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Group by :Switch typeMotif classProteinEnzymePathway         Hide inferred   Group Index    Colouring Info              Filtered: UNIPROT:P49418 (4 hits) x


x  Coloured by: Modifier evidence source
          Curated          inferred


x  Index
CK2 subfamily ()Casein kinase II subunit alpha


MotifProteinStartEndSwitch TypeSwitch SubtypeSwitch descriptionInformationEvidence

CK2 subfamily
LIG_Clathr_ClatBox_1 AMPH_HUMAN351355BinaryPhysicochemical compatibilityPhosphorylation of T350 adjacent to the clathrin-binding motif of Amphiphysin (AMPH) by CK2 subfamily inhibits binding to the Clathrin heavy chain 1 (CLTC). A second clathrin-binding motif in Amphiphysin (AMPH) is regulated in a similar manner (see switch details). Both these motifs cooperate in avidity-based binding to Clathrin heavy chain 1 (CLTC) (see switch details).
details
Curated
LIG_Clathr_ClatBox_2 AMPH_HUMAN380385BinaryPhysicochemical compatibilityPhosphorylation of T387 adjacent to the clathrin-binding motif of Amphiphysin (AMPH) by CK2 subfamily inhibits binding to the Clathrin heavy chain 1 (CLTC). A second clathrin-binding motif in Amphiphysin (AMPH) is regulated in a similar manner (see switch details). Both these motifs cooperate in avidity-based binding to Clathrin heavy chain 1 (CLTC) (see switch details).
details
Curated

Casein kinase II subunit alpha - CSNK2A1 -  Homo sapiens
LIG_Clathr_ClatBox_1 AMPH_HUMAN351355BinaryPhysicochemical compatibilityPhosphorylation of T350 adjacent to the clathrin-binding motif of Amphiphysin (AMPH) by CK2 subfamily inhibits binding to the Clathrin heavy chain 1 (CLTC). A second clathrin-binding motif in Amphiphysin (AMPH) is regulated in a similar manner (see switch details). Both these motifs cooperate in avidity-based binding to Clathrin heavy chain 1 (CLTC) (see switch details).
details
Inferred
LIG_Clathr_ClatBox_2 AMPH_HUMAN380385BinaryPhysicochemical compatibilityPhosphorylation of T387 adjacent to the clathrin-binding motif of Amphiphysin (AMPH) by CK2 subfamily inhibits binding to the Clathrin heavy chain 1 (CLTC). A second clathrin-binding motif in Amphiphysin (AMPH) is regulated in a similar manner (see switch details). Both these motifs cooperate in avidity-based binding to Clathrin heavy chain 1 (CLTC) (see switch details).
details
Inferred
           
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