Q1KL86

PR
Gene name
EPHA2
Protein name
Ephrin type-A receptor 2
Names
Species
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
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)

254-344 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q1KL86

Entry ID Method Resolution Chain Position Source
AF-Q1KL86-F1 Predicted AlphaFoldDB

No variants for Q1KL86

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q1KL86

No associated diseases with Q1KL86

13 regional properties for Q1KL86

Type Name Position InterPro Accession
domain Protein kinase domain 613 - 875 IPR000719
domain Ephrin receptor ligand binding domain 28 - 206 IPR001090
domain Serine-threonine/tyrosine-protein kinase, catalytic domain 614 - 871 IPR001245
conserved_site Tyrosine-protein kinase, receptor class V, conserved site 182 - 202 IPR001426-1
conserved_site Tyrosine-protein kinase, receptor class V, conserved site 247 - 267 IPR001426-2
domain Sterile alpha motif domain 901 - 968 IPR001660
domain Fibronectin type III 328 - 432 IPR003961-1
domain Fibronectin type III 436 - 529 IPR003961-2
active_site Tyrosine-protein kinase, active site 735 - 747 IPR008266
binding_site Protein kinase, ATP binding site 619 - 646 IPR017441
domain Tyrosine-protein kinase, catalytic domain 613 - 871 IPR020635
domain Ephrin receptor, transmembrane domain 538 - 610 IPR027936
domain Ephrin type-A receptor 2, ligand binding domain 28 - 201 IPR034263

Functions

Description
EC Number 2.7.10.1 Protein-tyrosine kinases
Subcellular Localization
  • Cell membrane ; Single-pass type I membrane protein
  • Cell projection, ruffle membrane ; Single-pass type I membrane protein
  • Cell projection, lamellipodium membrane ; Single-pass type I membrane protein
  • Cell junction, focal adhesion
  • Present at regions of cell-cell contacts but also at the leading edge of migrating cells
  • Relocates from the plasma membrane to the cytoplasmic and perinuclear regions in cancer cells
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

6 GO annotations of cellular component

Name Definition
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).
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.
lamellipodium A thin sheetlike process extended by the leading edge of a migrating cell or extending cell process; contains a dense meshwork of actin filaments.
lamellipodium membrane The portion of the plasma membrane surrounding a lamellipodium.
leading edge membrane The portion of the plasma membrane surrounding the leading edge of a motile cell.
ruffle membrane The portion of the plasma membrane surrounding a ruffle.

3 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ephrin receptor activity Combining with an ephrin receptor ligand to initiate a change in cell activity.
transmembrane receptor protein tyrosine kinase activity Combining with a signal and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity by catalysis of the reaction: ATP + a protein-L-tyrosine = ADP + a protein-L-tyrosine phosphate.

22 GO annotations of biological process

Name Definition
activation of GTPase activity Any process that initiates the activity of an inactive GTPase through the replacement of GDP by GTP.
angiogenesis Blood vessel formation when new vessels emerge from the proliferation of pre-existing blood vessels.
apoptotic process A programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died.
bone remodeling The continuous turnover of bone matrix and mineral that involves first, an increase in resorption (osteoclastic activity) and later, reactive bone formation (osteoblastic activity). The process of bone remodeling takes place in the adult skeleton at discrete foci. The process ensures the mechanical integrity of the skeleton throughout life and plays an important role in calcium homeostasis. An imbalance in the regulation of bone resorption and bone formation results in many of the metabolic bone diseases, such as osteoporosis.
branching involved in mammary gland duct morphogenesis The process in which the branching structure of the mammary gland duct is generated and organized. The mammary gland is a large compound sebaceous gland that in female mammals is modified to secrete milk.
cAMP metabolic process The chemical reactions and pathways involving the nucleotide cAMP (cyclic AMP, adenosine 3',5'-cyclophosphate).
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 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 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.
cell motility Any process involved in the controlled self-propelled movement of a cell that results in translocation of the cell from one place to another.
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.
lens fiber cell morphogenesis The process in which the structures of a lens fiber cell are generated and organized. This process occurs while the initially relatively unspecialized cell is acquiring the specialized features of a lens fiber cell. A lens fiber cell is any of the elongated, tightly packed cells that make up the bulk of the mature lens in a camera-type eye.
mammary gland epithelial cell proliferation The multiplication or reproduction of mammary gland epithelial cells, resulting in the expansion of a cell population. Mammary gland epithelial cells make up the covering of surfaces of the mammary gland. The mammary gland is a large compound sebaceous gland that in female mammals is modified to secrete milk.
negative regulation of protein kinase B signaling Any process that stops, prevents, or reduces the frequency, rate or extent of protein kinase B signaling, a series of reactions mediated by the intracellular serine/threonine kinase protein kinase B.
osteoblast differentiation The process whereby a relatively unspecialized cell acquires the specialized features of an osteoblast, a mesodermal or neural crest cell that gives rise to bone.
osteoclast differentiation The process in which a relatively unspecialized monocyte acquires the specialized features of an osteoclast. An osteoclast is a specialized phagocytic cell associated with the absorption and removal of the mineralized matrix of bone tissue.
positive regulation of protein localization to plasma membrane Any process that activates or increases the frequency, rate or extent of protein localization to plasma membrane.
protein kinase B signaling A series of reactions, mediated by the intracellular serine/threonine kinase protein kinase B (also called AKT), which occurs as a result of a single trigger reaction or compound.
regulation of angiogenesis Any process that modulates the frequency, rate or extent of angiogenesis.
regulation of cell adhesion mediated by integrin Any process that modulates the frequency, rate, or extent of cell adhesion mediated by integrin.
regulation of lamellipodium assembly Any process that modulates the rate, frequency or extent of the formation of a lamellipodium, a thin sheetlike extension of the surface of a migrating cell.
response to growth factor Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a growth factor stimulus.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MELWAARACF VLLWGCALAP ATAAQGKEVV LLDFAAAGGE LGWLTHPYGK GWDLMQNIMN
70 80 90 100 110 120
DMPIYMYSVC NVMSGDQDNW LRTNWVYRGE AERIFIELKF TVRDCNSFPG GASSCKETFN
130 140 150 160 170 180
LYYAESDLDY GTNFQKRLFT KIDTIAPDEI TVSSDFEARH VKLNVEERSV GPLTRKGFYL
190 200 210 220 230 240
AFQDIGACVA LLSVRVYYKK CPELLQSLAR FPETIAGSDA PSLATVAGTC VDHAVVPPGG
250 260 270 280 290 300
EEPRMHCAVD GEWLVPIGQC LCQAGYEKVE DACQACSPGF FKFEVSESPC LECPEHTLPS
310 320 330 340 350 360
PEGATSCECE EGFFRAPQDP MSMPCTRPPS APHYLTAVGM GAKVELRWTP PQDSGGREDI
370 380 390 400 410 420
VYSVTCEQCW PESGECGPCE SSVRYSEPPH GLTRTSVTVS DLEPHMNYTF TVEARNGVSG
430 440 450 460 470 480
LVTSRSFRTA SVSINQTEPP KVRLEGRSTT SLSVSWSIPP PQQSRVWKYE VTYRKKGDSN
490 500 510 520 530 540
SYNVRRTEGF SVTLDDLAPD TTYLVQVQAL TQEGQGAGSK VHEFQTLSPE GSGSLAVIGG
550 560 570 580 590 600
VAVCVVLLLL LAGAGFFIHR RRKNLRARQS PEDVYFSKSE QLKPLKTYVD PHTYEDPNQA
610 620 630 640 650 660
VLKFTTEIHP SCVTRQKVIG AGEFGEVYKG TLKTSSGKKE VPVAIKTLKA GYTEKQRVDF
670 680 690 700 710 720
LGEAGIMGQF SHHNIIRLEG VISKYKPMMI ITEFMENGAL DKFLREKDGE FSVLQLVGML
730 740 750 760 770 780
RGIAAGMKYL ANMNYVHRDL AARNILVNSN LVCKVSDFGL SRVLEDDPEA TYTTSGGKIP
790 800 810 820 830 840
IRWTAPEAIS YRKFTSASDV WSFGIVMWEV MTYGERPYWE LSNHEVMKAI NDGFRLPTPM
850 860 870 880 890 900
DCPSAIYQLM MQCWQQERAR RPKFADIVSI LDKLIRAPDS LKTLADFDPR VSIRLPSTSG
910 920 930 940 950 960
SEGVPFRTVS EWLESIKMQQ YTEHFMAAGY TAIEKVVQMT NDDIKRIGVR LPGHQKRIAY
970
SLLGLKDQVN TVGIPI