Gene Ontology annotation through association of InterPro records with GO terms

Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity

Annotation inferences using phylogenetic trees

Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt

Gene Ontology annotation based on curation of immunofluorescence data

Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara

Electronic Gene Ontology annotations created by ARBA machine learning models

Combined Automated Annotation using Multiple IEA Methods

Dominance of ErbB-1 heterodimers in lung epithelial cells overexpressing ErbB-2. Both ErbB-1 and ErbB-2 contribute significantly to tumorigenicity.

Class II phosphoinositide 3-kinases are downstream targets of activated polypeptide growth factor receptors.

Interaction between protein tyrosine phosphatase and protein tyrosine kinase is involved in androgen-promoted growth of human prostate cancer cells.

ErbB-2 activates Stat3 alpha in a Src- and JAK2-dependent manner.

Identification of a region within the ErbB2/HER2 intracellular domain that is necessary for ligand-independent association.

Assignment of backbone 1H, 13C, and 15N resonances of human Grb7-SH2 domain in complex with a phosphorylated peptide ligand.

Csk homologous kinase (CHK) and ErbB-2 interactions are directly coupled with CHK negative growth regulatory function in breast cancer.

Segregation of receptor and ligand regulates activation of epithelial growth factor receptor.

Solution structure of the human Grb7-SH2 domain/erbB2 peptide complex and structural basis for Grb7 binding to ErbB2.

LRIG1 restricts growth factor signaling by enhancing receptor ubiquitylation and degradation.

The leucine-rich repeat protein LRIG1 is a negative regulator of ErbB family receptor tyrosine kinases.

Tid1, the human homologue of a Drosophila tumor suppressor, reduces the malignant activity of ErbB-2 in carcinoma cells.

Identification and validation of novel ERBB2 (HER2, NEU) targets including genes involved in angiogenesis.

Phosphotyrosine signaling networks in epidermal growth factor receptor overexpressing squamous carcinoma cells.

Transforming growth factor {beta} (TGF-{beta})-Smad target gene protein tyrosine phosphatase receptor type kappa is required for TGF-{beta} function.

A quantitative protein interaction network for the ErbB receptors using protein microarrays.

Endosomal transport of ErbB-2: mechanism for nuclear entry of the cell surface receptor.

Activation of ErbB2 by 2-methyl-1,4-naphthoquinone (menadione) in human keratinocytes: role of EGFR and protein tyrosine phosphatases.

Altered neuregulin 1-erbB4 signaling contributes to NMDA receptor hypofunction in schizophrenia.

HER2 kinase domain mutation results in constitutive phosphorylation and activation of HER2 and EGFR and resistance to EGFR tyrosine kinase inhibitors.

A system for quantifying dynamic protein interactions defines a role for Herceptin in modulating ErbB2 interactions.

Growth stimulation of non-small cell lung cancer cell lines by antibody against epidermal growth factor receptor promoting formation of ErbB2/ErbB3 heterodimers.

Brk is coamplified with ErbB2 to promote proliferation in breast cancer.

Large-scale structural analysis of the classical human protein tyrosine phosphatome.

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.

Ligand-independent HER2/HER3/PI3K complex is disrupted by trastuzumab and is effectively inhibited by the PI3K inhibitor GDC-0941.

Flow cytometric in situ proximity ligation analyses of protein interactions and post-translational modification of the epidermal growth factor receptor family.

Regulation of Hsp90 client proteins by a Cullin5-RING E3 ubiquitin ligase.

Copine-III interacts with ErbB2 and promotes tumor cell migration.

An activated ErbB3/NRG1 autocrine loop supports in vivo proliferation in ovarian cancer cells.

Secreted heat shock protein 90alpha induces colorectal cancer cell invasion through CD91/LRP-1 and NF-kappaB-mediated integrin alphaV expression.

Degradation of HER2/neu by ANT2 shRNA suppresses migration and invasiveness of breast cancer cells.

In situ quantification of HER2-protein tyrosine kinase 6 (PTK6) protein-protein complexes in paraffin sections from breast cancer tissues.

Progesterone receptor induces ErbB-2 nuclear translocation to promote breast cancer growth via a novel transcriptional effect: ErbB-2 function as a coactivator of Stat3.

ErbB2 receptor controls microtubule capture by recruiting ACF7 to the plasma membrane of migrating cells.

Recombinant human erythropoietin antagonizes trastuzumab treatment of breast cancer cells via Jak2-mediated Src activation and PTEN inactivation.

HER2 phosphorylation is maintained by a PKB negative feedback loop in response to anti-HER2 herceptin in breast cancer.

The tumor suppressor RECK interferes with HER-2/Neu dimerization and attenuates its oncogenic signaling.

PI3K inhibition results in enhanced HER signaling and acquired ERK dependency in HER2-overexpressing breast cancer.

Activation of multiple proto-oncogenic tyrosine kinases in breast cancer via loss of the PTPN12 phosphatase.

Structural analysis of the mechanism of inhibition and allosteric activation of the kinase domain of HER2 protein.

Comparative analysis of fluorescence resonance energy transfer (FRET) and proximity ligation assay (PLA).

Nuclear ErbB2 enhances translation and cell growth by activating transcription of ribosomal RNA genes.

IQGAP1 protein binds human epidermal growth factor receptor 2 (HER2) and modulates trastuzumab resistance.

MEMO associated with an ErbB2 receptor phosphopeptide reveals a new phosphotyrosine motif.

ErbB2, EphrinB1, Src kinase and PTPN13 signaling complex regulates MAP kinase signaling in human cancers.

The atypical histone macroH2A1.2 interacts with HER-2 protein in cancer cells.

Functional isolation of activated and unilaterally phosphorylated heterodimers of ERBB2 and ERBB3 as scaffolds in ligand-dependent signaling.

Spontaneous and pronase-induced HER2 truncation increases the trastuzumab binding capacity of breast cancer tissues and cell lines.

Quantitative analysis of HSP90-client interactions reveals principles of substrate recognition.

Structural basis for endosomal trafficking of diverse transmembrane cargos by PX-FERM proteins.

Parallel visualization of multiple protein complexes in individual cells in tumor tissue.

Oncogenic ERBB3 mutations in human cancers.

Design, synthesis and characterization of peptidomimetic conjugate of BODIPY targeting HER2 protein extracellular domain.

Leucine-rich repeat and immunoglobulin domain-containing protein-1 (Lrig1) negative regulatory action toward ErbB receptor tyrosine kinases is opposed by leucine-rich repeat and immunoglobulin domain-containing protein 3 (Lrig3).

Lyn, a Src family kinase, regulates activation of epidermal growth factor receptors in lung adenocarcinoma cells.

Paralog-selective Hsp90 inhibitors define tumor-specific regulation of HER2.

Perturbation of the mutated EGFR interactome identifies vulnerabilities and resistance mechanisms.

Charting the molecular links between driver and susceptibility genes in colorectal cancer.

Characterisation of HER heterodimers in breast cancer using in situ proximity ligation assay.

The mammalian-membrane two-hybrid assay (MaMTH) for probing membrane-protein interactions in human cells.

Identification of a Src kinase SH3 binding site in the C-terminal domain of the human ErbB2 receptor tyrosine kinase.

A quantitative chaperone interaction network reveals the architecture of cellular protein homeostasis pathways.

The catalytic region and PEST domain of PTPN18 distinctly regulate the HER2 phosphorylation and ubiquitination barcodes.

Using an in situ proximity ligation assay to systematically profile endogenous protein-protein interactions in a pathway network.

Pharmacological targeting of the pseudokinase Her3.

Systematic identification of molecular links between core and candidate genes in breast cancer.

Client Proteins and Small Molecule Inhibitors Display Distinct Binding Preferences for Constitutive and Stress-Induced HSP90 Isoforms and Their Conformationally Restricted Mutants.

Crystal Structure and Substrate Specificity of PTPN12.

A Global Analysis of the Receptor Tyrosine Kinase-Protein Phosphatase Interactome.

SORLA regulates endosomal trafficking and oncogenic fitness of HER2.

Neuropeptide bombesin receptor activation stimulates growth of lung cancer cells through HER3 with a MAPK-dependent mechanism.

Extensive rewiring of the EGFR network in colorectal cancer cells expressing transforming levels of KRAS(G13D).

SH3BGRL confers innate drug resistance in breast cancer by stabilizing HER2 activation on cell membrane.

Dysregulation of the NRG1/ERBB pathway causes a developmental disorder with gastrointestinal dysmotility in humans.

Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.

Physical and functional interactome atlas of human receptor tyrosine kinases.

Systematic discovery of mutation-directed neo-protein-protein interactions in cancer.

Quantitative fragmentomics allow affinity mapping of interactomes.

A central chaperone-like role for 14-3-3 proteins in human cells.

IGFBP5 is an ROR1 ligand promoting glioblastoma invasion via ROR1/HER2-CREB signaling axis.

Mapping adipocyte interactome networks by HaloTag-enrichment-mass spectrometry.

Coexpression of erbB2 and erbB3 proteins reconstitutes a high affinity receptor for heregulin.

Heregulin-dependent regulation of HER2/neu oncogenic signaling by heterodimerization with HER3.

Binding of Neu differentiation factor with the extracellular domain of Her2 and Her3.

The epidermal growth factor receptor couples transforming growth factor-alpha, heparin-binding epidermal growth factor-like factor, and amphiregulin to Neu, ErbB-3, and ErbB-4.

Structural determinants of the interaction between the erbB2 receptor and the Src homology 2 domain of Grb7.

Requirement of ErbB2 for signalling by interleukin-6 in prostate carcinoma cells.

Reciprocal regulation of neu tyrosine kinase activity and caveolin-1 protein expression in vitro and in vivo. Implications for human breast cancer.

Tyrosine phosphorylation of c-ErbB-2 is regulated by the cellular form of prostatic acid phosphatase in human prostate cancer cells.

ERBB2 homodimerization

Trans-autophosphorylation of ERBB2 homodimer

Binding of PI3K to ERBB2:p-ERBB3 heterodimer

SHC1 phosphorylation by ERBB2 heterodimers

Binding of PI3K to p-ERBB2:p-ERBB4 CYT-1 heterodimers

PIP2 to PIP3 conversion by PI3K bound to phosphorylated heterodimer of ERBB2 and ERBB3

GRB7 binds phosphorylated heterodimer of ERBB2 and ERBB3

PIP2 to PIP3 conversion by PI3K bound to GRB2:GAB1 in complex with phosphorylated heterodimer of ERBB2 and EGFR

Binding of GRB2:GAB1 to p-ERBB2:p-EGFR

Binding of PI3K to GRB2:GAB1 in complex with phosphorylated heterodimer of ERBB2 and EGFR

GRB2:SOS1 complex binds phosphorylated ERBB4:ERBB2 heterodimers

RAS guanyl nucleotide exchange mediated by SOS1 bound to GRB2 in complex with phosphorylated ERBB4:ERBB2 heterodimers

PIP2 to PIP3 conversion by PI3K bound to phosphorylated heterodimer of ERBB2 and ERBB4 CYT1

RNF41 ubiquitinates activated ERBB3

RNF41 binds neuregulin-activated ERBB3

CHIP (STUB1) mediates ubiquitination of ERBB2

CUL5 mediates ubiquitination of ERBB2

MATK (CSK homologous kinase) binds phosphorylated ERBB2

Trans-autophosphorylation of p-Y877-ERBB2 heterodimers

Trans-autophosphorylation of ERBB2 heterodimers

SRC family kinases phosphorylate ERBB2

ERBB2 forms heterodimers with ligand-activated ERBB receptors: EGFR, ERBB3 and ERBB4

PI3K phosphorylates PIP2 to PIP3

PI3K inhibitors block PI3K catalytic activity

SEMA4D interacts with Plexin-B1:ErbB2

Activation of Rho by LARG and PDZ-RhoGEF

LARG and PDZ-RhoGEF binds to Plexin-B1

RAS GEFs promote RAS nucleotide exchange

Phosphorylated ERBB2 heterodimers bind MEMO1

MEMO1 binds RHOA:GTP:DIAPH1

Activated ERBB2 binds PTK6 (BRK)

ERBB2 promotes PTK6 autophosphorylation

PTPN12 dephosphorylates ERBB2 on tyrosine Y1248

PTPN18 binds ERBB2:EGFR heterodimers

PTPN18 dephosphorylates ERBB2 at Y1196, Y1112 and Y1248

TFAP2A,(TFAP2B,TFAP2C) homo- and heterodimers and YY1 stimulate ERBB2 gene expression

ERBB2 homodimer phosphorylates SHC1

SHC1 binds phosphorylated ERBB2 homodimer

Recruitment of GRB2:SOS1 to p-SHC1 in complex with phosphorylated ERBB2 homodimer

RAS guanyl-nucleotide exchange mediated by SOS1 in complex with GRB2 and ERBB2 homodimer:p-SHC1

ERBB2 KD mutants bind trastuzumab

ERBB2 binds TKIs

ERBB2 binds trastuzumab

ERBB2 KD mutants heterodimerize

ERBB2 KD mutants trans-autophosphorylate

Phosphorylated heterodimers of ERBB2 KD mutants and ERBB3 bind PI3K

PI3K bound to phosphorylated heterodimers of ERBB2 KD mutants and ERBB3 converts PIP2 to PIP3

Phosphorylated heterodimers of ERBB2 KD mutants and EGFR bind GRB2:GAB1

Phosphorylated heterodimers of ERBB2 KD mutants and EGFR, in complex with GRB2:GAB1, bind PI3K

PI3K bound to phosphorylated heterodimers of ERBB2 KD mutants and EGFR converts PIP2 to PIP3

Phosphorylated heterodimers of ERBB2 KD mutants bind SHC1

Phosphorylated heterodimers of ERBB2 KD mutants phosphorylate SHC1

Phosphorylated heterodimers of ERBB2 KD mutants recruit GRB2:SOS1 through SHC1

RAS activation by SOS1 bound to phosphorylated heterodimers of ERBB2 KD mutants

Phosphorylated heterodimers of ERBB2 KD mutants and EGFR bind GRB2:SOS1

RAS activation by SOS1 bound to phosphorylated heterodimers of ERBB2 KD mutants and EGFR

Phosphorylated heterodimers of ERBB2 KD mutants and EGFR phosphorylate PLCG1

Phosphorylated heterodimers of ERBB2 KD mutants and EGFR bind PLCG1

ERBB2 KD mutants bind TKIs

Resistant ERBB2 KD mutants do not bind trastuzumab

Resistant ERBB2 KD mutants do not bind AEE788

ERBB2 KD mutants do not bind osimertinib

Resistant ERBB2 KD mutants do not bind lapatinib

Resistant ERBB2 KD mutants do not bind neratinib

ERBB2 T862A does not bind sapitinib

ERBB2 T798M does not bind afatinib

ERBB2 T733I does not bind tesevatinib

ERBB2 ECD mutants heterodimerize with EGFR

Heterodimers of ERBB2 ECD mutants and EGFR trans-autophosphorylate

RAS guanyl nucleotide exchange mediated by the p-6Y- ERBB2 ECD mutants:EGF:p-6Y-EGFR:p-SHC1:GRB2:SOS1

ERBB2 ECD mutants bind trastuzumab

Phosphorylated heterodimers of ERBB2 ECD mutants and EGFR phosphorylate SHC1

PI3K bound to phosphorylated heterodimers of ERBB2 ECD mutants and EGFR converts PIP2 to PIP3

RAS activation by SOS1 bound to phosphorylated heterodimers of ERBB2 ECD mutants and EGFR through GRB2

GRB2:SOS1 binds to phosphorylated heterodimers of ERBB2 ECD mutants and EGFR

Phosphorylated heterodimers of ERBB2 ECD mutants and EGFR bind PLCG1

Phosphorylated heterodimers of ERBB2 ECD mutants and EGFR phosphorylate PLCG1

ERBB2 ECD mutants bind TKIs

Phosphorylated heterodimers of ERBB2 ECD mutants and EGFR recruit GRB2:SOS1 through SHC1

Phosphorylated heterodimers of ERBB2 ECD mutants and EGFR, in complex with GRB2:GAB1, bind PI3K

Phosphorylated heterodimers of ERBB2 ECD mutants and EGFR bind SHC1

Phosphorylated heterodimers of ERBB2 ECD mutants and EGFR bind GRB2:GAB1

ERBB2 TMD/JMD mutants bind trastuzumab

ERBB2 TMD/JMD mutants hetrodimerize

Phosphorylated heterodimers of ERBB2 TMD/JMD mutants and EGFR bind GRB2:SOS1

Phosphorylated heterodimers of ERBB2 TMD/JMD mutants recruit GRB2:SOS1 through SHC1

RAS activation by SOS1 bound to phosphorylated heterodimers of ERBB2 TMD/JMD mutants

Phosphorylated ERBB2 TMD/JMD heterodimers bind SHC1

ERBB2 TMD/JMD mutants bind TKIs

ERBB2 TMD/JMD mutants bind pertuzumab

Phosphorylated heterodimers of ERBB2 TMD/JMD mutants and EGFR phosphorylate PLCG1

Phosphorylated heterodimers of ERBB2 TMD/JMD mutants phosphorylate SHC1

Phosphorylated heterodimers of ERBB2 TMD/JMD mutants and EGFR bind PLCG1

RAS activation by SOS1 bound to phosphorylated heterodimers of ERBB2 TMD/JMD mutants and EGFR

ERBB2 TMD/JMD mutants do not bind pertuzumab

ERBB2 TMD/JMD heterodimers trans-autophosphorylate

ERBB2 binds pertuzumab

Shc1 binds phosphorylated ERBB2:EGFR heterodimers

Shc1 binds phosphorylated ERBB2:ERBB3 heterodimers

Plcg1 binds P-ERBB2:P-EGFR

Plcg1 phosphorylation by P-ERBB2:P-EGFR