HUMAN:EGFR

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Species (Taxon ID)	Homo sapiens (Human). ([1])
Gene Name(s)	EGFR (synonyms: ERBB1)
Protein Name(s)	Epidermal growth factor receptor Proto-oncogene c-ErbB-1 Receptor tyrosine-protein kinase erbB-1
External Links
EMBL	X00588 U95089 U48722 U48723 U48724 U48725 U48726 U48727 U48728 U48729 AF288738 AF288738 AF288738 AF288738 AF288738 AY698024 AY588246 AF277897 AF125253 AF125539 AF125538 X06370 X00663 M38425 M11234
IPI	IPI00018274 IPI00221346 IPI00221347 IPI00221348
PIR	A00641
RefSeq	NP_005219.2 NP_958439.1 NP_958440.1 NP_958441.1
UniGene	Hs.488293
PDB	1DNQ 1DNR 1IVO 1M14 1M17 1MOX 1NQL 1XKK 1YY9 1Z9I 2EB2 2EB3 2EXP 2EXQ 2GS2 2GS6 2GS7 2ITN 2ITO 2ITP 2ITQ 2ITT 2ITU 2ITV 2ITW 2ITX 2ITY 2ITZ 2J5E 2J5F 2J6M 2JIT 2JIU 2JIV 2KS1 2RF9 2RFD 2RFE 2RGP 3B2U 3B2V 3BEL 3BUO 3C09 3G5V 3G5Y 3GOP 3GT8 3IKA 3LZB 3NJP 3OB2 3OP0 3PFV 3POZ
PDBsum	1DNQ 1DNR 1IVO 1M14 1M17 1MOX 1NQL 1XKK 1YY9 1Z9I 2EB2 2EB3 2EXP 2EXQ 2GS2 2GS6 2GS7 2ITN 2ITO 2ITP 2ITQ 2ITT 2ITU 2ITV 2ITW 2ITX 2ITY 2ITZ 2J5E 2J5F 2J6M 2JIT 2JIU 2JIV 2KS1 2RF9 2RFD 2RFE 2RGP 3B2U 3B2V 3BEL 3BUO 3C09 3G5V 3G5Y 3GOP 3GT8 3IKA 3LZB 3NJP 3OB2 3OP0 3PFV 3POZ
ProteinModelPortal	P00533
SMR	P00533
DisProt	DP00309
DIP	DIP-405N DIP-5764N
IntAct	P00533
MINT	MINT-206389
STRING	P00533
GlycoSuiteDB	P00533
PhosphoSite	P00533
SWISS-2DPAGE	P00533
PeptideAtlas	P00533
PRIDE	P00533
Ensembl	ENST00000275493
GeneID	1956
KEGG	hsa:1956
UCSC	uc003tqi.1 uc003tqj.1 uc003tqk.1
CTD	1956
GeneCards	GC07P054860
H-InvDB	HIX0025338
HGNC	HGNC:3236
HPA	CAB000035 HPA001200 HPA018530
MIM	131550 211980
neXtProt	NX_P00533
Orphanet	360
PharmGKB	PA7360
HOVERGEN	HBG000490
InParanoid	P00533
OMA	MRRRHIV
PhylomeDB	P00533
BRENDA	2.7.10.1
Pathway_Interaction_DB	a6b1_a6b4_integrin_pathway arf6cyclingpathway endothelinpathway lysophospholipid_pathway telomerasepathway ptp1bpathway syndecan_3_pathway txa2pathway
Reactome	REACT_18266 REACT_9417
DrugBank	DB00002 DB00530 DB00317 DB01259 DB00281 DB01269 DB00072
NextBio	7931
PMAP-CutDB	P00533
ArrayExpress	P00533
Bgee	P00533
Genevestigator	P00533
GermOnline	ENSG00000146648
GO	GO:0016323 GO:0005789 GO:0005768 GO:0005615 GO:0000139 GO:0016021 GO:0031965 GO:0070435 GO:0051015 GO:0005524 GO:0003690 GO:0005006 GO:0042802 GO:0004710 GO:0046982 GO:0019903 GO:0004716 GO:0043006 GO:0007202 GO:0007411 GO:0008283 GO:0016337 GO:0043066 GO:0042059 GO:0001503 GO:0035413 GO:0030335 GO:0031659 GO:0050679 GO:0043406 GO:0045429 GO:0042327 GO:0051897 GO:0046777 GO:0051205 GO:0050999 GO:0050730 GO:0006950 GO:0070141
InterPro	IPR000494 IPR006211 IPR006212 IPR009030 IPR011009 IPR000719 IPR017441 IPR001245 IPR008266 IPR020635 IPR016245
Pfam	PF00757 PF07714 PF01030
PIRSF	PIRSF000619
PRINTS	PR00109
SMART	SM00261 SM00219
SUPFAM	SSF57184 SSF56112
PROSITE	PS00107 PS50011 PS00109

Annotations

Qualifier	GO ID	GO term name	Reference	Evidence Code	with/from	Aspect	Notes
	GO:0000139	Golgi membrane	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0134	C	Seeded From UniProt
	GO:0000166	nucleotide binding	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0547	F	Seeded From UniProt
	GO:0000902	cell morphogenesis	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000020329	P	Seeded From UniProt
	GO:0001503	ossification	PMID:12925580^[1]	NAS: Non-traceable Author Statement		P	Seeded From UniProt
	GO:0001892	embryonic placenta development	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000020329	P	Seeded From UniProt
	GO:0001942	hair follicle development	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000020329	P	Seeded From UniProt
	GO:0003690	double-stranded DNA binding	PMID:6325948^[2]	NAS: Non-traceable Author Statement		F	Seeded From UniProt
	GO:0004672	protein kinase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR000719	F	Seeded From UniProt
	GO:0004672	protein kinase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR001245	F	Seeded From UniProt
	GO:0004710	MAP/ERK kinase kinase activity	PMID:15542601^[3]	NAS: Non-traceable Author Statement		F	Seeded From UniProt
	GO:0004713	protein tyrosine kinase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR008266	F	Seeded From UniProt
	GO:0004713	protein tyrosine kinase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR020635	F	Seeded From UniProt
	GO:0004713	protein tyrosine kinase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0829	F	Seeded From UniProt
	GO:0004713	protein tyrosine kinase activity	PMID:14702346^[4]	IMP: Inferred from Mutant Phenotype		F	Seeded From UniProt
	GO:0004713	protein tyrosine kinase activity	PMID:16076471^[5]	TAS: Traceable Author Statement		F	Seeded From UniProt
	GO:0004713	protein tyrosine kinase activity	PMID:17599051^[6]	IDA: Inferred from Direct Assay		F	Seeded From UniProt
	GO:0004713	protein tyrosine kinase activity	Reactome:REACT_12491	TAS: Traceable Author Statement		F	Seeded From UniProt
	GO:0004713	protein tyrosine kinase activity	Reactome:REACT_12569	TAS: Traceable Author Statement		F	Seeded From UniProt
	GO:0004713	protein tyrosine kinase activity	Reactome:REACT_9388	TAS: Traceable Author Statement		F	Seeded From UniProt
	GO:0004714	transmembrane receptor protein tyrosine kinase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR006211	F	Seeded From UniProt
	GO:0004714	transmembrane receptor protein tyrosine kinase activity	GO_REF:0000003	IEA: Inferred from Electronic Annotation	EC:2.7.10.1	F	Seeded From UniProt
	GO:0004714	transmembrane receptor protein tyrosine kinase activity	Reactome:REACT_12592	TAS: Traceable Author Statement		F	Seeded From UniProt
	GO:0004716	receptor signaling protein tyrosine kinase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR016245	F	Seeded From UniProt
	GO:0004871	signal transducer activity	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000020329	F	Seeded From UniProt
	GO:0004872	receptor activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0675	F	Seeded From UniProt
	GO:0004888	transmembrane signaling receptor activity	PMID:7736574^[7]	IDA: Inferred from Direct Assay		F	Seeded From UniProt
	GO:0005006	epidermal growth factor-activated receptor activity	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000020329	F	Seeded From UniProt
	GO:0005006	epidermal growth factor-activated receptor activity	PMID:12435727^[8]	IDA: Inferred from Direct Assay		F	Seeded From UniProt
	GO:0005006	epidermal growth factor-activated receptor activity	PMID:2790960^[9]	NAS: Non-traceable Author Statement		F	Seeded From UniProt
	GO:0005006	epidermal growth factor-activated receptor activity	PMID:6325948^[2]	NAS: Non-traceable Author Statement		F	Seeded From UniProt
	GO:0005515	protein binding	PMID:10572067^[10]	IPI: Inferred from Physical Interaction	UniProtKB:P04626	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:10572067^[10]	IPI: Inferred from Physical Interaction	UniProtKB:P21860	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:10572067^[10]	IPI: Inferred from Physical Interaction	UniProtKB:P21860	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:10572067^[10]	IPI: Inferred from Physical Interaction	UniProtKB:Q15303	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:10572067^[10]	IPI: Inferred from Physical Interaction	UniProtKB:Q15303	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:10805725^[11]	IPI: Inferred from Physical Interaction	UniProtKB:O00750	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:11279102^[12]	IPI: Inferred from Physical Interaction	UniProtKB:Q9UNH7	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:11853560^[13]	IPI: Inferred from Physical Interaction	UniProtKB:P62161	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:12577067^[14]	IPI: Inferred from Physical Interaction	UniProtKB:P62993	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:12620237^[15]	IPI: Inferred from Physical Interaction	UniProtKB:P01133	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:15657067^[16]	IPI: Inferred from Physical Interaction	UniProtKB:P04626	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:15657067^[16]	IPI: Inferred from Physical Interaction	UniProtKB:P22681	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:15657067^[16]	IPI: Inferred from Physical Interaction	UniProtKB:P62993	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:15657067^[16]	IPI: Inferred from Physical Interaction	UniProtKB:P63104	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:16499958^[17]	IPI: Inferred from Physical Interaction	UniProtKB:Q9UJ41	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:16799092^[18]	IPI: Inferred from Physical Interaction	UniProtKB:P62158	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:17182860^[19]	IPI: Inferred from Physical Interaction	UniProtKB:O54967	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:17403676^[20]	IPI: Inferred from Physical Interaction	UniProtKB:Q13671	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:17599051^[6]	IPI: Inferred from Physical Interaction	UniProtKB:P05432	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:17909029^[21]	IPI: Inferred from Physical Interaction	UniProtKB:Q9Y2I7	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:18046415^[22]	IPI: Inferred from Physical Interaction	UniProtKB:Q9UJM3	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:18455122^[23]	IPI: Inferred from Physical Interaction	UniProtKB:P13866	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:18824549^[24]	IPI: Inferred from Physical Interaction	UniProtKB:Q9BZP6	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:19172738^[25]	IPI: Inferred from Physical Interaction	UniProtKB:Q9UQC2	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:19602593^[26]	IPI: Inferred from Physical Interaction	UniProtKB:P60468	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:20403327^[27]	IPI: Inferred from Physical Interaction	UniProtKB:Q8K424	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:20624308^[28]	IPI: Inferred from Physical Interaction	UniProtKB:P08581	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:20935677^[29]	IPI: Inferred from Physical Interaction	UniProtKB:P03372-4	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:20946980^[30]	IPI: Inferred from Physical Interaction	UniProtKB:Q99418	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:20946980^[30]	IPI: Inferred from Physical Interaction	UniProtKB:Q9UJM3	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:21278788^[31]	IPI: Inferred from Physical Interaction	UniProtKB:P12931	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:21278788^[31]	IPI: Inferred from Physical Interaction	UniProtKB:P29353	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:2176151^[32]	IPI: Inferred from Physical Interaction	UniProtKB:P20936	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:7657591^[33]	IPI: Inferred from Physical Interaction	UniProtKB:P22682	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:9419975^[34]	IPI: Inferred from Physical Interaction	UniProtKB:O14944	F	Seeded From UniProt
	GO:0005524	ATP binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR000719	F	Seeded From UniProt
	GO:0005524	ATP binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR006211	F	Seeded From UniProt
	GO:0005524	ATP binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR016245	F	Seeded From UniProt
	GO:0005524	ATP binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR017441	F	Seeded From UniProt
	GO:0005524	ATP binding	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0067	F	Seeded From UniProt
	GO:0005576	extracellular region	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0964	C	Seeded From UniProt
	GO:0005576	extracellular region	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0243	C	Seeded From UniProt
	GO:0005615	extracellular space	PMID:9103388^[35]	NAS: Non-traceable Author Statement		C	Seeded From UniProt
	GO:0005622	intracellular	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000020329	C	Seeded From UniProt
	GO:0005634	nucleus	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0539	C	Seeded From UniProt
	GO:0005634	nucleus	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000020329	C	Seeded From UniProt
	GO:0005634	nucleus	PMID:12828935^[36]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0005737	cytoplasm	PMID:12435727^[8]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0005737	cytoplasm	PMID:18029348^[37]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0005737	cytoplasm	PMID:7588596^[38]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0005768	endosome	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0967	C	Seeded From UniProt
	GO:0005768	endosome	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0101	C	Seeded From UniProt
	GO:0005768	endosome	PMID:14702346^[4]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0005768	endosome	PMID:17182860^[19]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0005783	endoplasmic reticulum	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0256	C	Seeded From UniProt
	GO:0005789	endoplasmic reticulum membrane	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0097	C	Seeded From UniProt
	GO:0005794	Golgi apparatus	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0333	C	Seeded From UniProt
	GO:0005886	plasma membrane	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-1003	C	Seeded From UniProt
	GO:0005886	plasma membrane	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000020329	C	Seeded From UniProt
	GO:0005886	plasma membrane	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0039	C	Seeded From UniProt
	GO:0005886	plasma membrane	PMID:15465819^[39]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0005886	plasma membrane	PMID:18029348^[37]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0005886	plasma membrane	Reactome:REACT_12381	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005886	plasma membrane	Reactome:REACT_12386	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005886	plasma membrane	Reactome:REACT_12387	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005886	plasma membrane	Reactome:REACT_12390	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005886	plasma membrane	Reactome:REACT_12392	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005886	plasma membrane	Reactome:REACT_12401	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005886	plasma membrane	Reactome:REACT_12402	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005886	plasma membrane	Reactome:REACT_12407	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005886	plasma membrane	Reactome:REACT_12412	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005886	plasma membrane	Reactome:REACT_12423	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005886	plasma membrane	Reactome:REACT_12424	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005886	plasma membrane	Reactome:REACT_12425	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005886	plasma membrane	Reactome:REACT_12432	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005886	plasma membrane	Reactome:REACT_12451	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005886	plasma membrane	Reactome:REACT_12466	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005886	plasma membrane	Reactome:REACT_12490	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005886	plasma membrane	Reactome:REACT_12491	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005886	plasma membrane	Reactome:REACT_12495	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005886	plasma membrane	Reactome:REACT_12501	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005886	plasma membrane	Reactome:REACT_12514	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005886	plasma membrane	Reactome:REACT_12515	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005886	plasma membrane	Reactome:REACT_12520	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005886	plasma membrane	Reactome:REACT_12521	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005886	plasma membrane	Reactome:REACT_12527	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005886	plasma membrane	Reactome:REACT_12534	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005886	plasma membrane	Reactome:REACT_12562	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005886	plasma membrane	Reactome:REACT_12569	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005886	plasma membrane	Reactome:REACT_12580	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005886	plasma membrane	Reactome:REACT_12592	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005886	plasma membrane	Reactome:REACT_12601	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005886	plasma membrane	Reactome:REACT_12605	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005886	plasma membrane	Reactome:REACT_12626	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005886	plasma membrane	Reactome:REACT_12629	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005886	plasma membrane	Reactome:REACT_12632	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005886	plasma membrane	Reactome:REACT_12636	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005886	plasma membrane	Reactome:REACT_22196	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005886	plasma membrane	Reactome:REACT_9388	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005886	plasma membrane	Reactome:REACT_9397	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005886	plasma membrane	Reactome:REACT_9401	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005886	plasma membrane	Reactome:REACT_9481	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0006468	protein phosphorylation	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR000719	P	Seeded From UniProt
	GO:0006468	protein phosphorylation	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR001245	P	Seeded From UniProt
	GO:0006468	protein phosphorylation	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR006211	P	Seeded From UniProt
	GO:0006468	protein phosphorylation	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR008266	P	Seeded From UniProt
	GO:0006468	protein phosphorylation	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR016245	P	Seeded From UniProt
	GO:0006950	response to stress	PMID:12828935^[36]	NAS: Non-traceable Author Statement		P	Seeded From UniProt
	GO:0007165	signal transduction	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000020329	P	Seeded From UniProt
	GO:0007165	signal transduction	PMID:10572067^[10]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0007165	signal transduction	Reactome:REACT_12478	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0007166	cell surface receptor linked signaling pathway	PMID:7736574^[7]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0007169	transmembrane receptor protein tyrosine kinase signaling pathway	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR006211	P	Seeded From UniProt
	GO:0007169	transmembrane receptor protein tyrosine kinase signaling pathway	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR016245	P	Seeded From UniProt
	GO:0007173	epidermal growth factor receptor signaling pathway	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000020329	P	Seeded From UniProt
	GO:0007173	epidermal growth factor receptor signaling pathway	PMID:10734107^[40]	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0007173	epidermal growth factor receptor signaling pathway	PMID:12435727^[8]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0007173	epidermal growth factor receptor signaling pathway	PMID:2790960^[9]	NAS: Non-traceable Author Statement		P	Seeded From UniProt
	GO:0007173	epidermal growth factor receptor signaling pathway	PMID:6325948^[2]	NAS: Non-traceable Author Statement		P	Seeded From UniProt
	GO:0007173	epidermal growth factor receptor signaling pathway	PMID:7736574^[7]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0007173	epidermal growth factor receptor signaling pathway	Reactome:REACT_9417	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0007202	activation of phospholipase C activity	PMID:12435727^[8]	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0007411	axon guidance	Reactome:REACT_18266	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0007435	salivary gland morphogenesis	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000020329	P	Seeded From UniProt
	GO:0008283	cell proliferation	PMID:10861448^[41]	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0008284	positive regulation of cell proliferation	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000020329	P	Seeded From UniProt
	GO:0008284	positive regulation of cell proliferation	PMID:7736574^[7]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0008544	epidermis development	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000020329	P	Seeded From UniProt
	GO:0016020	membrane	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR000494	C	Seeded From UniProt
	GO:0016020	membrane	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR006211	C	Seeded From UniProt
	GO:0016020	membrane	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0472	C	Seeded From UniProt
	GO:0016020	membrane	PMID:12435727^[8]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0016021	integral to membrane	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR016245	C	Seeded From UniProt
	GO:0016021	integral to membrane	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0812	C	Seeded From UniProt
	GO:0016301	kinase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0418	F	Seeded From UniProt
	GO:0016301	kinase activity	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000020329	F	Seeded From UniProt
	GO:0016310	phosphorylation	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0418	P	Seeded From UniProt
	GO:0016323	basolateral plasma membrane	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000020329	C	Seeded From UniProt
	GO:0016323	basolateral plasma membrane	PMID:12646923^[42]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0016337	cell-cell adhesion	PMID:12435727^[8]	IMP: Inferred from Mutant Phenotype		P	Seeded From UniProt
	GO:0016740	transferase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0808	F	Seeded From UniProt
	GO:0016772	transferase activity, transferring phosphorus-containing groups	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR011009	F	Seeded From UniProt
	GO:0019899	enzyme binding	PMID:12009895^[43]	IPI: Inferred from Physical Interaction	UniProtKB:O15162	F	Seeded From UniProt
	GO:0019903	protein phosphatase binding	PMID:15899872^[44]	IPI: Inferred from Physical Interaction	UniProtKB:Q15262	F	Seeded From UniProt
	GO:0021795	cerebral cortex cell migration	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000020329	P	Seeded From UniProt
	GO:0030139	endocytic vesicle	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000020329	C	Seeded From UniProt
	GO:0030335	positive regulation of cell migration	PMID:12435727^[8]	IMP: Inferred from Mutant Phenotype		P	Seeded From UniProt
	GO:0031659	positive regulation of cyclin-dependent protein kinase activity involved in G1/S	PMID:18483258^[45]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0031965	nuclear membrane	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0182	C	Seeded From UniProt
	GO:0035413	positive regulation of catenin import into nucleus	PMID:20302655^[46]	IMP: Inferred from Mutant Phenotype		P	Seeded From UniProt
	GO:0042059	negative regulation of epidermal growth factor receptor signaling pathway	Reactome:REACT_12484	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0042127	regulation of cell proliferation	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000020329	P	Seeded From UniProt
	GO:0042327	positive regulation of phosphorylation	PMID:15082764^[47]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0042802	identical protein binding	PMID:21480528^[48]	IPI: Inferred from Physical Interaction	UniProtKB:P00533	F	Seeded From UniProt
	GO:0043006	activation of phospholipase A2 activity by calcium-mediated signaling	PMID:12435727^[8]	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0043066	negative regulation of apoptosis	PMID:18070883^[49]	IMP: Inferred from Mutant Phenotype		P	Seeded From UniProt
	GO:0043406	positive regulation of MAP kinase activity	PMID:10572067^[10]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0045121	membrane raft	PMID:12009895^[43]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0045429	positive regulation of nitric oxide biosynthetic process	PMID:12828935^[36]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0046777	protein autophosphorylation	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000020329	P	Seeded From UniProt
	GO:0046777	protein autophosphorylation	PMID:18070883^[49]	IMP: Inferred from Mutant Phenotype		P	Seeded From UniProt
	GO:0046982	protein heterodimerization activity	PMID:10572067^[10]	IDA: Inferred from Direct Assay		F	Seeded From UniProt
	GO:0048146	positive regulation of fibroblast proliferation	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000020329	P	Seeded From UniProt
	GO:0048471	perinuclear region of cytoplasm	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000020329	C	Seeded From UniProt
	GO:0048546	digestive tract morphogenesis	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000020329	P	Seeded From UniProt
	GO:0050679	positive regulation of epithelial cell proliferation	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000020329	P	Seeded From UniProt
	GO:0050679	positive regulation of epithelial cell proliferation	PMID:10572067^[10]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0050730	regulation of peptidyl-tyrosine phosphorylation	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000020329	P	Seeded From UniProt
	GO:0050730	regulation of peptidyl-tyrosine phosphorylation	PMID:12435727^[8]	IMP: Inferred from Mutant Phenotype		P	Seeded From UniProt
	GO:0050999	regulation of nitric-oxide synthase activity	PMID:12828935^[36]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0051015	actin filament binding	PMID:14702346^[4]	IDA: Inferred from Direct Assay		F	Seeded From UniProt
	GO:0051205	protein insertion into membrane	PMID:12435727^[8]	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0051897	positive regulation of protein kinase B signaling cascade	PMID:17655843^[50]	IMP: Inferred from Mutant Phenotype		P	Seeded From UniProt
	GO:0060571	morphogenesis of an epithelial fold	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000020329	P	Seeded From UniProt
	GO:0070141	response to UV-A	PMID:18483258^[45]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0070435	Shc-EGFR complex	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:Q9QX70	C	Seeded From UniProt
	GO:0030122	AP-2 adaptor complex	PMID:14702346^[4]	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0030235	nitric-oxide synthase regulator activity	PMID:12828935^[36]	IDA: Inferred from Direct Assay		F	Seeded From UniProt
edit table

Notes

References

See Help:References for how to manage references in GONUTS.

↑ Sibilia M et al. (2003) Mice humanised for the EGF receptor display hypomorphic phenotypes in skin, bone and heart. Development 130: 4515-25 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 Mroczkowski B et al. (1984) ATP-stimulated interaction between epidermal growth factor receptor and supercoiled DNA. Nature 309: 270-3 PubMed GONUTS page
↑ Monick MM et al. (2005) Activation of the epidermal growth factor receptor by respiratory syncytial virus results in increased inflammation and delayed apoptosis. J Biol Chem 280: 2147-58 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 ^4.3 Stoorvogel W et al. (2004) Sorting of ligand-activated epidermal growth factor receptor to lysosomes requires its actin-binding domain. J Biol Chem 279: 11562-9 PubMed GONUTS page
↑ Dreux AC et al. (2006) The epidermal growth factor receptors and their family of ligands: their putative role in atherogenesis. Atherosclerosis 186: 38-53 PubMed GONUTS page
↑ ^6.0 ^6.1 Anastasi S et al. (2007) The evolutionarily conserved EBR module of RALT/MIG6 mediates suppression of the EGFR catalytic activity. Oncogene 26: 7833-46 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 ^7.3 Miyazaki T et al. (1995) Three distinct IL-2 signaling pathways mediated by bcl-2, c-myc, and lck cooperate in hematopoietic cell proliferation. Cell 81: 223-31 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 ^8.3 ^8.4 ^8.5 ^8.6 ^8.7 ^8.8 ^8.9 Andl CD et al. (2003) Epidermal growth factor receptor mediates increased cell proliferation, migration, and aggregation in esophageal keratinocytes in vitro and in vivo. J Biol Chem 278: 1824-30 PubMed GONUTS page
↑ ^9.0 ^9.1 Chen WS et al. (1989) Functional independence of the epidermal growth factor receptor from a domain required for ligand-induced internalization and calcium regulation. Cell 59: 33-43 PubMed GONUTS page
↑ ^10.0 ^10.1 ^10.2 ^10.3 ^10.4 ^10.5 ^10.6 ^10.7 ^10.8 Fernandes AM et al. (1999) Dominance of ErbB-1 heterodimers in lung epithelial cells overexpressing ErbB-2. Both ErbB-1 and ErbB-2 contribute significantly to tumorigenicity. Am J Respir Cell Mol Biol 21: 701-9 PubMed GONUTS page
↑ Arcaro A et al. (2000) Class II phosphoinositide 3-kinases are downstream targets of activated polypeptide growth factor receptors. Mol Cell Biol 20: 3817-30 PubMed GONUTS page
↑ Parks WT et al. (2001) Sorting nexin 6, a novel SNX, interacts with the transforming growth factor-beta family of receptor serine-threonine kinases. J Biol Chem 276: 19332-9 PubMed GONUTS page
↑ Li H & Villalobo A (2002) Evidence for the direct interaction between calmodulin and the human epidermal growth factor receptor. Biochem J 362: 499-505 PubMed GONUTS page
↑ Blagoev B et al. (2003) A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling. Nat Biotechnol 21: 315-8 PubMed GONUTS page
↑ Ferguson KM et al. (2003) EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization. Mol Cell 11: 507-17 PubMed GONUTS page
↑ ^16.0 ^16.1 ^16.2 ^16.3 Thelemann A et al. (2005) Phosphotyrosine signaling networks in epidermal growth factor receptor overexpressing squamous carcinoma cells. Mol Cell Proteomics 4: 356-76 PubMed GONUTS page
↑ Penengo L et al. (2006) Crystal structure of the ubiquitin binding domains of rabex-5 reveals two modes of interaction with ubiquitin. Cell 124: 1183-95 PubMed GONUTS page
↑ Wu SL et al. (2006) Dynamic profiling of the post-translational modifications and interaction partners of epidermal growth factor receptor signaling after stimulation by epidermal growth factor using Extended Range Proteomic Analysis (ERPA). Mol Cell Proteomics 5: 1610-27 PubMed GONUTS page
↑ ^19.0 ^19.1 Shen F et al. (2007) Activated Cdc42-associated kinase 1 is a component of EGF receptor signaling complex and regulates EGF receptor degradation. Mol Biol Cell 18: 732-42 PubMed GONUTS page
↑ Kong C et al. (2007) Rin1 interacts with signal-transducing adaptor molecule (STAM) and mediates epidermal growth factor receptor trafficking and degradation. J Biol Chem 282: 15294-301 PubMed GONUTS page
↑ Kim J et al. (2007) The phosphoinositide kinase PIKfyve mediates epidermal growth factor receptor trafficking to the nucleus. Cancer Res 67: 9229-37 PubMed GONUTS page
↑ Zhang X et al. (2007) Inhibition of the EGF receptor by binding of MIG6 to an activating kinase domain interface. Nature 450: 741-4 PubMed GONUTS page
↑ Weihua Z et al. (2008) Survival of cancer cells is maintained by EGFR independent of its kinase activity. Cancer Cell 13: 385-93 PubMed GONUTS page
↑ Hartl D et al. (2008) Acidic mammalian chitinase is secreted via an ADAM17/epidermal growth factor receptor-dependent pathway and stimulates chemokine production by pulmonary epithelial cells. J Biol Chem 283: 33472-82 PubMed GONUTS page
↑ Brummer T et al. (2008) Phosphorylation-dependent binding of 14-3-3 terminates signalling by the Gab2 docking protein. EMBO J 27: 2305-16 PubMed GONUTS page
↑ Liao HJ & Carpenter G (2009) Cetuximab/C225-induced intracellular trafficking of epidermal growth factor receptor. Cancer Res 69: 6179-83 PubMed GONUTS page
↑ Cheng X et al. (2010) TRP channel regulates EGFR signaling in hair morphogenesis and skin barrier formation. Cell 141: 331-43 PubMed GONUTS page
↑ Mueller KL et al. (2010) EGFR/Met association regulates EGFR TKI resistance in breast cancer. J Mol Signal 5: 8 PubMed GONUTS page
↑ Zhang XT et al. (2011) A positive feedback loop of ER-α36/EGFR promotes malignant growth of ER-negative breast cancer cells. Oncogene 30: 770-80 PubMed GONUTS page
↑ ^30.0 ^30.1 Bill A et al. (2010) Cytohesins are cytoplasmic ErbB receptor activators. Cell 143: 201-11 PubMed GONUTS page
↑ ^31.0 ^31.1 Jung J et al. (2011) Translationally controlled tumor protein induces human breast epithelial cell transformation through the activation of Src. Oncogene 30: 2264-74 PubMed GONUTS page
↑ Margolis B et al. (1990) The tyrosine phosphorylated carboxyterminus of the EGF receptor is a binding site for GAP and PLC-gamma. EMBO J 9: 4375-80 PubMed GONUTS page
↑ Galisteo ML et al. (1995) Tyrosine phosphorylation of the c-cbl proto-oncogene protein product and association with epidermal growth factor (EGF) receptor upon EGF stimulation. J Biol Chem 270: 20242-5 PubMed GONUTS page
↑ Komurasaki T et al. (1997) Epiregulin binds to epidermal growth factor receptor and ErbB-4 and induces tyrosine phosphorylation of epidermal growth factor receptor, ErbB-2, ErbB-3 and ErbB-4. Oncogene 15: 2841-8 PubMed GONUTS page
↑ Ilekis JV et al. (1997) Expression of a truncated epidermal growth factor receptor-like protein (TEGFR) in ovarian cancer. Gynecol Oncol 65: 36-41 PubMed GONUTS page
↑ ^36.0 ^36.1 ^36.2 ^36.3 ^36.4 Liu B & Neufeld AH (2003) Activation of epidermal growth factor receptor signals induction of nitric oxide synthase-2 in human optic nerve head astrocytes in glaucomatous optic neuropathy. Neurobiol Dis 13: 109-23 PubMed GONUTS page
↑ ^37.0 ^37.1 Barbe L et al. (2008) Toward a confocal subcellular atlas of the human proteome. Mol Cell Proteomics 7: 499-508 PubMed GONUTS page
↑ Englert C et al. (1995) WT1 suppresses synthesis of the epidermal growth factor receptor and induces apoptosis. EMBO J 14: 4662-75 PubMed GONUTS page
↑ de Melker AA et al. (2004) Ubiquitin ligase activity of c-Cbl guides the epidermal growth factor receptor into clathrin-coated pits by two distinct modes of Eps15 recruitment. J Biol Chem 279: 55465-73 PubMed GONUTS page
↑ Maudsley S et al. (2000) The beta(2)-adrenergic receptor mediates extracellular signal-regulated kinase activation via assembly of a multi-receptor complex with the epidermal growth factor receptor. J Biol Chem 275: 9572-80 PubMed GONUTS page
↑ Watson SA et al. (2000) Transforming growth factor-alpha-mediated growth pathways in human gastro-intestinal cell lines in relation to the gastrin autocrine pathway. Int J Cancer 87: 20-8 PubMed GONUTS page
↑ Vermeer PD et al. (2003) Segregation of receptor and ligand regulates activation of epithelial growth factor receptor. Nature 422: 322-6 PubMed GONUTS page
↑ ^43.0 ^43.1 Sun J et al. (2002) Plasma membrane phospholipid scramblase 1 is enriched in lipid rafts and interacts with the epidermal growth factor receptor. Biochemistry 41: 6338-45 PubMed GONUTS page
↑ Wang SE et al. (2005) Transforming growth factor {beta} (TGF-{beta})-Smad target gene protein tyrosine phosphatase receptor type kappa is required for TGF-{beta} function. Mol Cell Biol 25: 4703-15 PubMed GONUTS page
↑ ^45.0 ^45.1 He YY et al. (2008) UVA-induced cell cycle progression is mediated by a disintegrin and metalloprotease/epidermal growth factor receptor/AKT/Cyclin D1 pathways in keratinocytes. Cancer Res 68: 3752-8 PubMed GONUTS page
↑ Lee CH et al. (2010) Epidermal growth factor receptor regulates beta-catenin location, stability, and transcriptional activity in oral cancer. Mol Cancer 9: 64 PubMed GONUTS page
↑ Baldwin BR et al. (2004) Epidermal growth factor receptor stimulation activates the RNA binding protein CUG-BP1 and increases expression of C/EBPbeta-LIP in mammary epithelial cells. Mol Cell Biol 24: 3682-91 PubMed GONUTS page
↑ Mocanu MM et al. (2011) Comparative analysis of fluorescence resonance energy transfer (FRET) and proximity ligation assay (PLA). Proteomics 11: 2063-70 PubMed GONUTS page
↑ ^49.0 ^49.1 Edwin F & Patel TB (2008) A novel role of Sprouty 2 in regulating cellular apoptosis. J Biol Chem 283: 3181-90 PubMed GONUTS page
↑ Buffin-Meyer B et al. (2007) EGF receptor transactivation and PI3-kinase mediate stimulation of ERK by alpha(2A)-adrenoreceptor in intestinal epithelial cells: a role in wound healing. Eur J Pharmacol 574: 85-93 PubMed GONUTS page

[PMID:12925580-0] Sibilia M et al. (2003) Mice humanised for the EGF receptor display hypomorphic phenotypes in skin, bone and heart. Development 130: 4515-25 PubMed GONUTS page

[PMID:6325948-1] 2.0 ^2.1 ^2.2 Mroczkowski B et al. (1984) ATP-stimulated interaction between epidermal growth factor receptor and supercoiled DNA. Nature 309: 270-3 PubMed GONUTS page

[PMID:15542601-2] Monick MM et al. (2005) Activation of the epidermal growth factor receptor by respiratory syncytial virus results in increased inflammation and delayed apoptosis. J Biol Chem 280: 2147-58 PubMed GONUTS page

[PMID:14702346-3] 4.0 ^4.1 ^4.2 ^4.3 Stoorvogel W et al. (2004) Sorting of ligand-activated epidermal growth factor receptor to lysosomes requires its actin-binding domain. J Biol Chem 279: 11562-9 PubMed GONUTS page

[PMID:16076471-4] Dreux AC et al. (2006) The epidermal growth factor receptors and their family of ligands: their putative role in atherogenesis. Atherosclerosis 186: 38-53 PubMed GONUTS page

[PMID:17599051-5] 6.0 ^6.1 Anastasi S et al. (2007) The evolutionarily conserved EBR module of RALT/MIG6 mediates suppression of the EGFR catalytic activity. Oncogene 26: 7833-46 PubMed GONUTS page

[PMID:7736574-6] 7.0 ^7.1 ^7.2 ^7.3 Miyazaki T et al. (1995) Three distinct IL-2 signaling pathways mediated by bcl-2, c-myc, and lck cooperate in hematopoietic cell proliferation. Cell 81: 223-31 PubMed GONUTS page

[PMID:12435727-7] 8.0 ^8.1 ^8.2 ^8.3 ^8.4 ^8.5 ^8.6 ^8.7 ^8.8 ^8.9 Andl CD et al. (2003) Epidermal growth factor receptor mediates increased cell proliferation, migration, and aggregation in esophageal keratinocytes in vitro and in vivo. J Biol Chem 278: 1824-30 PubMed GONUTS page

[PMID:2790960-8] 9.0 ^9.1 Chen WS et al. (1989) Functional independence of the epidermal growth factor receptor from a domain required for ligand-induced internalization and calcium regulation. Cell 59: 33-43 PubMed GONUTS page

[PMID:10572067-9] 10.0 ^10.1 ^10.2 ^10.3 ^10.4 ^10.5 ^10.6 ^10.7 ^10.8 Fernandes AM et al. (1999) Dominance of ErbB-1 heterodimers in lung epithelial cells overexpressing ErbB-2. Both ErbB-1 and ErbB-2 contribute significantly to tumorigenicity. Am J Respir Cell Mol Biol 21: 701-9 PubMed GONUTS page

[PMID:10805725-10] Arcaro A et al. (2000) Class II phosphoinositide 3-kinases are downstream targets of activated polypeptide growth factor receptors. Mol Cell Biol 20: 3817-30 PubMed GONUTS page

[PMID:11279102-11] Parks WT et al. (2001) Sorting nexin 6, a novel SNX, interacts with the transforming growth factor-beta family of receptor serine-threonine kinases. J Biol Chem 276: 19332-9 PubMed GONUTS page

[PMID:11853560-12] Li H & Villalobo A (2002) Evidence for the direct interaction between calmodulin and the human epidermal growth factor receptor. Biochem J 362: 499-505 PubMed GONUTS page

[PMID:12577067-13] Blagoev B et al. (2003) A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling. Nat Biotechnol 21: 315-8 PubMed GONUTS page

[PMID:12620237-14] Ferguson KM et al. (2003) EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization. Mol Cell 11: 507-17 PubMed GONUTS page

[PMID:15657067-15] 16.0 ^16.1 ^16.2 ^16.3 Thelemann A et al. (2005) Phosphotyrosine signaling networks in epidermal growth factor receptor overexpressing squamous carcinoma cells. Mol Cell Proteomics 4: 356-76 PubMed GONUTS page

[PMID:16499958-16] Penengo L et al. (2006) Crystal structure of the ubiquitin binding domains of rabex-5 reveals two modes of interaction with ubiquitin. Cell 124: 1183-95 PubMed GONUTS page

[PMID:16799092-17] Wu SL et al. (2006) Dynamic profiling of the post-translational modifications and interaction partners of epidermal growth factor receptor signaling after stimulation by epidermal growth factor using Extended Range Proteomic Analysis (ERPA). Mol Cell Proteomics 5: 1610-27 PubMed GONUTS page

[PMID:17182860-18] 19.0 ^19.1 Shen F et al. (2007) Activated Cdc42-associated kinase 1 is a component of EGF receptor signaling complex and regulates EGF receptor degradation. Mol Biol Cell 18: 732-42 PubMed GONUTS page

[PMID:17403676-19] Kong C et al. (2007) Rin1 interacts with signal-transducing adaptor molecule (STAM) and mediates epidermal growth factor receptor trafficking and degradation. J Biol Chem 282: 15294-301 PubMed GONUTS page

[PMID:17909029-20] Kim J et al. (2007) The phosphoinositide kinase PIKfyve mediates epidermal growth factor receptor trafficking to the nucleus. Cancer Res 67: 9229-37 PubMed GONUTS page

[PMID:18046415-21] Zhang X et al. (2007) Inhibition of the EGF receptor by binding of MIG6 to an activating kinase domain interface. Nature 450: 741-4 PubMed GONUTS page

[PMID:18455122-22] Weihua Z et al. (2008) Survival of cancer cells is maintained by EGFR independent of its kinase activity. Cancer Cell 13: 385-93 PubMed GONUTS page

[PMID:18824549-23] Hartl D et al. (2008) Acidic mammalian chitinase is secreted via an ADAM17/epidermal growth factor receptor-dependent pathway and stimulates chemokine production by pulmonary epithelial cells. J Biol Chem 283: 33472-82 PubMed GONUTS page

[PMID:19172738-24] Brummer T et al. (2008) Phosphorylation-dependent binding of 14-3-3 terminates signalling by the Gab2 docking protein. EMBO J 27: 2305-16 PubMed GONUTS page

[PMID:19602593-25] Liao HJ & Carpenter G (2009) Cetuximab/C225-induced intracellular trafficking of epidermal growth factor receptor. Cancer Res 69: 6179-83 PubMed GONUTS page

[PMID:20403327-26] Cheng X et al. (2010) TRP channel regulates EGFR signaling in hair morphogenesis and skin barrier formation. Cell 141: 331-43 PubMed GONUTS page

[PMID:20624308-27] Mueller KL et al. (2010) EGFR/Met association regulates EGFR TKI resistance in breast cancer. J Mol Signal 5: 8 PubMed GONUTS page

[PMID:20935677-28] Zhang XT et al. (2011) A positive feedback loop of ER-α36/EGFR promotes malignant growth of ER-negative breast cancer cells. Oncogene 30: 770-80 PubMed GONUTS page

[PMID:20946980-29] 30.0 ^30.1 Bill A et al. (2010) Cytohesins are cytoplasmic ErbB receptor activators. Cell 143: 201-11 PubMed GONUTS page

[PMID:21278788-30] 31.0 ^31.1 Jung J et al. (2011) Translationally controlled tumor protein induces human breast epithelial cell transformation through the activation of Src. Oncogene 30: 2264-74 PubMed GONUTS page

[PMID:2176151-31] Margolis B et al. (1990) The tyrosine phosphorylated carboxyterminus of the EGF receptor is a binding site for GAP and PLC-gamma. EMBO J 9: 4375-80 PubMed GONUTS page

[PMID:7657591-32] Galisteo ML et al. (1995) Tyrosine phosphorylation of the c-cbl proto-oncogene protein product and association with epidermal growth factor (EGF) receptor upon EGF stimulation. J Biol Chem 270: 20242-5 PubMed GONUTS page

[PMID:9419975-33] Komurasaki T et al. (1997) Epiregulin binds to epidermal growth factor receptor and ErbB-4 and induces tyrosine phosphorylation of epidermal growth factor receptor, ErbB-2, ErbB-3 and ErbB-4. Oncogene 15: 2841-8 PubMed GONUTS page

[PMID:9103388-34] Ilekis JV et al. (1997) Expression of a truncated epidermal growth factor receptor-like protein (TEGFR) in ovarian cancer. Gynecol Oncol 65: 36-41 PubMed GONUTS page

[PMID:12828935-35] 36.0 ^36.1 ^36.2 ^36.3 ^36.4 Liu B & Neufeld AH (2003) Activation of epidermal growth factor receptor signals induction of nitric oxide synthase-2 in human optic nerve head astrocytes in glaucomatous optic neuropathy. Neurobiol Dis 13: 109-23 PubMed GONUTS page

[PMID:18029348-36] 37.0 ^37.1 Barbe L et al. (2008) Toward a confocal subcellular atlas of the human proteome. Mol Cell Proteomics 7: 499-508 PubMed GONUTS page

[PMID:7588596-37] Englert C et al. (1995) WT1 suppresses synthesis of the epidermal growth factor receptor and induces apoptosis. EMBO J 14: 4662-75 PubMed GONUTS page

[PMID:15465819-38] Melker AA et al. (2004) Ubiquitin ligase activity of c-Cbl guides the epidermal growth factor receptor into clathrin-coated pits by two distinct modes of Eps15 recruitment. J Biol Chem 279: 55465-73 PubMed GONUTS page

[PMID:10734107-39] Maudsley S et al. (2000) The beta(2)-adrenergic receptor mediates extracellular signal-regulated kinase activation via assembly of a multi-receptor complex with the epidermal growth factor receptor. J Biol Chem 275: 9572-80 PubMed GONUTS page

[PMID:10861448-40] Watson SA et al. (2000) Transforming growth factor-alpha-mediated growth pathways in human gastro-intestinal cell lines in relation to the gastrin autocrine pathway. Int J Cancer 87: 20-8 PubMed GONUTS page

[PMID:12646923-41] Vermeer PD et al. (2003) Segregation of receptor and ligand regulates activation of epithelial growth factor receptor. Nature 422: 322-6 PubMed GONUTS page

[PMID:12009895-42] 43.0 ^43.1 Sun J et al. (2002) Plasma membrane phospholipid scramblase 1 is enriched in lipid rafts and interacts with the epidermal growth factor receptor. Biochemistry 41: 6338-45 PubMed GONUTS page

[PMID:15899872-43] Wang SE et al. (2005) Transforming growth factor {beta} (TGF-{beta})-Smad target gene protein tyrosine phosphatase receptor type kappa is required for TGF-{beta} function. Mol Cell Biol 25: 4703-15 PubMed GONUTS page

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