switches.ELM

Group by :Switch type Motif class Protein Enzyme Pathway Hide inferred Group Index Colouring Info Filtered: UNIPROT:P12931 (6 hits) x

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Curated inferred

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Proto-oncogene tyrosine-protein kinase Src

Proto-oncogene tyrosine-protein kinase Src (Rattus)

Tyrosine-protein kinase CSK

Motif

Protein

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Information

Evidence

Proto-oncogene tyrosine-protein kinase Src - SRC - Rattus norvegicus
LIG_SH2_SRC	SRC_HUMAN	530	533	Binary	Physicochemical compatibility	Phosphorylation of Y530 in the SH2-binding motif of Proto-oncogene tyrosine-protein kinase Src (SRC) induces an intramolecular interaction with the SH2 domain of Proto-oncogene tyrosine-protein kinase Src (SRC) resulting in inhibition of its activity and preventing intermolecular interactions of its SH2 domain.	details	Inferred
Proto-oncogene tyrosine-protein kinase Src - SRC - Homo sapiens
LIG_SH2_SRC	SRC_HUMAN	530	533	Binary	Physicochemical compatibility	Phosphorylation of Y530 in the SH2-binding motif of Proto-oncogene tyrosine-protein kinase Src (SRC) induces an intramolecular interaction with the SH2 domain of Proto-oncogene tyrosine-protein kinase Src (SRC) resulting in inhibition of its activity and preventing intermolecular interactions of its SH2 domain.	details	Inferred
TRG_ENDOCYTIC_2	L1CAM_HUMAN	1176	1179	Binary	Physicochemical compatibility	Phosphorylation of Y1176 by Proto-oncogene tyrosine-protein kinase Src (SRC) in the endocytosis motif of Neural cell adhesion molecule L1 (L1CAM) inhibits binding to AP-2 complex subunit mu (AP2M1).	details	Curated
TRG_ENDOCYTIC_2	L1CAM_HUMAN	1176	1179	Binary	Physicochemical compatibility	Phosphorylation of Y1176 in the endocytotic motif of Neural cell adhesion molecule L1 (L1CAM) by Proto-oncogene tyrosine-protein kinase Src (SRC) abolishes binding to the AP-2 complex subunit mu (AP2M1) and thereby inhibits internalisation of Neural cell adhesion molecule L1 (L1CAM).	details	Curated
Tyrosine-protein kinase CSK - CSK - Homo sapiens
LIG_SH2_SRC	SRC_HUMAN	530	533	Binary	Physicochemical compatibility	Phosphorylation of Y530 in the SH2-binding motif of Proto-oncogene tyrosine-protein kinase Src (SRC) induces an intramolecular interaction with the SH2 domain of Proto-oncogene tyrosine-protein kinase Src (SRC) resulting in inhibition of its activity and preventing intermolecular interactions of its SH2 domain.	details	Inferred
LIG_SH2_SRC	SRC_HUMAN	530	533	Binary	Physicochemical compatibility	Phosphorylation of Y530 in the SH2-binding motif of Proto-oncogene tyrosine-protein kinase Src (SRC) induces an intramolecular interaction with the SH2 domain of Proto-oncogene tyrosine-protein kinase Src (SRC) resulting in inhibition of its activity and preventing intermolecular interactions of its SH2 domain.	details	Inferred