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Group by :Switch typeMotif classProteinEnzymePathway            Group Index    Colouring Info              Filtered: UNIPROT:P08965 (4 hits) x
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  Domain hiding  Altered binding specificity  Motif hiding  Composite binding site formation
  Uncategorised  Rheostatic  Allostery  Avidity-sensing
  Physicochemical compatibility  Pre-translational  Competition

x  Index
LIG_14-3-3_1LIG_14-3-3_2


ProteinStartEndSwitch TypeSwitch SubtypeSwitch DescriptionInformation

LIG_14-3-3_1 - Mode 1 interacting phospho-motif for 14-3-3 proteins with key conservation RxxSxP.
MEI2_SCHPO435
523		440
529		SpecificityDomain hidingBinding of meiRNA meiotic non-coding RNA (meiRNA) to the RRM domains of Meiosis protein mei2 (mei2) is essential for promotion of premeiotic DNA synthesis and meiosis I and is blocked by Pat1-mediated phosphorylation-induced binding of the 14-3-3 protein DNA damage checkpoint protein rad24 (rad24) to 2 14-3-3 binding motifs in mei2
details
MEI2_SCHPO435440Avidity‑sensingPhosphorylation of two 14-3-3-binding motifs in Meiosis protein mei2 (mei2) by Negative regulator of sexual conjugation and meiosis (ran1) induces high-avidity binding to dimeric DNA damage checkpoint protein rad24 (rad24), with pT527 being the high-affinity interaction site.
details

LIG_14-3-3_2 - Longer mode 2 interacting phospho-motif for 14-3-3 proteins with key conservation RxxxS#p.
MEI2_SCHPO435
523		440
529		SpecificityDomain hidingBinding of meiRNA meiotic non-coding RNA (meiRNA) to the RRM domains of Meiosis protein mei2 (mei2) is essential for promotion of premeiotic DNA synthesis and meiosis I and is blocked by Pat1-mediated phosphorylation-induced binding of the 14-3-3 protein DNA damage checkpoint protein rad24 (rad24) to 2 14-3-3 binding motifs in mei2
details
MEI2_SCHPO523529Avidity‑sensingPhosphorylation of two 14-3-3-binding motifs in Meiosis protein mei2 (mei2) by Negative regulator of sexual conjugation and meiosis (ran1) induces high-avidity binding to dimeric DNA damage checkpoint protein rad24 (rad24), with pT527 being the high-affinity interaction site.
details
           
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