Predicate | Object |
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rdf:type | |
http://www.biopax.org/relea... |
cpath:CPATH-LOCAL-422776,
cpath:CPATH-LOCAL-422776,
cpath:CPATH-LOCAL-422777,
cpath:CPATH-LOCAL-422777,
cpath:CPATH-LOCAL-422778,
cpath:CPATH-LOCAL-422778,
cpath:CPATH-LOCAL-422779,
cpath:CPATH-LOCAL-422779,
cpath:CPATH-LOCAL-422780,
cpath:CPATH-LOCAL-422780,
cpath:CPATH-LOCAL-422781,
cpath:CPATH-LOCAL-422781,
cpath:CPATH-LOCAL-422782,
cpath:CPATH-LOCAL-422782,
cpath:CPATH-LOCAL-427237,
cpath:CPATH-LOCAL-427237
|
http://www.biopax.org/relea... |
Mitogen-activated protein kinase 3,
Mitogen-activated protein kinase 3
|
http://www.biopax.org/relea... |
MK03_HUMAN,
MK03_HUMAN
|
http://www.biopax.org/relea... | |
http://www.biopax.org/relea... |
2.7.11.24,
2.7.11.24,
ERK-1,
ERK-1,
ERT2,
ERT2,
Extracellular signal-regulated kinase 1,
Extracellular signal-regulated kinase 1,
Insulin-stimulated MAP2 kinase,
Insulin-stimulated MAP2 kinase,
MAP kinase 1,
MAP kinase 1,
MAP kinase 3,
MAP kinase 3,
MAP kinase isoform p44,
MAP kinase isoform p44,
MAPK 1,
MAPK 1,
MAPK 3,
MAPK 3,
Microtubule-associated protein 2 kinase,
Microtubule-associated protein 2 kinase,
Mitogen-activated protein kinase 1,
Mitogen-activated protein kinase 1,
p44-ERK1,
p44-ERK1,
p44-MAPK,
p44-MAPK
|
http://www.biopax.org/relea... |
FUNCTION: Involved in both the initiation and regulation of meiosis, mitosis, and postmitotic functions in differentiated cells by phosphorylating a number of transcription factors such as ELK-1. Phosphorylates EIF4EBP1; required for initiation of translation. Phosphorylates microtubule-associated protein 2 (MAP2). Phosphorylates SPZ1 (By similarity). Phosphorylates heat shock factor protein 4 (HSF4). CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. COFACTOR: Magnesium (By similarity). ENZYME REGULATION: Activated by tyrosine phosphorylation in response to insulin and NGF. SUBUNIT: Interacts with MORG1. Found in a complex with at least BRAF, HRAS1, MAP2K1, MAPK3 and RGS14 (By similarity). Binds to HIV-1 Nef. This interaction inhibits its kinase activity. Interacts with HSF4 and NISCH. Interacts with ARRB2. Interacts with ADAM15. DOMAIN: The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases. PTM: Phosphorylated upon FLT3 signaling (By similarity). Dually phosphorylated on Thr-202 and Tyr-204, which activates the enzyme. Dephosphorylated by PTPRJ at Tyr-204. SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily. SIMILARITY: Contains 1 protein kinase domain. GENE SYNONYMS: ERK1 PRKM3. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.,
FUNCTION: Involved in both the initiation and regulation of meiosis, mitosis, and postmitotic functions in differentiated cells by phosphorylating a number of transcription factors such as ELK-1. Phosphorylates EIF4EBP1; required for initiation of translation. Phosphorylates microtubule-associated protein 2 (MAP2). Phosphorylates SPZ1 (By similarity). Phosphorylates heat shock factor protein 4 (HSF4). CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. COFACTOR: Magnesium (By similarity). ENZYME REGULATION: Activated by tyrosine phosphorylation in response to insulin and NGF. SUBUNIT: Interacts with MORG1. Found in a complex with at least BRAF, HRAS1, MAP2K1, MAPK3 and RGS14 (By similarity). Binds to HIV-1 Nef. This interaction inhibits its kinase activity. Interacts with HSF4 and NISCH. Interacts with ARRB2. Interacts with ADAM15. DOMAIN: The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases. PTM: Phosphorylated upon FLT3 signaling (By similarity). Dually phosphorylated on Thr-202 and Tyr-204, which activates the enzyme. Dephosphorylated by PTPRJ at Tyr-204. SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily. SIMILARITY: Contains 1 protein kinase domain. GENE SYNONYMS: ERK1 PRKM3. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
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skos:exactMatch | |
skos:closeMatch |