Egfr
entrez
13649
canonical
uniprot
Q01279
canonical
ensembl
ENSMUSG00000020122
resolver
ensp
ENSMUSP00000020329
resolver
ensp
ENSMUSP00000099948
resolver
ensp
ENSMUSP00000289947
resolver
enst
ENSMUST00000020329
resolver
enst
ENSMUST00000102884
resolver
genesymbol
Egfr
resolver
uniprot
F6QWQ6
resolver
uniprot
Q3TQS6
resolver
uniprot
Q5SVE9
resolver
uniprot
Q9EP98
resolver
uniprot
Q9WVF5
resolver
uniprot_entry
EGFR_MOUSE
resolver
uniprot_entry
F6QWQ6_MOUSE
resolver
uniprot_entry
Q3TQS6_MOUSE
resolver
uniprot_entry
Q9EP98_MOUSE
resolver
uniprot_entry
Q9WVF5_MOUSE
resolver
uniprot_sec
Q5SVE9
resolver
activity_regulation
ACTIVITY REGULATION: Endocytosis and inhibition of the activated EGFR by phosphatases like PTPRJ and PTPRK constitute immediate regulatory mechanisms. Upon EGF-binding phosphorylates EPS15 that regulates EGFR endocytosis and activity. Moreover, inducible feedback inhibitors including LRIG1, SOCS4, SOCS5 and ERRFI1 constitute alternative regulatory mechanisms for the EGFR signaling. {ECO:0000269|PubMed:10953014}.
uniprot
proteins
amino_acid_sequence
MRPSGTARTTLLVLLTALCAAGGALEEKKVCQGTSNRLTQLGTFEDHFLSLQRMYNNCEVVLGNLEITYVQRNYDLSFLKTIQEVAGYVLIALNTVERIPLENLQIIRGNALYENTYALAILSNYGTNRTGLRELPMRNLQEILIGAVRFSNNPILCNMDTIQWRDIVQNVFMSNMSMDLQSHPSSCPKCDPSCPNGSCWGGGEENCQKLTKIICAQQCSHRCRGRSPSDCCHNQCAAGCTGPRESDCLVCQKFQDEATCKDTCPPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYVVTDHGSCVRACGPDYYEVEEDGIRKCKKCDGPCRKVCNGIGIGEFKDTLSINATNIKHFKYCTAISGDLHILPVAFKGDSFTRTPPLDPRELEILKTVKEITGFLLIQAWPDNWTDLHAFENLEIIRGRTKQHGQFSLAVVGLNITSLGLRSLKEISDGDVIISGNRNLCYANTINWKKLFGTPNQKTKIMNNRAEKDCKAVNHVCNPLCSSEGCWGPEPRDCVSCQNVSRGRECVEKCNILEGEPREFVENSECIQCHPECLPQAMNITCTGRGPDNCIQCAHYIDGPHCVKTCPAGIMGENNTLVWKYADANNVCHLCHANCTYGCAGPGLQGCEVWPSGPKIPSIATGIVGGLLFIVVVALGIGLFMRRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQAHLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPYGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASDISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFRELILEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMEDVVDADEYLIPQQGFFNSPSTSRTPLLSSLSATSNNSTVACINRNGSCRVKEDAFLQRYSSDPTGAVTEDNIDDAFLPVPEYVNQSVPKRPAGSVQNPVYHNQPLHPAPGRDLHYQNPHSNAVGNPEYLNTAQPTCLSSGFNSPALWIQKGSHQMSLDNPDYQQDFFPKETKPNGIFKGPTAENAEYLRVAPPSSEFIGA
uniprot
proteins
ec_number
2.7.10.1
uniprot
proteins
function
FUNCTION: Receptor tyrosine kinase binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses (PubMed:10953014, PubMed:8404850). Known ligands include EGF, TGFA/TGF-alpha, AREG, epigen/EPGN, BTC/betacellulin, epiregulin/EREG and HBEGF/heparin-binding EGF (By similarity). Ligand binding triggers receptor homo- and/or heterodimerization and autophosphorylation on key cytoplasmic residues (By similarity). The phosphorylated receptor recruits adapter proteins like GRB2 which in turn activates complex downstream signaling cascades (By similarity). Activates at least 4 major downstream signaling cascades including the RAS-RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC and STATs modules (By similarity). May also activate the NF-kappa-B signaling cascade (By similarity). Also directly phosphorylates other proteins like RGS16, activating its GTPase activity and probably coupling the EGF receptor signaling to the G protein-coupled receptor signaling (By similarity). Also phosphorylates MUC1 and increases its interaction with SRC and CTNNB1/beta-catenin (By similarity). Positively regulates cell migration via interaction with CCDC88A/GIV which retains EGFR at the cell membrane following ligand stimulation, promoting EGFR signaling which triggers cell migration (By similarity). Acts as a positive regulator of cGAS-STING signaling by mediating tyrosine phosphorylation of STING1, promoting production of type I interferon (IFN-alpha and IFN-beta), while inhibiting STING1 ability to regulate autophagy (By similarity). Plays a role in enhancing learning and memory performance (PubMed:20639532). Plays a role in mammalian pain signaling (long-lasting hypersensitivity) (PubMed:35131940). {ECO:0000250|UniProtKB:P00533, ECO:0000269|PubMed:10953014, ECO:0000269|PubMed:20639532, ECO:0000269|PubMed:35131940, ECO:0000269|PubMed:8404850}.
uniprot
proteins
mass_dalton
134853
uniprot
proteins
post_translational_modification
PTM: Monoubiquitinated and polyubiquitinated upon EGF stimulation; which does not affect tyrosine kinase activity or signaling capacity but may play a role in lysosomal targeting. Polyubiquitin linkage is mainly through 'Lys-63', but linkage through 'Lys-48', 'Lys-11' and 'Lys-29' also occurs. Deubiquitinated by OTUD7B, preventing degradation (By similarity). Ubiquitinated by RNF115 and RNF126. Ubiquitinated by ZNRF1 or CBL at different lysines in response to EGF stimulation; leading to recruitment of the ESCRT machinery and subsequent degradation in the lysosomes (By similarity). Deubiquitinated by UCHL1 leading to the inhibition of its degradation (PubMed:32494592). {ECO:0000250|UniProtKB:P00533, ECO:0000269|PubMed:23418353, ECO:0000269|PubMed:32494592}.; PTM: Phosphorylated on Tyr residues in response to EGF. Phosphorylation at Ser-697 is partial and occurs only if Thr-695 is phosphorylated. Phosphorylation at Thr-680 and Thr-695 by PRKD1 inhibits EGF-induced MAPK8/JNK1 activation. Dephosphorylation by PTPRJ prevents endocytosis and stabilizes the receptor at the plasma membrane. Autophosphorylation at Tyr-1199 is stimulated by methylation at Arg-1199 and enhances interaction with PTPN6. Autophosphorylation at Tyr-1092 and/or Tyr-1110 recruits STAT3. Dephosphorylated by PTPN1 and PTPN2. {ECO:0000250|UniProtKB:P00533}.; PTM: Palmitoylated on Cys residues by ZDHHC20. Palmitoylation inhibits internalization after ligand binding, and increases the persistence of tyrosine-phosphorylated EGFR at the cell membrane. Palmitoylation increases the amplitude and duration of EGFR signaling. {ECO:0000250|UniProtKB:P00533}.; PTM: Neddylated; by NEDD8 (By similarity). Neddylation results in localization to the cell membrane when activated by EGF. Neddylation also increases protein stability (By similarity). {ECO:0000250|UniProtKB:P00533}.; PTM: Methylated. Methylation at Arg-1199 by PRMT5 stimulates phosphorylation at Tyr-1197. {ECO:0000250|UniProtKB:P00533}.
uniprot
proteins
protein_family
EGF receptor subfamily
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
Tyr protein kinase family
uniprot
proteins
pubmed
10953014
uniprot
proteins
pubmed
1408137
uniprot
proteins
pubmed
16420529
uniprot
proteins
pubmed
16944957
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
17330941
uniprot
proteins
pubmed
17909029
uniprot
proteins
pubmed
2030916
uniprot
proteins
pubmed
20639532
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23418353
uniprot
proteins
pubmed
25744720
uniprot
proteins
pubmed
32494592
uniprot
proteins
pubmed
35131940
uniprot
proteins
pubmed
7618084
uniprot
proteins
pubmed
7618085
uniprot
proteins
pubmed
7630400
uniprot
proteins
pubmed
7678348
uniprot
proteins
pubmed
8125255
uniprot
proteins
pubmed
8404850
uniprot
proteins
sequence_length
1210
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P00533}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P00533}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P00533}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P00533}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P00533}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P00533}. Nucleus membrane {ECO:0000250|UniProtKB:P00533}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P00533}. Endosome {ECO:0000250|UniProtKB:P00533}. Endosome membrane {ECO:0000250|UniProtKB:P00533}. Nucleus {ECO:0000250|UniProtKB:P00533}. Note=In response to EGF, translocated from the cell membrane to the nucleus via Golgi and ER. Endocytosed upon activation by ligand. Colocalized with GPER1 in the nucleus of estrogen agonist-induced cancer-associated fibroblasts (CAF). {ECO:0000250|UniProtKB:P00533}.
uniprot
proteins
transmembrane_region
TRANSMEM 648..670; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins