Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.7.10.1 extracted from

  • He, L.; Shobnam, N.; Hristova, K.
    Specific inhibition of a pathogenic receptor tyrosine kinase by its transmembrane domain (2011), Biochim. Biophys. Acta, 1808, 253-259.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.10.1

Cloned(Commentary)

Cloned (Comment) Organism
expression in HEK 293 and B104-1-1 cells Rattus norvegicus
expression in HEK 293 and B104-1-1 cells Homo sapiens

Protein Variants

Protein Variants Comment Organism
A391E germ-line mutation in Crouzon syndrome with acanthosis nigricans. The transmembrane domains are able to dimerize, and mutation A391E increases the cross-linking propensities of the two domains Homo sapiens
additional information expression of the isolated transmembrane domain in HEK 293 and B104-1-1 cells and localization to the cell membrane. The transmembrane domains are able to dimerize, and mutation A391E increases the cross-linking propensities of the two domains Homo sapiens
additional information expression of the isolated transmembrane domain in HEK 293 and B104-1-1 cells and localization to the cell membrane. The transmembrane domains are able to dimerize, and mutation V664E increases the cross-linking propensities of the two domains. The transmembrane domain of mutant V664E specifically inhibits the phosphorylation of full-length mutant V664E, while the wild-type transmembrane domain does not. Mutant V664E transmembrane domain does not affect the phosphorylation levels of human full-length tyrosine kinase receptor FGFR3 mutant A391E Rattus norvegicus
V664E oncogenic mutation in TM domain, mutation increases the dimerizing propensities of the transmembrane domains Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Homo sapiens P22607
-
-
Rattus norvegicus P06494
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein the transmembrane domain of mutant V664E specifically inhibits the phosphorylation of full-length mutant V664E, while the wild-type transmembrane domain does not. Mutant V664E transmembrane domain does not affect the phosphorylation levels of human full-length tyrosine kinase receptor FGFR3 mutant A391E Rattus norvegicus
phosphoprotein the transmembrane domain of mutant V664E specifically inhibits the phosphorylation of full-length mutant V664E, while the wild-type transmembrane domain does not. Mutant V664E transmembrane domain does not affect the phosphorylation levels of human full-length tyrosine kinase receptor FGFR3 mutant A391E Homo sapiens

Synonyms

Synonyms Comment Organism
ErbB2
-
 Rattus norvegicus
FGFR3
-
 Homo sapiens
fibroblast growth factor receptor 3
-
 Homo sapiens
Neu
-
 Rattus norvegicus
receptor tyrosine-protein kinase erbB-2
-
 Rattus norvegicus