Q61792
Gene name |
Lasp1 (Mln50) |
Protein name |
LIM and SH3 domain protein 1 |
Names |
LAG-3, Activation-induced cytidine deaminase-linked autoimmunity protein, Aida, LASP-1, Metastatic lymph node gene 50 protein, MLN 50 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:16796 |
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 Q61792
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q61792-F1 | Predicted | AlphaFoldDB |
16 variants for Q61792
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs240015106 | 3 | P>L | No | EVA | |
| rs3402837451 | 5 | C>S | No | EVA | |
| rs3389210950 | 29 | C>Y | No | EVA | |
| rs3389201407 | 59 | K>M | No | EVA | |
| rs3389191383 | 64 | M>I | No | EVA | |
| rs3389208917 | 96 | K>* | No | EVA | |
| rs3402972646 | 102 | A>P | No | EVA | |
| rs3389133359 | 107 | L>P | No | EVA | |
| rs3389172099 | 110 | I>V | No | EVA | |
| rs3389133323 | 126 | F>I | No | EVA | |
| rs3389133390 | 128 | K>M | No | EVA | |
| rs3389199845 | 146 | A>T | No | EVA | |
| rs3389198889 | 150 | S>C | No | EVA | |
| rs3389168348 | 197 | I>L | No | EVA | |
| rs3389205202 | 207 | K>* | No | EVA | |
| rs3389199830 | 232 | V>A | No | EVA |
No associated diseases with Q61792
5 regional properties for Q61792
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| repeat | Nebulin repeat | 61 - 95 | IPR000900-1 |
| repeat | Nebulin repeat | 97 - 131 | IPR000900-2 |
| domain | SH3 domain | 204 - 263 | IPR001452 |
| domain | Zinc finger, LIM-type | 3 - 63 | IPR001781 |
| domain | Lasp1, SH3 domain | 205 - 263 | IPR035630 |
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| cortical actin cytoskeleton | The portion of the actin cytoskeleton, comprising filamentous actin and associated proteins, that lies just beneath the plasma membrane. |
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| 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). |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| actin filament binding | Binding to an actin filament, also known as F-actin, a helical filamentous polymer of globular G-actin subunits. |
| ion transmembrane transporter activity | Enables the transfer of an ion from one side of a membrane to the other. |
| metal ion binding | Binding to a metal ion. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| ion transport | The directed movement of charged atoms or small charged molecules into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. |
4 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q3B7M5 | LASP1 | LIM and SH3 domain protein 1 | Bos taurus (Bovine) | PR |
| Q14847 | LASP1 | LIM and SH3 domain protein 1 | Homo sapiens (Human) | PR |
| Q99MZ8 | Lasp1 | LIM and SH3 domain protein 1 | Rattus norvegicus (Rat) | PR |
| P34416 | F42H10.3 | LIM and SH3 domain protein F42H10.3 | Caenorhabditis elegans | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MNPNCARCGK | IVYPTEKVNC | LDKYWHKACF | HCETCKMTLN | MKNYKGYEKK | PYCNAHYPKQ |
| 70 | 80 | 90 | 100 | 110 | 120 |
| SFTMVADTPE | NLRLKQQSEL | QSQVRYKEEF | EKNKGKGFSV | VADTPELQRI | KKTQDQISNI |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KYHEEFEKSR | MGPSGGEGVE | PERREAQDSS | SYRRPTEQQQ | PQPHHIPTSA | PVYQQPQQQQ |
| 190 | 200 | 210 | 220 | 230 | 240 |
| MTSSYGGYKE | PAAPVSIQRS | APGGGGKRYR | AVYDYSAADE | DEVSFQDGDT | IVNVQQIDDG |
| 250 | 260 | ||||
| WMYGTVERTG | DTGMLPANYV | EAI |