Q9ES46
Gene name |
Parvb |
Protein name |
Beta-parvin |
Names |
|
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:170736 |
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 Q9ES46
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9ES46-F1 | Predicted | AlphaFoldDB |
11 variants for Q9ES46
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3389348994 | 31 | A>V | No | EVA | |
| rs3389369170 | 50 | I>V | No | EVA | |
| rs258352743 | 73 | E>Q | No | EVA | |
| rs225743594 | 77 | I>V | No | EVA | |
| rs3389342083 | 157 | V>L | No | EVA | |
| rs3389349011 | 236 | G>S | No | EVA | |
| rs236871531 | 291 | L>I | No | EVA | |
| rs3406343731 | 317 | V>E | No | EVA | |
| rs3389371854 | 324 | F>L | No | EVA | |
| rs3389385617 | 333 | K>* | No | EVA | |
| rs3406408232 | 337 | A>G | No | EVA |
No associated diseases with Q9ES46
2 regional properties for Q9ES46
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Calponin homology domain | 88 - 195 | IPR001715-1 |
| domain | Calponin homology domain | 255 - 362 | IPR001715-2 |
Functions
6 GO annotations of cellular component
| Name | Definition |
|---|---|
| actin cytoskeleton | The part of the cytoskeleton (the internal framework of a cell) composed of actin and associated proteins. Includes actin cytoskeleton-associated complexes. |
| 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). |
| 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. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
| Z disc | Platelike region of a muscle sarcomere to which the plus ends of actin filaments are attached. |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| actin binding | Binding to monomeric or multimeric forms of actin, including actin filaments. |
6 GO annotations of biological process
| Name | Definition |
|---|---|
| actin cytoskeleton reorganization | A process that is carried out at the cellular level which results in dynamic structural changes to the arrangement of constituent parts of cytoskeletal structures comprising actin filaments and their associated proteins. |
| cell projection assembly | Formation of a prolongation or process extending from a cell, e.g. a flagellum or axon. |
| establishment or maintenance of cell polarity | Any cellular process that results in the specification, formation or maintenance of anisotropic intracellular organization or cell growth patterns. |
| establishment or maintenance of cell polarity regulating cell shape | Any cellular process that results in the specification, formation or maintenance of a polarized intracellular organization or cell growth patterns that regulate the shape of a cell. |
| lamellipodium assembly | Formation of a lamellipodium, a thin sheetlike extension of the surface of a migrating cell. |
| substrate adhesion-dependent cell spreading | The morphogenetic process that results in flattening of a cell as a consequence of its adhesion to a substrate. |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSSAPPRSPT | PRAPKMKKDE | SFLGKLGGTL | ARKKKTREVT | DLQEEGKSAI | NSPMAPALVD |
| 70 | 80 | 90 | 100 | 110 | 120 |
| IHPEDTQLEE | NEERTMIDPT | SREDPKFKEL | VKVLLDWIND | VLAEERIIVK | QLEEDLYDGQ |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VLQKLLEKLA | HCKLNVAEVT | QSEIGQKQKL | QTVLEAVQDL | LRPHGWPLRW | NVDSIHGKNL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| VAILHLLVSL | AMHFRAPIHL | PEHVTVQVVV | VRKREGLLHS | SHISEELTTT | TEIMMGRFER |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DAFDTLFDHA | PDKLNLVKKS | LITFVNKHLN | KLNLEVTDLE | TQFADGVYLV | LLLGLLEDYF |
| 310 | 320 | 330 | 340 | 350 | 360 |
| VPLHNFYLTP | DSFDQKVHNV | AFAFELMLDG | GLKKPKARPE | DVVNLDLKST | LRVLYTLFTK |
| YKDVE |