P06332
Gene name |
Cd4 |
Protein name |
T-cell surface glycoprotein CD4 |
Names |
|
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:12504 |
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 P06332
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P06332-F1 | Predicted | AlphaFoldDB |
34 variants for P06332
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs46280311 | 4 | A>G | No | EVA | |
| rs3388844775 | 15 | L>P | No | EVA | |
| rs3388862004 | 48 | K>Q | No | EVA | |
| rs3388860907 | 52 | F>L | No | EVA | |
| rs3388855228 | 122 | E>Q | No | EVA | |
| rs258799216 | 157 | T>I | No | EVA | |
| rs3388850415 | 161 | H>Y | No | EVA | |
| rs241199810 | 163 | K>R | No | EVA | |
| rs216696357 | 165 | K>R | No | EVA | |
| rs3397335066 | 185 | F>S | No | EVA | |
| rs51521529 | 196 | K>R | No | EVA | |
| rs217236309 | 237 | W>R | No | EVA | |
| rs47132330 | 252 | P>S | No | EVA | |
| rs3388858238 | 271 | D>E | No | EVA | |
| rs3388863602 | 279 | T>M | No | EVA | |
| rs3388858331 | 291 | L>R | No | EVA | |
| rs3388850476 | 293 | F>L | No | EVA | |
| rs3388850456 | 296 | S>Y | No | EVA | |
| rs3388858309 | 325 | T>I | No | EVA | |
| rs3388860946 | 330 | V>M | No | EVA | |
| rs3388858273 | 332 | G>E | No | EVA | |
| rs229227834 | 338 | M>T | No | EVA | |
| rs50728834 | 341 | T>S | No | EVA | |
| rs3388850430 | 351 | V>D | No | EVA | |
| rs237953978 | 357 | V>L | No | EVA | |
| rs262666607 | 365 | T>I | No | EVA | |
| rs247476370 | 376 | D>E | No | EVA | |
| rs3388823659 | 377 | K>N | No | EVA | |
| rs3388854368 | 395 | V>M | No | EVA | |
| rs248119676 | 399 | C>G | No | EVA | |
| rs3388855194 | 402 | G>D | No | EVA | |
| rs3388841897 | 404 | S>T | No | EVA | |
| rs3388860897 | 456 | L>I | No | EVA | |
| rs3388854316 | 458 | I>L | No | EVA |
No associated diseases with P06332
10 regional properties for P06332
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Immunoglobulin subtype | 27 - 126 | IPR003599-1 |
| domain | Immunoglobulin subtype | 131 - 206 | IPR003599-2 |
| domain | Immunoglobulin subtype | 212 - 317 | IPR003599-3 |
| domain | Immunoglobulin-like domain | 34 - 122 | IPR007110 |
| domain | Immunoglobulin C2-set | 128 - 206 | IPR008424-1 |
| domain | Immunoglobulin C2-set | 317 - 387 | IPR008424-2 |
| domain | Immunoglobulin V-set domain | 37 - 114 | IPR013106 |
| domain | Immunoglobulin | 26 - 126 | IPR013151 |
| domain | CD4, extracellular | 212 - 316 | IPR015274 |
| domain | T cell CD4 receptor C-terminal region | 427 - 452 | IPR021963 |
7 GO annotations of cellular component
| Name | Definition |
|---|---|
| cell surface | The external part of the cell wall and/or plasma membrane. |
| endoplasmic reticulum lumen | The volume enclosed by the membranes of the endoplasmic reticulum. |
| endoplasmic reticulum membrane | The lipid bilayer surrounding the endoplasmic reticulum. |
| external side of plasma membrane | The leaflet of the plasma membrane that faces away from the cytoplasm and any proteins embedded or anchored in it or attached to its surface. |
| integral component of plasma membrane | The component of the plasma membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
| membrane raft | Any of the small (10-200 nm), heterogeneous, highly dynamic, sterol- and sphingolipid-enriched membrane domains that compartmentalize cellular processes. Small rafts can sometimes be stabilized to form larger platforms through protein-protein and protein-lipid interactions. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
13 GO annotations of molecular function
| Name | Definition |
|---|---|
| coreceptor activity | Combining with an extracellular or intracellular messenger, and in cooperation with a nearby primary receptor, initiating a change in cell activity. |
| enzyme binding | Binding to an enzyme, a protein with catalytic activity. |
| identical protein binding | Binding to an identical protein or proteins. |
| immunoglobulin binding | Binding to an immunoglobulin. |
| interleukin-16 binding | Binding to interleukin-16. |
| interleukin-16 receptor activity | Combining with interleukin-16 and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity. |
| MHC class II protein binding | Binding to a major histocompatibility complex class II molecule; a set of molecules displayed on cell surfaces that are responsible for lymphocyte recognition and antigen presentation. |
| MHC class II protein complex binding | Binding to a class II major histocompatibility complex. |
| protein homodimerization activity | Binding to an identical protein to form a homodimer. |
| protein kinase binding | Binding to a protein kinase, any enzyme that catalyzes the transfer of a phosphate group, usually from ATP, to a protein substrate. |
| protein tyrosine kinase binding | Binding to protein tyrosine kinase. |
| 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. |
| zinc ion binding | Binding to a zinc ion (Zn). |
30 GO annotations of biological process
| Name | Definition |
|---|---|
| adaptive immune response | An immune response mediated by cells expressing specific receptors for antigen produced through a somatic diversification process, and allowing for an enhanced secondary response to subsequent exposures to the same antigen (immunological memory). |
| calcium-mediated signaling | Any intracellular signal transduction in which the signal is passed on within the cell via calcium ions. |
| cell adhesion | The attachment of a cell, either to another cell or to an underlying substrate such as the extracellular matrix, via cell adhesion molecules. |
| cell surface receptor signaling pathway | The series of molecular signals initiated by activation of a receptor on the surface of a cell. The pathway begins with binding of an extracellular ligand to a cell surface receptor, or for receptors that signal in the absence of a ligand, by ligand-withdrawal or the activity of a constitutively active receptor. The pathway ends with regulation of a downstream cellular process, e.g. transcription. |
| cellular response to granulocyte macrophage colony-stimulating factor stimulus | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a granulocyte macrophage colony-stimulating factor stimulus. |
| defense response to Gram-negative bacterium | Reactions triggered in response to the presence of a Gram-negative bacterium that act to protect the cell or organism. |
| helper T cell enhancement of adaptive immune response | Positive regulation of an adaptive immune response mediated via cytokine production by helper T cell. |
| interleukin-15-mediated signaling pathway | The series of molecular signals initiated by interleukin-15 binding to its receptor on the surface of a target cell, and ending with the regulation of a downstream cellular process, e.g. transcription. |
| macrophage differentiation | The process in which a relatively unspecialized monocyte acquires the specialized features of a macrophage. |
| maintenance of protein location in cell | Any process in which a protein is maintained in a specific location within, or in the membrane of, a cell, and is prevented from moving elsewhere. |
| peptidyl-tyrosine phosphorylation | The phosphorylation of peptidyl-tyrosine to form peptidyl-O4'-phospho-L-tyrosine. |
| positive regulation of calcium ion transport into cytosol | Any process that increases the rate of the directed movement of calcium ions into the cytosol of a cell. The cytosol is that part of the cytoplasm that does not contain membranous or particulate subcellular components. |
| positive regulation of calcium-mediated signaling | Any process that activates or increases the frequency, rate or extent of calcium-mediated signaling. |
| positive regulation of DNA-templated transcription | Any process that activates or increases the frequency, rate or extent of cellular DNA-templated transcription. |
| positive regulation of ERK1 and ERK2 cascade | Any process that activates or increases the frequency, rate or extent of signal transduction mediated by the ERK1 and ERK2 cascade. |
| positive regulation of I-kappaB kinase/NF-kappaB signaling | Any process that activates or increases the frequency, rate or extent of I-kappaB kinase/NF-kappaB signaling. |
| positive regulation of kinase activity | Any process that activates or increases the frequency, rate or extent of kinase activity, the catalysis of the transfer of a phosphate group, usually from ATP, to a substrate molecule. |
| positive regulation of MAPK cascade | Any process that activates or increases the frequency, rate or extent of signal transduction mediated by the MAPK cascade. |
| positive regulation of monocyte differentiation | Any process that activates or increases the frequency, rate or extent of monocyte differentiation. |
| positive regulation of peptidyl-tyrosine phosphorylation | Any process that activates or increases the frequency, rate or extent of the phosphorylation of peptidyl-tyrosine. |
| positive regulation of protein kinase activity | Any process that activates or increases the frequency, rate or extent of protein kinase activity. |
| positive regulation of protein phosphorylation | Any process that activates or increases the frequency, rate or extent of addition of phosphate groups to amino acids within a protein. |
| positive regulation of T cell activation | Any process that activates or increases the frequency, rate or extent of T cell activation. |
| positive regulation of T cell proliferation | Any process that activates or increases the rate or extent of T cell proliferation. |
| positive regulation of viral entry into host cell | Any process that activates or increases the frequency, rate or extent of the introduction of viral entry into the host cell. |
| regulation of calcium ion transport | Any process that modulates the frequency, rate or extent of the directed movement of calcium ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. |
| regulation of T cell activation | Any process that modulates the frequency, rate or extent of T cell activation. |
| T cell activation | The change in morphology and behavior of a mature or immature T cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific. |
| T cell differentiation | The process in which a precursor cell type acquires characteristics of a more mature T-cell. A T cell is a type of lymphocyte whose definin characteristic is the expression of a T cell receptor complex. |
| T cell selection | The process in which T cells that express T cell receptors that are restricted by self MHC protein complexes and tolerant to self antigens are selected for further maturation. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MCRAISLRRL | LLLLLQLSQL | LAVTQGKTLV | LGKEGESAEL | PCESSQKKIT | VFTWKFSDQR |
| 70 | 80 | 90 | 100 | 110 | 120 |
| KILGQHGKGV | LIRGGSPSQF | DRFDSKKGAW | EKGSFPLIIN | KLKMEDSQTY | ICELENRKEE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VELWVFKVTF | SPGTSLLQGQ | SLTLTLDSNS | KVSNPLTECK | HKKGKVVSGS | KVLSMSNLRV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| QDSDFWNCTV | TLDQKKNWFG | MTLSVLGFQS | TAITAYKSEG | ESAEFSFPLN | FAEENGWGEL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| MWKAEKDSFF | QPWISFSIKN | KEVSVQKSTK | DLKLQLKETL | PLTLKIPQVS | LQFAGSGNLT |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LTLDKGTLHQ | EVNLVVMKVA | QLNNTLTCEV | MGPTSPKMRL | TLKQENQEAR | VSEEQKVVQV |
| 370 | 380 | 390 | 400 | 410 | 420 |
| VAPETGLWQC | LLSEGDKVKM | DSRIQVLSRG | VNQTVFLACV | LGGSFGFLGF | LGLCILCCVR |
| 430 | 440 | 450 | |||
| CRHQQRQAAR | MSQIKRLLSE | KKTCQCPHRM | QKSHNLI |