Statements in which the resource exists as a subject.
PredicateObject
rdf:type
http://www.biopax.org/relea...
http://www.biopax.org/relea...
Mitogen-activated protein kinase 1, Mitogen-activated protein kinase 1, Mitogen-activated protein kinase 1
http://www.biopax.org/relea...
MK01_HUMAN, MK01_HUMAN, MK01_HUMAN
http://www.biopax.org/relea...
http://www.biopax.org/relea...
2.7.11.24, 2.7.11.24, 2.7.11.24, ERK-2, ERK-2, ERK-2, ERT1, ERT1, ERT1, Extracellular signal-regulated kinase 2, Extracellular signal-regulated kinase 2, Extracellular signal-regulated kinase 2, MAP kinase 1, MAP kinase 1, MAP kinase 1, MAP kinase 2, MAP kinase 2, MAP kinase 2, MAP kinase isoform p42, MAP kinase isoform p42, MAP kinase isoform p42, MAPK 1, MAPK 1, MAPK 1, MAPK 2, MAPK 2, MAPK 2, Mitogen-activated protein kinase 2, Mitogen-activated protein kinase 2, Mitogen-activated protein kinase 2, p42-MAPK, p42-MAPK, p42-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 ELK1. Phosphorylates EIF4EBP1; required for initiation of translation. Phosphorylates microtubule-associated protein 2 (MAP2). Phosphorylates SPZ1 (By similarity). Phosphorylates heat shock factor protein 4 (HSF4) and ARHGEF2. FUNCTION: Acts as a transcriptional repressor. Binds to a [GC]AAA[GC] consensus sequence. Repress the expression of interferon gamma-induced genes. Seems to bind to the promoter of CCL5, DMP1, IFIH1, IFITM1, IRF7, IRF9, LAMP3, OAS1, OAS2, OAS3 and STAT1. Transcriptional activity is independent of kinase activity. CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. COFACTOR: Magnesium (By similarity). ENZYME REGULATION: Activated by phosphorylation on tyrosine and threonine in response to insulin and NGF. Both phosphorylations are required for activity (By similarity). SUBUNIT: Interacts with MORG1 (By similarity). Binds to HIV-1 Nef through its SH3 domain. This interaction inhibits its tyrosine- kinase activity. Interacts with its substrates HSF4 and ARHGEF2. Interacts (phosphorylated form) with CAV2 ('Tyr-19'-phosphorylated form); the interaction, promoted by insulin, leads to nuclear location and MAPK1 activation (By similarity). Interacts with NISCH. Interacts with ARRB2. Interacts with ADAM15. Interacts with isoform 1 of NEK2. SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, centrosome. 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-185 and Tyr-187, which activates the enzyme. Dephosphorylated by PTPRJ at Tyr-187. SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily. SIMILARITY: Contains 1 protein kinase domain. SEQUENCE CAUTION: Sequence=CAA77753.1; Type=Erroneous initiation; Note=Translation N-terminally extended; WEB RESOURCE: Name=Wikipedia; Note=Extracellular signal-regulated kinase entry; URL="http://en.wikipedia.org/wiki/Extracellular_signal-regulated_kinase"; GENE SYNONYMS: ERK2 PRKM1 PRKM2. 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 ELK1. Phosphorylates EIF4EBP1; required for initiation of translation. Phosphorylates microtubule-associated protein 2 (MAP2). Phosphorylates SPZ1 (By similarity). Phosphorylates heat shock factor protein 4 (HSF4) and ARHGEF2. FUNCTION: Acts as a transcriptional repressor. Binds to a [GC]AAA[GC] consensus sequence. Repress the expression of interferon gamma-induced genes. Seems to bind to the promoter of CCL5, DMP1, IFIH1, IFITM1, IRF7, IRF9, LAMP3, OAS1, OAS2, OAS3 and STAT1. Transcriptional activity is independent of kinase activity. CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. COFACTOR: Magnesium (By similarity). ENZYME REGULATION: Activated by phosphorylation on tyrosine and threonine in response to insulin and NGF. Both phosphorylations are required for activity (By similarity). SUBUNIT: Interacts with MORG1 (By similarity). Binds to HIV-1 Nef through its SH3 domain. This interaction inhibits its tyrosine- kinase activity. Interacts with its substrates HSF4 and ARHGEF2. Interacts (phosphorylated form) with CAV2 ('Tyr-19'-phosphorylated form); the interaction, promoted by insulin, leads to nuclear location and MAPK1 activation (By similarity). Interacts with NISCH. Interacts with ARRB2. Interacts with ADAM15. Interacts with isoform 1 of NEK2. SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, centrosome. 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-185 and Tyr-187, which activates the enzyme. Dephosphorylated by PTPRJ at Tyr-187. SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily. SIMILARITY: Contains 1 protein kinase domain. SEQUENCE CAUTION: Sequence=CAA77753.1; Type=Erroneous initiation; Note=Translation N-terminally extended; WEB RESOURCE: Name=Wikipedia; Note=Extracellular signal-regulated kinase entry; URL="http://en.wikipedia.org/wiki/Extracellular_signal-regulated_kinase"; GENE SYNONYMS: ERK2 PRKM1 PRKM2. 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 ELK1. Phosphorylates EIF4EBP1; required for initiation of translation. Phosphorylates microtubule-associated protein 2 (MAP2). Phosphorylates SPZ1 (By similarity). Phosphorylates heat shock factor protein 4 (HSF4) and ARHGEF2. FUNCTION: Acts as a transcriptional repressor. Binds to a [GC]AAA[GC] consensus sequence. Repress the expression of interferon gamma-induced genes. Seems to bind to the promoter of CCL5, DMP1, IFIH1, IFITM1, IRF7, IRF9, LAMP3, OAS1, OAS2, OAS3 and STAT1. Transcriptional activity is independent of kinase activity. CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. COFACTOR: Magnesium (By similarity). ENZYME REGULATION: Activated by phosphorylation on tyrosine and threonine in response to insulin and NGF. Both phosphorylations are required for activity (By similarity). SUBUNIT: Interacts with MORG1 (By similarity). Binds to HIV-1 Nef through its SH3 domain. This interaction inhibits its tyrosine- kinase activity. Interacts with its substrates HSF4 and ARHGEF2. Interacts (phosphorylated form) with CAV2 ('Tyr-19'-phosphorylated form); the interaction, promoted by insulin, leads to nuclear location and MAPK1 activation (By similarity). Interacts with NISCH. Interacts with ARRB2. Interacts with ADAM15. Interacts with isoform 1 of NEK2. SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, centrosome. 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-185 and Tyr-187, which activates the enzyme. Dephosphorylated by PTPRJ at Tyr-187. SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily. SIMILARITY: Contains 1 protein kinase domain. SEQUENCE CAUTION: Sequence=CAA77753.1; Type=Erroneous initiation; Note=Translation N-terminally extended; WEB RESOURCE: Name=Wikipedia; Note=Extracellular signal-regulated kinase entry; URL="http://en.wikipedia.org/wiki/Extracellular_signal-regulated_kinase"; GENE SYNONYMS: ERK2 PRKM1 PRKM2. 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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