | 690 | 700 | ||
| RELRTIIETM | KDQQKREIKQ | LLSELDEEKK | IRLRLQMEVN | DIKKALQSK |