|Entry||Database: PDB / ID: 1zzp|
|Title||Solution structure of the F-actin binding domain of Bcr-Abl/c-Abl|
|Components||Proto-oncogene tyrosine-protein kinase ABL1|
|Keywords||TRANSFERASE / four helix bundle / nuclear export signal|
|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 / positive regulation blood vessel branching / nicotinate-nucleotide adenylyltransferase activity ...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 / positive regulation blood vessel branching / nicotinate-nucleotide adenylyltransferase activity / alpha-beta T cell differentiation / B cell proliferation involved in immune response / regulation of modification of synaptic structure / positive regulation of microtubule binding / positive regulation of Wnt signaling pathway, planar cell polarity pathway / microspike assembly / 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 / regulation of T cell differentiation / negative regulation of ubiquitin-protein transferase activity / negative regulation of BMP signaling pathway / regulation of microtubule polymerization / regulation of actin cytoskeleton reorganization / mitogen-activated protein kinase binding / positive regulation of interferon-gamma production => GO:0032729 / proline-rich region binding / syntaxin binding / DNA damage induced protein phosphorylation / cellular response to dopamine / positive regulation of osteoblast proliferation / negative regulation of cell-cell adhesion / 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 / positive regulation of actin cytoskeleton reorganization / regulation of endocytosis / mismatch repair / regulation of hematopoietic stem cell differentiation / negative regulation of endothelial cell apoptotic process / regulation of cell adhesion / 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 / four-way junction DNA binding / positive regulation of stress fiber assembly / signal transduction in response to DNA damage / regulation of actin cytoskeleton organization / positive regulation of endothelial cell migration / substrate adhesion-dependent cell spreading / sequence-specific double-stranded DNA binding / regulation of autophagy / cellular protein modification process / spleen development / negative regulation of I-kappaB kinase/NF-kappaB signaling / post-embryonic development / positive regulation of mitotic cell cycle / positive regulation of release of sequestered calcium ion into cytosol / 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 / actin cytoskeleton organization / non-specific protein-tyrosine kinase / non-membrane spanning protein tyrosine kinase activity / establishment of protein localization / SH3 domain binding / autophagy / postsynapse / 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
Tyrosine-protein kinase, catalytic domain / Tyrosine-protein kinase, active site / F-actin binding / Protein kinase, ATP binding site / SH3 domain / Tyrosine-protein kinase ABL1/transforming protein Abl / Tyrosine-protein kinase ABL, SH2 domain / Serine-threonine/tyrosine-protein kinase, catalytic domain / SH2 domain / SH3-like domain superfamily ...Tyrosine-protein kinase, catalytic domain / Tyrosine-protein kinase, active site / F-actin binding / Protein kinase, ATP binding site / SH3 domain / Tyrosine-protein kinase ABL1/transforming protein Abl / Tyrosine-protein kinase ABL, SH2 domain / Serine-threonine/tyrosine-protein kinase, catalytic domain / SH2 domain / SH3-like domain superfamily / SH2 domain superfamily / F-actin binding / Protein kinase domain / Protein kinase-like domain superfamily / Nucleotidyltransferases domain 2 / Four Helix Bundle (Hemerythrin (Met), subunit A) / Up-down Bundle / Mainly Alpha
Tyrosine-protein kinase ABL1
|Biological species||Homo sapiens (human)|
|Authors||Hantschel, O. / Wiesner, S. / Guttler, T. / Mackereth, C.D. / Rix, L.L.R. / Mikes, Z. / Dehne, J. / Gorlich, D. / Sattler, M. / Superti-Furga, G.|
|Citation||Journal: Mol.Cell / Year: 2005|
Title: Structural Basis for the Cytoskeletal Association of Bcr-Abl/c-Abl.
Authors: Hantschel, O. / Wiesner, S. / Guttler, T. / Mackereth, C.D. / Rix, L.L.R. / Mikes, Z. / Dehne, J. / Gorlich, D. / Sattler, M. / Superti-Furga, G.
SummaryFull reportAbout validation report
|Remark 999||SEQUENCE Two additional C-terminal residues (LE) result from primer design.|
|Structure viewer||Molecule: |
Downloads & links
A: Proto-oncogene tyrosine-protein kinase ABL1
|#1: Protein|| |
Mass: 14150.119 Da / Num. of mol.: 1 / Fragment: F-actin binding domain (residues 1007-1130)
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ABL1, ABL, JTK7 / Plasmid: modified pET24d / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P00519, EC: 22.214.171.124
|Experiment||Method: SOLUTION NMR|
|Radiation||Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M|
|Radiation wavelength||Relative weight: 1|
|NMR representative||Selection criteria: lowest energy|
|NMR ensemble||Conformer selection criteria: structures with the lowest energy|
Conformers calculated total number: 100 / Conformers submitted total number: 10
-Aug 12, 2020. New: Covid-19 info
New: Covid-19 info
Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data
-Mar 5, 2020. Novel coronavirus structure data
Novel coronavirus structure data
- International Committee on Taxonomy of Viruses (ICTV) defined the short name of the 2019 coronavirus as "SARS-CoV-2".
The species Severe acute respiratory syndrome-related coronavirus: classifying 2019-nCoV and naming it SARS-CoV-2 - nature microbiology
- In the structure databanks used in Yorodumi, some data are registered as the other names, "COVID-19 virus" and "2019-nCoV". Here are the details of the virus and the list of structure data.
Related info.:Yorodumi Speices / Aug 12, 2020. New: Covid-19 info
+Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)
EMDB accession codes are about to change! (news from PDBe EMDB page)
- The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force. (see PDBe EMDB page)
- The EM Navigator/Yorodumi systems omit the EMD- prefix.
Related info.:Q: What is "EMD"? / ID/Accession-code notation in Yorodumi/EM Navigator
+Jul 12, 2017. Major update of PDB
Major update of PDB
- wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary. This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated. See below links for details.
- In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software). Now, EM Navigator and Yorodumi are based on the updated data.
+Jun 16, 2017. Omokage search with filter
Omokage search with filter
- Result of Omokage search can be filtered by keywords and the database types
Related info.:Omokage search
Thousand views of thousand structures
- Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
- This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi