登録情報 | データベース: PDB / ID: 2m1r |
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タイトル | PHD domain of ING4 N214D mutant |
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要素 | Inhibitor of growth protein 4 |
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キーワード | GENE REGULATION / ING4 / PHD / TRANSCRIPTION |
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機能・相同性 | 機能・相同性情報
DNA replication-dependent chromatin disassembly / regulation of DNA biosynthetic process / negative regulation of growth / intermediate filament cytoskeleton / histone H3K4me3 reader activity / regulation of cell cycle G2/M phase transition / positive regulation of DNA damage response, signal transduction by p53 class mediator / protein acetylation / : / histone acetyltransferase complex ...DNA replication-dependent chromatin disassembly / regulation of DNA biosynthetic process / negative regulation of growth / intermediate filament cytoskeleton / histone H3K4me3 reader activity / regulation of cell cycle G2/M phase transition / positive regulation of DNA damage response, signal transduction by p53 class mediator / protein acetylation / : / histone acetyltransferase complex / regulation of cell growth / HATs acetylate histones / transcription coactivator activity / regulation of cell cycle / positive regulation of apoptotic process / chromatin remodeling / negative regulation of cell population proliferation / negative regulation of DNA-templated transcription / apoptotic process / regulation of DNA-templated transcription / zinc ion binding / nucleoplasm / nucleus / cytosol類似検索 - 分子機能 Inhibitor of growth protein, N-terminal histone-binding / Inhibitor of growth proteins N-terminal histone-binding / Inhibitor of growth proteins N-terminal histone-binding / ING family / Zinc/RING finger domain, C3HC4 (zinc finger) / Herpes Virus-1 / Zinc finger, PHD-type, conserved site / Zinc finger PHD-type signature. / Zinc finger PHD-type profile. / Zinc finger, PHD-finger ...Inhibitor of growth protein, N-terminal histone-binding / Inhibitor of growth proteins N-terminal histone-binding / Inhibitor of growth proteins N-terminal histone-binding / ING family / Zinc/RING finger domain, C3HC4 (zinc finger) / Herpes Virus-1 / Zinc finger, PHD-type, conserved site / Zinc finger PHD-type signature. / Zinc finger PHD-type profile. / Zinc finger, PHD-finger / Zinc finger, PHD-type / PHD zinc finger / Zinc finger, FYVE/PHD-type / Zinc finger, RING/FYVE/PHD-type / 2-Layer Sandwich / Alpha Beta類似検索 - ドメイン・相同性 |
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生物種 | Homo sapiens (ヒト) |
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手法 | 溶液NMR / torsion angle dynamics, molecular dynamics |
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Model details | lowest energy, model1 |
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データ登録者 | Blanco, F.J. |
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引用 | ジャーナル: Carcinogenesis / 年: 2010 タイトル: Functional impact of cancer-associated mutations in the tumor suppressor protein ING4. 著者: Moreno, A. / Palacios, A. / Orgaz, J.L. / Jimenez, B. / Blanco, F.J. / Palmero, I. |
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履歴 | 登録 | 2012年12月5日 | 登録サイト: BMRB / 処理サイト: RCSB |
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改定 1.0 | 2012年12月26日 | Provider: repository / タイプ: Initial release |
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改定 1.1 | 2024年5月1日 | Group: Data collection / Database references / Derived calculations カテゴリ: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_nmr_software / pdbx_nmr_spectrometer / pdbx_struct_conn_angle / struct_conn / struct_ref_seq_dif / struct_site Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name / _pdbx_nmr_spectrometer.model / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id |
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