HUMAN:ERBB2

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	ERBB2 (synonyms: HER2, MLN19, NEU, NGL)
Protein Name(s)	Receptor tyrosine-protein kinase erbB-2 Metastatic lymph node gene 19 protein MLN 19 Proto-oncogene Neu Proto-oncogene c-ErbB-2 Tyrosine kinase-type cell surface receptor HER2 p185erbB2
External Links
UniProt	P04626
EMBL	AH001455 X03363 M11730 M12036 AY208911 AK295195 CH471152 BC167147 M16792 M16789 M16790 M16791 KJ534964 L29395 M95667
CCDS	CCDS32642.1 CCDS45667.1 CCDS74052.1
PIR	A24571
RefSeq	NP_001005862.1 NP_001276865.1 NP_001276867.1 NP_004439.2 XP_005257197.1
UniGene	Hs.446352
PDB	1MFG 1MFL 1MW4 1N8Z 1OVC 1QR1 1S78 2A91 2JWA 2KS1 2L4K 3BE1 3H3B 3MZW 3N85 3PP0 3RCD 4GFU 4HRL 4HRM 4HRN
PDBsum	1MFG 1MFL 1MW4 1N8Z 1OVC 1QR1 1S78 2A91 2JWA 2KS1 2L4K 3BE1 3H3B 3MZW 3N85 3PP0 3RCD 4GFU 4HRL 4HRM 4HRN
ProteinModelPortal	P04626
SMR	P04626
BioGrid	108376
DIP	DIP-8N
IntAct	P04626
MINT	MINT-158636
STRING	9606.ENSP00000269571
BindingDB	P04626
ChEMBL	CHEMBL2363049
DrugBank	DB05773 DB08916 DB01259 DB06366 DB00072
GuidetoPHARMACOLOGY	2019
PhosphoSite	P04626
DMDM	119533
MaxQB	P04626
PaxDb	P04626
PRIDE	P04626
DNASU	2064
Ensembl	ENST00000269571 ENST00000406381 ENST00000541774 ENST00000584601
GeneID	2064
KEGG	hsa:2064
UCSC	uc002hsm.3 uc010cwa.3
CTD	2064
GeneCards	GC17P037844
HGNC	HGNC:3430
HPA	CAB000043 CAB020416 CAB062555 HPA001338 HPA001383
MIM	137215 137800 164870 167000 211980 613659
neXtProt	NX_P04626
PharmGKB	PA27844
eggNOG	COG0515
GeneTree	ENSGT00760000118799
HOGENOM	HOG000230982
HOVERGEN	HBG000490
InParanoid	P04626
KO	K05083
OMA	ACYPLCA
OrthoDB	EOG7V49XM
PhylomeDB	P04626
TreeFam	TF106002
Reactome	REACT_115662 REACT_115720 REACT_115755 REACT_115854 REACT_115896 REACT_115993 REACT_116008 REACT_147727 REACT_19277 REACT_75829
SignaLink	P04626
ChiTaRS	ERBB2
EvolutionaryTrace	P04626
GeneWiki	HER2/neu
GenomeRNAi	2064
NextBio	8385
PMAP-CutDB	P04626
PRO	PR:P04626
Proteomes	UP000005640
Bgee	P04626
CleanEx	HS_ERBB2
ExpressionAtlas	P04626
Genevestigator	P04626
GO	GO:0016324 GO:0016323 GO:0005737 GO:0031410 GO:0010008 GO:0016021 GO:0005634 GO:0048471 GO:0005886 GO:0043235 GO:0005524 GO:0043125 GO:0042802 GO:0008022 GO:0046983 GO:0046982 GO:0019903 GO:0004713 GO:0004716 GO:0001042 GO:0004714 GO:0004888 GO:0007411 GO:0008283 GO:0007166 GO:0007167 GO:0007173 GO:0038095 GO:0008543 GO:0007507 GO:0045087 GO:0008045 GO:0042552 GO:0033088 GO:0007528 GO:0048011 GO:0048709 GO:0018108 GO:0007422 GO:0014065 GO:0048015 GO:0045785 GO:0030307 GO:0050679 GO:0043406 GO:0001934 GO:0032321 GO:0045943 GO:0045945 GO:0045727 GO:0046777 GO:0006468 GO:0045765 GO:0070372 GO:0032886 GO:0007165 GO:0023014 GO:0006351 GO:0007169 GO:0042060
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	Notes	Status
involved_in	GO:0071364	cellular response to epidermal growth factor stimulus	PMID:27134172^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0090314	positive regulation of protein targeting to membrane	PMID:20010870^[2]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0071363	cellular response to growth factor stimulus	PMID:20010870^[2]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:20010870^[2]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0046982	protein heterodimerization activity	PMID:7556068^[3]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P21860	F	Seeded From UniProt	complete
involved_in	GO:0046777	protein autophosphorylation	PMID:7556068^[3]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0045785	positive regulation of cell adhesion	PMID:7556068^[3]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0043235	receptor complex	PMID:7514177^[4]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0042060	wound healing	PMID:12646923^[5]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0043547	positive regulation of GTPase activity	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P70424	P	Seeded From UniProt	complete
contributes_to	GO:0019838	growth factor binding	PMID:7514177^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0016323	basolateral plasma membrane	PMID:12646923^[5]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0014065	phosphatidylinositol 3-kinase signaling	PMID:7556068^[3]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0007169	transmembrane receptor protein tyrosine kinase signaling pathway	PMID:7514177^[4]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0004888	transmembrane signaling receptor activity	PMID:7514177^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004714	transmembrane receptor protein tyrosine kinase activity	PMID:7514177^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004713	protein tyrosine kinase activity	PMID:7556068^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0001934	positive regulation of protein phosphorylation	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P70424	P	Seeded From UniProt	complete
involved_in	GO:0070372	regulation of ERK1 and ERK2 cascade	PMID:16314522^[6]	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^[7]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0046983	protein dimerization activity	PMID:12000754^[8]	ECO:0000303	author statement without traceable support used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0046982	protein heterodimerization activity	PMID:10572067^[7]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0035556	intracellular signal transduction	PMID:19372587^[9]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0045943	positive regulation of transcription by RNA polymerase I	PMID:21555369^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0045765	regulation of angiogenesis	PMID:15609325^[11]	ECO:0000303	author statement without traceable support used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0045727	positive regulation of translation	PMID:21555369^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0043406	positive regulation of MAP kinase activity	PMID:10572067^[7]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0032886	regulation of microtubule-based process	PMID:20937854^[12]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0030307	positive regulation of cell growth	PMID:21555369^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0019903	protein phosphatase binding	PMID:15899872^[13]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q15262	F	Seeded From UniProt	complete
part_of	GO:0016021	integral component of membrane	PMID:15609325^[11]	ECO:0000303	author statement without traceable support used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0010008	endosome membrane	PMID:16314522^[6]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0008022	protein C-terminus binding	PMID:15520177^[14]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q96EY1-2	F	Seeded From UniProt	complete
enables	GO:0008022	protein C-terminus binding	PMID:15520177^[14]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q96EY1-1	F	Seeded From UniProt	complete
involved_in	GO:0007165	signal transduction	PMID:10572067^[7]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:12000754^[8]	ECO:0000303	author statement without traceable support used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:16314522^[6]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:21555369^[10]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0001042	RNA polymerase I core binding	PMID:21555369^[10]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0043410	positive regulation of MAPK cascade	PMID:21873635^[15]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002814594 RGD:2561 UniProtKB:P04626	P	Seeded From UniProt	complete
part_of	GO:0043235	receptor complex	PMID:21873635^[15]	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:0030182	neuron differentiation	PMID:21873635^[15]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:95410 PANTHER:PTN002814594 ZFIN:ZDB-GENE-031118-121	P	Seeded From UniProt	complete
part_of	GO:0009925	basal plasma membrane	PMID:21873635^[15]	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^[15]	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^[15]	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^[15]	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
	GO:0001934	positive regulation of protein phosphorylation	PMID:25655188^[16]	ECO:0000315			P	Figure 1; amplication or deletion of protein	complete CACAO 10632
enables	GO:0004714	transmembrane receptor protein tyrosine kinase activity	PMID:21873635^[15]	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^[17]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0007166	cell surface receptor signaling pathway	PMID:9685399^[18]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0004713	protein tyrosine kinase activity	PMID:7556068^[3]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:O75810	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:21480528^[19]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P04626	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:21255571^[20]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P04626	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:21203579^[21]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P04626	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:19650109^[22]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P04626	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:17148612^[23]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P04626	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:16843263^[24]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P04626	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:23436906^[25]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P04626	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:22733765^[26]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P04626	F	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
part_of	GO:0005829	cytosol	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0018108	peptidyl-tyrosine phosphorylation	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0004714	P	Seeded From UniProt	complete
involved_in	GO:0018108	peptidyl-tyrosine phosphorylation	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0004713	P	Seeded From UniProt	complete
involved_in	GO:0018108	peptidyl-tyrosine phosphorylation	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0004713	P	Seeded From UniProt	complete
involved_in	GO:0018108	peptidyl-tyrosine phosphorylation	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0004714	P	Seeded From UniProt	complete
involved_in	GO:0018108	peptidyl-tyrosine phosphorylation	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0004713	P	Seeded From UniProt	complete
involved_in	GO:0018108	peptidyl-tyrosine phosphorylation	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0004713	P	Seeded From UniProt	complete
involved_in	GO:0018108	peptidyl-tyrosine phosphorylation	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0004714	P	Seeded From UniProt	complete
involved_in	GO:0018108	peptidyl-tyrosine phosphorylation	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0004713	P	Seeded From UniProt	complete
involved_in	GO:0018108	peptidyl-tyrosine phosphorylation	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0004714	P	Seeded From UniProt	complete
involved_in	GO:0048709	oligodendrocyte differentiation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P70424 ensembl:ENSMUSP00000053897	P	Seeded From UniProt	complete
involved_in	GO:0043547	positive regulation of GTPase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P70424 ensembl:ENSMUSP00000053897	P	Seeded From UniProt	complete
part_of	GO:0043209	myelin sheath	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P70424 ensembl:ENSMUSP00000053897	C	Seeded From UniProt	complete
involved_in	GO:0042552	myelination	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P70424 ensembl:ENSMUSP00000053897	P	Seeded From UniProt	complete
involved_in	GO:0033088	negative regulation of immature T cell proliferation in thymus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P70424 ensembl:ENSMUSP00000053897	P	Seeded From UniProt	complete
part_of	GO:0031410	cytoplasmic vesicle	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P70424 ensembl:ENSMUSP00000053897	C	Seeded From UniProt	complete
part_of	GO:0016324	apical plasma membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P70424 ensembl:ENSMUSP00000053897	C	Seeded From UniProt	complete
involved_in	GO:0010628	positive regulation of gene expression	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P70424 ensembl:ENSMUSP00000053897	P	Seeded From UniProt	complete
involved_in	GO:0008045	motor neuron axon guidance	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P70424 ensembl:ENSMUSP00000053897	P	Seeded From UniProt	complete
involved_in	GO:0007528	neuromuscular junction development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P70424 ensembl:ENSMUSP00000053897	P	Seeded From UniProt	complete
involved_in	GO:0007507	heart development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P70424 ensembl:ENSMUSP00000053897	P	Seeded From UniProt	complete
involved_in	GO:0007422	peripheral nervous system development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P70424 ensembl:ENSMUSP00000053897	P	Seeded From UniProt	complete
involved_in	GO:0007399	nervous system development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P70424 ensembl:ENSMUSP00000053897	P	Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P70424 ensembl:ENSMUSP00000053897	C	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P70424 ensembl:ENSMUSP00000053897	C	Seeded From UniProt	complete
involved_in	GO:0001934	positive regulation of protein phosphorylation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P70424 ensembl:ENSMUSP00000053897	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
enables	GO:0043125	ErbB-3 class receptor binding	PMID:9590694^[27]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0007167	enzyme linked receptor protein signaling pathway	PMID:9590694^[27]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	PMID:10851066^[28]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0043235	receptor complex	PMID:7556068^[3]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0007169	transmembrane receptor protein tyrosine kinase signaling pathway	PMID:7556068^[3]	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: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: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: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-1248753 Reactome:R-NUL-1248744 Reactome:R-HSA-8864466 Reactome:R-HSA-8864125 Reactome:R-HSA-8864105 Reactome:R-HSA-8863804 Reactome:R-HSA-8848005 Reactome:R-HSA-8847995 Reactome:R-HSA-6785648 Reactome:R-HSA-6785636 Reactome:R-HSA-5672965 Reactome:R-HSA-416594 Reactome:R-HSA-416588 Reactome:R-HSA-373750 Reactome:R-HSA-2400009 Reactome:R-HSA-2316434 Reactome:R-HSA-1963589 Reactome:R-HSA-1963586 Reactome:R-HSA-1963582 Reactome:R-HSA-1963581 Reactome:R-HSA-1963563 Reactome:R-HSA-1918095 Reactome:R-HSA-1918092 Reactome:R-HSA-1358798 Reactome:R-HSA-1358792 Reactome:R-HSA-1306979 Reactome:R-HSA-1306972 Reactome:R-HSA-1306969 Reactome:R-HSA-1306965 Reactome:R-HSA-1306963 Reactome:R-HSA-1306957 Reactome:R-HSA-1306953 Reactome:R-HSA-1250462 Reactome:R-HSA-1250346 Reactome:R-HSA-1250195 Reactome:R-HSA-1250189	ECO:0000304	author statement supported by traceable reference used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0004713	protein tyrosine kinase activity	Reactome:R-HSA-373750	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: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:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	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:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	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
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: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
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
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
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
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:0048471	perinuclear region of cytoplasm	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0198	C	Seeded From UniProt	complete
edit table

Notes

References

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

↑ Li, H et al. (2016) Crystal Structure and Substrate Specificity of PTPN12. Cell Rep 15 1345-58 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 Heinrich, C et al. (2010) Copine-III interacts with ErbB2 and promotes tumor cell migration. Oncogene 29 1598-610 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 ^3.4 ^3.5 ^3.6 ^3.7 Wallasch, C et al. (1995) Heregulin-dependent regulation of HER2/neu oncogenic signaling by heterodimerization with HER3. EMBO J. 14 4267-75 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 ^4.3 ^4.4 Sliwkowski, MX et al. (1994) Coexpression of erbB2 and erbB3 proteins reconstitutes a high affinity receptor for heregulin. J. Biol. Chem. 269 14661-5 PubMed GONUTS page
↑ ^5.0 ^5.1 Vermeer, PD et al. (2003) Segregation of receptor and ligand regulates activation of epithelial growth factor receptor. Nature 422 322-6 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 Giri, DK et al. (2005) Endosomal transport of ErbB-2: mechanism for nuclear entry of the cell surface receptor. Mol. Cell. Biol. 25 11005-18 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 ^7.3 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
↑ ^8.0 ^8.1 Penuel, E et al. (2002) Identification of a region within the ErbB2/HER2 intracellular domain that is necessary for ligand-independent association. J. Biol. Chem. 277 28468-73 PubMed GONUTS page
↑ Hawthorne, VS et al. (2009) ErbB2-mediated Src and signal transducer and activator of transcription 3 activation leads to transcriptional up-regulation of p21Cip1 and chemoresistance in breast cancer cells. Mol. Cancer Res. 7 592-600 PubMed GONUTS page
↑ ^10.0 ^10.1 ^10.2 ^10.3 ^10.4 Li, LY et al. (2011) Nuclear ErbB2 enhances translation and cell growth by activating transcription of ribosomal RNA genes. Cancer Res. 71 4269-79 PubMed GONUTS page
↑ ^11.0 ^11.1 Beckers, J et al. (2005) Identification and validation of novel ERBB2 (HER2, NEU) targets including genes involved in angiogenesis. Int. J. Cancer 114 590-7 PubMed GONUTS page
↑ Zaoui, K et al. (2010) ErbB2 receptor controls microtubule capture by recruiting ACF7 to the plasma membrane of migrating cells. Proc. Natl. Acad. Sci. U.S.A. 107 18517-22 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
↑ ^14.0 ^14.1 Kim, SW et al. (2004) Tid1, the human homologue of a Drosophila tumor suppressor, reduces the malignant activity of ErbB-2 in carcinoma cells. Cancer Res. 64 7732-9 PubMed GONUTS page
↑ ^15.0 ^15.1 ^15.2 ^15.3 ^15.4 ^15.5 ^15.6 ^15.7 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Hansen, TV et al. (2015) High-density SNP arrays improve detection of HER2 amplification and polyploidy in breast tumors. BMC Cancer 15 35 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
↑ Engelman, JA et al. (1998) Reciprocal regulation of neu tyrosine kinase activity and caveolin-1 protein expression in vitro and in vivo. Implications for human breast cancer. J. Biol. Chem. 273 20448-55 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
↑ Hong, KJ et al. (2011) The tumor suppressor RECK interferes with HER-2/Neu dimerization and attenuates its oncogenic signaling. FEBS Lett. 585 591-5 PubMed GONUTS page
↑ Gijsen, M et al. (2010) HER2 phosphorylation is maintained by a PKB negative feedback loop in response to anti-HER2 herceptin in breast cancer. PLoS Biol. 8 e1000563 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
↑ 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
↑ Wang, SE et al. (2006) HER2 kinase domain mutation results in constitutive phosphorylation and activation of HER2 and EGFR and resistance to EGFR tyrosine kinase inhibitors. Cancer Cell 10 25-38 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
↑ Zhang, Q et al. (2012) Functional isolation of activated and unilaterally phosphorylated heterodimers of ERBB2 and ERBB3 as scaffolds in ligand-dependent signaling. Proc. Natl. Acad. Sci. U.S.A. 109 13237-42 PubMed GONUTS page
↑ ^27.0 ^27.1 Qiu, Y et al. (1998) Requirement of ErbB2 for signalling by interleukin-6 in prostate carcinoma cells. Nature 393 83-5 PubMed GONUTS page
↑ Meng, TC et al. (2000) Interaction between protein tyrosine phosphatase and protein tyrosine kinase is involved in androgen-promoted growth of human prostate cancer cells. Oncogene 19 2664-77 PubMed GONUTS page

[PMID:27134172-1] Li, H et al. (2016) Crystal Structure and Substrate Specificity of PTPN12. Cell Rep 15 1345-58 PubMed GONUTS page

[PMID:20010870-2] 2.0 ^2.1 ^2.2 Heinrich, C et al. (2010) Copine-III interacts with ErbB2 and promotes tumor cell migration. Oncogene 29 1598-610 PubMed GONUTS page

[PMID:7556068-3] 3.0 ^3.1 ^3.2 ^3.3 ^3.4 ^3.5 ^3.6 ^3.7 Wallasch, C et al. (1995) Heregulin-dependent regulation of HER2/neu oncogenic signaling by heterodimerization with HER3. EMBO J. 14 4267-75 PubMed GONUTS page

[PMID:7514177-4] 4.0 ^4.1 ^4.2 ^4.3 ^4.4 Sliwkowski, MX et al. (1994) Coexpression of erbB2 and erbB3 proteins reconstitutes a high affinity receptor for heregulin. J. Biol. Chem. 269 14661-5 PubMed GONUTS page

[PMID:12646923-5] 5.0 ^5.1 Vermeer, PD et al. (2003) Segregation of receptor and ligand regulates activation of epithelial growth factor receptor. Nature 422 322-6 PubMed GONUTS page

[PMID:16314522-6] 6.0 ^6.1 ^6.2 Giri, DK et al. (2005) Endosomal transport of ErbB-2: mechanism for nuclear entry of the cell surface receptor. Mol. Cell. Biol. 25 11005-18 PubMed GONUTS page

[PMID:10572067-7] 7.0 ^7.1 ^7.2 ^7.3 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:12000754-8] 8.0 ^8.1 Penuel, E et al. (2002) Identification of a region within the ErbB2/HER2 intracellular domain that is necessary for ligand-independent association. J. Biol. Chem. 277 28468-73 PubMed GONUTS page

[PMID:19372587-9] Hawthorne, VS et al. (2009) ErbB2-mediated Src and signal transducer and activator of transcription 3 activation leads to transcriptional up-regulation of p21Cip1 and chemoresistance in breast cancer cells. Mol. Cancer Res. 7 592-600 PubMed GONUTS page

[PMID:21555369-10] 10.0 ^10.1 ^10.2 ^10.3 ^10.4 Li, LY et al. (2011) Nuclear ErbB2 enhances translation and cell growth by activating transcription of ribosomal RNA genes. Cancer Res. 71 4269-79 PubMed GONUTS page

[PMID:15609325-11] 11.0 ^11.1 Beckers, J et al. (2005) Identification and validation of novel ERBB2 (HER2, NEU) targets including genes involved in angiogenesis. Int. J. Cancer 114 590-7 PubMed GONUTS page

[PMID:20937854-12] Zaoui, K et al. (2010) ErbB2 receptor controls microtubule capture by recruiting ACF7 to the plasma membrane of migrating cells. Proc. Natl. Acad. Sci. U.S.A. 107 18517-22 PubMed GONUTS page

[PMID:15899872-13] 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:15520177-14] 14.0 ^14.1 Kim, SW et al. (2004) Tid1, the human homologue of a Drosophila tumor suppressor, reduces the malignant activity of ErbB-2 in carcinoma cells. Cancer Res. 64 7732-9 PubMed GONUTS page

[PMID:21873635-15] 15.0 ^15.1 ^15.2 ^15.3 ^15.4 ^15.5 ^15.6 ^15.7 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:25655188-16] Hansen, TV et al. (2015) High-density SNP arrays improve detection of HER2 amplification and polyploidy in breast tumors. BMC Cancer 15 35 PubMed GONUTS page

[PMID:23382219-17] 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:9685399-18] Engelman, JA et al. (1998) Reciprocal regulation of neu tyrosine kinase activity and caveolin-1 protein expression in vitro and in vivo. Implications for human breast cancer. J. Biol. Chem. 273 20448-55 PubMed GONUTS page

[PMID:21480528-19] 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:21255571-20] Hong, KJ et al. (2011) The tumor suppressor RECK interferes with HER-2/Neu dimerization and attenuates its oncogenic signaling. FEBS Lett. 585 591-5 PubMed GONUTS page

[PMID:21203579-21] Gijsen, M et al. (2010) HER2 phosphorylation is maintained by a PKB negative feedback loop in response to anti-HER2 herceptin in breast cancer. PLoS Biol. 8 e1000563 PubMed GONUTS page

[PMID:19650109-22] 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:17148612-23] 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:16843263-24] Wang, SE et al. (2006) HER2 kinase domain mutation results in constitutive phosphorylation and activation of HER2 and EGFR and resistance to EGFR tyrosine kinase inhibitors. Cancer Cell 10 25-38 PubMed GONUTS page

[PMID:23436906-25] 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:22733765-26] Zhang, Q et al. (2012) Functional isolation of activated and unilaterally phosphorylated heterodimers of ERBB2 and ERBB3 as scaffolds in ligand-dependent signaling. Proc. Natl. Acad. Sci. U.S.A. 109 13237-42 PubMed GONUTS page

[PMID:9590694-27] 27.0 ^27.1 Qiu, Y et al. (1998) Requirement of ErbB2 for signalling by interleukin-6 in prostate carcinoma cells. Nature 393 83-5 PubMed GONUTS page

[PMID:10851066-28] Meng, TC et al. (2000) Interaction between protein tyrosine phosphatase and protein tyrosine kinase is involved in androgen-promoted growth of human prostate cancer cells. Oncogene 19 2664-77 PubMed GONUTS page

[1]

[2]

[3]

[4]

[5]

[6]

[7]

[8]

[9]

[10]

[11]

[12]

[13]

[14]

[15]

[16]

[17]

[18]

[19]

[20]

[21]

[22]

[23]

[24]

[25]

[26]

[27]

[28]

HUMAN:ERBB2

Contents

Annotations

Notes

References

a

b

c

e

g

h

i

k

m

n

o

p

r

s

t

v

w

Navigation menu

Personal tools

Namespaces

Variants

Views

More

Search

Navigation

Cacao

Links

Tools