HUMAN:EGFR original

Species (Taxon ID)	Homo sapiens (Human). (taxon:9606)
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
UniProt Identifier	EGFR_HUMAN
UniProt Accessions	P00533, O00688, O00732, P06268, Q14225, Q68GS5, Q92795, Q9BZS2, Q9GZX1, Q9H2C9, Q9H3C9, Q9UMD7, Q9UMD8, Q9UMG5,
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,
PIR	A00641,
RefSeq	NP_005219.2, NP_958439.1, NP_958440.1, NP_958441.1,
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,
IntAct	P00533,
Ensembl	ENST00000275493,
Pfam	PF00757, PF07714, PF01030,

Annotations

Qualifier	GO ID	GO term name	Reference	Evidence Code	with/from	Aspect
	GO:0000139	Golgi membrane	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0134	C
	GO:0000166	nucleotide binding	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0547	F
	GO:0001503	ossification	PMID:12925580^[1]	NAS: Non-traceable Author Statement		P
	GO:0003690	double-stranded DNA binding	PMID:6325948^[2]	NAS: Non-traceable Author Statement		F
	GO:0004672	protein kinase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR000719	F
	GO:0004672	protein kinase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR001245	F
	GO:0004672	protein kinase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR017441	F
	GO:0004710	MAP/ERK kinase kinase activity	PMID:15542601^[3]	NAS: Non-traceable Author Statement		F
	GO:0004713	protein tyrosine kinase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR008266	F
	GO:0004713	protein tyrosine kinase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0829	F
	GO:0004713	protein tyrosine kinase activity	PMID:14702346^[4]	IMP: Inferred from Mutant Phenotype		F
	GO:0004713	protein tyrosine kinase activity	PMID:16076471^[5]	TAS: Traceable Author Statement		F
	GO:0004713	protein tyrosine kinase activity	PMID:17599051^[6]	IDA: Inferred from Direct Assay		F
	GO:0004713	protein tyrosine kinase activity	Reactome:REACT_12424	TAS: Traceable Author Statement		F
	GO:0004713	protein tyrosine kinase activity	Reactome:REACT_12491	TAS: Traceable Author Statement		F
	GO:0004713	protein tyrosine kinase activity	Reactome:REACT_12569	TAS: Traceable Author Statement		F
	GO:0004713	protein tyrosine kinase activity	Reactome:REACT_9388	TAS: Traceable Author Statement		F
	GO:0004714	transmembrane receptor protein tyrosine kinase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR006211	F
	GO:0004714	transmembrane receptor protein tyrosine kinase activity	GO_REF:0000003	IEA: Inferred from Electronic Annotation	EC:2.7.10.1	F
	GO:0004714	transmembrane receptor protein tyrosine kinase activity	Reactome:REACT_12592	TAS: Traceable Author Statement		F
	GO:0004716	receptor signaling protein tyrosine kinase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR016245	F
	GO:0004872	receptor activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0675	F
	GO:0004888	transmembrane receptor activity	PMID:7736574^[7]	IDA: Inferred from Direct Assay		F
	GO:0005006	epidermal growth factor receptor activity	PMID:12435727^[8]	IDA: Inferred from Direct Assay		F
	GO:0005006	epidermal growth factor receptor activity	PMID:2790960^[9]	NAS: Non-traceable Author Statement		F
	GO:0005006	epidermal growth factor receptor activity	PMID:6325948^[2]	NAS: Non-traceable Author Statement		F
	GO:0005515	protein binding	PMID:10572067^[10]	IPI: Inferred from Physical Interaction	UniProtKB:P04626	F
	GO:0005515	protein binding	PMID:10572067^[10]	IPI: Inferred from Physical Interaction	UniProtKB:P04626	F
	GO:0005515	protein binding	PMID:10572067^[10]	IPI: Inferred from Physical Interaction	UniProtKB:P21860	F
	GO:0005515	protein binding	PMID:10572067^[10]	IPI: Inferred from Physical Interaction	UniProtKB:P21860	F
	GO:0005515	protein binding	PMID:10572067^[10]	IPI: Inferred from Physical Interaction	UniProtKB:Q15303	F
	GO:0005515	protein binding	PMID:10572067^[10]	IPI: Inferred from Physical Interaction	UniProtKB:Q15303	F
	GO:0005515	protein binding	PMID:10805725^[11]	IPI: Inferred from Physical Interaction	UniProtKB:O00750	F
	GO:0005515	protein binding	PMID:11279102^[12]	IPI: Inferred from Physical Interaction	UniProtKB:Q9UNH7	F
	GO:0005515	protein binding	PMID:11853560^[13]	IPI: Inferred from Physical Interaction	UniProtKB:P62161	F
	GO:0005515	protein binding	PMID:12577067^[14]	IPI: Inferred from Physical Interaction	UniProtKB:P62993	F
	GO:0005515	protein binding	PMID:12620237^[15]	IPI: Inferred from Physical Interaction	UniProtKB:P01133	F
	GO:0005515	protein binding	PMID:14960328^[16]	IPI: Inferred from Physical Interaction	UniProtKB:P62158	F
	GO:0005515	protein binding	PMID:14960328^[16]	IPI: Inferred from Physical Interaction	UniProtKB:P62204	F
	GO:0005515	protein binding	PMID:15225635^[17]	IPI: Inferred from Physical Interaction	UniProtKB:P63104	F
	GO:0005515	protein binding	PMID:16499958^[18]	IPI: Inferred from Physical Interaction	UniProtKB:Q9UJ41	F
	GO:0005515	protein binding	PMID:17182860^[19]	IPI: Inferred from Physical Interaction	UniProtKB:O54967	F
	GO:0005515	protein binding	PMID:17403676^[20]	IPI: Inferred from Physical Interaction	UniProtKB:Q13671	F
	GO:0005515	protein binding	PMID:17599051^[6]	IPI: Inferred from Physical Interaction	UniProtKB:P05432	F
	GO:0005515	protein binding	PMID:17909029^[21]	IPI: Inferred from Physical Interaction	UniProtKB:Q9Y2I7	F
	GO:0005515	protein binding	PMID:18046415^[22]	IPI: Inferred from Physical Interaction	UniProtKB:Q9UJM3	F
	GO:0005515	protein binding	PMID:18455122^[23]	IPI: Inferred from Physical Interaction	UniProtKB:P13866	F
	GO:0005515	protein binding	PMID:18824549^[24]	IPI: Inferred from Physical Interaction	UniProtKB:Q9BZP6	F
	GO:0005515	protein binding	PMID:19167335^[25]	IPI: Inferred from Physical Interaction	UniProtKB:P08575	F
	GO:0005515	protein binding	PMID:19167335^[25]	IPI: Inferred from Physical Interaction	UniProtKB:P23467	F
	GO:0005515	protein binding	PMID:19167335^[25]	IPI: Inferred from Physical Interaction	UniProtKB:Q12913	F
	GO:0005515	protein binding	PMID:19172738^[26]	IPI: Inferred from Physical Interaction	UniProtKB:Q9UQC2	F
	GO:0005515	protein binding	PMID:19602593^[27]	IPI: Inferred from Physical Interaction	UniProtKB:P60468	F
	GO:0005515	protein binding	PMID:20403327^[28]	IPI: Inferred from Physical Interaction	UniProtKB:Q8K424	F
	GO:0005515	protein binding	PMID:20624308^[29]	IPI: Inferred from Physical Interaction	UniProtKB:P08581	F
	GO:0005515	protein binding	PMID:20946980^[30]	IPI: Inferred from Physical Interaction	UniProtKB:Q99418	F
	GO:0005515	protein binding	PMID:20946980^[30]	IPI: Inferred from Physical Interaction	UniProtKB:Q9UJM3	F
	GO:0005515	protein binding	PMID:2176151^[31]	IPI: Inferred from Physical Interaction	UniProtKB:P20936	F
	GO:0005515	protein binding	PMID:7657591^[32]	IPI: Inferred from Physical Interaction	UniProtKB:P22681	F
	GO:0005515	protein binding	PMID:7657591^[32]	IPI: Inferred from Physical Interaction	UniProtKB:P22682	F
	GO:0005515	protein binding	PMID:8887653^[33]	IPI: Inferred from Physical Interaction	UniProtKB:P62993	F
	GO:0005515	protein binding	PMID:8887653^[33]	IPI: Inferred from Physical Interaction	UniProtKB:P98083	F
	GO:0005515	protein binding	PMID:9419975^[34]	IPI: Inferred from Physical Interaction	UniProtKB:O14944	F
	GO:0005515	protein binding	PMID:9425043^[35]	IPI: Inferred from Physical Interaction	UniProtKB:P62157	F
	GO:0005515	protein binding	PMID:9425043^[35]	IPI: Inferred from Physical Interaction	UniProtKB:Q29376	F
	GO:0005524	ATP binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR000719	F
	GO:0005524	ATP binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR006211	F
	GO:0005524	ATP binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR016245	F
	GO:0005524	ATP binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR017441	F
	GO:0005524	ATP binding	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0067	F
	GO:0005576	extracellular region	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0964	C
	GO:0005576	extracellular region	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0243	C
	GO:0005615	extracellular space	PMID:9103388^[36]	NAS: Non-traceable Author Statement		C
	GO:0005634	nucleus	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0539	C
	GO:0005634	nucleus	PMID:12828935^[37]	IDA: Inferred from Direct Assay		C
	GO:0005737	cytoplasm	PMID:12435727^[8]	IDA: Inferred from Direct Assay		C
	GO:0005737	cytoplasm	PMID:18029348^[38]	IDA: Inferred from Direct Assay		C
	GO:0005737	cytoplasm	PMID:7588596^[39]	IDA: Inferred from Direct Assay		C
	GO:0005768	endosome	PMID:14702346^[4]	IDA: Inferred from Direct Assay		C
	GO:0005768	endosome	PMID:17182860^[19]	IDA: Inferred from Direct Assay		C
	GO:0005783	endoplasmic reticulum	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0256	C
	GO:0005789	endoplasmic reticulum membrane	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0097	C
	GO:0005794	Golgi apparatus	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0333	C
	GO:0005886	plasma membrane	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-1003	C
	GO:0005886	plasma membrane	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0039	C
	GO:0005886	plasma membrane	PMID:10567358^[40]	EXP: Inferred from Experiment		C
	GO:0005886	plasma membrane	PMID:10648629^[41]	EXP: Inferred from Experiment		C
	GO:0005886	plasma membrane	PMID:10734310^[42]	EXP: Inferred from Experiment		C
	GO:0005886	plasma membrane	PMID:10913131^[43]	EXP: Inferred from Experiment		C
	GO:0005886	plasma membrane	PMID:11823423^[44]	EXP: Inferred from Experiment		C
	GO:0005886	plasma membrane	PMID:11894095^[45]	EXP: Inferred from Experiment		C
	GO:0005886	plasma membrane	PMID:12218189^[46]	EXP: Inferred from Experiment		C
	GO:0005886	plasma membrane	PMID:12593796^[47]	EXP: Inferred from Experiment		C
	GO:0005886	plasma membrane	PMID:14560030^[48]	EXP: Inferred from Experiment		C
	GO:0005886	plasma membrane	PMID:14665621^[49]	EXP: Inferred from Experiment		C
	GO:0005886	plasma membrane	PMID:14718570^[50]	EXP: Inferred from Experiment		C
	GO:0005886	plasma membrane	PMID:15465819^[51]	IDA: Inferred from Direct Assay		C
	GO:0005886	plasma membrane	PMID:15475003^[52]	EXP: Inferred from Experiment		C
	GO:0005886	plasma membrane	PMID:15574420^[53]	EXP: Inferred from Experiment		C
	GO:0005886	plasma membrane	PMID:15962011^[54]	EXP: Inferred from Experiment		C
	GO:0005886	plasma membrane	PMID:16407834^[55]	EXP: Inferred from Experiment		C
	GO:0005886	plasma membrane	PMID:18029348^[38]	IDA: Inferred from Direct Assay		C
	GO:0005886	plasma membrane	PMID:8493579^[56]	EXP: Inferred from Experiment		C
	GO:0005886	plasma membrane	PMID:8639530^[57]	EXP: Inferred from Experiment		C
	GO:0005886	plasma membrane	PMID:8845374^[58]	EXP: Inferred from Experiment		C
	GO:0005886	plasma membrane	PMID:9356464^[59]	EXP: Inferred from Experiment		C
	GO:0005886	plasma membrane	PMID:9544989^[60]	EXP: Inferred from Experiment		C
	GO:0005886	plasma membrane	Reactome:REACT_12392	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	Reactome:REACT_12401	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	Reactome:REACT_12407	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	Reactome:REACT_12424	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	Reactome:REACT_12466	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	Reactome:REACT_12490	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	Reactome:REACT_12491	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	Reactome:REACT_12515	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	Reactome:REACT_12527	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	Reactome:REACT_12562	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	Reactome:REACT_12569	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	Reactome:REACT_12592	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	Reactome:REACT_9388	TAS: Traceable Author Statement		C
	GO:0006468	protein phosphorylation	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR000719	P
	GO:0006468	protein phosphorylation	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR001245	P
	GO:0006468	protein phosphorylation	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR006211	P
	GO:0006468	protein phosphorylation	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR008266	P
	GO:0006468	protein phosphorylation	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR016245	P
	GO:0006468	protein phosphorylation	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR017441	P
	GO:0006950	response to stress	PMID:12828935^[37]	NAS: Non-traceable Author Statement		P
	GO:0007165	signal transduction	PMID:10572067^[10]	IDA: Inferred from Direct Assay		P
	GO:0007165	signal transduction	PMID:1501243^[61]	EXP: Inferred from Experiment		P
	GO:0007166	cell surface receptor linked signaling pathway	PMID:7736574^[7]	IDA: Inferred from Direct Assay		P
	GO:0007169	transmembrane receptor protein tyrosine kinase signaling pathway	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR006211	P
	GO:0007169	transmembrane receptor protein tyrosine kinase signaling pathway	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR016245	P
	GO:0007173	epidermal growth factor receptor signaling pathway	PMID:10734107^[62]	TAS: Traceable Author Statement		P
	GO:0007173	epidermal growth factor receptor signaling pathway	PMID:12435727^[8]	IDA: Inferred from Direct Assay		P
	GO:0007173	epidermal growth factor receptor signaling pathway	PMID:2790960^[9]	NAS: Non-traceable Author Statement		P
	GO:0007173	epidermal growth factor receptor signaling pathway	PMID:6325948^[2]	NAS: Non-traceable Author Statement		P
	GO:0007173	epidermal growth factor receptor signaling pathway	PMID:7736574^[7]	IDA: Inferred from Direct Assay		P
	GO:0007173	epidermal growth factor receptor signaling pathway	Reactome:REACT_9417	TAS: Traceable Author Statement		P
	GO:0007202	activation of phospholipase C activity	PMID:12435727^[8]	TAS: Traceable Author Statement		P
	GO:0007411	axon guidance	Reactome:REACT_18266	TAS: Traceable Author Statement		P
	GO:0008283	cell proliferation	PMID:10861448^[63]	TAS: Traceable Author Statement		P
	GO:0008284	positive regulation of cell proliferation	PMID:7736574^[7]	IDA: Inferred from Direct Assay		P
	GO:0016020	membrane	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR000494	C
	GO:0016020	membrane	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR006211	C
	GO:0016020	membrane	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0472	C
	GO:0016020	membrane	PMID:12435727^[8]	IDA: Inferred from Direct Assay		C
	GO:0016021	integral to membrane	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR016245	C
	GO:0016021	integral to membrane	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0812	C
	GO:0016301	kinase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0418	F
	GO:0016310	phosphorylation	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0418	P
	GO:0016323	basolateral plasma membrane	PMID:12646923^[64]	IDA: Inferred from Direct Assay		C
	GO:0016337	cell-cell adhesion	PMID:12435727^[8]	IMP: Inferred from Mutant Phenotype		P
	GO:0016740	transferase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0808	F
	GO:0019903	protein phosphatase binding	PMID:15899872^[65]	IPI: Inferred from Physical Interaction	UniProtKB:Q15262	F
	GO:0030335	positive regulation of cell migration	PMID:12435727^[8]	IMP: Inferred from Mutant Phenotype		P
	GO:0031659	positive regulation of cyclin-dependent protein kinase activity involved in G1/S	PMID:18483258^[66]	IDA: Inferred from Direct Assay		P
	GO:0031965	nuclear membrane	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0182	C
	GO:0035413	positive regulation of catenin import into nucleus	PMID:20302655^[67]	IMP: Inferred from Mutant Phenotype		P
	GO:0042059	negative regulation of epidermal growth factor receptor signaling pathway	Reactome:REACT_12484	TAS: Traceable Author Statement		P
	GO:0042327	positive regulation of phosphorylation	PMID:15082764^[68]	IDA: Inferred from Direct Assay		P
	GO:0042802	identical protein binding	PMID:20946980^[30]	IPI: Inferred from Physical Interaction	UniProtKB:P00533	F
	GO:0043006	activation of phospholipase A2 activity by calcium-mediated signaling	PMID:12435727^[8]	TAS: Traceable Author Statement		P
	GO:0043066	negative regulation of apoptosis	PMID:18070883^[69]	IMP: Inferred from Mutant Phenotype		P
	GO:0043406	positive regulation of MAP kinase activity	PMID:10572067^[10]	IDA: Inferred from Direct Assay		P
	GO:0045429	positive regulation of nitric oxide biosynthetic process	PMID:12828935^[37]	IDA: Inferred from Direct Assay		P
	GO:0046777	protein autophosphorylation	PMID:18070883^[69]	IMP: Inferred from Mutant Phenotype		P
	GO:0046982	protein heterodimerization activity	PMID:10572067^[10]	IDA: Inferred from Direct Assay		F
	GO:0050679	positive regulation of epithelial cell proliferation	PMID:10572067^[10]	IDA: Inferred from Direct Assay		P
	GO:0050730	regulation of peptidyl-tyrosine phosphorylation	PMID:12435727^[8]	IMP: Inferred from Mutant Phenotype		P
	GO:0050999	regulation of nitric-oxide synthase activity	PMID:12828935^[37]	IDA: Inferred from Direct Assay		P
	GO:0051015	actin filament binding	PMID:14702346^[4]	IDA: Inferred from Direct Assay		F
	GO:0051205	protein insertion into membrane	PMID:12435727^[8]	TAS: Traceable Author Statement		P
	GO:0051897	positive regulation of protein kinase B signaling cascade	PMID:17655843^[70]	IMP: Inferred from Mutant Phenotype		P
	GO:0070141	response to UV-A	PMID:18483258^[66]	IDA: Inferred from Direct Assay		P
	GO:0070435	Shc-EGFR complex	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:Q9QX70	C
	GO:0030122	AP-2 adaptor complex	PMID:14702346^[4]	TAS: Traceable Author Statement		C
	GO:0030235	nitric-oxide synthase regulator activity	PMID:12828935^[37]	IDA: Inferred from Direct Assay		F
	GO:0000139	Golgi membrane	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0134	C
	GO:0000166	nucleotide binding	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0547	F
	GO:0000902	cell morphogenesis	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000020329	P
	GO:0001503	ossification	PMID:12925580^[1]	NAS: Non-traceable Author Statement		P
	GO:0001892	embryonic placenta development	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000020329	P
	GO:0001942	hair follicle development	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000020329	P
	GO:0003690	double-stranded DNA binding	PMID:6325948^[2]	NAS: Non-traceable Author Statement		F
	GO:0004672	protein kinase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR000719	F
	GO:0004672	protein kinase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR001245	F
	GO:0004710	MAP/ERK kinase kinase activity	PMID:15542601^[3]	NAS: Non-traceable Author Statement		F
	GO:0004713	protein tyrosine kinase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR008266	F
	GO:0004713	protein tyrosine kinase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR020635	F
	GO:0004713	protein tyrosine kinase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0829	F
	GO:0004713	protein tyrosine kinase activity	PMID:14702346^[4]	IMP: Inferred from Mutant Phenotype		F
	GO:0004713	protein tyrosine kinase activity	PMID:16076471^[5]	TAS: Traceable Author Statement		F
	GO:0004713	protein tyrosine kinase activity	PMID:17599051^[6]	IDA: Inferred from Direct Assay		F
	GO:0004713	protein tyrosine kinase activity	Reactome:REACT_12491	TAS: Traceable Author Statement		F
	GO:0004713	protein tyrosine kinase activity	Reactome:REACT_12569	TAS: Traceable Author Statement		F
	GO:0004713	protein tyrosine kinase activity	Reactome:REACT_9388	TAS: Traceable Author Statement		F
	GO:0004714	transmembrane receptor protein tyrosine kinase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR006211	F
	GO:0004714	transmembrane receptor protein tyrosine kinase activity	GO_REF:0000003	IEA: Inferred from Electronic Annotation	EC:2.7.10.1	F
	GO:0004714	transmembrane receptor protein tyrosine kinase activity	Reactome:REACT_12592	TAS: Traceable Author Statement		F
	GO:0004716	receptor signaling protein tyrosine kinase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR016245	F
	GO:0004871	signal transducer activity	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000020329	F
	GO:0004872	receptor activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0675	F
	GO:0004888	transmembrane signaling receptor activity	PMID:7736574^[7]	IDA: Inferred from Direct Assay		F
	GO:0005006	epidermal growth factor receptor activity	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000020329	F
	GO:0005006	epidermal growth factor receptor activity	PMID:12435727^[8]	IDA: Inferred from Direct Assay		F
	GO:0005006	epidermal growth factor receptor activity	PMID:2790960^[9]	NAS: Non-traceable Author Statement		F
	GO:0005006	epidermal growth factor receptor activity	PMID:6325948^[2]	NAS: Non-traceable Author Statement		F
	GO:0005515	protein binding	PMID:10572067^[10]	IPI: Inferred from Physical Interaction	UniProtKB:P04626	F
	GO:0005515	protein binding	PMID:10572067^[10]	IPI: Inferred from Physical Interaction	UniProtKB:P04626	F
	GO:0005515	protein binding	PMID:10572067^[10]	IPI: Inferred from Physical Interaction	UniProtKB:P21860	F
	GO:0005515	protein binding	PMID:10572067^[10]	IPI: Inferred from Physical Interaction	UniProtKB:P21860	F
	GO:0005515	protein binding	PMID:10572067^[10]	IPI: Inferred from Physical Interaction	UniProtKB:Q15303	F
	GO:0005515	protein binding	PMID:10572067^[10]	IPI: Inferred from Physical Interaction	UniProtKB:Q15303	F
	GO:0005515	protein binding	PMID:10805725^[11]	IPI: Inferred from Physical Interaction	UniProtKB:O00750	F
	GO:0005515	protein binding	PMID:11279102^[12]	IPI: Inferred from Physical Interaction	UniProtKB:Q9UNH7	F
	GO:0005515	protein binding	PMID:11853560^[13]	IPI: Inferred from Physical Interaction	UniProtKB:P62161	F
	GO:0005515	protein binding	PMID:12577067^[14]	IPI: Inferred from Physical Interaction	UniProtKB:P62993	F
	GO:0005515	protein binding	PMID:12620237^[15]	IPI: Inferred from Physical Interaction	UniProtKB:P01133	F
	GO:0005515	protein binding	PMID:14960328^[16]	IPI: Inferred from Physical Interaction	UniProtKB:P62158	F
	GO:0005515	protein binding	PMID:14960328^[16]	IPI: Inferred from Physical Interaction	UniProtKB:P62204	F
	GO:0005515	protein binding	PMID:15225635^[17]	IPI: Inferred from Physical Interaction	UniProtKB:P63104	F
	GO:0005515	protein binding	PMID:16499958^[18]	IPI: Inferred from Physical Interaction	UniProtKB:Q9UJ41	F
	GO:0005515	protein binding	PMID:17182860^[19]	IPI: Inferred from Physical Interaction	UniProtKB:O54967	F
	GO:0005515	protein binding	PMID:17403676^[20]	IPI: Inferred from Physical Interaction	UniProtKB:Q13671	F
	GO:0005515	protein binding	PMID:17599051^[6]	IPI: Inferred from Physical Interaction	UniProtKB:P05432	F
	GO:0005515	protein binding	PMID:17909029^[21]	IPI: Inferred from Physical Interaction	UniProtKB:Q9Y2I7	F
	GO:0005515	protein binding	PMID:18046415^[22]	IPI: Inferred from Physical Interaction	UniProtKB:Q9UJM3	F
	GO:0005515	protein binding	PMID:18455122^[23]	IPI: Inferred from Physical Interaction	UniProtKB:P13866	F
	GO:0005515	protein binding	PMID:18824549^[24]	IPI: Inferred from Physical Interaction	UniProtKB:Q9BZP6	F
	GO:0005515	protein binding	PMID:19167335^[25]	IPI: Inferred from Physical Interaction	UniProtKB:P08575	F
	GO:0005515	protein binding	PMID:19167335^[25]	IPI: Inferred from Physical Interaction	UniProtKB:P23467	F
	GO:0005515	protein binding	PMID:19167335^[25]	IPI: Inferred from Physical Interaction	UniProtKB:Q12913	F
	GO:0005515	protein binding	PMID:19172738^[26]	IPI: Inferred from Physical Interaction	UniProtKB:Q9UQC2	F
	GO:0005515	protein binding	PMID:19602593^[27]	IPI: Inferred from Physical Interaction	UniProtKB:P60468	F
	GO:0005515	protein binding	PMID:20403327^[28]	IPI: Inferred from Physical Interaction	UniProtKB:Q8K424	F
	GO:0005515	protein binding	PMID:20624308^[29]	IPI: Inferred from Physical Interaction	UniProtKB:P08581	F
	GO:0005515	protein binding	PMID:20946980^[30]	IPI: Inferred from Physical Interaction	UniProtKB:Q99418	F
	GO:0005515	protein binding	PMID:20946980^[30]	IPI: Inferred from Physical Interaction	UniProtKB:Q9UJM3	F
	GO:0005515	protein binding	PMID:2176151^[31]	IPI: Inferred from Physical Interaction	UniProtKB:P20936	F
	GO:0005515	protein binding	PMID:7657591^[32]	IPI: Inferred from Physical Interaction	UniProtKB:P22681	F
	GO:0005515	protein binding	PMID:7657591^[32]	IPI: Inferred from Physical Interaction	UniProtKB:P22682	F
	GO:0005515	protein binding	PMID:8887653^[33]	IPI: Inferred from Physical Interaction	UniProtKB:P62993	F
	GO:0005515	protein binding	PMID:8887653^[33]	IPI: Inferred from Physical Interaction	UniProtKB:P98083	F
	GO:0005515	protein binding	PMID:9419975^[34]	IPI: Inferred from Physical Interaction	UniProtKB:O14944	F
	GO:0005515	protein binding	PMID:9425043^[35]	IPI: Inferred from Physical Interaction	UniProtKB:P62157	F
	GO:0005515	protein binding	PMID:9425043^[35]	IPI: Inferred from Physical Interaction	UniProtKB:Q29376	F
	GO:0005524	ATP binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR000719	F
	GO:0005524	ATP binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR006211	F
	GO:0005524	ATP binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR016245	F
	GO:0005524	ATP binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR017441	F
	GO:0005524	ATP binding	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0067	F
	GO:0005576	extracellular region	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0964	C
	GO:0005576	extracellular region	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0243	C
	GO:0005615	extracellular space	PMID:9103388^[36]	NAS: Non-traceable Author Statement		C
	GO:0005622	intracellular	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000020329	C
	GO:0005634	nucleus	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0539	C
	GO:0005634	nucleus	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000020329	C
	GO:0005634	nucleus	PMID:12828935^[37]	IDA: Inferred from Direct Assay		C
	GO:0005737	cytoplasm	PMID:12435727^[8]	IDA: Inferred from Direct Assay		C
	GO:0005737	cytoplasm	PMID:18029348^[38]	IDA: Inferred from Direct Assay		C
	GO:0005737	cytoplasm	PMID:7588596^[39]	IDA: Inferred from Direct Assay		C
	GO:0005768	endosome	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0967	C
	GO:0005768	endosome	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0101	C
	GO:0005768	endosome	PMID:14702346^[4]	IDA: Inferred from Direct Assay		C
	GO:0005768	endosome	PMID:17182860^[19]	IDA: Inferred from Direct Assay		C
	GO:0005783	endoplasmic reticulum	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0256	C
	GO:0005789	endoplasmic reticulum membrane	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0097	C
	GO:0005794	Golgi apparatus	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0333	C
	GO:0005886	plasma membrane	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-1003	C
	GO:0005886	plasma membrane	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000020329	C
	GO:0005886	plasma membrane	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0039	C
	GO:0005886	plasma membrane	PMID:15465819^[51]	IDA: Inferred from Direct Assay		C
	GO:0005886	plasma membrane	PMID:18029348^[38]	IDA: Inferred from Direct Assay		C
	GO:0005886	plasma membrane	Reactome:REACT_12381	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	Reactome:REACT_12386	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	Reactome:REACT_12387	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	Reactome:REACT_12390	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	Reactome:REACT_12392	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	Reactome:REACT_12401	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	Reactome:REACT_12402	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	Reactome:REACT_12407	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	Reactome:REACT_12412	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	Reactome:REACT_12423	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	Reactome:REACT_12424	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	Reactome:REACT_12425	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	Reactome:REACT_12432	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	Reactome:REACT_12451	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	Reactome:REACT_12466	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	Reactome:REACT_12490	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	Reactome:REACT_12491	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	Reactome:REACT_12495	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	Reactome:REACT_12501	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	Reactome:REACT_12514	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	Reactome:REACT_12515	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	Reactome:REACT_12520	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	Reactome:REACT_12521	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	Reactome:REACT_12527	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	Reactome:REACT_12534	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	Reactome:REACT_12562	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	Reactome:REACT_12569	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	Reactome:REACT_12580	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	Reactome:REACT_12592	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	Reactome:REACT_12601	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	Reactome:REACT_12605	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	Reactome:REACT_12626	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	Reactome:REACT_12629	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	Reactome:REACT_12632	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	Reactome:REACT_12636	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	Reactome:REACT_22196	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	Reactome:REACT_9388	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	Reactome:REACT_9397	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	Reactome:REACT_9401	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	Reactome:REACT_9481	TAS: Traceable Author Statement		C
	GO:0006468	protein phosphorylation	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR000719	P
	GO:0006468	protein phosphorylation	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR001245	P
	GO:0006468	protein phosphorylation	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR006211	P
	GO:0006468	protein phosphorylation	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR008266	P
	GO:0006468	protein phosphorylation	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR016245	P
	GO:0006950	response to stress	PMID:12828935^[37]	NAS: Non-traceable Author Statement		P
	GO:0007165	signal transduction	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000020329	P
	GO:0007165	signal transduction	PMID:10572067^[10]	IDA: Inferred from Direct Assay		P
	GO:0007165	signal transduction	Reactome:REACT_12478	TAS: Traceable Author Statement		P
	GO:0007166	cell surface receptor linked signaling pathway	PMID:7736574^[7]	IDA: Inferred from Direct Assay		P
	GO:0007169	transmembrane receptor protein tyrosine kinase signaling pathway	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR006211	P
	GO:0007169	transmembrane receptor protein tyrosine kinase signaling pathway	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR016245	P
	GO:0007173	epidermal growth factor receptor signaling pathway	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000020329	P
	GO:0007173	epidermal growth factor receptor signaling pathway	PMID:10734107^[62]	TAS: Traceable Author Statement		P
	GO:0007173	epidermal growth factor receptor signaling pathway	PMID:12435727^[8]	IDA: Inferred from Direct Assay		P
	GO:0007173	epidermal growth factor receptor signaling pathway	PMID:2790960^[9]	NAS: Non-traceable Author Statement		P
	GO:0007173	epidermal growth factor receptor signaling pathway	PMID:6325948^[2]	NAS: Non-traceable Author Statement		P
	GO:0007173	epidermal growth factor receptor signaling pathway	PMID:7736574^[7]	IDA: Inferred from Direct Assay		P
	GO:0007173	epidermal growth factor receptor signaling pathway	Reactome:REACT_9417	TAS: Traceable Author Statement		P
	GO:0007202	activation of phospholipase C activity	PMID:12435727^[8]	TAS: Traceable Author Statement		P
	GO:0007411	axon guidance	Reactome:REACT_18266	TAS: Traceable Author Statement		P
	GO:0007435	salivary gland morphogenesis	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000020329	P
	GO:0008283	cell proliferation	PMID:10861448^[63]	TAS: Traceable Author Statement		P
	GO:0008284	positive regulation of cell proliferation	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000020329	P
	GO:0008284	positive regulation of cell proliferation	PMID:7736574^[7]	IDA: Inferred from Direct Assay		P
	GO:0008544	epidermis development	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000020329	P
	GO:0016020	membrane	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR000494	C
	GO:0016020	membrane	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR006211	C
	GO:0016020	membrane	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0472	C
	GO:0016020	membrane	PMID:12435727^[8]	IDA: Inferred from Direct Assay		C
	GO:0016021	integral to membrane	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR016245	C
	GO:0016021	integral to membrane	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0812	C
	GO:0016301	kinase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0418	F
	GO:0016301	kinase activity	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000020329	F
	GO:0016310	phosphorylation	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0418	P
	GO:0016323	basolateral plasma membrane	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000020329	C
	GO:0016323	basolateral plasma membrane	PMID:12646923^[64]	IDA: Inferred from Direct Assay		C
	GO:0016337	cell-cell adhesion	PMID:12435727^[8]	IMP: Inferred from Mutant Phenotype		P
	GO:0016740	transferase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0808	F
	GO:0016772	transferase activity, transferring phosphorus-containing groups	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR011009	F
	GO:0019903	protein phosphatase binding	PMID:15899872^[65]	IPI: Inferred from Physical Interaction	UniProtKB:Q15262	F
	GO:0021795	cerebral cortex cell migration	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000020329	P
	GO:0030139	endocytic vesicle	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000020329	C
	GO:0030335	positive regulation of cell migration	PMID:12435727^[8]	IMP: Inferred from Mutant Phenotype		P
	GO:0031659	positive regulation of cyclin-dependent protein kinase activity involved in G1/S	PMID:18483258^[66]	IDA: Inferred from Direct Assay		P
	GO:0031965	nuclear membrane	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0182	C
	GO:0035413	positive regulation of catenin import into nucleus	PMID:20302655^[67]	IMP: Inferred from Mutant Phenotype		P
	GO:0042059	negative regulation of epidermal growth factor receptor signaling pathway	Reactome:REACT_12484	TAS: Traceable Author Statement		P
	GO:0042127	regulation of cell proliferation	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000020329	P
	GO:0042327	positive regulation of phosphorylation	PMID:15082764^[68]	IDA: Inferred from Direct Assay		P
	GO:0042802	identical protein binding	PMID:20946980^[30]	IPI: Inferred from Physical Interaction	UniProtKB:P00533	F
	GO:0043006	activation of phospholipase A2 activity by calcium-mediated signaling	PMID:12435727^[8]	TAS: Traceable Author Statement		P
	GO:0043066	negative regulation of apoptosis	PMID:18070883^[69]	IMP: Inferred from Mutant Phenotype		P
	GO:0043406	positive regulation of MAP kinase activity	PMID:10572067^[10]	IDA: Inferred from Direct Assay		P
	GO:0045429	positive regulation of nitric oxide biosynthetic process	PMID:12828935^[37]	IDA: Inferred from Direct Assay		P
	GO:0046777	protein autophosphorylation	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000020329	P
	GO:0046777	protein autophosphorylation	PMID:18070883^[69]	IMP: Inferred from Mutant Phenotype		P
	GO:0046982	protein heterodimerization activity	PMID:10572067^[10]	IDA: Inferred from Direct Assay		F
	GO:0048146	positive regulation of fibroblast proliferation	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000020329	P
	GO:0048471	perinuclear region of cytoplasm	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000020329	C
	GO:0048546	digestive tract morphogenesis	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000020329	P
	GO:0050679	positive regulation of epithelial cell proliferation	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000020329	P
	GO:0050679	positive regulation of epithelial cell proliferation	PMID:10572067^[10]	IDA: Inferred from Direct Assay		P
	GO:0050730	regulation of peptidyl-tyrosine phosphorylation	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000020329	P
	GO:0050730	regulation of peptidyl-tyrosine phosphorylation	PMID:12435727^[8]	IMP: Inferred from Mutant Phenotype		P
	GO:0050999	regulation of nitric-oxide synthase activity	PMID:12828935^[37]	IDA: Inferred from Direct Assay		P
	GO:0051015	actin filament binding	PMID:14702346^[4]	IDA: Inferred from Direct Assay		F
	GO:0051205	protein insertion into membrane	PMID:12435727^[8]	TAS: Traceable Author Statement		P
	GO:0051897	positive regulation of protein kinase B signaling cascade	PMID:17655843^[70]	IMP: Inferred from Mutant Phenotype		P
	GO:0060571	morphogenesis of an epithelial fold	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000020329	P
	GO:0070141	response to UV-A	PMID:18483258^[66]	IDA: Inferred from Direct Assay		P
	GO:0070435	Shc-EGFR complex	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:Q9QX70	C
colocalizes_with	GO:0030122	AP-2 adaptor complex	PMID:14702346^[4]	TAS: Traceable Author Statement		C
contributes_to	GO:0030235	nitric-oxide synthase regulator activity	PMID:12828935^[37]	IDA: Inferred from Direct Assay		F
edit table

Notes

References

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

↑ ^1.0 ^1.1 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 ^2.3 ^2.4 ^2.5 Mroczkowski, B et al. () ATP-stimulated interaction between epidermal growth factor receptor and supercoiled DNA. Nature 309 270-3 PubMed GONUTS page
↑ ^3.0 ^3.1 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 ^4.4 ^4.5 ^4.6 ^4.7 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
↑ ^5.0 ^5.1 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 ^6.2 ^6.3 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 ^7.4 ^7.5 ^7.6 ^7.7 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
↑ ^8.00 ^8.01 ^8.02 ^8.03 ^8.04 ^8.05 ^8.06 ^8.07 ^8.08 ^8.09 ^8.10 ^8.11 ^8.12 ^8.13 ^8.14 ^8.15 ^8.16 ^8.17 ^8.18 ^8.19 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 ^9.2 ^9.3 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
↑ ^10.00 ^10.01 ^10.02 ^10.03 ^10.04 ^10.05 ^10.06 ^10.07 ^10.08 ^10.09 ^10.10 ^10.11 ^10.12 ^10.13 ^10.14 ^10.15 ^10.16 ^10.17 ^10.18 ^10.19 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
↑ ^11.0 ^11.1 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
↑ ^12.0 ^12.1 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
↑ ^13.0 ^13.1 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
↑ ^14.0 ^14.1 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
↑ ^15.0 ^15.1 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 Li, H et al. (2004) Endogenous calmodulin interacts with the epidermal growth factor receptor in living cells. FEBS Lett. 559 175-80 PubMed GONUTS page
↑ ^17.0 ^17.1 Oksvold, MP et al. (2004) Identification of 14-3-3zeta as an EGF receptor interacting protein. FEBS Lett. 569 207-10 PubMed GONUTS page
↑ ^18.0 ^18.1 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
↑ ^19.0 ^19.1 ^19.2 ^19.3 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
↑ ^20.0 ^20.1 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
↑ ^21.0 ^21.1 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
↑ ^22.0 ^22.1 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
↑ ^23.0 ^23.1 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
↑ ^24.0 ^24.1 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
↑ ^25.0 ^25.1 ^25.2 ^25.3 ^25.4 ^25.5 Barr, AJ et al. (2009) Large-scale structural analysis of the classical human protein tyrosine phosphatome. Cell 136 352-63 PubMed GONUTS page
↑ ^26.0 ^26.1 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
↑ ^27.0 ^27.1 Liao, HJ & Carpenter, G (2009) Cetuximab/C225-induced intracellular trafficking of epidermal growth factor receptor. Cancer Res. 69 6179-83 PubMed GONUTS page
↑ ^28.0 ^28.1 Cheng, X et al. (2010) TRP channel regulates EGFR signaling in hair morphogenesis and skin barrier formation. Cell 141 331-43 PubMed GONUTS page
↑ ^29.0 ^29.1 Mueller, KL et al. (2010) EGFR/Met association regulates EGFR TKI resistance in breast cancer. J Mol Signal 5 8 PubMed GONUTS page
↑ ^30.0 ^30.1 ^30.2 ^30.3 ^30.4 ^30.5 Bill, A et al. (2010) Cytohesins are cytoplasmic ErbB receptor activators. Cell 143 201-11 PubMed GONUTS page
↑ ^31.0 ^31.1 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
↑ ^32.0 ^32.1 ^32.2 ^32.3 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
↑ ^33.0 ^33.1 ^33.2 ^33.3 Borg, JP et al. (1996) The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein. Mol. Cell. Biol. 16 6229-41 PubMed GONUTS page
↑ ^34.0 ^34.1 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
↑ ^35.0 ^35.1 ^35.2 ^35.3 Martín-Nieto, J & Villalobo, A (1998) The human epidermal growth factor receptor contains a juxtamembrane calmodulin-binding site. Biochemistry 37 227-36 PubMed GONUTS page
↑ ^36.0 ^36.1 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
↑ ^37.0 ^37.1 ^37.2 ^37.3 ^37.4 ^37.5 ^37.6 ^37.7 ^37.8 ^37.9 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
↑ ^38.0 ^38.1 ^38.2 ^38.3 Barbe, L et al. (2008) Toward a confocal subcellular atlas of the human proteome. Mol. Cell Proteomics 7 499-508 PubMed GONUTS page
↑ ^39.0 ^39.1 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
↑ Rosenthal, JA et al. (1999) The epsins define a family of proteins that interact with components of the clathrin coat and contain a new protein module. J. Biol. Chem. 274 33959-65 PubMed GONUTS page
↑ Rodrigues, GA et al. (2000) A novel positive feedback loop mediated by the docking protein Gab1 and phosphatidylinositol 3-kinase in epidermal growth factor receptor signaling. Mol. Cell. Biol. 20 1448-59 PubMed GONUTS page
↑ Gual, P et al. (2000) Sustained recruitment of phospholipase C-gamma to Gab1 is required for HGF-induced branching tubulogenesis. Oncogene 19 1509-18 PubMed GONUTS page
↑ Lock, LS et al. (2000) Identification of an atypical Grb2 carboxyl-terminal SH3 domain binding site in Gab docking proteins reveals Grb2-dependent and -independent recruitment of Gab1 to receptor tyrosine kinases. J. Biol. Chem. 275 31536-45 PubMed GONUTS page
↑ Waterman, H et al. (2002) A mutant EGF-receptor defective in ubiquitylation and endocytosis unveils a role for Grb2 in negative signaling. EMBO J. 21 303-13 PubMed GONUTS page
↑ Soubeyran, P et al. (2002) Cbl-CIN85-endophilin complex mediates ligand-induced downregulation of EGF receptors. Nature 416 183-7 PubMed GONUTS page
↑ Haglund, K et al. (2002) Cbl-directed monoubiquitination of CIN85 is involved in regulation of ligand-induced degradation of EGF receptors. Proc. Natl. Acad. Sci. U.S.A. 99 12191-6 PubMed GONUTS page
↑ Hall, AB et al. (2003) hSpry2 is targeted to the ubiquitin-dependent proteasome pathway by c-Cbl. Curr. Biol. 13 308-14 PubMed GONUTS page
↑ Agazie, YM & Hayman, MJ (2003) Molecular mechanism for a role of SHP2 in epidermal growth factor receptor signaling. Mol. Cell. Biol. 23 7875-86 PubMed GONUTS page
↑ Ren, Y et al. (2004) Roles of Gab1 and SHP2 in paxillin tyrosine dephosphorylation and Src activation in response to epidermal growth factor. J. Biol. Chem. 279 8497-505 PubMed GONUTS page
↑ Islam, R et al. (2004) Activation of EGF receptor kinase by L1-mediated homophilic cell interactions. Mol. Biol. Cell 15 2003-12 PubMed GONUTS page
↑ ^51.0 ^51.1 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
↑ Grøvdal, LM et al. (2004) Direct interaction of Cbl with pTyr 1045 of the EGF receptor (EGFR) is required to sort the EGFR to lysosomes for degradation. Exp. Cell Res. 300 388-95 PubMed GONUTS page
↑ Montagner, A et al. (2005) A novel role for Gab1 and SHP2 in epidermal growth factor-induced Ras activation. J. Biol. Chem. 280 5350-60 PubMed GONUTS page
↑ Haglund, K et al. (2005) Sprouty2 acts at the Cbl/CIN85 interface to inhibit epidermal growth factor receptor downregulation. EMBO Rep. 6 635-41 PubMed GONUTS page
↑ Schmidt, MH et al. (2006) Cbl escapes Cdc42-mediated inhibition by downregulation of the adaptor molecule betaPix. Oncogene 25 3071-8 PubMed GONUTS page
↑ Chardin, P et al. (1993) Human Sos1: a guanine nucleotide exchange factor for Ras that binds to GRB2. Science 260 1338-43 PubMed GONUTS page
↑ Sherrill, JM & Kyte, J (1996) Activation of epidermal growth factor receptor by epidermal growth factor. Biochemistry 35 5705-18 PubMed GONUTS page
↑ Lombardo, CR et al. (1995) In vitro phosphorylation of the epidermal growth factor receptor autophosphorylation domain by c-src: identification of phosphorylation sites and c-src SH2 domain binding sites. Biochemistry 34 16456-66 PubMed GONUTS page
↑ Holgado-Madruga, M et al. (1997) Grb2-associated binder-1 mediates phosphatidylinositol 3-kinase activation and the promotion of cell survival by nerve growth factor. Proc. Natl. Acad. Sci. U.S.A. 94 12419-24 PubMed GONUTS page
↑ Sakaguchi, K et al. (1998) Shc phosphotyrosine-binding domain dominantly interacts with epidermal growth factor receptors and mediates Ras activation in intact cells. Mol. Endocrinol. 12 536-43 PubMed GONUTS page
↑ Hernández-Sotomayor, SM & Carpenter, G (1992) Epidermal growth factor receptor: elements of intracellular communication. J. Membr. Biol. 128 81-9 PubMed GONUTS page
↑ ^62.0 ^62.1 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
↑ ^63.0 ^63.1 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
↑ ^64.0 ^64.1 Vermeer, PD et al. (2003) Segregation of receptor and ligand regulates activation of epithelial growth factor receptor. Nature 422 322-6 PubMed GONUTS page
↑ ^65.0 ^65.1 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
↑ ^66.0 ^66.1 ^66.2 ^66.3 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
↑ ^67.0 ^67.1 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
↑ ^68.0 ^68.1 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
↑ ^69.0 ^69.1 ^69.2 ^69.3 Edwin, F & Patel, TB (2008) A novel role of Sprouty 2 in regulating cellular apoptosis. J. Biol. Chem. 283 3181-90 PubMed GONUTS page
↑ ^70.0 ^70.1 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:12925580-1] 1.0 ^1.1 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:6325948-2] 2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 Mroczkowski, B et al. () ATP-stimulated interaction between epidermal growth factor receptor and supercoiled DNA. Nature 309 270-3 PubMed GONUTS page

[PMID:15542601-3] 3.0 ^3.1 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:14702346-4] 4.0 ^4.1 ^4.2 ^4.3 ^4.4 ^4.5 ^4.6 ^4.7 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:16076471-5] 5.0 ^5.1 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:17599051-6] 6.0 ^6.1 ^6.2 ^6.3 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:7736574-7] 7.0 ^7.1 ^7.2 ^7.3 ^7.4 ^7.5 ^7.6 ^7.7 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:12435727-8] 8.00 ^8.01 ^8.02 ^8.03 ^8.04 ^8.05 ^8.06 ^8.07 ^8.08 ^8.09 ^8.10 ^8.11 ^8.12 ^8.13 ^8.14 ^8.15 ^8.16 ^8.17 ^8.18 ^8.19 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:2790960-9] 9.0 ^9.1 ^9.2 ^9.3 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:10572067-10] 10.00 ^10.01 ^10.02 ^10.03 ^10.04 ^10.05 ^10.06 ^10.07 ^10.08 ^10.09 ^10.10 ^10.11 ^10.12 ^10.13 ^10.14 ^10.15 ^10.16 ^10.17 ^10.18 ^10.19 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:10805725-11] 11.0 ^11.1 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:11279102-12] 12.0 ^12.1 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:11853560-13] 13.0 ^13.1 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:12577067-14] 14.0 ^14.1 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:12620237-15] 15.0 ^15.1 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:14960328-16] 16.0 ^16.1 ^16.2 ^16.3 Li, H et al. (2004) Endogenous calmodulin interacts with the epidermal growth factor receptor in living cells. FEBS Lett. 559 175-80 PubMed GONUTS page

[PMID:15225635-17] 17.0 ^17.1 Oksvold, MP et al. (2004) Identification of 14-3-3zeta as an EGF receptor interacting protein. FEBS Lett. 569 207-10 PubMed GONUTS page

[PMID:16499958-18] 18.0 ^18.1 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:17182860-19] 19.0 ^19.1 ^19.2 ^19.3 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:17403676-20] 20.0 ^20.1 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:17909029-21] 21.0 ^21.1 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:18046415-22] 22.0 ^22.1 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:18455122-23] 23.0 ^23.1 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:18824549-24] 24.0 ^24.1 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:19167335-25] 25.0 ^25.1 ^25.2 ^25.3 ^25.4 ^25.5 Barr, AJ et al. (2009) Large-scale structural analysis of the classical human protein tyrosine phosphatome. Cell 136 352-63 PubMed GONUTS page

[PMID:19172738-26] 26.0 ^26.1 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:19602593-27] 27.0 ^27.1 Liao, HJ & Carpenter, G (2009) Cetuximab/C225-induced intracellular trafficking of epidermal growth factor receptor. Cancer Res. 69 6179-83 PubMed GONUTS page

[PMID:20403327-28] 28.0 ^28.1 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:20624308-29] 29.0 ^29.1 Mueller, KL et al. (2010) EGFR/Met association regulates EGFR TKI resistance in breast cancer. J Mol Signal 5 8 PubMed GONUTS page

[PMID:20946980-30] 30.0 ^30.1 ^30.2 ^30.3 ^30.4 ^30.5 Bill, A et al. (2010) Cytohesins are cytoplasmic ErbB receptor activators. Cell 143 201-11 PubMed GONUTS page

[PMID:2176151-31] 31.0 ^31.1 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] 32.0 ^32.1 ^32.2 ^32.3 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:8887653-33] 33.0 ^33.1 ^33.2 ^33.3 Borg, JP et al. (1996) The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein. Mol. Cell. Biol. 16 6229-41 PubMed GONUTS page

[PMID:9419975-34] 34.0 ^34.1 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:9425043-35] 35.0 ^35.1 ^35.2 ^35.3 Martín-Nieto, J & Villalobo, A (1998) The human epidermal growth factor receptor contains a juxtamembrane calmodulin-binding site. Biochemistry 37 227-36 PubMed GONUTS page

[PMID:9103388-36] 36.0 ^36.1 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:12828935-37] 37.0 ^37.1 ^37.2 ^37.3 ^37.4 ^37.5 ^37.6 ^37.7 ^37.8 ^37.9 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:18029348-38] 38.0 ^38.1 ^38.2 ^38.3 Barbe, L et al. (2008) Toward a confocal subcellular atlas of the human proteome. Mol. Cell Proteomics 7 499-508 PubMed GONUTS page

[PMID:7588596-39] 39.0 ^39.1 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:10567358-40] Rosenthal, JA et al. (1999) The epsins define a family of proteins that interact with components of the clathrin coat and contain a new protein module. J. Biol. Chem. 274 33959-65 PubMed GONUTS page

[PMID:10648629-41] Rodrigues, GA et al. (2000) A novel positive feedback loop mediated by the docking protein Gab1 and phosphatidylinositol 3-kinase in epidermal growth factor receptor signaling. Mol. Cell. Biol. 20 1448-59 PubMed GONUTS page

[PMID:10734310-42] Gual, P et al. (2000) Sustained recruitment of phospholipase C-gamma to Gab1 is required for HGF-induced branching tubulogenesis. Oncogene 19 1509-18 PubMed GONUTS page

[PMID:10913131-43] Lock, LS et al. (2000) Identification of an atypical Grb2 carboxyl-terminal SH3 domain binding site in Gab docking proteins reveals Grb2-dependent and -independent recruitment of Gab1 to receptor tyrosine kinases. J. Biol. Chem. 275 31536-45 PubMed GONUTS page

[PMID:11823423-44] Waterman, H et al. (2002) A mutant EGF-receptor defective in ubiquitylation and endocytosis unveils a role for Grb2 in negative signaling. EMBO J. 21 303-13 PubMed GONUTS page

[PMID:11894095-45] Soubeyran, P et al. (2002) Cbl-CIN85-endophilin complex mediates ligand-induced downregulation of EGF receptors. Nature 416 183-7 PubMed GONUTS page

[PMID:12218189-46] Haglund, K et al. (2002) Cbl-directed monoubiquitination of CIN85 is involved in regulation of ligand-induced degradation of EGF receptors. Proc. Natl. Acad. Sci. U.S.A. 99 12191-6 PubMed GONUTS page

[PMID:12593796-47] Hall, AB et al. (2003) hSpry2 is targeted to the ubiquitin-dependent proteasome pathway by c-Cbl. Curr. Biol. 13 308-14 PubMed GONUTS page

[PMID:14560030-48] Agazie, YM & Hayman, MJ (2003) Molecular mechanism for a role of SHP2 in epidermal growth factor receptor signaling. Mol. Cell. Biol. 23 7875-86 PubMed GONUTS page

[PMID:14665621-49] Ren, Y et al. (2004) Roles of Gab1 and SHP2 in paxillin tyrosine dephosphorylation and Src activation in response to epidermal growth factor. J. Biol. Chem. 279 8497-505 PubMed GONUTS page

[PMID:14718570-50] Islam, R et al. (2004) Activation of EGF receptor kinase by L1-mediated homophilic cell interactions. Mol. Biol. Cell 15 2003-12 PubMed GONUTS page

[PMID:15465819-51] 51.0 ^51.1 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

[PMID:15475003-52] Grøvdal, LM et al. (2004) Direct interaction of Cbl with pTyr 1045 of the EGF receptor (EGFR) is required to sort the EGFR to lysosomes for degradation. Exp. Cell Res. 300 388-95 PubMed GONUTS page

[PMID:15574420-53] Montagner, A et al. (2005) A novel role for Gab1 and SHP2 in epidermal growth factor-induced Ras activation. J. Biol. Chem. 280 5350-60 PubMed GONUTS page

[PMID:15962011-54] Haglund, K et al. (2005) Sprouty2 acts at the Cbl/CIN85 interface to inhibit epidermal growth factor receptor downregulation. EMBO Rep. 6 635-41 PubMed GONUTS page

[PMID:16407834-55] Schmidt, MH et al. (2006) Cbl escapes Cdc42-mediated inhibition by downregulation of the adaptor molecule betaPix. Oncogene 25 3071-8 PubMed GONUTS page

[PMID:8493579-56] Chardin, P et al. (1993) Human Sos1: a guanine nucleotide exchange factor for Ras that binds to GRB2. Science 260 1338-43 PubMed GONUTS page

[PMID:8639530-57] Sherrill, JM & Kyte, J (1996) Activation of epidermal growth factor receptor by epidermal growth factor. Biochemistry 35 5705-18 PubMed GONUTS page

[PMID:8845374-58] Lombardo, CR et al. (1995) In vitro phosphorylation of the epidermal growth factor receptor autophosphorylation domain by c-src: identification of phosphorylation sites and c-src SH2 domain binding sites. Biochemistry 34 16456-66 PubMed GONUTS page

[PMID:9356464-59] Holgado-Madruga, M et al. (1997) Grb2-associated binder-1 mediates phosphatidylinositol 3-kinase activation and the promotion of cell survival by nerve growth factor. Proc. Natl. Acad. Sci. U.S.A. 94 12419-24 PubMed GONUTS page

[PMID:9544989-60] Sakaguchi, K et al. (1998) Shc phosphotyrosine-binding domain dominantly interacts with epidermal growth factor receptors and mediates Ras activation in intact cells. Mol. Endocrinol. 12 536-43 PubMed GONUTS page

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