O70318
PR
Gene name |
Epb41l2 |
Protein name |
Band 4.1-like protein 2 |
Names |
Erythrocyte membrane protein band 4.1-like 2, Generally expressed protein 4.1, 4.1G |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:13822 |
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 O70318
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-O70318-F1 | Predicted | AlphaFoldDB |
49 variants for O70318
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3389086421 | 3 | T>I | No | EVA | |
| rs218977640 | 23 | S>P | No | EVA | |
| rs3389090134 | 27 | A>D | No | EVA | |
| rs3389086426 | 55 | Q>L | No | EVA | |
| rs3389093315 | 116 | S>F | No | EVA | |
| rs3389086501 | 121 | E>* | No | EVA | |
| rs3389080484 | 138 | E>D | No | EVA | |
| rs265719561 | 154 | V>A | No | EVA | |
| rs253868968 | 154 | V>L | No | EVA | |
| rs224260670 | 165 | D>N | No | EVA | |
| rs49809459 | 169 | T>M | No | EVA | |
| rs3389037199 | 171 | Q>* | No | EVA | |
| rs3389103047 | 178 | L>M | No | EVA | |
| rs3389095788 | 185 | R>K | No | EVA | |
| rs3389067582 | 207 | K>N | No | EVA | |
| rs3389067592 | 215 | V>L | No | EVA | |
| rs3389093071 | 223 | Y>H | No | EVA | |
| rs3389060658 | 224 | S>N | No | EVA | |
| rs1133889233 | 241 | C>G | No | EVA | |
| rs1132332524 | 244 | L>V | No | EVA | |
| rs3389097690 | 276 | L>P | No | EVA | |
| rs3389072148 | 277 | K>Q | No | EVA | |
| rs3389037166 | 323 | F>L | No | EVA | |
| rs3389103059 | 325 | T>S | No | EVA | |
| rs3389093362 | 351 | L>F | No | EVA | |
| rs3389093097 | 358 | P>Q | No | EVA | |
| rs3389104657 | 359 | A>P | No | EVA | |
| rs3389104668 | 361 | T>I | No | EVA | |
| rs3389067602 | 379 | S>T | No | EVA | |
| rs3389103036 | 408 | E>K | No | EVA | |
| rs3389080426 | 418 | A>V | No | EVA | |
| rs3389090152 | 443 | Y>F | No | EVA | |
| rs3389037140 | 461 | E>D | No | EVA | |
| rs3400981412 | 510 | Y>C | No | EVA | |
| rs216407094 | 596 | N>Y | No | EVA | |
| rs3389072169 | 606 | Y>N | No | EVA | |
| rs3389067593 | 611 | N>K | No | EVA | |
| rs3389103110 | 619 | K>N | No | EVA | |
| rs3389093381 | 623 | A>S | No | EVA | |
| rs48852134 | 629 | A>S | No | EVA | |
| rs29380930 | 640 | A>T | No | EVA | |
| rs3389067614 | 686 | S>R | No | EVA | |
| rs3389093375 | 707 | R>H | No | EVA | |
| rs3389093382 | 714 | H>R | No | EVA | |
| rs3412800557 | 751 | E>G | No | EVA | |
| rs47078429 | 767 | G>A | No | EVA | |
| rs217020397 | 781 | V>I | No | EVA | |
| rs3389103078 | 894 | I>T | No | EVA | |
| rs3389060634 | 976 | V>L | No | EVA |
No associated diseases with O70318
8 regional properties for O70318
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | FERM domain | 43 - 327 | IPR000299 |
| domain | FERM adjacent | 336 - 380 | IPR014847 |
| domain | FERM, N-terminal | 47 - 109 | IPR018979 |
| domain | FERM, C-terminal PH-like domain | 239 - 331 | IPR018980 |
| conserved_site | FERM conserved site | 97 - 126 | IPR019747-1 |
| conserved_site | FERM conserved site | 205 - 234 | IPR019747-2 |
| domain | FERM central domain | 127 - 235 | IPR019748 |
| domain | Band 4.1 domain | 39 - 235 | IPR019749 |
7 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. |
| cell cortex | The region of a cell that lies just beneath the plasma membrane and often, but not always, contains a network of actin filaments and associated proteins. |
| cell junction | A cellular component that forms a specialized region of connection between two or more cells, or between a cell and the extracellular matrix, or between two membrane-bound components of a cell, such as flagella. |
| COP9 signalosome | A protein complex that catalyzes the deneddylation of proteins, including the cullin component of SCF ubiquitin E3 ligase; deneddylation increases the activity of cullin family ubiquitin ligases. The signalosome is involved in many regulatory process, including some which control development, in many species; also regulates photomorphogenesis in plants; in many species its subunits are highly similar to those of the proteasome. |
| 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. |
| nucleoplasm | That part of the nuclear content other than the chromosomes or the nucleolus. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| actin binding | Binding to monomeric or multimeric forms of actin, including actin filaments. |
| PH domain binding | Binding to a PH domain (pleckstrin homology) of a protein, a domain of about 100 residues that occurs in a wide range of proteins involved in intracellular signaling or as constituents of the cytoskeleton. |
| spectrin binding | Binding to spectrin, a protein that is the major constituent of the erythrocyte cytoskeletal network. It associates with band 4.1 (see band protein) and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane. It is composed of nonhomologous chains, alpha and beta, which aggregate side-to-side in an antiparallel fashion to form dimers, tetramers, and higher polymers. |
| structural molecule activity | The action of a molecule that contributes to the structural integrity of a complex or its assembly within or outside a cell. |
7 GO annotations of biological process
| Name | Definition |
|---|---|
| actin 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 comprising actin filaments and their associated proteins. |
| actomyosin structure 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 containing both actin and myosin or paramyosin. The myosin may be organized into filaments. |
| cell cycle | The progression of biochemical and morphological phases and events that occur in a cell during successive cell replication or nuclear replication events. Canonically, the cell cycle comprises the replication and segregation of genetic material followed by the division of the cell, but in endocycles or syncytial cells nuclear replication or nuclear division may not be followed by cell division. |
| cell division | The process resulting in division and partitioning of components of a cell to form more cells; may or may not be accompanied by the physical separation of a cell into distinct, individually membrane-bounded daughter cells. |
| cortical actin cytoskeleton organization | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of actin-based cytoskeletal structures in the cell cortex, i.e. just beneath the plasma membrane. |
| positive regulation of protein localization to cell cortex | Any process that activates or increases the frequency, rate or extent of protein localization to cell cortex. |
| regulation of cell shape | Any process that modulates the surface configuration of a cell. |
13 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q9N179 | EPB41 | Protein 4.1 | Bos taurus (Bovine) | PR |
| P11171 | EPB41 | Protein 4.1 | Homo sapiens (Human) | PR |
| Q9H4G0 | EPB41L1 | Band 4.1-like protein 1 | Homo sapiens (Human) | PR |
| Q9Y2J2 | EPB41L3 | Band 4.1-like protein 3 | Homo sapiens (Human) | PR |
| O43491 | EPB41L2 | Band 4.1-like protein 2 | Homo sapiens (Human) | PR |
| P52963 | Epb41l4a | Band 4.1-like protein 4A | Mus musculus (Mouse) | PR |
| Q8BGS1 | Epb41l5 | Band 4.1-like protein 5 | Mus musculus (Mouse) | PR |
| Q6P5H6 | Frmd5 | FERM domain-containing protein 5 | Mus musculus (Mouse) | PR |
| Q8BHD4 | Frmd3 | FERM domain-containing protein 3 | Mus musculus (Mouse) | PR |
| Q9Z2H5 | Epb41l1 | Band 4.1-like protein 1 | Mus musculus (Mouse) | PR |
| P48193 | Epb41 | Protein 4.1 | Mus musculus (Mouse) | PR |
| Q9WV92 | Epb41l3 | Band 4.1-like protein 3 | Mus musculus (Mouse) | PR |
| Q9WTP0 | Epb41l1 | Band 4.1-like protein 1 | Rattus norvegicus (Rat) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTTEVGSASE | VKKGSDQAGA | DASKEKAKEV | ENEQTPVSEP | EEEKGSQPGP | PVERQSTPRL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| RKRGKDPSEN | RGISRFIPPW | LKKQRSYNLV | VAKDGGDKKE | PTQADVEDQI | LGKEESLPEE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| ESRAKGDAEE | MAQRKHLEVQ | VEVREAKPAL | KSSVETQPAE | EVRKDKEETI | QDTQEEKLEG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| GAAKRETKEV | QTSELKAEVA | SQKATKKTKT | VLAKVTLLDG | TEYSCDLEKR | AKGQVLFDRV |
| 250 | 260 | 270 | 280 | 290 | 300 |
| CEHLNLLEKD | YFGLLFQDHP | EQKNWLDPAK | EIKRQLKNLP | WLFTFNVKFY | PPDPSQLTED |
| 310 | 320 | 330 | 340 | 350 | 360 |
| ITRYFLCLQL | RQDIASGRLP | CSFVTHALLG | SYTLQAEHGD | YDPEEYDSID | LGDFQFAPAH |
| 370 | 380 | 390 | 400 | 410 | 420 |
| TKELEEKVSE | LHKTHRGLSP | AQADSQFLEN | AKRLSMYGVD | LHHAKDSEGV | DIKLGVCANG |
| 430 | 440 | 450 | 460 | 470 | 480 |
| LLIYKDRLRI | NRFAWPKILK | ISYKRSNFYI | KVRPAELEQF | ESTIGFKLPN | HRAAKRLWKV |
| 490 | 500 | 510 | 520 | 530 | 540 |
| CVEHHTFYRL | VSPEQPPKTK | FLTLGSKFRY | SGRTQAQTRE | ASTLIDRPAP | QFERASSKRV |
| 550 | 560 | 570 | 580 | 590 | 600 |
| SRSLDGAPIG | VVDQSPPGEG | SVPGPGVISY | TTIQDGRRDS | KSPTKATPLP | AEGKKNTLRV |
| 610 | 620 | 630 | 640 | 650 | 660 |
| DGDNIYVRHS | NLMLEDLDKA | QEAILKHQAS | ISELKRNFMA | STPEPRPSEW | EKRRVTPLPF |
| 670 | 680 | 690 | 700 | 710 | 720 |
| QPQASSHETL | NVVEEKKRAE | VGKDESVITE | EMNGKEMSPG | HGPGETRKVE | PVAHKDSTSL |
| 730 | 740 | 750 | 760 | 770 | 780 |
| SSESSSSSSE | SEEDVGEYQP | HHRVTEGTIR | EEQEECDEEL | EEEPGQGAKV | VEREAAVPDA |
| 790 | 800 | 810 | 820 | 830 | 840 |
| VPDRQAGASV | LPVETEAQEH | VVAQKLPGEK | GAHGGTAEQD | PREEAEEDPH | RVNGEVPHLD |
| 850 | 860 | 870 | 880 | 890 | 900 |
| LDGLPEIICC | SEPPVVKTEM | VTISDASQRT | EISTKEVPIV | QTETKTITYE | SPQIDGGAGG |
| 910 | 920 | 930 | 940 | 950 | 960 |
| DSGVLLTAQT | ITSESASTTT | TTHITKTVKG | GISETRIEKR | IVITGDAALD | HDQALAQAIR |
| 970 | 980 | ||||
| EAREQHPDMS | VTRVVVHKET | ELAEEGEE |