HUMAN:EGFR

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	EGFR (synonyms: ERBB, ERBB1, HER1)
Protein Name(s)	Epidermal growth factor receptor Proto-oncogene c-ErbB-1 Receptor tyrosine-protein kinase erbB-1
External Links
UniProt	P00533
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
CCDS	CCDS47587.1 CCDS5514.1 CCDS5515.1 CCDS5516.1
PIR	A00641
RefSeq	NP_005219.2 NP_958439.1 NP_958440.1 NP_958441.1
UniGene	Hs.488293 Hs.605083
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 2M0B 2M20 2RF9 2RFD 2RFE 2RGP 3B2U 3B2V 3BEL 3BUO 3C09 3G5V 3G5Y 3GOP 3GT8 3IKA 3LZB 3NJP 3OB2 3OP0 3P0Y 3PFV 3POZ 3QWQ 3UG1 3UG2 3VJN 3VJO 3VRP 3VRR 3W2O 3W2P 3W2Q 3W2R 3W2S 3W32 3W33 4G5J 4G5P 4HJO 4I1Z 4I20 4I21 4I22 4I23 4I24 4JQ7 4JQ8 4JR3 4JRV 4KRL 4KRM 4KRO 4KRP 4LI5 4LL0 4LQM 4LRM 4R5S 4TKS 4WKQ 4WRG
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 2M0B 2M20 2RF9 2RFD 2RFE 2RGP 3B2U 3B2V 3BEL 3BUO 3C09 3G5V 3G5Y 3GOP 3GT8 3IKA 3LZB 3NJP 3OB2 3OP0 3P0Y 3PFV 3POZ 3QWQ 3UG1 3UG2 3VJN 3VJO 3VRP 3VRR 3W2O 3W2P 3W2Q 3W2R 3W2S 3W32 3W33 4G5J 4G5P 4HJO 4I1Z 4I20 4I21 4I22 4I23 4I24 4JQ7 4JQ8 4JR3 4JRV 4KRL 4KRM 4KRO 4KRP 4LI5 4LL0 4LQM 4LRM 4R5S 4TKS 4WKQ 4WRG
DisProt	DP00309
ProteinModelPortal	P00533
SMR	P00533
BioGrid	108276
DIP	DIP-405N
IntAct	P00533
MINT	MINT-206389
BindingDB	P00533
ChEMBL	CHEMBL2363049
DrugBank	DB08916 DB00002 DB00530 DB00317 DB01259 DB00281 DB01269 DB00072 DB05294
GuidetoPHARMACOLOGY	1797
PhosphoSite	P00533
UniCarbKB	P00533
DMDM	2811086
SWISS-2DPAGE	P00533
MaxQB	P00533
PaxDb	P00533
PeptideAtlas	P00533
PRIDE	P00533
DNASU	1956
Ensembl	ENST00000275493 ENST00000342916 ENST00000344576 ENST00000420316
GeneID	1956
KEGG	hsa:1956
UCSC	uc003tqh.3 uc003tqi.3 uc003tqj.3 uc003tqk.3
CTD	1956
GeneCards	GC07P055054
HGNC	HGNC:3236
HPA	CAB000035 HPA001200 HPA018530
MIM	131550 211980
neXtProt	NX_P00533
Orphanet	251579 251576 357191
PharmGKB	PA7360
eggNOG	COG0515
GeneTree	ENSGT00760000118799
HOVERGEN	HBG000490
InParanoid	P00533
KO	K04361
OMA	FYRTLME
PhylomeDB	P00533
TreeFam	TF106002
BRENDA	2.7.10.1
Reactome	REACT_115596 REACT_115720 REACT_115755 REACT_115852 REACT_115854 REACT_115993 REACT_116008 REACT_121096 REACT_12478 REACT_12484 REACT_12578 REACT_12579 REACT_12606 REACT_147727 REACT_22272 REACT_75829 REACT_9417
SignaLink	P00533
ChiTaRS	EGFR
EvolutionaryTrace	P00533
GeneWiki	Epidermal_growth_factor_receptor
GenomeRNAi	1956
NextBio	7931
PMAP-CutDB	P00533
PRO	PR:P00533
Proteomes	UP000005640
Bgee	P00533
ExpressionAtlas	P00533
Genevestigator	P00533
GO	GO:0016324 GO:0016323 GO:0009986 GO:0005737 GO:0030139 GO:0005789 GO:0005768 GO:0010008 GO:0005615 GO:0005925 GO:0000139 GO:0016021 GO:0016020 GO:0045121 GO:0031965 GO:0005634 GO:0048471 GO:0005886 GO:0043235 GO:0070435 GO:0051015 GO:0005524 GO:0003682 GO:0003690 GO:0019899 GO:0005006 GO:0042802 GO:0004709 GO:0046982 GO:0019903 GO:0004713 GO:0004716 GO:0004714 GO:0004888 GO:0031625 GO:0043006 GO:0007202 GO:0019694 GO:0048143 GO:0007411 GO:0008283 GO:0007166 GO:0071230 GO:0071549 GO:0035690 GO:0071364 GO:0071392 GO:0071260 GO:0021795 GO:0007623 GO:0048546 GO:0016101 GO:0001892 GO:0007173 GO:0038095 GO:0008543 GO:0001942 GO:0042743 GO:0045087 GO:0007611 GO:0001889 GO:0030324 GO:0010960 GO:0000165 GO:0060571 GO:0043066 GO:0042059 GO:0045930 GO:0042177 GO:0048011 GO:0001503 GO:0042698 GO:0018108 GO:0048015 GO:0035413 GO:0030335 GO:0008284 GO:0031659 GO:0045739 GO:0045740 GO:0050679 GO:0070374 GO:0048146 GO:0050729 GO:0043406 GO:0045429 GO:0042327 GO:0051897 GO:0001934 GO:0048661 GO:0032930 GO:0051968 GO:0045944 GO:0045907 GO:0045909 GO:0046777 GO:0051205 GO:0050999 GO:0050730 GO:0051592 GO:0033590 GO:0033594 GO:0006970 GO:0006979 GO:0006950 GO:0070141 GO:0007435 GO:0007165 GO:0016337 GO:0043586 GO:0006412
Gene3D	3.80.20.20
InterPro	IPR006211 IPR006212 IPR009030 IPR011009 IPR000719 IPR017441 IPR000494 IPR001245 IPR008266 IPR020635 IPR016245
Pfam	PF00757 PF07714 PF01030
PIRSF	PIRSF000619
PRINTS	PR00109
SMART	SM00261 SM00219
SUPFAM	SSF56112 SSF57184
PROSITE	PS00107 PS50011 PS00109

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
enables	GO:0019903	protein phosphatase binding	PMID:28759036^[1]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P51452	F		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:22298428^[2]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:22298428^[2]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:1900087	positive regulation of G1/S transition of mitotic cell cycle	PMID:18483258^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0046328	regulation of JNK cascade	PMID:26514923^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0014066	regulation of phosphatidylinositol 3-kinase signaling	PMID:26514923^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0070372	regulation of ERK1 and ERK2 cascade	PMID:26514923^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1901224	positive regulation of NIK/NF-kappaB signaling	PMID:26514923^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045893	positive regulation of transcription, DNA-templated	PMID:26514923^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0071276	cellular response to cadmium ion	PMID:26514923^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0034614	cellular response to reactive oxygen species	PMID:26514923^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:20878056^[5]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0004713	protein tyrosine kinase activity	PMID:20878056^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0038083	peptidyl-tyrosine autophosphorylation	PMID:20878056^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0033138	positive regulation of peptidyl-serine phosphorylation	PMID:20878056^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007173	epidermal growth factor receptor signaling pathway	PMID:20878056^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
colocalizes_with	GO:0005768	endosome	PMID:16554368^[6]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:1905208	negative regulation of cardiocyte differentiation	PMID:23069713^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_in:(CL:0000134)	Seeded From UniProt	complete
involved_in	GO:0008284	positive regulation of cell population proliferation	PMID:27057632^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0030335	positive regulation of cell migration	PMID:25678558^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0045296	cadherin binding	PMID:25468996^[10]	ECO:0007005	high throughput direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:22732145^[11]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005768	endosome	PMID:22732145^[11]	ECO:0000314	direct assay evidence used in manual assertion		C	exists_during:(GO:0004697)	Seeded From UniProt	complete
involved_in	GO:1900020	positive regulation of protein kinase C activity	PMID:22732145^[11]	ECO:0000314	direct assay evidence used in manual assertion		P	positively_regulates:(GO:0072659)	Seeded From UniProt	complete
involved_in	GO:1903078	positive regulation of protein localization to plasma membrane	PMID:22732145^[11]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P52824)	Seeded From UniProt	complete
involved_in	GO:1903800	positive regulation of production of miRNAs involved in gene silencing by miRNA	PMID:21673316^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0070374	positive regulation of ERK1 and ERK2 cascade	PMID:21673316^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0009986	cell surface	PMID:25666625^[13]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0097489	multivesicular body, internal vesicle lumen	PMID:17714434^[14]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0031901	early endosome membrane	PMID:17714434^[14]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0031625	ubiquitin protein ligase binding	PMID:23418353^[15]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9D0C1	F		Seeded From UniProt	complete
enables	GO:0031625	ubiquitin protein ligase binding	PMID:23418353^[15]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q91YL2	F		Seeded From UniProt	complete
part_of	GO:0010008	endosome membrane	PMID:22719997^[16]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005925	focal adhesion	PMID:21423176^[17]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0000057)	Seeded From UniProt	complete
involved_in	GO:0030307	positive regulation of cell growth	PMID:15467833^[18]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0005006	epidermal growth factor-activated receptor activity	PMID:22732145^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0018108	peptidyl-tyrosine phosphorylation	PMID:22732145^[11]	ECO:0000314	direct assay evidence used in manual assertion		P	has_input:(UniProtKB:P52824)	Seeded From UniProt	complete
part_of	GO:0070435	Shc-EGFR complex	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q9QX70	C		Seeded From UniProt	complete
involved_in	GO:0070141	response to UV-A	PMID:18483258^[3]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051897	positive regulation of protein kinase B signaling	PMID:17655843^[19]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0090263	positive regulation of canonical Wnt signaling pathway	PMID:20302655^[20]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045737	positive regulation of cyclin-dependent protein serine/threonine kinase activity	PMID:18483258^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0016323	basolateral plasma membrane	PMID:12646923^[21]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:15465819^[22]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0071392	cellular response to estradiol stimulus	PMID:20551055^[23]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0071364	cellular response to epidermal growth factor stimulus	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:G3V6K6	P		Seeded From UniProt	complete
involved_in	GO:0070374	positive regulation of ERK1 and ERK2 cascade	PMID:20551055^[23]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0051015	actin filament binding	PMID:14702346^[24]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0050999	regulation of nitric-oxide synthase activity	PMID:12828935^[25]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0050730	regulation of peptidyl-tyrosine phosphorylation	PMID:12435727^[26]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0050679	positive regulation of epithelial cell proliferation	PMID:10572067^[27]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0046982	protein heterodimerization activity	PMID:10572067^[27]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0046777	protein autophosphorylation	PMID:18070883^[28]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045944	positive regulation of transcription by RNA polymerase II	PMID:20551055^[23]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045740	positive regulation of DNA replication	PMID:17115032^[29]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045739	positive regulation of DNA repair	PMID:17115032^[29]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010750	positive regulation of nitric oxide mediated signal transduction	PMID:12828935^[25]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0045121	membrane raft	PMID:12009895^[30]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0043406	positive regulation of MAP kinase activity	PMID:10572067^[27]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043066	negative regulation of apoptotic process	PMID:18070883^[28]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0042327	positive regulation of phosphorylation	PMID:15082764^[31]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0042177	negative regulation of protein catabolic process	PMID:17115032^[29]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0030335	positive regulation of cell migration	PMID:12435727^[26]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
contributes_to	GO:0030235	nitric-oxide synthase regulator activity	PMID:12828935^[25]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0019903	protein phosphatase binding	PMID:15899872^[32]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q15262	F		Seeded From UniProt	complete
enables	GO:0019899	enzyme binding	PMID:12009895^[30]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O15162	F		Seeded From UniProt	complete
involved_in	GO:0098609	cell-cell adhesion	PMID:12435727^[26]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0016020	membrane	PMID:12435727^[26]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0008283	cell population proliferation	PMID:17115032^[29]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007611	learning or memory	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:G3V6K6	P		Seeded From UniProt	complete
involved_in	GO:0007173	epidermal growth factor receptor signaling pathway	PMID:12435727^[26]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007165	signal transduction	PMID:10572067^[27]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005768	endosome	PMID:17182860^[33]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005768	endosome	PMID:14702346^[24]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:12435727^[26]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:7588596^[34]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:20551055^[23]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:17115032^[29]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:12828935^[25]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:9103388^[35]	ECO:0000303	author statement without traceable support used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0005006	epidermal growth factor-activated receptor activity	PMID:17115032^[29]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0005006	epidermal growth factor-activated receptor activity	PMID:12435727^[26]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0005006	epidermal growth factor-activated receptor activity	PMID:6325948^[36]	ECO:0000303	author statement without traceable support used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0005006	epidermal growth factor-activated receptor activity	PMID:2790960^[37]	ECO:0000303	author statement without traceable support used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004713	protein tyrosine kinase activity	PMID:14702346^[24]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004713	protein tyrosine kinase activity	PMID:17115032^[29]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004713	protein tyrosine kinase activity	PMID:17599051^[38]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004709	MAP kinase kinase kinase activity	PMID:15542601^[39]	ECO:0000303	author statement without traceable support used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003690	double-stranded DNA binding	PMID:6325948^[36]	ECO:0000303	author statement without traceable support used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003682	chromatin binding	PMID:20551055^[23]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0001934	positive regulation of protein phosphorylation	PMID:20551055^[23]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0001503	ossification	PMID:12925580^[40]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0050679	positive regulation of epithelial cell proliferation	PMID:21873635^[41]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:95294 PANTHER:PTN002814603 UniProtKB:P00533	P		Seeded From UniProt	complete
enables	GO:0048408	epidermal growth factor binding	PMID:21873635^[41]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:95294 PANTHER:PTN000698838 RGD:2543	F		Seeded From UniProt	complete
part_of	GO:0043235	receptor complex	PMID:21873635^[41]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0015380 FB:FBgn0024245 FB:FBgn0033791 PANTHER:PTN002356460 UniProtKB:A6QR62 UniProtKB:O15146 UniProtKB:P00533 UniProtKB:P04626 UniProtKB:P04629 UniProtKB:P06213 UniProtKB:P07949 UniProtKB:P08069 UniProtKB:P11362 UniProtKB:P14616 UniProtKB:P17948 UniProtKB:P21860 UniProtKB:P35916 UniProtKB:Q01973 UniProtKB:Q08345 UniProtKB:Q15303 UniProtKB:Q16288 UniProtKB:Q16620	C		Seeded From UniProt	complete
involved_in	GO:0043066	negative regulation of apoptotic process	PMID:21873635^[41]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002814603 RGD:2543 UniProtKB:P00533	P		Seeded From UniProt	complete
involved_in	GO:0030154	cell differentiation	PMID:21873635^[41]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002814603 RGD:2543	P		Seeded From UniProt	complete
part_of	GO:0009925	basal plasma membrane	PMID:21873635^[41]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000698827 RGD:2561	C		Seeded From UniProt	complete
involved_in	GO:0008284	positive regulation of cell population proliferation	PMID:21873635^[41]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0003731 MGI:MGI:104771 MGI:MGI:95294 PANTHER:PTN000698827 RGD:2543 RGD:2561 RGD:620486 UniProtKB:P00533 UniProtKB:P04626 UniProtKB:Q15303	P		Seeded From UniProt	complete
involved_in	GO:0007169	transmembrane receptor protein tyrosine kinase signaling pathway	PMID:21873635^[41]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0003366 FB:FBgn0003731 FB:FBgn0003733 FB:FBgn0283499 MGI:MGI:104757 MGI:MGI:109378 MGI:MGI:1096337 MGI:MGI:1339758 MGI:MGI:1345277 MGI:MGI:95276 MGI:MGI:95278 MGI:MGI:95294 MGI:MGI:95522 MGI:MGI:95523 MGI:MGI:95524 MGI:MGI:95525 MGI:MGI:95558 MGI:MGI:95561 MGI:MGI:96575 MGI:MGI:96677 MGI:MGI:96683 MGI:MGI:96969 MGI:MGI:97384 MGI:MGI:97530 MGI:MGI:97531 MGI:MGI:97902 MGI:MGI:98277 MGI:MGI:99216 MGI:MGI:99611 MGI:MGI:99612 MGI:MGI:99654 PANTHER:PTN002356460 RGD:2543 RGD:2611 RGD:2612 RGD:2621 RGD:2869 RGD:2917 RGD:2965 RGD:3082 RGD:3213 RGD:3214 RGD:3284 RGD:3285 RGD:620144 RGD:620714 RGD:620831 RGD:621737 RGD:69323 UniProtKB:A6QR62 UniProtKB:P00533 UniProtKB:P04626 UniProtKB:P04629 UniProtKB:P06213 UniProtKB:P07949 UniProtKB:P08069 UniProtKB:P09619 UniProtKB:P10721 UniProtKB:P11362 UniProtKB:P16234 UniProtKB:P17948 UniProtKB:P21709 UniProtKB:P21802 UniProtKB:P22455 UniProtKB:P22607 UniProtKB:P29317 UniProtKB:P29320 UniProtKB:P35916 UniProtKB:P35968 UniProtKB:P54753 UniProtKB:P54760 UniProtKB:P54762 UniProtKB:P54764 UniProtKB:Q02763 UniProtKB:Q08345 UniProtKB:Q15303 UniProtKB:Q15375 UniProtKB:Q16288 UniProtKB:Q16620 UniProtKB:Q16832 UniProtKB:Q5JZY3 UniProtKB:Q91987 WB:WBGene00001184 WB:WBGene00006868 ZFIN:ZDB-GENE-020503-1 ZFIN:ZDB-GENE-020503-2 ZFIN:ZDB-GENE-060503-14 ZFIN:ZDB-GENE-070713-2 ZFIN:ZDB-GENE-980526-255 ZFIN:ZDB-GENE-980526-326 ZFIN:ZDB-GENE-990415-62	P		Seeded From UniProt	complete
part_of	GO:0005887	integral component of plasma membrane	PMID:21873635^[41]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0003366 FB:FBgn0003731 FB:FBgn0003733 FB:FBgn0011829 FB:FBgn0015380 FB:FBgn0032006 FB:FBgn0283499 MGI:MGI:103581 MGI:MGI:104771 MGI:MGI:109378 MGI:MGI:98277 MGI:MGI:99611 PANTHER:PTN002356460 RGD:1560587 RGD:3213 RGD:3214 RGD:70957 UniProtKB:P04629 UniProtKB:P06213 UniProtKB:P07949 UniProtKB:P16234 UniProtKB:P17948 UniProtKB:P21709 UniProtKB:P21802 UniProtKB:P22455 UniProtKB:P22607 UniProtKB:P29317 UniProtKB:P29320 UniProtKB:P35968 UniProtKB:P54753 UniProtKB:P54760 UniProtKB:P54762 UniProtKB:Q02763 UniProtKB:Q16620 UniProtKB:Q9UM73 WB:WBGene00000289 WB:WBGene00000898	C		Seeded From UniProt	complete
enables	GO:0005006	epidermal growth factor-activated receptor activity	PMID:21873635^[41]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:95294 PANTHER:PTN000698838 RGD:2543 UniProtKB:P00533	F		Seeded From UniProt	complete
enables	GO:0004714	transmembrane receptor protein tyrosine kinase activity	PMID:21873635^[41]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0003733 FB:FBgn0040505 FB:FBgn0283499 MGI:MGI:109378 MGI:MGI:1339758 MGI:MGI:1345277 MGI:MGI:95276 MGI:MGI:95294 MGI:MGI:95522 MGI:MGI:95524 MGI:MGI:95558 MGI:MGI:95561 MGI:MGI:96677 MGI:MGI:96683 MGI:MGI:96969 MGI:MGI:97384 MGI:MGI:97530 MGI:MGI:97902 MGI:MGI:98277 MGI:MGI:99611 MGI:MGI:99612 MGI:MGI:99654 PANTHER:PTN002356460 RGD:2543 RGD:2611 RGD:2621 RGD:2869 RGD:2917 RGD:2965 RGD:3082 RGD:3213 RGD:3214 RGD:3284 RGD:3285 RGD:620144 RGD:620714 RGD:620831 RGD:621737 UniProtKB:P00533 UniProtKB:P04626 UniProtKB:P04629 UniProtKB:P06213 UniProtKB:P07333 UniProtKB:P07949 UniProtKB:P08069 UniProtKB:P09619 UniProtKB:P10721 UniProtKB:P11362 UniProtKB:P14616 UniProtKB:P16234 UniProtKB:P17948 UniProtKB:P21709 UniProtKB:P21802 UniProtKB:P22455 UniProtKB:P22607 UniProtKB:P29317 UniProtKB:P29320 UniProtKB:P35916 UniProtKB:P35968 UniProtKB:P54753 UniProtKB:P54760 UniProtKB:P54762 UniProtKB:Q08345 UniProtKB:Q15303 UniProtKB:Q16620 UniProtKB:Q16832 UniProtKB:Q5JZY3 UniProtKB:Q91987 UniProtKB:Q9UM73 WB:WBGene00000289 WB:WBGene00006868 WB:WBGene00020504 ZFIN:ZDB-GENE-980526-255	F		Seeded From UniProt	complete
part_of	GO:0043235	receptor complex	PMID:23382219^[42]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0008284	positive regulation of cell population proliferation	PMID:7736574^[43]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007173	epidermal growth factor receptor signaling pathway	PMID:7736574^[43]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007166	cell surface receptor signaling pathway	PMID:7736574^[43]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0004888	transmembrane signaling receptor activity	PMID:7736574^[43]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:24135280^[44]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P00533	F	occurs_in:(GO:0005938)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:23636329^[45]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P00533	F	occurs_in:(GO:0005938)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:23436906^[46]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P00533	F	occurs_in:(GO:0005938)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:23374349^[47]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P00533	F	occurs_in:(GO:0005938)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:23273428^[48]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P00533	F	occurs_in:(GO:0005938)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:22579287^[49]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P00533	F	occurs_in:(GO:0005938)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:22232519^[50]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P00533	F	occurs_in:(GO:0005938)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:21482778^[51]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P00533	F	occurs_in:(GO:0005938)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:21480528^[52]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P00533	F	occurs_in:(GO:0005938)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:21278786^[53]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P00533	F	occurs_in:(GO:0005938)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:20359299^[54]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P00533	F	occurs_in:(GO:0005938)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:20029029^[55]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P00533	F	occurs_in:(GO:0005938)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:20007378^[56]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P00533	F	occurs_in:(GO:0005938)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:19650109^[57]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P00533	F	occurs_in:(GO:0005938)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:19563760^[58]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P00533	F	occurs_in:(GO:0005938)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:18042729^[59]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P00533	F	occurs_in:(GO:0005938)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:17148612^[60]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P00533	F	occurs_in:(GO:0005938)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:16777603^[61]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P00533	F	occurs_in:(GO:0005938)	Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0046718	viral entry into host cell	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0001618	P		Seeded From UniProt	complete
involved_in	GO:1902722	positive regulation of prolactin secretion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	P		Seeded From UniProt	complete
involved_in	GO:0097755	positive regulation of blood vessel diameter	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	P		Seeded From UniProt	complete
involved_in	GO:0097421	liver regeneration	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	P		Seeded From UniProt	complete
involved_in	GO:0071549	cellular response to dexamethasone stimulus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	P		Seeded From UniProt	complete
involved_in	GO:0071364	cellular response to epidermal growth factor stimulus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	P		Seeded From UniProt	complete
involved_in	GO:0071363	cellular response to growth factor stimulus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	P		Seeded From UniProt	complete
involved_in	GO:0071260	cellular response to mechanical stimulus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	P		Seeded From UniProt	complete
involved_in	GO:0051968	positive regulation of synaptic transmission, glutamatergic	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	P		Seeded From UniProt	complete
involved_in	GO:0051592	response to calcium ion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	P		Seeded From UniProt	complete
involved_in	GO:0050729	positive regulation of inflammatory response	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	P		Seeded From UniProt	complete
involved_in	GO:0048812	neuron projection morphogenesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	P		Seeded From UniProt	complete
involved_in	GO:0048661	positive regulation of smooth muscle cell proliferation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	P		Seeded From UniProt	complete
enables	GO:0048408	epidermal growth factor binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	F		Seeded From UniProt	complete
involved_in	GO:0048143	astrocyte activation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	P		Seeded From UniProt	complete
enables	GO:0046982	protein heterodimerization activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	F		Seeded From UniProt	complete
involved_in	GO:0046777	protein autophosphorylation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	P		Seeded From UniProt	complete
involved_in	GO:0045930	negative regulation of mitotic cell cycle	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	P		Seeded From UniProt	complete
involved_in	GO:0045907	positive regulation of vasoconstriction	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	P		Seeded From UniProt	complete
involved_in	GO:0045780	positive regulation of bone resorption	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	P		Seeded From UniProt	complete
part_of	GO:0045202	synapse	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	C		Seeded From UniProt	complete
part_of	GO:0045121	membrane raft	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	C		Seeded From UniProt	complete
involved_in	GO:0043586	tongue development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	P		Seeded From UniProt	complete
involved_in	GO:0043066	negative regulation of apoptotic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	P		Seeded From UniProt	complete
involved_in	GO:0042743	hydrogen peroxide metabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	P		Seeded From UniProt	complete
involved_in	GO:0042698	ovulation cycle	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	P		Seeded From UniProt	complete
involved_in	GO:0042060	wound healing	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	P		Seeded From UniProt	complete
involved_in	GO:0035690	cellular response to drug	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	P		Seeded From UniProt	complete
involved_in	GO:0035556	intracellular signal transduction	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	P		Seeded From UniProt	complete
involved_in	GO:0033993	response to lipid	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	P		Seeded From UniProt	complete
involved_in	GO:0033594	response to hydroxyisoflavone	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	P		Seeded From UniProt	complete
involved_in	GO:0033590	response to cobalamin	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	P		Seeded From UniProt	complete
involved_in	GO:0032930	positive regulation of superoxide anion generation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	P		Seeded From UniProt	complete
involved_in	GO:0032355	response to estradiol	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	P		Seeded From UniProt	complete
enables	GO:0031625	ubiquitin protein ligase binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	F		Seeded From UniProt	complete
involved_in	GO:0030324	lung development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	P		Seeded From UniProt	complete
part_of	GO:0030139	endocytic vesicle	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	C		Seeded From UniProt	complete
enables	GO:0019901	protein kinase binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	F		Seeded From UniProt	complete
involved_in	GO:0018108	peptidyl-tyrosine phosphorylation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	P		Seeded From UniProt	complete
part_of	GO:0016324	apical plasma membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	C		Seeded From UniProt	complete
part_of	GO:0016323	basolateral plasma membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	C		Seeded From UniProt	complete
involved_in	GO:0016101	diterpenoid metabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	P		Seeded From UniProt	complete
involved_in	GO:0014070	response to organic cyclic compound	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	P		Seeded From UniProt	complete
involved_in	GO:0010960	magnesium ion homeostasis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	P		Seeded From UniProt	complete
part_of	GO:0009986	cell surface	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	C		Seeded From UniProt	complete
involved_in	GO:0007623	circadian rhythm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	P		Seeded From UniProt	complete
involved_in	GO:0007611	learning or memory	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	P		Seeded From UniProt	complete
involved_in	GO:0007494	midgut development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	P		Seeded From UniProt	complete
involved_in	GO:0007173	epidermal growth factor receptor signaling pathway	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	P		Seeded From UniProt	complete
involved_in	GO:0007165	signal transduction	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	P		Seeded From UniProt	complete
involved_in	GO:0006979	response to oxidative stress	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	P		Seeded From UniProt	complete
involved_in	GO:0006970	response to osmotic stress	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	P		Seeded From UniProt	complete
involved_in	GO:0006412	translation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	P		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	C		Seeded From UniProt	complete
part_of	GO:0005768	endosome	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	C		Seeded From UniProt	complete
enables	GO:0005516	calmodulin binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	F		Seeded From UniProt	complete
enables	GO:0005178	integrin binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	F		Seeded From UniProt	complete
enables	GO:0005102	signaling receptor binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	F		Seeded From UniProt	complete
enables	GO:0005006	epidermal growth factor-activated receptor activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	F		Seeded From UniProt	complete
enables	GO:0004713	protein tyrosine kinase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	F		Seeded From UniProt	complete
involved_in	GO:0001942	hair follicle development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	P		Seeded From UniProt	complete
involved_in	GO:0001889	liver development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	P		Seeded From UniProt	complete
involved_in	GO:0000186	activation of MAPKK activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V6K6 ensembl:ENSRNOP00000006087	P		Seeded From UniProt	complete
involved_in	GO:0071363	cellular response to growth factor stimulus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q01279 ensembl:ENSMUSP00000020329	P		Seeded From UniProt	complete
involved_in	GO:0071230	cellular response to amino acid stimulus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q01279 ensembl:ENSMUSP00000020329	P		Seeded From UniProt	complete
involved_in	GO:0061029	eyelid development in camera-type eye	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q01279 ensembl:ENSMUSP00000020329	P		Seeded From UniProt	complete
involved_in	GO:0060571	morphogenesis of an epithelial fold	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q01279 ensembl:ENSMUSP00000020329	P		Seeded From UniProt	complete
involved_in	GO:0050730	regulation of peptidyl-tyrosine phosphorylation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q01279 ensembl:ENSMUSP00000020329	P		Seeded From UniProt	complete
involved_in	GO:0050679	positive regulation of epithelial cell proliferation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q01279 ensembl:ENSMUSP00000020329	P		Seeded From UniProt	complete
involved_in	GO:0048546	digestive tract morphogenesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q01279 ensembl:ENSMUSP00000020329	P		Seeded From UniProt	complete
part_of	GO:0048471	perinuclear region of cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q01279 ensembl:ENSMUSP00000020329	C		Seeded From UniProt	complete
enables	GO:0048408	epidermal growth factor binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q01279 ensembl:ENSMUSP00000020329	F		Seeded From UniProt	complete
involved_in	GO:0048146	positive regulation of fibroblast proliferation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q01279 ensembl:ENSMUSP00000020329	P		Seeded From UniProt	complete
involved_in	GO:0046777	protein autophosphorylation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q01279 ensembl:ENSMUSP00000020329	P		Seeded From UniProt	complete
involved_in	GO:0042127	regulation of cell population proliferation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q01279 ensembl:ENSMUSP00000020329	P		Seeded From UniProt	complete
part_of	GO:0030139	endocytic vesicle	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q01279 ensembl:ENSMUSP00000020329	C		Seeded From UniProt	complete
involved_in	GO:0021795	cerebral cortex cell migration	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q01279 ensembl:ENSMUSP00000020329	P		Seeded From UniProt	complete
part_of	GO:0016323	basolateral plasma membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q01279 ensembl:ENSMUSP00000020329	C		Seeded From UniProt	complete
enables	GO:0016301	kinase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q01279 ensembl:ENSMUSP00000020329	F		Seeded From UniProt	complete
part_of	GO:0009986	cell surface	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q01279 ensembl:ENSMUSP00000020329	C		Seeded From UniProt	complete
involved_in	GO:0008544	epidermis development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q01279 ensembl:ENSMUSP00000020329	P		Seeded From UniProt	complete
involved_in	GO:0008284	positive regulation of cell population proliferation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q01279 ensembl:ENSMUSP00000020329	P		Seeded From UniProt	complete
involved_in	GO:0007435	salivary gland morphogenesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q01279 ensembl:ENSMUSP00000020329	P		Seeded From UniProt	complete
involved_in	GO:0007173	epidermal growth factor receptor signaling pathway	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q01279 ensembl:ENSMUSP00000020329	P		Seeded From UniProt	complete
involved_in	GO:0007165	signal transduction	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q01279 ensembl:ENSMUSP00000020329	P		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q01279 ensembl:ENSMUSP00000020329	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q01279 ensembl:ENSMUSP00000020329	C		Seeded From UniProt	complete
enables	GO:0005006	epidermal growth factor-activated receptor activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q01279 ensembl:ENSMUSP00000020329	F		Seeded From UniProt	complete
involved_in	GO:0001942	hair follicle development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q01279 ensembl:ENSMUSP00000020329	P		Seeded From UniProt	complete
involved_in	GO:0001892	embryonic placenta development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q01279 ensembl:ENSMUSP00000020329	P		Seeded From UniProt	complete
involved_in	GO:0000902	cell morphogenesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q01279 ensembl:ENSMUSP00000020329	P		Seeded From UniProt	complete
enables	GO:0004672	protein kinase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000719 InterPro:IPR001245 InterPro:IPR008266	F		Seeded From UniProt	complete
enables	GO:0004713	protein tyrosine kinase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR016245 InterPro:IPR020635	F		Seeded From UniProt	complete
enables	GO:0004714	transmembrane receptor protein tyrosine kinase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR006211	F		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000719 InterPro:IPR006211 InterPro:IPR016245 InterPro:IPR017441	F		Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000719 InterPro:IPR001245 InterPro:IPR006211 InterPro:IPR008266 InterPro:IPR016245 InterPro:IPR020635	P		Seeded From UniProt	complete
involved_in	GO:0007169	transmembrane receptor protein tyrosine kinase signaling pathway	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR006211 InterPro:IPR016245	P		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR006211	C		Seeded From UniProt	complete
part_of	GO:0016021	integral component of membrane	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR016245	C		Seeded From UniProt	complete
enables	GO:0004714	transmembrane receptor protein tyrosine kinase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:2.7.10.1	F		Seeded From UniProt	complete
involved_in	GO:0038083	peptidyl-tyrosine autophosphorylation	PMID:22732145^[11]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051205	protein insertion into membrane	PMID:12435727^[26]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043006	activation of phospholipase A2 activity by calcium-mediated signaling	PMID:12435727^[26]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007202	activation of phospholipase C activity	PMID:12435727^[26]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0004713	protein tyrosine kinase activity	PMID:16076471^[62] Reactome:R-HSA-8867041 Reactome:R-HSA-212710 Reactome:R-HSA-183058 Reactome:R-HSA-182969 Reactome:R-HSA-177934 Reactome:R-HSA-177930	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0030665	clathrin-coated vesicle membrane	Reactome:R-HSA-8871193 Reactome:R-HSA-8869438 Reactome:R-HSA-8868661 Reactome:R-HSA-8868660 Reactome:R-HSA-8868659 Reactome:R-HSA-8868658 Reactome:R-HSA-8871194	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0007173	epidermal growth factor receptor signaling pathway	Reactome:R-HSA-177929	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007165	signal transduction	Reactome:R-HSA-212718	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006357	regulation of transcription by RNA polymerase II	Reactome:R-HSA-8866910	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	Reactome:R-NUL-1251929 Reactome:R-NUL-1251923 Reactome:R-NUL-1248744 Reactome:R-HSA-9018573 Reactome:R-HSA-9018572 Reactome:R-HSA-8951490 Reactome:R-HSA-8874797 Reactome:R-HSA-8868661 Reactome:R-HSA-8868651 Reactome:R-HSA-8868648 Reactome:R-HSA-8868236 Reactome:R-HSA-8868230 Reactome:R-HSA-8868072 Reactome:R-HSA-8868071 Reactome:R-HSA-8867756 Reactome:R-HSA-8867754 Reactome:R-HSA-8867047 Reactome:R-HSA-8867044 Reactome:R-HSA-8867041 Reactome:R-HSA-8866279 Reactome:R-HSA-8864125 Reactome:R-HSA-8864105 Reactome:R-HSA-8864029 Reactome:R-HSA-8863804 Reactome:R-HSA-8857583 Reactome:R-HSA-8857577 Reactome:R-HSA-8857565 Reactome:R-HSA-8857555 Reactome:R-HSA-8857549 Reactome:R-HSA-8848005 Reactome:R-HSA-8847995 Reactome:R-HSA-6785648 Reactome:R-HSA-6785636 Reactome:R-HSA-5672965 Reactome:R-HSA-5638137 Reactome:R-HSA-5637808 Reactome:R-HSA-5637806 Reactome:R-HSA-5637801 Reactome:R-HSA-5637800 Reactome:R-HSA-5637798 Reactome:R-HSA-5637796 Reactome:R-HSA-5637795 Reactome:R-HSA-5637794 Reactome:R-HSA-5637792 Reactome:R-HSA-5637770 Reactome:R-HSA-5637766 Reactome:R-HSA-5637765 Reactome:R-HSA-5637764 Reactome:R-HSA-445069 Reactome:R-HSA-2400009 Reactome:R-HSA-2316434 Reactome:R-HSA-2179415 Reactome:R-HSA-2179407 Reactome:R-HSA-2179387 Reactome:R-HSA-212713 Reactome:R-HSA-212710 Reactome:R-HSA-212706 Reactome:R-HSA-1977959 Reactome:R-HSA-1963589 Reactome:R-HSA-1963586 Reactome:R-HSA-1963582 Reactome:R-HSA-1963581 Reactome:R-HSA-1963563 Reactome:R-HSA-183089 Reactome:R-HSA-183084 Reactome:R-HSA-183072 Reactome:R-HSA-183067 Reactome:R-HSA-183058 Reactome:R-HSA-183055 Reactome:R-HSA-183051 Reactome:R-HSA-183036 Reactome:R-HSA-183002 Reactome:R-HSA-182994 Reactome:R-HSA-182993 Reactome:R-HSA-182990 Reactome:R-HSA-182986 Reactome:R-HSA-182969 Reactome:R-HSA-177945 Reactome:R-HSA-177944 Reactome:R-HSA-177943 Reactome:R-HSA-177942 Reactome:R-HSA-177941 Reactome:R-HSA-177939 Reactome:R-HSA-177938 Reactome:R-HSA-177937 Reactome:R-HSA-177936 Reactome:R-HSA-177935 Reactome:R-HSA-177934 Reactome:R-HSA-177933 Reactome:R-HSA-177930 Reactome:R-HSA-177927 Reactome:R-HSA-177926 Reactome:R-HSA-177925 Reactome:R-HSA-177924 Reactome:R-HSA-177923 Reactome:R-HSA-177922 Reactome:R-HSA-1306965 Reactome:R-HSA-1306963 Reactome:R-HSA-1306957 Reactome:R-HSA-1250195 Reactome:R-HSA-1248677 Reactome:R-HSA-1248655 Reactome:R-HSA-1248002 Reactome:R-HSA-1247999 Reactome:R-HSA-1247844 Reactome:R-HSA-1247842 Reactome:R-HSA-1247841 Reactome:R-HSA-1226016 Reactome:R-HSA-1226014 Reactome:R-HSA-1226012 Reactome:R-HSA-1225978 Reactome:R-HSA-1225961 Reactome:R-HSA-1225960 Reactome:R-HSA-1225957 Reactome:R-HSA-1225956 Reactome:R-HSA-1225952 Reactome:R-HSA-1225951 Reactome:R-HSA-1225950 Reactome:R-HSA-1225949 Reactome:R-HSA-1225947 Reactome:R-HSA-1220614 Reactome:R-HSA-1220613 Reactome:R-HSA-1220612 Reactome:R-HSA-1220611 Reactome:R-HSA-1220610 Reactome:R-HSA-1218833 Reactome:R-HSA-1169421	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0004714	transmembrane receptor protein tyrosine kinase activity	Reactome:R-HSA-177933	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0000165	MAPK cascade	Reactome:R-HSA-5673001	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:2000145	regulation of cell motility	Reactome:R-HSA-6785631	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1901185	negative regulation of ERBB signaling pathway	Reactome:R-HSA-8864125	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0061024	membrane organization	Reactome:R-HSA-199991	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051897	positive regulation of protein kinase B signaling	Reactome:R-HSA-2316434	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045746	negative regulation of Notch signaling pathway	Reactome:R-HSA-9018573 Reactome:R-HSA-9018572	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0042059	negative regulation of epidermal growth factor receptor signaling pathway	Reactome:R-HSA-182971	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0038128	ERBB2 signaling pathway	Reactome:R-HSA-1227986	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0016310	phosphorylation	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0418	P		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0964 UniProtKB-SubCell:SL-0243	C		Seeded From UniProt	complete
enables	GO:0004713	protein tyrosine kinase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0829	F		Seeded From UniProt	complete
part_of	GO:0016021	integral component of membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0812	C		Seeded From UniProt	complete
part_of	GO:0005768	endosome	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0967 UniProtKB-SubCell:SL-0101	C		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F		Seeded From UniProt	complete
enables	GO:0016301	kinase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0418	F		Seeded From UniProt	complete
part_of	GO:0005794	Golgi apparatus	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0333	C		Seeded From UniProt	complete
involved_in	GO:0007275	multicellular organism development	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0217	P		Seeded From UniProt	complete
enables	GO:0001618	virus receptor activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1183	F		Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F		Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0256	C		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1003 UniProtKB-SubCell:SL-0039	C		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C		Seeded From UniProt	complete
enables	GO:0016740	transferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0808	F		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C		Seeded From UniProt	complete
part_of	GO:0031965	nuclear membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0182	C		Seeded From UniProt	complete
part_of	GO:0010008	endosome membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0100	C		Seeded From UniProt	complete
part_of	GO:0005789	endoplasmic reticulum membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0097	C		Seeded From UniProt	complete
part_of	GO:0000139	Golgi membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0134	C		Seeded From UniProt	complete
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Notes

References

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

↑ Chen, YR et al. (2017) Deficiency in VHR/DUSP3, a suppressor of focal adhesion kinase, reveals its role in regulating cell adhesion and migration. Oncogene 36 6509-6517 PubMed GONUTS page
↑ ^2.0 ^2.1 Tanno, H et al. (2012) The Ankrd 13 family of UIM-bearing proteins regulates EGF receptor endocytosis from the plasma membrane. Mol. Biol. Cell 23 1343-53 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 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
↑ ^4.0 ^4.1 ^4.2 ^4.3 ^4.4 ^4.5 ^4.6 Lian, S et al. (2015) Cadmium induces matrix metalloproteinase-9 expression via ROS-dependent EGFR, NF-кB, and AP-1 pathways in human endothelial cells. Toxicology 338 104-16 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 ^5.3 ^5.4 Ajiro, M et al. (2010) Critical involvement of RQCD1 in the EGFR-Akt pathway in mammary carcinogenesis. Int. J. Oncol. 37 1085-93 PubMed GONUTS page
↑ Bache, KG et al. (2006) The ESCRT-III subunit hVps24 is required for degradation but not silencing of the epidermal growth factor receptor. Mol. Biol. Cell 17 2513-23 PubMed GONUTS page
↑ Lee, SY et al. (2013) The promotion of cardiogenic differentiation of hMSCs by targeting epidermal growth factor receptor using microRNA-133a. Biomaterials 34 92-9 PubMed GONUTS page
↑ Zhu, K et al. (2016) Tumor-suppressive miR-218-5p inhibits cancer cell proliferation and migration via EGFR in non-small cell lung cancer. Oncotarget 7 28075-85 PubMed GONUTS page
↑ Cohen-Dvashi, H et al. (2015) Navigator-3, a modulator of cell migration, may act as a suppressor of breast cancer progression. EMBO Mol Med 7 299-314 PubMed GONUTS page
↑ Guo, Z et al. (2014) E-cadherin interactome complexity and robustness resolved by quantitative proteomics. Sci Signal 7 rs7 PubMed GONUTS page
↑ ^11.0 ^11.1 ^11.2 ^11.3 ^11.4 ^11.5 ^11.6 van Baal, J et al. (2012) Diacylglycerol kinase θ counteracts protein kinase C-mediated inactivation of the EGF receptor. Int. J. Biochem. Cell Biol. 44 1791-9 PubMed GONUTS page
↑ ^12.0 ^12.1 Stinson, S et al. (2011) TRPS1 targeting by miR-221/222 promotes the epithelial-to-mesenchymal transition in breast cancer. Sci Signal 4 ra41 PubMed GONUTS page
↑ Dong, A et al. (2015) Epidermal growth factor receptor (EGFR) signaling requires a specific endoplasmic reticulum thioredoxin for the post-translational control of receptor presentation to the cell surface. J. Biol. Chem. 290 8016-27 PubMed GONUTS page
↑ ^14.0 ^14.1 Malerød, L et al. (2007) Vps22/EAP30 in ESCRT-II mediates endosomal sorting of growth factor and chemokine receptors destined for lysosomal degradation. Traffic 8 1617-29 PubMed GONUTS page
↑ ^15.0 ^15.1 Smith, CJ et al. (2013) The E3 ubiquitin ligases RNF126 and Rabring7 regulate endosomal sorting of the epidermal growth factor receptor. J. Cell. Sci. 126 1366-80 PubMed GONUTS page
↑ Pons, V et al. (2012) SNX12 role in endosome membrane transport. PLoS ONE 7 e38949 PubMed GONUTS page
↑ Kuo, JC et al. (2011) Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for β-Pix in negative regulation of focal adhesion maturation. Nat. Cell Biol. 13 383-93 PubMed GONUTS page
↑ Abou-Rjaily, GA et al. (2004) CEACAM1 modulates epidermal growth factor receptor--mediated cell proliferation. J. Clin. Invest. 114 944-52 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
↑ 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
↑ Vermeer, PD et al. (2003) Segregation of receptor and ligand regulates activation of epithelial growth factor receptor. Nature 422 322-6 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
↑ ^23.0 ^23.1 ^23.2 ^23.3 ^23.4 ^23.5 Madeo, A & Maggiolini, M (2010) Nuclear alternate estrogen receptor GPR30 mediates 17beta-estradiol-induced gene expression and migration in breast cancer-associated fibroblasts. Cancer Res. 70 6036-46 PubMed GONUTS page
↑ ^24.0 ^24.1 ^24.2 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
↑ ^25.0 ^25.1 ^25.2 ^25.3 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
↑ ^26.0 ^26.1 ^26.2 ^26.3 ^26.4 ^26.5 ^26.6 ^26.7 ^26.8 ^26.9 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
↑ ^27.0 ^27.1 ^27.2 ^27.3 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
↑ ^28.0 ^28.1 Edwin, F & Patel, TB (2008) A novel role of Sprouty 2 in regulating cellular apoptosis. J. Biol. Chem. 283 3181-90 PubMed GONUTS page
↑ ^29.0 ^29.1 ^29.2 ^29.3 ^29.4 ^29.5 ^29.6 Wang, SC et al. (2006) Tyrosine phosphorylation controls PCNA function through protein stability. Nat. Cell Biol. 8 1359-68 PubMed GONUTS page
↑ ^30.0 ^30.1 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
↑ 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
↑ 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
↑ 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
↑ 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
↑ 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 Mroczkowski, B et al. () ATP-stimulated interaction between epidermal growth factor receptor and supercoiled DNA. Nature 309 270-3 PubMed GONUTS page
↑ 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
↑ 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
↑ 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
↑ 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
↑ ^41.00 ^41.01 ^41.02 ^41.03 ^41.04 ^41.05 ^41.06 ^41.07 ^41.08 ^41.09 ^41.10 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Ghai, R et al. (2013) Structural basis for endosomal trafficking of diverse transmembrane cargos by PX-FERM proteins. Proc. Natl. Acad. Sci. U.S.A. 110 E643-52 PubMed GONUTS page
↑ ^43.0 ^43.1 ^43.2 ^43.3 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
↑ Fan, QW et al. (2013) EGFR phosphorylates tumor-derived EGFRvIII driving STAT3/5 and progression in glioblastoma. Cancer Cell 24 438-49 PubMed GONUTS page
↑ Shen, J et al. (2013) EGFR modulates microRNA maturation in response to hypoxia through phosphorylation of AGO2. Nature 497 383-7 PubMed GONUTS page
↑ Leuchowius, KJ et al. (2013) Parallel visualization of multiple protein complexes in individual cells in tumor tissue. Mol. Cell Proteomics 12 1563-71 PubMed GONUTS page
↑ Endres, NF et al. (2013) Conformational coupling across the plasma membrane in activation of the EGF receptor. Cell 152 543-56 PubMed GONUTS page
↑ Gajiwala, KS et al. (2013) Insights into the aberrant activity of mutant EGFR kinase domain and drug recognition. Structure 21 209-19 PubMed GONUTS page
↑ Shan, Y et al. (2012) Oncogenic mutations counteract intrinsic disorder in the EGFR kinase and promote receptor dimerization. Cell 149 860-70 PubMed GONUTS page
↑ Gajadhar, AS et al. (2012) In situ analysis of mutant EGFRs prevalent in glioblastoma multiforme reveals aberrant dimerization, activation, and differential response to anti-EGFR targeted therapy. Mol. Cancer Res. 10 428-40 PubMed GONUTS page
↑ Swift, JL et al. (2011) Quantification of receptor tyrosine kinase transactivation through direct dimerization and surface density measurements in single cells. Proc. Natl. Acad. Sci. U.S.A. 108 7016-21 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
↑ Serra, V et al. (2011) PI3K inhibition results in enhanced HER signaling and acquired ERK dependency in HER2-overexpressing breast cancer. Oncogene 30 2547-57 PubMed GONUTS page
↑ Gajadhar, A & Guha, A (2010) A proximity ligation assay using transiently transfected, epitope-tagged proteins: application for in situ detection of dimerized receptor tyrosine kinases. BioTechniques 48 145-52 PubMed GONUTS page
↑ Deribe, YL et al. (2009) Regulation of epidermal growth factor receptor trafficking by lysine deacetylase HDAC6. Sci Signal 2 ra84 PubMed GONUTS page
↑ Jura, N et al. (2009) Structural analysis of the catalytically inactive kinase domain of the human EGF receptor 3. Proc. Natl. Acad. Sci. U.S.A. 106 21608-13 PubMed GONUTS page
↑ Leuchowius, KJ et al. (2009) Flow cytometric in situ proximity ligation analyses of protein interactions and post-translational modification of the epidermal growth factor receptor family. Cytometry A 75 833-9 PubMed GONUTS page
↑ Jura, N et al. (2009) Mechanism for activation of the EGF receptor catalytic domain by the juxtamembrane segment. Cell 137 1293-307 PubMed GONUTS page
↑ Thiel, KW & Carpenter, G (2007) Epidermal growth factor receptor juxtamembrane region regulates allosteric tyrosine kinase activation. Proc. Natl. Acad. Sci. U.S.A. 104 19238-43 PubMed GONUTS page
↑ Wehrman, TS et al. (2006) A system for quantifying dynamic protein interactions defines a role for Herceptin in modulating ErbB2 interactions. Proc. Natl. Acad. Sci. U.S.A. 103 19063-8 PubMed GONUTS page
↑ Zhang, X et al. (2006) An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor. Cell 125 1137-49 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

[PMID:28759036-1] Chen, YR et al. (2017) Deficiency in VHR/DUSP3, a suppressor of focal adhesion kinase, reveals its role in regulating cell adhesion and migration. Oncogene 36 6509-6517 PubMed GONUTS page

[PMID:22298428-2] 2.0 ^2.1 Tanno, H et al. (2012) The Ankrd 13 family of UIM-bearing proteins regulates EGF receptor endocytosis from the plasma membrane. Mol. Biol. Cell 23 1343-53 PubMed GONUTS page

[PMID:18483258-3] 3.0 ^3.1 ^3.2 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

[PMID:26514923-4] 4.0 ^4.1 ^4.2 ^4.3 ^4.4 ^4.5 ^4.6 Lian, S et al. (2015) Cadmium induces matrix metalloproteinase-9 expression via ROS-dependent EGFR, NF-кB, and AP-1 pathways in human endothelial cells. Toxicology 338 104-16 PubMed GONUTS page

[PMID:20878056-5] 5.0 ^5.1 ^5.2 ^5.3 ^5.4 Ajiro, M et al. (2010) Critical involvement of RQCD1 in the EGFR-Akt pathway in mammary carcinogenesis. Int. J. Oncol. 37 1085-93 PubMed GONUTS page

[PMID:16554368-6] Bache, KG et al. (2006) The ESCRT-III subunit hVps24 is required for degradation but not silencing of the epidermal growth factor receptor. Mol. Biol. Cell 17 2513-23 PubMed GONUTS page

[PMID:23069713-7] Lee, SY et al. (2013) The promotion of cardiogenic differentiation of hMSCs by targeting epidermal growth factor receptor using microRNA-133a. Biomaterials 34 92-9 PubMed GONUTS page

[PMID:27057632-8] Zhu, K et al. (2016) Tumor-suppressive miR-218-5p inhibits cancer cell proliferation and migration via EGFR in non-small cell lung cancer. Oncotarget 7 28075-85 PubMed GONUTS page

[PMID:25678558-9] Cohen-Dvashi, H et al. (2015) Navigator-3, a modulator of cell migration, may act as a suppressor of breast cancer progression. EMBO Mol Med 7 299-314 PubMed GONUTS page

[PMID:25468996-10] Guo, Z et al. (2014) E-cadherin interactome complexity and robustness resolved by quantitative proteomics. Sci Signal 7 rs7 PubMed GONUTS page

[PMID:22732145-11] 11.0 ^11.1 ^11.2 ^11.3 ^11.4 ^11.5 ^11.6 van Baal, J et al. (2012) Diacylglycerol kinase θ counteracts protein kinase C-mediated inactivation of the EGF receptor. Int. J. Biochem. Cell Biol. 44 1791-9 PubMed GONUTS page

[PMID:21673316-12] 12.0 ^12.1 Stinson, S et al. (2011) TRPS1 targeting by miR-221/222 promotes the epithelial-to-mesenchymal transition in breast cancer. Sci Signal 4 ra41 PubMed GONUTS page

[PMID:25666625-13] Dong, A et al. (2015) Epidermal growth factor receptor (EGFR) signaling requires a specific endoplasmic reticulum thioredoxin for the post-translational control of receptor presentation to the cell surface. J. Biol. Chem. 290 8016-27 PubMed GONUTS page

[PMID:17714434-14] 14.0 ^14.1 Malerød, L et al. (2007) Vps22/EAP30 in ESCRT-II mediates endosomal sorting of growth factor and chemokine receptors destined for lysosomal degradation. Traffic 8 1617-29 PubMed GONUTS page

[PMID:23418353-15] 15.0 ^15.1 Smith, CJ et al. (2013) The E3 ubiquitin ligases RNF126 and Rabring7 regulate endosomal sorting of the epidermal growth factor receptor. J. Cell. Sci. 126 1366-80 PubMed GONUTS page

[PMID:22719997-16] Pons, V et al. (2012) SNX12 role in endosome membrane transport. PLoS ONE 7 e38949 PubMed GONUTS page

[PMID:21423176-17] Kuo, JC et al. (2011) Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for β-Pix in negative regulation of focal adhesion maturation. Nat. Cell Biol. 13 383-93 PubMed GONUTS page

[PMID:15467833-18] Abou-Rjaily, GA et al. (2004) CEACAM1 modulates epidermal growth factor receptor--mediated cell proliferation. J. Clin. Invest. 114 944-52 PubMed GONUTS page

[PMID:17655843-19] 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:20302655-20] 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

[PMID:12646923-21] 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:15465819-22] 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:20551055-23] 23.0 ^23.1 ^23.2 ^23.3 ^23.4 ^23.5 Madeo, A & Maggiolini, M (2010) Nuclear alternate estrogen receptor GPR30 mediates 17beta-estradiol-induced gene expression and migration in breast cancer-associated fibroblasts. Cancer Res. 70 6036-46 PubMed GONUTS page

[PMID:14702346-24] 24.0 ^24.1 ^24.2 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:12828935-25] 25.0 ^25.1 ^25.2 ^25.3 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:12435727-26] 26.0 ^26.1 ^26.2 ^26.3 ^26.4 ^26.5 ^26.6 ^26.7 ^26.8 ^26.9 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:10572067-27] 27.0 ^27.1 ^27.2 ^27.3 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:18070883-28] 28.0 ^28.1 Edwin, F & Patel, TB (2008) A novel role of Sprouty 2 in regulating cellular apoptosis. J. Biol. Chem. 283 3181-90 PubMed GONUTS page

[PMID:17115032-29] 29.0 ^29.1 ^29.2 ^29.3 ^29.4 ^29.5 ^29.6 Wang, SC et al. (2006) Tyrosine phosphorylation controls PCNA function through protein stability. Nat. Cell Biol. 8 1359-68 PubMed GONUTS page

[PMID:12009895-30] 30.0 ^30.1 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:15082764-31] 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

[PMID:15899872-32] 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

[PMID:17182860-33] 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:7588596-34] 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:9103388-35] 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:6325948-36] 36.0 ^36.1 Mroczkowski, B et al. () ATP-stimulated interaction between epidermal growth factor receptor and supercoiled DNA. Nature 309 270-3 PubMed GONUTS page

[PMID:2790960-37] 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:17599051-38] 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:15542601-39] 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:12925580-40] 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:21873635-41] 41.00 ^41.01 ^41.02 ^41.03 ^41.04 ^41.05 ^41.06 ^41.07 ^41.08 ^41.09 ^41.10 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:23382219-42] Ghai, R et al. (2013) Structural basis for endosomal trafficking of diverse transmembrane cargos by PX-FERM proteins. Proc. Natl. Acad. Sci. U.S.A. 110 E643-52 PubMed GONUTS page

[PMID:7736574-43] 43.0 ^43.1 ^43.2 ^43.3 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:24135280-44] Fan, QW et al. (2013) EGFR phosphorylates tumor-derived EGFRvIII driving STAT3/5 and progression in glioblastoma. Cancer Cell 24 438-49 PubMed GONUTS page

[PMID:23636329-45] Shen, J et al. (2013) EGFR modulates microRNA maturation in response to hypoxia through phosphorylation of AGO2. Nature 497 383-7 PubMed GONUTS page

[PMID:23436906-46] Leuchowius, KJ et al. (2013) Parallel visualization of multiple protein complexes in individual cells in tumor tissue. Mol. Cell Proteomics 12 1563-71 PubMed GONUTS page

[PMID:23374349-47] Endres, NF et al. (2013) Conformational coupling across the plasma membrane in activation of the EGF receptor. Cell 152 543-56 PubMed GONUTS page

[PMID:23273428-48] Gajiwala, KS et al. (2013) Insights into the aberrant activity of mutant EGFR kinase domain and drug recognition. Structure 21 209-19 PubMed GONUTS page

[PMID:22579287-49] Shan, Y et al. (2012) Oncogenic mutations counteract intrinsic disorder in the EGFR kinase and promote receptor dimerization. Cell 149 860-70 PubMed GONUTS page

[PMID:22232519-50] Gajadhar, AS et al. (2012) In situ analysis of mutant EGFRs prevalent in glioblastoma multiforme reveals aberrant dimerization, activation, and differential response to anti-EGFR targeted therapy. Mol. Cancer Res. 10 428-40 PubMed GONUTS page

[PMID:21482778-51] Swift, JL et al. (2011) Quantification of receptor tyrosine kinase transactivation through direct dimerization and surface density measurements in single cells. Proc. Natl. Acad. Sci. U.S.A. 108 7016-21 PubMed GONUTS page

[PMID:21480528-52] 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

[PMID:21278786-53] Serra, V et al. (2011) PI3K inhibition results in enhanced HER signaling and acquired ERK dependency in HER2-overexpressing breast cancer. Oncogene 30 2547-57 PubMed GONUTS page

[PMID:20359299-54] Gajadhar, A & Guha, A (2010) A proximity ligation assay using transiently transfected, epitope-tagged proteins: application for in situ detection of dimerized receptor tyrosine kinases. BioTechniques 48 145-52 PubMed GONUTS page

[PMID:20029029-55] Deribe, YL et al. (2009) Regulation of epidermal growth factor receptor trafficking by lysine deacetylase HDAC6. Sci Signal 2 ra84 PubMed GONUTS page

[PMID:20007378-56] Jura, N et al. (2009) Structural analysis of the catalytically inactive kinase domain of the human EGF receptor 3. Proc. Natl. Acad. Sci. U.S.A. 106 21608-13 PubMed GONUTS page

[PMID:19650109-57] Leuchowius, KJ et al. (2009) Flow cytometric in situ proximity ligation analyses of protein interactions and post-translational modification of the epidermal growth factor receptor family. Cytometry A 75 833-9 PubMed GONUTS page

[PMID:19563760-58] Jura, N et al. (2009) Mechanism for activation of the EGF receptor catalytic domain by the juxtamembrane segment. Cell 137 1293-307 PubMed GONUTS page

[PMID:18042729-59] Thiel, KW & Carpenter, G (2007) Epidermal growth factor receptor juxtamembrane region regulates allosteric tyrosine kinase activation. Proc. Natl. Acad. Sci. U.S.A. 104 19238-43 PubMed GONUTS page

[PMID:17148612-60] Wehrman, TS et al. (2006) A system for quantifying dynamic protein interactions defines a role for Herceptin in modulating ErbB2 interactions. Proc. Natl. Acad. Sci. U.S.A. 103 19063-8 PubMed GONUTS page

[PMID:16777603-61] Zhang, X et al. (2006) An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor. Cell 125 1137-49 PubMed GONUTS page

[PMID:16076471-62] 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

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