Linked Life Data

CPATH-63663

Source:http://cbio.mskcc.org/cpath#CPATH-63663

Statements in which the resource exists.
SubjectPredicateObjectContext
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cpath:CPATH-63663http://www.biopax.org/relea...FUNCTION: Carries out a dual function: signal transduction and activation of transcription. Binds to the GAS element and activates PRL-induced transcription. SUBUNIT: Forms a homodimer or a heterodimer with a related family member. Binds NR3C1 (By similarity). Interacts with NCOA1 and SOCS7. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Translocated into the nucleus in response to phosphorylation. PTM: Tyrosine phosphorylated in response to IL-2, IL-3, IL-7, IL- 15, GM-CSF, growth hormone, prolactin, erythropoietin and thrombopoietin. Tyrosine phosphorylation is required for DNA- binding activity and dimerization. Serine phosphorylation is also required for maximal transcriptional activity (By similarity). Tyrosine phosphorylated in response to signaling via activated FLT3; wild-type FLT3 results in much weaker phosphorylation than constitutively activated mutant FLT3. Alternatively, can be phosporylated by JAK2 at Tyr-694. SIMILARITY: Belongs to the transcription factor STAT family. SIMILARITY: Contains 1 SH2 domain. WEB RESOURCE: Name=Wikipedia; Note=STAT5 entry; URL="http://en.wikipedia.org/wiki/STAT5"; GENE SYNONYMS: STAT5. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.lld:biogrid
cpath:CPATH-63663http://www.biopax.org/relea...FUNCTION: Carries out a dual function: signal transduction and activation of transcription. Binds to the GAS element and activates PRL-induced transcription. SUBUNIT: Forms a homodimer or a heterodimer with a related family member. Binds NR3C1 (By similarity). Interacts with NCOA1 and SOCS7. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Translocated into the nucleus in response to phosphorylation. PTM: Tyrosine phosphorylated in response to IL-2, IL-3, IL-7, IL- 15, GM-CSF, growth hormone, prolactin, erythropoietin and thrombopoietin. Tyrosine phosphorylation is required for DNA- binding activity and dimerization. Serine phosphorylation is also required for maximal transcriptional activity (By similarity). Tyrosine phosphorylated in response to signaling via activated FLT3; wild-type FLT3 results in much weaker phosphorylation than constitutively activated mutant FLT3. Alternatively, can be phosporylated by JAK2 at Tyr-694. SIMILARITY: Belongs to the transcription factor STAT family. SIMILARITY: Contains 1 SH2 domain. WEB RESOURCE: Name=Wikipedia; Note=STAT5 entry; URL="http://en.wikipedia.org/wiki/STAT5"; GENE SYNONYMS: STAT5. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.lld:cellmap
cpath:CPATH-63663http://www.biopax.org/relea...FUNCTION: Carries out a dual function: signal transduction and activation of transcription. Binds to the GAS element and activates PRL-induced transcription. SUBUNIT: Forms a homodimer or a heterodimer with a related family member. Binds NR3C1 (By similarity). Interacts with NCOA1 and SOCS7. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Translocated into the nucleus in response to phosphorylation. PTM: Tyrosine phosphorylated in response to IL-2, IL-3, IL-7, IL- 15, GM-CSF, growth hormone, prolactin, erythropoietin and thrombopoietin. Tyrosine phosphorylation is required for DNA- binding activity and dimerization. Serine phosphorylation is also required for maximal transcriptional activity (By similarity). Tyrosine phosphorylated in response to signaling via activated FLT3; wild-type FLT3 results in much weaker phosphorylation than constitutively activated mutant FLT3. Alternatively, can be phosporylated by JAK2 at Tyr-694. SIMILARITY: Belongs to the transcription factor STAT family. SIMILARITY: Contains 1 SH2 domain. WEB RESOURCE: Name=Wikipedia; Note=STAT5 entry; URL="http://en.wikipedia.org/wiki/STAT5"; GENE SYNONYMS: STAT5. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.lld:imid
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