Q91736
Gene name |
ephb1-b (xelk) |
Protein name |
Ephrin type-B receptor 1-B |
Names |
Tyrosine-protein kinase receptor XELK |
Species |
Xenopus laevis (African clawed frog) |
KEGG Pathway |
|
EC number |
2.7.10.1: Protein-tyrosine kinases |
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
679-707 (Activation loop from InterPro)
Target domain |
537-800 (Protein kinase domain) |
Relief mechanism |
|
Assay |
|
Autoinhibited structure
Activated structure
1 structures for Q91736
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q91736-F1 | Predicted | AlphaFoldDB |
No variants for Q91736
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q91736 | |||||
No associated diseases with Q91736
12 regional properties for Q91736
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Protein kinase domain | 537 - 800 | IPR000719 |
| domain | Ephrin receptor ligand binding domain | 1 - 119 | IPR001090 |
| domain | Serine-threonine/tyrosine-protein kinase, catalytic domain | 538 - 796 | IPR001245 |
| conserved_site | Tyrosine-protein kinase, receptor class V, conserved site | 95 - 115 | IPR001426-1 |
| conserved_site | Tyrosine-protein kinase, receptor class V, conserved site | 158 - 178 | IPR001426-2 |
| domain | Sterile alpha motif domain | 826 - 893 | IPR001660 |
| domain | Fibronectin type III | 240 - 448 | IPR003961 |
| active_site | Tyrosine-protein kinase, active site | 658 - 670 | IPR008266 |
| binding_site | Protein kinase, ATP binding site | 543 - 569 | IPR017441 |
| domain | Tyrosine-protein kinase, catalytic domain | 537 - 796 | IPR020635 |
| domain | Ephrin receptor, transmembrane domain | 460 - 534 | IPR027936 |
| domain | EphB1, SAM domain | 826 - 893 | IPR042819 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.7.10.1 | Protein-tyrosine kinases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| dendrite | A neuron projection that has a short, tapering, morphology. Dendrites receive and integrate signals from other neurons or from sensory stimuli, and conduct nerve impulses towards the axon or the cell body. In most neurons, the impulse is conveyed from dendrites to axon via the cell body, but in some types of unipolar neuron, the impulse does not travel via the cell body. |
| early endosome membrane | The lipid bilayer surrounding an early endosome. |
| 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. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| transmembrane-ephrin receptor activity | Combining with a transmembrane ephrin to initiate a change in cell activity. |
11 GO annotations of biological process
| Name | Definition |
|---|---|
| axon guidance | The chemotaxis process that directs the migration of an axon growth cone to a specific target site in response to a combination of attractive and repulsive cues. |
| cell chemotaxis | The directed movement of a motile cell guided by a specific chemical concentration gradient. Movement may be towards a higher concentration (positive chemotaxis) or towards a lower concentration (negative chemotaxis). |
| cell-substrate adhesion | The attachment of a cell to the underlying substrate via adhesion molecules. |
| dendritic spine development | The process whose specific outcome is the progression of the dendritic spine over time, from its formation to the mature structure. A dendritic spine is a protrusion from a dendrite and a specialized subcellular compartment involved in synaptic transmission. |
| dendritic spine morphogenesis | The process in which the anatomical structures of a dendritic spine are generated and organized. A dendritic spine is a protrusion from a dendrite and a specialized subcellular compartment involved in synaptic transmission. |
| ephrin receptor signaling pathway | The series of molecular signals initiated by ephrin binding to its receptor, and ending with the regulation of a downstream cellular process, e.g. transcription. |
| establishment of cell polarity | The specification and formation of anisotropic intracellular organization or cell growth patterns. |
| positive regulation of synapse assembly | Any process that activates, maintains or increases the frequency, rate or extent of synapse assembly, the aggregation, arrangement and bonding together of a set of components to form a synapse. |
| protein autophosphorylation | The phosphorylation by a protein of one or more of its own amino acid residues (cis-autophosphorylation), or residues on an identical protein (trans-autophosphorylation). |
| regulation of ERK1 and ERK2 cascade | Any process that modulates the frequency, rate or extent of signal transduction mediated by the ERK1 and ERK2 cascade. |
| regulation of JNK cascade | Any process that modulates the frequency, rate or extent of signal transduction mediated by the JNK cascade. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| HRVYVEMRFT | VRDCSSLPNV | PGSCKETFNL | YYYETDSNID | NKISTFWNES | PYLKVDTIAA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| DESFSQVDFG | GRLMKVNTEV | RSFGPLTRSG | FYLAFQDYGA | CMSLLSVRVF | FKKCPSVVQN |
| 130 | 140 | 150 | 160 | 170 | 180 |
| FAVFPETMTG | AESTSLVIAR | GTCIPNAEEV | DVPIKLYCNG | DGEWMVPIGK | CTCKAGYEPE |
| 190 | 200 | 210 | 220 | 230 | 240 |
| NHVVCKACPA | AMFKANQGMG | ICAQCPANSR | STSEASPICI | CRNGYYRADF | DTPEAPCTSV |
| 250 | 260 | 270 | 280 | 290 | 300 |
| PSGPRNVISI | VNETAITLEW | HPPRETGGRD | DVNYNIICKK | CQSDRRGCSH | CDDNVDFVPR |
| 310 | 320 | 330 | 340 | 350 | 360 |
| QLGLTDTRVF | ISNLWVHTPY | TFEIQAVNGV | TNKSPFPPQH | VSVNITTNQA | APSSVPIMHQ |
| 370 | 380 | 390 | 400 | 410 | 420 |
| VKATMKSITL | SWPQPEQPNG | IILDYEIRYY | EKDHHEFNSS | LARSQTNTAS | IEGLRPGVVY |
| 430 | 440 | 450 | 460 | 470 | 480 |
| VVQVRARTVA | GYGKFSSKMC | FQTLTEEDYK | SELREQLPLI | AGSAAAGVVF | IVSLVAISIV |
| 490 | 500 | 510 | 520 | 530 | 540 |
| CSRKRTYSKE | AVYSDKLQHY | STGRGSPGMK | IYIDPFTYED | PNEAVREFAK | EIDVSFVKIE |
| 550 | 560 | 570 | 580 | 590 | 600 |
| EVIGAGEFGE | VYKGRLKLPS | KREISVAIKT | LKAGYSEKQR | RDFLSEASIM | GQFDHPNIIR |
| 610 | 620 | 630 | 640 | 650 | 660 |
| LEGVVTKSRP | VMIITEFMEN | GALDSFLRQN | DGQFTVIQLV | GMLRGIAAGM | KYLSEMNYVH |
| 670 | 680 | 690 | 700 | 710 | 720 |
| RDLAARNILV | NSNLVCKVSD | FGLSRYLQDD | TSDPTYTSSL | GGKIPVRWTA | PEAIRYRKFT |
| 730 | 740 | 750 | 760 | 770 | 780 |
| SASDVWSYGI | VMWEVMSYGE | RPYWDMSNQD | VINAIEQDYR | LPPPMDCPAA | LHQLMLDCWQ |
| 790 | 800 | 810 | 820 | 830 | 840 |
| KDRNSRPRFG | EIVNTLDKMI | RNPASLKTVA | TIPAVPSQPL | LDRSIPDISA | FTSVDDWLSA |
| 850 | 860 | 870 | 880 | 890 | 900 |
| IKMGQYRDNF | LSSGFTSLHV | VAQMTSEDLL | RIGITLAGHQ | KKILNSIQSM | RVQISQSPTS |
| IA |