ERBB2 TMD/JMD heterodimers trans-autophosphorylate

Stable Identifier
R-HSA-9665709
Type
Reaction [transition]
Species
Homo sapiens
Compartment
plasma membrane, cytosol
ReviewStatus
5/5
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ERBB2 TMD/JMD heterodimers trans-autophosphorylate
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Phosphorylation of tyrosine residues in the C-tail of ERBB2 was shown for the following ERBB2 TMD/JMD mutants:
ERBB2 V659E (Pahuja et al. 2018);
ERBB2 V659K (Pahuja et al. 2018);
ERBB2 G660D (Pahuja et al. 2018);
ERBB2 G660R (Pahuja et al. 2018);
ERBB2 S653C (de Martino et al. 2014 - phosphorylation at Y1248 demonstrated);
ERBB2 R677L (Pahuja et al. 2018);
ERBB2 R678Q (Bose et al. 2013; de Martino et al. 2014 - phosphorylation at Y1248 demonstrated; Pahuja et al. 2018); ERBB2 Q709L (Pahuja et al. 2018)

Phosphorylation of tyrosine residues in the C-tail of EGFR was demonstrated for ERBB2 S653C (de Martino et al. 2014 - phosphorylation at Y1068) and ERBB2 R678Q (Bose et al. 2013; de Martino et al. 2014 - phosphorylation at Y1068).

Phosphorylation of tyrosine residues in the C-tail of ERBB3 was demonstrated for ERBB2 S653C (de Martino et al. 2014 - phosphorylation at Y1197) and ERBB2 R678Q (Bose et al. 2013; de Martino et al. 2014 - phosphorylation at Y1197).

Signaling by ERBB2 V659K, ERBB2 G660D, ERBB2 G660R, ERBB2 R677L, ERBB2 E693K and ERBB2 Q709L has not been sufficiently studied and they are annotated as candidates.
Literature References
PubMed ID Title Journal Year
24971884 Impact of ERBB2 mutations on in vitro sensitivity of bladder cancer to lapatinib

Rieken, M, Xylinas, E, Klatte, T, Shariat, SF, Rouprêt, M, Elemento, O, Clozel, T, Zhuang, D, Krzywinski, M, de Martino, M

Cancer Biol. Ther. 2014
30449325 Actionable Activating Oncogenic ERBB2/HER2 Transmembrane and Juxtamembrane Domain Mutations

Antony, A, Khanna-Gupta, A, Singh, A, Pahuja, KB, Kljavin, NM, Bueno, R, Chougule, A, Dutt, A, Phalke, S, Prabhash, K, Gupta, R, Ziai, J, Banavali, SD, Kumar, P, Trivedi, V, Seshagiri, S, Jaiswal, BS, Nguyen, TT, DeGrado, WF, Ramprasad, V, Vargas, D, Senger, K, Chaudhuri, S, Sokol, ES, Trabucco, SE, Patil, V, Joshi, A, Thaker, TM, Noronha, V, Hartmaier, RJ, Durinck, S, Mravic, M, Stawiski, EW, Jura, N

Cancer Cell 2018
23220880 Activating HER2 mutations in HER2 gene amplification negative breast cancer

Bose, R, Shen, W, Aronson, AB, Goel, N, Koboldt, DC, Li, S, Searleman, AC, Ma, CX, Ellis, MJ, Shen, D, Ding, L, Monsey, J, Mardis, ER, Kavuri, SM

Cancer Discov 2013
Participants
Input
Output
Participates
as an event of
Catalyst Activity

protein tyrosine kinase activity of ERBB2 TMD/JMD mutants:Ligand-Activated EGFR,ERBB3,(ERBB4) [plasma membrane]

Physical Entity
ERBB2 TMD/JMD mutants:Ligand-Activated EGFR,ERBB3,(ERBB4) [plasma membrane] (Homo sapiens)
Activity
protein tyrosine kinase activity (GO:0004713)
Normal reaction
Trans-autophosphorylation of ERBB2 heterodimers (Homo sapiens)
Functional status

Gain of function of ERBB2 TMD/JMD mutants:Ligand-Activated EGFR,ERBB3,(ERBB4) [plasma membrane]

Normal Entity
Disease Entity
Status
Disease
Name Identifier Synonyms
cancer DOID:162 malignant tumor, malignant neoplasm, primary cancer
Authored
Orlic-Milacic, M  (2019-10-31)
Reviewed
Bose, R  (2019-10-25)
Kancha, RK  (2019-11-03)
Krishna, A  (2019-10-25)
Created
Orlic-Milacic, M  (2019-10-31)
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