Entry | Database: PDB / ID: 6c9d |
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Title | Crystal structure of KA1-autoinhibited MARK1 kinase |
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Components | Serine/threonine-protein kinase MARK1,Serine/threonine-protein kinase MARK1 |
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Keywords | TRANSFERASE / Kinase / CAMKL / KA1 domain / autoinhibition |
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Function / homology | Function and homology information
establishment of mitochondrion localization / regulation of dendrite development / phosphatidic acid binding / tau-protein kinase / negative regulation of epithelial to mesenchymal transition / regulation of neuron projection development / tau-protein kinase activity / phosphatidylserine binding / cytoskeleton organization / phosphatidylinositol-4,5-bisphosphate binding ...establishment of mitochondrion localization / regulation of dendrite development / phosphatidic acid binding / tau-protein kinase / negative regulation of epithelial to mesenchymal transition / regulation of neuron projection development / tau-protein kinase activity / phosphatidylserine binding / cytoskeleton organization / phosphatidylinositol-4,5-bisphosphate binding / neuron migration / tau protein binding / Wnt signaling pathway / microtubule cytoskeleton organization / microtubule cytoskeleton / peptidyl-serine phosphorylation / cytoskeleton / non-specific serine/threonine protein kinase / intracellular signal transduction / protein phosphorylation / negative regulation of gene expression / protein serine kinase activity / protein serine/threonine kinase activity / dendrite / positive regulation of gene expression / magnesium ion binding / ATP binding / plasma membrane / cytoplasmSimilarity search - Function : / Kinase associated domain 1 (KA1) / Kinase associated domain 1 / Kinase associated domain 1 (KA1) profile. / KA1 domain/Ssp2, C-terminal / UBA/TS-N domain / Ubiquitin associated domain / Ubiquitin-associated domain / Ubiquitin-associated domain (UBA) profile. / Serine/threonine-protein kinase, active site ...: / Kinase associated domain 1 (KA1) / Kinase associated domain 1 / Kinase associated domain 1 (KA1) profile. / KA1 domain/Ssp2, C-terminal / UBA/TS-N domain / Ubiquitin associated domain / Ubiquitin-associated domain / Ubiquitin-associated domain (UBA) profile. / Serine/threonine-protein kinase, active site / Serine/Threonine protein kinases active-site signature. / Protein kinase domain / Serine/Threonine protein kinases, catalytic domain / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamilySimilarity search - Domain/homology |
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Biological species | Homo sapiens (human) |
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Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.499 Å |
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Authors | Emptage, R.P. / Marmorstein, R. |
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Funding support | United States, 2items Organization | Grant number | Country |
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National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS) | F32GM115098 | United States | National Institutes of Health/National Cancer Institute (NIH/NCI) | 5P01CA114046 | United States |
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Citation | Journal: Structure / Year: 2018 Title: Structural Basis for MARK1 Kinase Autoinhibition by Its KA1 Domain. Authors: Emptage, R.P. / Lemmon, M.A. / Ferguson, K.M. / Marmorstein, R. |
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History | Deposition | Jan 26, 2018 | Deposition site: RCSB / Processing site: RCSB |
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Revision 1.0 | Jul 11, 2018 | Provider: repository / Type: Initial release |
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Revision 1.1 | Aug 29, 2018 | Group: Data collection / Database references / Category: citation Item: _citation.journal_id_ISSN / _citation.journal_volume ..._citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.pdbx_database_id_PubMed / _citation.title |
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Revision 1.2 | Dec 4, 2019 | Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization |
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Revision 1.3 | Oct 4, 2023 | Group: Data collection / Database references / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_ncs_dom_lim Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id |
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