Q62219
Gene name |
Tgfb1i1 (Ara55) |
Protein name |
Transforming growth factor beta-1-induced transcript 1 protein |
Names |
Androgen receptor-associated protein of 55 kDa, Hydrogen peroxide-inducible clone 5 protein, Hic-5, TGF beta-stimulated clone 5, TSC-5 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:21804 |
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 Q62219
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q62219-F1 | Predicted | AlphaFoldDB |
20 variants for Q62219
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs224225928 | 53 | T>A | No | EVA | |
| rs3388931492 | 68 | S>F | No | EVA | |
| rs257827035 | 73 | A>T | No | EVA | |
| rs3388946490 | 76 | A>P | No | EVA | |
| rs3388946509 | 80 | S>T | No | EVA | |
| rs3388956014 | 103 | T>I | No | EVA | |
| rs3388951511 | 163 | A>T | No | EVA | |
| rs3388925156 | 203 | S>T | No | EVA | |
| rs3388947069 | 215 | L>I | No | EVA | |
| rs3398537072 | 223 | Q>E | No | EVA | |
| rs13479519 | 225 | K>N | No | EVA | |
| rs3398119998 | 241 | T>S | No | EVA | |
| rs3388947045 | 271 | G>R | No | EVA | |
| rs3388954604 | 285 | P>S | No | EVA | |
| rs221198355 | 336 | R>Q | No | EVA | |
| rs3388956006 | 368 | D>Y | No | EVA | |
| rs3388940383 | 384 | F>S | No | EVA | |
| rs3388925165 | 390 | R>C | No | EVA | |
| rs3388947068 | 435 | L>P | No | EVA | |
| rs3388955981 | 448 | S>C | No | EVA |
No associated diseases with Q62219
5 regional properties for Q62219
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Zinc finger, LIM-type | 226 - 285 | IPR001781-1 |
| domain | Zinc finger, LIM-type | 286 - 343 | IPR001781-2 |
| domain | Zinc finger, LIM-type | 344 - 403 | IPR001781-3 |
| domain | Zinc finger, LIM-type | 404 - 461 | IPR001781-4 |
| domain | Paxillin/TGFB1I1, LIM domain 1 | 228 - 280 | IPR047075 |
Functions
5 GO annotations of cellular component
| Name | Definition |
|---|---|
| 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. |
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| 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). |
| nuclear matrix | The dense fibrillar network lying on the inner side of the nuclear membrane. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
6 GO annotations of molecular function
| Name | Definition |
|---|---|
| I-SMAD binding | Binding to an inhibitory SMAD signaling protein. |
| metal ion binding | Binding to a metal ion. |
| nuclear androgen receptor binding | Binding to a nuclear androgen receptor. |
| Roundabout binding | Binding to Roundabout (ROBO) receptor, a transmembrane receptor. |
| transcription coactivator activity | A transcription coregulator activity that activates or increases the transcription of specific gene sets via binding to a DNA-bound DNA-binding transcription factor, either on its own or as part of a complex. Coactivators often act by altering chromatin structure and modifications. For example, one class of transcription coactivators modifies chromatin structure through covalent modification of histones. A second class remodels the conformation of chromatin in an ATP-dependent fashion. A third class modulates interactions of DNA-bound DNA-binding transcription factors with other transcription coregulators. A fourth class of coactivator activity is the bridging of a DNA-binding transcription factor to the general (basal) transcription machinery. The Mediator complex, which bridges sequence-specific DNA binding transcription factors and RNA polymerase, is also a transcription coactivator. |
| transcription coregulator activity | A transcription regulator activity that modulates the transcription of specific gene sets via binding to a DNA-bound DNA-binding transcription factor, either on its own or as part of a complex. Coregulators often act by altering chromatin structure and modifications. For example, one class of transcription coregulators modifies chromatin structure through covalent modification of histones. A second class remodels the conformation of chromatin in an ATP-dependent fashion. A third class modulates interactions of DNA-bound DNA-binding transcription factors with other transcription coregulators. |
12 GO annotations of biological process
| Name | Definition |
|---|---|
| cell fate commitment | The commitment of cells to specific cell fates and their capacity to differentiate into particular kinds of cells. Positional information is established through protein signals that emanate from a localized source within a cell (the initial one-cell zygote) or within a developmental field. |
| epithelial cell differentiation | The process in which a relatively unspecialized cell acquires specialized features of an epithelial cell, any of the cells making up an epithelium. |
| fat cell differentiation | The process in which a relatively unspecialized cell acquires specialized features of an adipocyte, an animal connective tissue cell specialized for the synthesis and storage of fat. |
| morphogenesis of embryonic epithelium | The process in which the anatomical structures of embryonic epithelia are generated and organized. |
| negative regulation of fat cell differentiation | Any process that stops, prevents, or reduces the frequency, rate or extent of adipocyte differentiation. |
| negative regulation of transforming growth factor beta receptor signaling pathway | Any process that stops, prevents, or reduces the frequency, rate or extent of any TGF-beta receptor signaling pathway. |
| positive regulation of DNA-templated transcription | Any process that activates or increases the frequency, rate or extent of cellular DNA-templated transcription. |
| positive regulation of epithelial to mesenchymal transition | Any process that increases the rate, frequency, or extent of epithelial to mesenchymal transition. Epithelial to mesenchymal transition is where an epithelial cell loses apical/basolateral polarity, severs intercellular adhesive junctions, degrades basement membrane components and becomes a migratory mesenchymal cell. |
| positive regulation of transforming growth factor beta receptor signaling pathway | Any process that activates or increases the frequency, rate or extent of TGF-beta receptor signaling pathway activity. |
| response to heat | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a heat stimulus, a temperature stimulus above the optimal temperature for that organism. |
| ubiquitin-dependent SMAD protein catabolic process | The chemical reactions and pathways resulting in the breakdown of SMAD signaling proteins by ubiquitination and targeting to the proteasome. |
| Wnt signaling pathway | The series of molecular signals initiated by binding of a Wnt protein to a frizzled family receptor on the surface of the target cell and ending with a change in cell state. |
10 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q3SYZ8 | PDLIM3 | PDZ and LIM domain protein 3 | Bos taurus (Bovine) | PR |
| P49024 | PXN | Paxillin | Gallus gallus (Chicken) | PR |
| Q9PU47 | PDLIM3 | PDZ and LIM domain protein 3 | Gallus gallus (Chicken) | PR |
| P49023 | PXN | Paxillin | Homo sapiens (Human) | PR |
| Q53GG5 | PDLIM3 | PDZ and LIM domain protein 3 | Homo sapiens (Human) | PR |
| O43294 | TGFB1I1 | Transforming growth factor beta-1-induced transcript 1 protein | Homo sapiens (Human) | PR |
| O70209 | Pdlim3 | PDZ and LIM domain protein 3 | Mus musculus (Mouse) | PR |
| Q8VI36 | Pxn | Paxillin | Mus musculus (Mouse) | PR |
| Q6QGC0 | PDLIM3 | PDZ and LIM domain protein 3 | Sus scrofa (Pig) | PR |
| Q66H76 | Pxn | Paxillin | Rattus norvegicus (Rat) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MEDLDALLSD | LETTTSHMSR | LGAPKERPPE | TLTPPPPYGH | QPQTGSGESS | GTTGDKDHLY |
| 70 | 80 | 90 | 100 | 110 | 120 |
| STVCKPRSPK | PVAPVAPPFS | SSSGVLGNGL | CELDRLLQEL | NATQFNITDE | IMSQFPSSKM |
| 130 | 140 | 150 | 160 | 170 | 180 |
| AEGEEKEDQS | EDKSSPTVPP | SPFPAPSKPS | ATSATQELDR | LMASLSDFRV | QNHLPASGPP |
| 190 | 200 | 210 | 220 | 230 | 240 |
| QPPAASPTRE | GCPSPPGQTS | KGSLDTMLGL | LQSDLSRRGV | PTQAKGLCGS | CNKPIAGQVV |
| 250 | 260 | 270 | 280 | 290 | 300 |
| TALGRAWHPE | HFLCSGCSTT | LGGSSFFEKD | GAPFCPECYF | ERFSPRCGFC | NQPIRHKMVT |
| 310 | 320 | 330 | 340 | 350 | 360 |
| ALGTHWHPEH | FCCVSCGEPF | GEEGFHEREG | RPYCRRDFLQ | LFAPRCQGCQ | GPILDNYISA |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LSALWHPDCF | VCRECLAPFS | GGSFFEHEGR | PLCENHFHAQ | RGSLCATCGL | PVTGRCVSAL |
| 430 | 440 | 450 | 460 | ||
| GRRFHPDHFT | CTFCLRPLTK | GSFQERASKP | YCQPCFLKLF | G |