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Literature summary for 2.7.10.1 extracted from

  • Sharonov, G.; Bocharov, E.; Kolosov, P.; Astapova, M.; Arseniev, A.; Feofanov, A.
    Point mutations in dimerization motifs of the transmembrane domain stabilize active or inactive state of the EphA2 receptor tyrosine kinase (2014), J. Biol. Chem., 289, 14955-14964.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.10.1

Cloned(Commentary)

Cloned (Comment) Organism
expressed in HEK-293T cells Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
plasma membrane
-
 Homo sapiens 5886
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + a [protein]-L-tyrosine Homo sapiens
-
 ADP + a [protein]-L-tyrosine phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens P29317
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + a [protein]-L-tyrosine
-
 Homo sapiens ADP + a [protein]-L-tyrosine phosphate
-
 ?

Subunits

Subunits Comment Organism
homodimer
-
 Homo sapiens

Synonyms

Synonyms Comment Organism
EphA2
-
 Homo sapiens

General Information

General Information Comment Organism
physiological function EphA2 receptor tyrosine kinase plays a central role in the regulation of cell adhesion and guidance Homo sapiens