Q9Z2H5
PR
Gene name |
Epb41l1 |
Protein name |
Band 4.1-like protein 1 |
Names |
Erythrocyte membrane protein band 4.1-like 1, Neuronal protein 4.1, 4.1N |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:13821 |
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 Q9Z2H5
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9Z2H5-F1 | Predicted | AlphaFoldDB |
No variants for Q9Z2H5
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q9Z2H5 | |||||
No associated diseases with Q9Z2H5
10 regional properties for Q9Z2H5
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | FERM domain | 97 - 378 | IPR000299 |
| domain | SAB domain | 493 - 544 | IPR007477 |
| domain | Band 4.1, C-terminal | 786 - 865 | IPR008379 |
| domain | FERM adjacent | 384 - 430 | IPR014847 |
| domain | FERM, N-terminal | 101 - 163 | IPR018979 |
| domain | FERM, C-terminal PH-like domain | 292 - 382 | IPR018980 |
| conserved_site | FERM conserved site | 151 - 179 | IPR019747-1 |
| conserved_site | FERM conserved site | 258 - 287 | IPR019747-2 |
| domain | FERM central domain | 181 - 288 | IPR019748 |
| domain | Band 4.1 domain | 93 - 288 | IPR019749 |
6 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. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
| postsynaptic density | An electron dense network of proteins within and adjacent to the postsynaptic membrane of an asymmetric, neuron-neuron synapse. Its major components include neurotransmitter receptors and the proteins that spatially and functionally organize them such as anchoring and scaffolding molecules, signaling enzymes and cytoskeletal components. |
| protein-containing complex | A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together. |
| synaptic membrane | A specialized area of membrane on either the presynaptic or the postsynaptic side of a synapse, the junction between a nerve fiber of one neuron and another neuron or muscle fiber or glial cell. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| actin binding | Binding to monomeric or multimeric forms of actin, including actin filaments. |
| signaling receptor binding | Binding to one or more specific sites on a receptor molecule, a macromolecule that undergoes combination with a hormone, neurotransmitter, drug or intracellular messenger to initiate a change in cell function. |
| 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. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| 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. |
| 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. |
13 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q9N179 | EPB41 | Protein 4.1 | Bos taurus (Bovine) | PR |
| O43491 | EPB41L2 | Band 4.1-like protein 2 | Homo sapiens (Human) | PR |
| Q9Y2J2 | EPB41L3 | Band 4.1-like protein 3 | Homo sapiens (Human) | PR |
| P11171 | EPB41 | Protein 4.1 | Homo sapiens (Human) | PR |
| Q9H4G0 | EPB41L1 | Band 4.1-like protein 1 | Homo sapiens (Human) | PR |
| Q8BGS1 | Epb41l5 | Band 4.1-like protein 5 | Mus musculus (Mouse) | PR |
| P52963 | Epb41l4a | Band 4.1-like protein 4A | 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 |
| O70318 | Epb41l2 | Band 4.1-like protein 2 | 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 |
| MTTETGPDSE | VKKAQEETPQ | QPEAAAAVTT | PVTPAGHSHP | ETNSNEKHLT | QQDTRPAEQS |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LDMDDKDYSE | ADGLSERTTP | SKAQKSPQKI | AKKFKSAICR | VTLLDASEYE | CEVEKHGRGQ |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VLFDLVCEHL | NLLEKDYFGL | TFCDADSQKN | WLDPSKEIKK | QIRSSPWNFA | FTVKFYPPDP |
| 190 | 200 | 210 | 220 | 230 | 240 |
| AQLTEDITRY | YLCLQLRADI | ITGRLPCSFV | THALLGSYAV | QAELGDYDAE | EHVGNYVSEL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| RFAPNQTREL | EERIMELHKT | YRGMTPGEAE | IHFLENAKKL | SMYGVDLHHA | KDSEGIDIML |
| 310 | 320 | 330 | 340 | 350 | 360 |
| GVCANGLLIY | RDRLRINRFA | WPKILKISYK | RSNFYIKIRP | GEYEQFESTI | GFKLPNHRSA |
| 370 | 380 | 390 | 400 | 410 | 420 |
| KRLWKVCIEH | HTFFRLVSPE | PPPKGFLVMG | SKFRYSGRTQ | AQTRQASALI | DRPAPFFERS |
| 430 | 440 | 450 | 460 | 470 | 480 |
| SSKRYTMSRS | LDGAEFSRPA | SVSENHDAGP | EGDKREDDAE | SGGRRSEAEE | GEVRTPTKIK |
| 490 | 500 | 510 | 520 | 530 | 540 |
| ELKPEQETTP | RHKQEFLDKP | EDVLLKHQAS | INELKRTLKE | PNSKLIHRDR | DWDRERRLPS |
| 550 | 560 | 570 | 580 | 590 | 600 |
| SPASPSPKGT | PEKASERAGL | REGSEEKVKP | PRPRAPESDM | GDEDQDQERD | AVFLKDNHLA |
| 610 | 620 | 630 | 640 | 650 | 660 |
| IERKCSSITV | SSTSSLEAEV | DFTVIGDYHG | GAFEDFSRSL | PELDRDKSDS | ETEGLVFAQD |
| 670 | 680 | 690 | 700 | 710 | 720 |
| LKGPSSQEDE | SGGLEDSPDR | GACSTPEMPQ | FESVKAETMT | VSSLAIRKKI | EPEAMLQSRV |
| 730 | 740 | 750 | 760 | 770 | 780 |
| SAADSTQVDG | GTPMVKDFMT | TPPCITTETI | STTMENSLKS | GKGAAAMIPG | PQTVATEIRS |
| 790 | 800 | 810 | 820 | 830 | 840 |
| LSPIIGKDVL | TSTYGATAET | LSTSTTTHVT | KTVKGGFSET | RIEKRIIITG | DEDVDQDQAL |
| 850 | 860 | 870 | |||
| ALAIKEAKLQ | HPDMLVTKAV | VYRETDPSPE | ERDKKPQES |