登録情報 データベース : PDB / ID : 4ubf 構造の表示 ダウンロードとリンクタイトル HsMCAK motor domain complex 要素(Kinesin-like protein KIF2C) x 2 詳細 キーワード CELL CYCLE / MCAK / Kif2c / Complex / Motor domain機能・相同性 機能・相同性情報分子機能 ドメイン・相同性 構成要素
postsynaptic cytoskeleton organization / regulation of chromosome segregation / establishment or maintenance of microtubule cytoskeleton polarity / metaphase chromosome alignment / centromeric DNA binding / microtubule plus-end / attachment of mitotic spindle microtubules to kinetochore / microtubule plus-end binding / Kinesins / kinesin complex ... postsynaptic cytoskeleton organization / regulation of chromosome segregation / establishment or maintenance of microtubule cytoskeleton polarity / metaphase chromosome alignment / centromeric DNA binding / microtubule plus-end / attachment of mitotic spindle microtubules to kinetochore / microtubule plus-end binding / Kinesins / kinesin complex / microtubule depolymerization / microtubule motor activity / COPI-dependent Golgi-to-ER retrograde traffic / microtubule-based movement / mitotic metaphase chromosome alignment / regulation of neurotransmitter receptor localization to postsynaptic specialization membrane / chromosome, centromeric region / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / MHC class II antigen presentation / Resolution of Sister Chromatid Cohesion / RHO GTPases Activate Formins / kinetochore / spindle / Separation of Sister Chromatids / presynapse / microtubule cytoskeleton / microtubule binding / microtubule / postsynapse / cell division / centrosome / glutamatergic synapse / ATP hydrolysis activity / ATP binding / nucleus / membrane / cytosol / cytoplasm 類似検索 - 分子機能 : / Kinesin-like protein KIF2A-like, N-terminal / Kinesin motor domain / Kinesin / Kinesin-like protein / Kinesin motor domain signature. / Kinesin motor domain, conserved site / Kinesin motor domain / Kinesin motor domain profile. / Kinesin motor, catalytic domain. ATPase. ... : / Kinesin-like protein KIF2A-like, N-terminal / Kinesin motor domain / Kinesin / Kinesin-like protein / Kinesin motor domain signature. / Kinesin motor domain, conserved site / Kinesin motor domain / Kinesin motor domain profile. / Kinesin motor, catalytic domain. ATPase. / Kinesin motor domain / Kinesin motor domain superfamily / P-loop containing nucleoside triphosphate hydrolase / 3-Layer(aba) Sandwich / Alpha Beta 類似検索 - ドメイン・相同性 ADENOSINE-5'-DIPHOSPHATE / Kinesin-like protein KIF2C 類似検索 - 構成要素生物種 Homo sapiens (ヒト)手法 X線回折 / シンクロトロン / 分子置換 / 解像度 : 3 Å 詳細データ登録者 Welburn, J.P.I. / Talapatra, S.K. 資金援助 英国, 1件 詳細 詳細を隠す組織 認可番号 国 Cancer Research UK 543WJW_R42094 英国
引用ジャーナル : Elife / 年 : 2015タイトル : The C-terminal region of the motor protein MCAK controls its structure and activity through a conformational switch.著者 : Talapatra, S.K. / Harker, B. / Welburn, J.P. 履歴 登録 2014年8月12日 登録サイト : RCSB / 処理サイト : PDBE改定 1.0 2015年5月6日 Provider : repository / タイプ : Initial release改定 1.1 2017年8月30日 Group : Author supporting evidence / カテゴリ : pdbx_audit_support / Item : _pdbx_audit_support.funding_organization改定 1.2 2018年6月6日 Group : Data collection / Database references / カテゴリ : citation / citation_authorItem : _citation.country / _citation.journal_abbrev ... _citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year 改定 1.3 2023年12月20日 Group : Data collection / Database references ... Data collection / Database references / Derived calculations / Refinement description カテゴリ : chem_comp_atom / chem_comp_bond ... chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn Item : _database_2.pdbx_DOI / _database_2.pdbx_database_accession ... _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_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.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id
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