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Group by :Switch typeMotif classProteinEnzymePathway            Group Index    Colouring Info              Filtered: UNIPROT:O43521 (3 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

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Bcl-2-like protein 11Bcl-2-like protein 11


MotifStartEndSwitch TypeSwitch SubtypeSwitch DescriptionInformation

Bcl-2-like protein 11 - BCL2L11 -  Homo sapiens
DEG_SCF_TRCP1_29398BinaryPre‑translationalAlternative splicing removes the extended SCF-TrCP degron motif of Bcl-2-like protein 11 (BCL2L11), abrogating binding to F-box/WD repeat-containing protein 1A (BTRC). Upon mitogen survival signals, RPS6KA1 and RPS6KA2 kinases are up-regulated and rapidly phosphorylate the three serines of Isoform Bim(EL) of Bcl-2-like protein 11 (BCL2L11). This facilitates the binding of betaTrCP and subsequent ubiquitination and degradation of Isoform Bim(EL) of Bcl-2-like protein 11 (BCL2L11).
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LIG_Dynein_DLC8_1110116BinaryPre‑translationalAlternative splicing removes the Dynein-binding motif of Bcl-2-like protein 11 (BCL2L11), abrogating binding to Dynein light chain 1, cytoplasmic (DYNLL1). Most BCL2L11 in healthy cells is sequestered away bound to DYNLL1 (the exception is Bim-S Isoform BCL2-like 11 transcript variant 9 of Bcl-2-like protein 11 (BCL2L11)). Cells exposed to environmental stress up-regulate c-Jun NH(2)-terminal kinases (JNK) that phosphorylate both BCL2L11 and BMF, releasing them from motor complexes and promoting apoptosis.
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Bcl-2-like protein 11 - BCL2L11 -  Homo sapiens
LIG_Dynein_DLC8_15056BinaryPhysicochemical compatibilityPhosphorylation of T56 by Mitogen-activated protein kinase 8 (MAPK8) in the Dynein-binding motif of Isoform Bim(L) of Bcl-2-like protein 11 (BCL2L11) inhibits binding to Dynein light chain 1, cytoplasmic (DYNLL1). Most Bim in healthy cells is sequestered away bound to light chain dynein molecules. Cells exposed to environmental stress up-regulate c-Jun NH(2)-terminal kinase (JNK) that phosphorylates both Bim and Bmf, releasing them from motor complexes and promoting apoptosis.
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