|Entry||Database: PDB / ID: 1ab2|
|Title||THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE SRC HOMOLOGY 2 DOMAIN OF C-ABL|
|Components||C-ABL TYROSINE KINASE SH2 DOMAIN|
|Function / homology|
Function and homology information
mitochondrial depolarization / positive regulation of interleukin-2 production => GO:0032743 / transitional one stage B cell differentiation / positive regulation of actin filament binding / DNA conformation change / negative regulation of phospholipase C activity / regulation of extracellular matrix organization / activation of protein kinase C activity / nicotinate-nucleotide adenylyltransferase activity / B cell proliferation involved in immune response ...mitochondrial depolarization / positive regulation of interleukin-2 production => GO:0032743 / transitional one stage B cell differentiation / positive regulation of actin filament binding / DNA conformation change / negative regulation of phospholipase C activity / regulation of extracellular matrix organization / activation of protein kinase C activity / nicotinate-nucleotide adenylyltransferase activity / B cell proliferation involved in immune response / positive regulation blood vessel branching / regulation of modification of synaptic structure / positive regulation of microtubule binding / microspike assembly / positive regulation of Wnt signaling pathway, planar cell polarity pathway / neuroepithelial cell differentiation / cerebellum morphogenesis / collateral sprouting / B-1 B cell homeostasis / actin filament branching / positive regulation of oxidoreductase activity / activated T cell proliferation / circulatory system development => GO:0072359 / neuropilin binding / neuropilin signaling pathway / bubble DNA binding / regulation of Cdc42 protein signal transduction / negative regulation of protein serine/threonine kinase activity / alpha-beta T cell differentiation / regulation of T cell differentiation / negative regulation of ubiquitin-protein transferase activity / regulation of microtubule polymerization / negative regulation of BMP signaling pathway / regulation of actin cytoskeleton reorganization / positive regulation of interferon-gamma production => GO:0032729 / mitogen-activated protein kinase binding / proline-rich region binding / syntaxin binding / DNA damage induced protein phosphorylation / cellular response to dopamine / negative regulation of cell-cell adhesion / positive regulation of osteoblast proliferation / negative regulation of cellular senescence / regulation of response to DNA damage stimulus / regulation of axon extension / platelet-derived growth factor receptor-beta signaling pathway / positive regulation of cell migration involved in sprouting angiogenesis / cell leading edge / negative regulation of long-term synaptic potentiation / actin monomer binding / neuromuscular process controlling balance / Bergmann glial cell differentiation / positive regulation of focal adhesion assembly / regulation of endocytosis / positive regulation of actin cytoskeleton reorganization / mismatch repair / regulation of cell adhesion / regulation of hematopoietic stem cell differentiation / negative regulation of endothelial cell apoptotic process / regulation of cell motility / negative regulation of mitotic cell cycle / positive regulation of substrate adhesion-dependent cell spreading / endothelial cell migration / positive regulation of muscle cell differentiation / positive regulation of stress fiber assembly / four-way junction DNA binding / signal transduction in response to DNA damage / regulation of actin cytoskeleton organization / positive regulation of endothelial cell migration / substrate adhesion-dependent cell spreading / regulation of autophagy / cellular protein modification process / spleen development / negative regulation of I-kappaB kinase/NF-kappaB signaling / post-embryonic development / positive regulation of release of sequestered calcium ion into cytosol / positive regulation of mitotic cell cycle / SH2 domain binding / negative regulation of ERK1 and ERK2 cascade / thymus development / phosphotyrosine residue binding / protein kinase C binding / neural tube closure / ephrin receptor binding / integrin-mediated signaling pathway / peptidyl-tyrosine autophosphorylation / sequence-specific double-stranded DNA binding / actin cytoskeleton organization / non-specific protein-tyrosine kinase / non-membrane spanning protein tyrosine kinase activity / establishment of protein localization / SH3 domain binding / postsynapse / autophagy / cell cycle arrest / epidermal growth factor receptor signaling pathway / cellular response to hydrogen peroxide / positive regulation of neuron death / B cell receptor signaling pathway / Fc-gamma receptor signaling pathway involved in phagocytosis
Protein kinase, ATP binding site / Tyrosine-protein kinase, active site / F-actin binding / SH3 domain / Serine-threonine/tyrosine-protein kinase, catalytic domain / SH2 domain / Tyrosine-protein kinase, catalytic domain / Tyrosine-protein kinase ABL1/transforming protein Abl / Protein kinase domain / Tyrosine-protein kinase ABL, SH2 domain ...Protein kinase, ATP binding site / Tyrosine-protein kinase, active site / F-actin binding / SH3 domain / Serine-threonine/tyrosine-protein kinase, catalytic domain / SH2 domain / Tyrosine-protein kinase, catalytic domain / Tyrosine-protein kinase ABL1/transforming protein Abl / Protein kinase domain / Tyrosine-protein kinase ABL, SH2 domain / SH3-like domain superfamily / SH2 domain superfamily / SH2 domain / Protein kinase-like domain superfamily / SH2 domain / SHC Adaptor Protein / 2-Layer Sandwich / Alpha Beta
Tyrosine-protein kinase ABL1
|Biological species||Homo sapiens (human)|
|Authors||Overduin, M. / Rios, C.B. / Mayer, B.J. / Baltimore, D. / Cowburn, D.|
Journal: Cell(Cambridge,Mass.) / Year: 1992
Title: Three-dimensional solution structure of the src homology 2 domain of c-abl.
Authors: Overduin, M. / Rios, C.B. / Mayer, B.J. / Baltimore, D. / Cowburn, D.
SummaryFull reportAbout validation report
|Structure viewer||Molecule: |
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A: C-ABL TYROSINE KINASE SH2 DOMAIN
|#1: Protein|| |
Mass: 12159.387 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / References: UniProt: P00519, EC: 220.127.116.11
|Experiment||Method: SOLUTION NMR|
*PLUSMethod: other / Details: NMR
|NMR ensemble||Conformers submitted total number: 20|
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