Q9ERG0
PR
Gene name |
Lima1 (D15Ertd366e, Eplin) |
Protein name |
LIM domain and actin-binding protein 1 |
Names |
Epithelial protein lost in neoplasm, mEPLIN |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:65970 |
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 Q9ERG0
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9ERG0-F1 | Predicted | AlphaFoldDB |
40 variants for Q9ERG0
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3389352041 | 19 | T>I | No | EVA | |
| rs3389390457 | 37 | I>V | No | EVA | |
| rs3405980710 | 62 | Q>PPGSPTSSLTQTGSLF* | No | EVA | |
| rs13459535 | 85 | F>L | No | EVA | |
| rs13459534 | 104 | P>R | No | EVA | |
| rs228066622 | 121 | E>G | No | EVA | |
| rs3389386613 | 201 | F>L | No | EVA | |
| rs3406628134 | 265 | T>S | No | EVA | |
| rs3389383922 | 303 | Q>H | No | EVA | |
| rs3389352009 | 309 | P>S | No | EVA | |
| rs261615151 | 317 | H>Q | No | EVA | |
| rs221583577 | 325 | T>A | No | EVA | |
| rs246946212 | 346 | V>A | No | EVA | |
| rs32036445 | 353 | P>S | No | EVA | |
| rs3389339985 | 417 | Y>H | No | EVA | |
| rs3389390421 | 453 | G>* | No | EVA | |
| rs3389405444 | 459 | H>Q | No | EVA | |
| rs3389368731 | 475 | R>K | No | EVA | |
| rs3389383584 | 483 | G>R | No | EVA | |
| rs239906469 | 486 | P>S | No | EVA | |
| rs3389388492 | 505 | S>R | No | EVA | |
| rs257042961 | 516 | R>K | No | EVA | |
| rs250576930 | 518 | D>G | No | EVA | |
| rs221758205 | 538 | G>S | No | EVA | |
| rs3389395932 | 543 | L>R | No | EVA | |
| rs3406628189 | 568 | D>A | No | EVA | |
| rs3389383923 | 578 | R>Q | No | EVA | |
| rs32113648 | 605 | A>T | No | EVA | |
| rs3389307903 | 605 | A>V | No | EVA | |
| rs242956009 | 630 | M>T | No | EVA | |
| rs3389405431 | 649 | K>N | No | EVA | |
| rs3389383617 | 655 | E>V | No | EVA | |
| rs232415860 | 664 | S>G | No | EVA | |
| rs3389339920 | 665 | S>T | No | EVA | |
| rs3389390502 | 672 | N>K | No | EVA | |
| rs3389400258 | 712 | E>K | No | EVA | |
| rs3389386623 | 722 | D>N | No | EVA | |
| rs3389368719 | 731 | V>I | No | EVA | |
| rs3389383583 | 743 | N>K | No | EVA | |
| rs3389383578 | 744 | R>G | No | EVA |
No associated diseases with Q9ERG0
Functions
9 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. |
| brush border | The dense covering of microvilli on the apical surface of an epithelial cell in tissues such as the intestine, kidney, and choroid plexus; the microvilli aid absorption by increasing the surface area of the cell. |
| brush border membrane | The portion of the plasma membrane surrounding the brush border. |
| cleavage furrow | The cleavage furrow is a plasma membrane invagination at the cell division site. The cleavage furrow begins as a shallow groove and eventually deepens to divide the cytoplasm. |
| 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). |
| 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. |
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. |
| actin monomer binding | Binding to monomeric actin, also known as G-actin. |
| metal ion binding | Binding to a metal ion. |
7 GO annotations of biological process
| Name | Definition |
|---|---|
| actin filament bundle assembly | The assembly of actin filament bundles; actin filaments are on the same axis but may be oriented with the same or opposite polarities and may be packed with different levels of tightness. |
| 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. |
| cholesterol homeostasis | Any process involved in the maintenance of an internal steady state of cholesterol within an organism or cell. |
| cholesterol metabolic process | The chemical reactions and pathways involving cholesterol, cholest-5-en-3 beta-ol, the principal sterol of vertebrates and the precursor of many steroids, including bile acids and steroid hormones. It is a component of the plasma membrane lipid bilayer and of plasma lipoproteins and can be found in all animal tissues. |
| intestinal cholesterol absorption | Uptake of cholesterol into the blood by absorption from the small intestine. |
| negative regulation of actin filament depolymerization | Any process that stops, prevents, or reduces the frequency, rate or extent of actin depolymerization. |
| ruffle organization | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a ruffle, a projection at the leading edge of a crawling cell. |
6 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| F1MH07 | MICAL1 | [F-actin]-monooxygenase MICAL1 | Bos taurus (Bovine) | SS |
| Q9BT23 | LIMD2 | LIM domain-containing protein 2 | Homo sapiens (Human) | PR |
| Q8TDZ2 | MICAL1 | [F-actin]-monooxygenase MICAL1 | Homo sapiens (Human) | EV |
| Q8VDP3 | Mical1 | [F-actin]-monooxygenase MICAL1 | Mus musculus (Mouse) | EV |
| Q8BGB5 | Limd2 | LIM domain-containing protein 2 | Mus musculus (Mouse) | PR |
| D3ZBP4 | Mical1 | [F-actin]-monooxygenase MICAL1 | Rattus norvegicus (Rat) | SS |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MESTPFNRRQ | WTSLSLRVTA | KELSLVNKNK | SSAIVEIFSK | YQKAAEEANM | ERKKNNPESL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| PQHFRRGTLS | VLKKKWENPV | AGAEFHTDSL | PNSSSEGGHT | ADYPPAEVTD | KPAPGVRADR |
| 130 | 140 | 150 | 160 | 170 | 180 |
| EEHTQPKPRF | GSRPEAVIQS | RYPRSENSHD | FKAQATESQK | MENCLGDSRH | EAEKPETSEN |
| 190 | 200 | 210 | 220 | 230 | 240 |
| TETSGKIEKY | NVPLNRLKMM | FEKGEHNQTK | SLWTQSRNAG | GRRLSENNCS | LDDWEIGAGH |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LSSSAFNSEK | NESKRNLELP | RLSETSIKDR | MAKYQAAVSK | QSSPASYTNE | LKTSESKTHK |
| 310 | 320 | 330 | 340 | 350 | 360 |
| WEQKENVPPG | PEACSVHQEG | SKVSTTENSL | VALSVPAEDD | TCNSQVKSEA | QQPMHPKPLS |
| 370 | 380 | 390 | 400 | 410 | 420 |
| PDARTSSLPE | SSPSKTAKKF | QAPAKESCVE | CQKTVYPMER | LLANQQVFHI | SCFRCSYCNN |
| 430 | 440 | 450 | 460 | 470 | 480 |
| KLSLGTYASL | HGRIYCKPHF | NQLFKSKGNY | DEGFGHKQHK | DLWASKSDNE | ETLGRPAQPP |
| 490 | 500 | 510 | 520 | 530 | 540 |
| NAGESPHSPG | VEDAPIAKVG | VLAASMEAKA | SSQREREDKP | AETKKLRIAW | PPPAELGGSG |
| 550 | 560 | 570 | 580 | 590 | 600 |
| SALEEGIKVS | KPKWPPEDDV | CKTEAPEDVD | LDLKKLRRSS | SLKERSRPFT | VAASFRTSSI |
| 610 | 620 | 630 | 640 | 650 | 660 |
| KSPKASSPSL | RKGWSESEQS | EEFGGGIATM | ERKQTENARP | SGEKENVGKS | RWQGEEVPRS |
| 670 | 680 | 690 | 700 | 710 | 720 |
| KDRSSFELES | ENFMENGANI | AEDDNHVHAQ | QSPLEPEAPG | WSGFVDTTAA | KEFTTQNQKS |
| 730 | 740 | 750 | |||
| QDVGFWEGEV | VRELSVEEQI | KRNRYYDEDE | DEE |