ACTIN ACTIVATED ATPASE
\ˈaktɪn ˈaktɪvˌe͡ɪtɪd at pˈe͡ɪs], \ˈaktɪn ˈaktɪvˌeɪtɪd at pˈeɪs], \ˈa_k_t_ɪ_n ˈa_k_t_ɪ_v_ˌeɪ_t_ɪ_d a_t p_ˈeɪ_s]\
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A diverse superfamily of proteins that function as translocating proteins. They share the common characteristics of being able to bind ACTINS and hydrolyse MgATP. Myosins generally consist of heavy chains which are involved in locomotion, and light chains which are are involve in regulation. Within the structure of myosin heavy chain are three domains: the head, the neck and the tail. The head region of the heavy chain contains the actin binding domain and MgATPase domain which provides energy for locomotion. The neck region is involved in binding the light-chains. The tail region provides the anchoring point that maintains the position of the heavy chain. The superfamily of myosins is organized into structural classes based upon the type and arrangement of the subunits they contain.
By DataStellar Co., Ltd
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Proto Oncogene Proteins c erbB 2
- cell surface protein-tyrosine kinase that is found to be overexpressed in significant number adenocarcinomas. It has extensive homology can heterodimerize EGF EPIDERMAL GROWTH FACTOR), 3 receptor (RECEPTOR, 3) and the 4 receptor. Activation of erbB-2 receptor occurs during heterodimer formation with a ligand-bound erbB family members. EC 2.7.11.-.
Nearby Words
- actidione
- actifed
- actihaemyl
- actilyse
- actin
- Actin Activated ATPase
- actin binding proteins
- actin filament
- actin filaments
- actin s1 atpase
- actinal