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Group by :Switch typeMotif classProteinEnzymePathway            Group Index    Colouring Info              Filtered: UNIPROT:O95644 (5 hits) x


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  Domain hiding  Altered binding specificity  Motif hiding  Composite binding site formation
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  Physicochemical compatibility  Pre-translational  Competition

x  Index
MOD_GSK3_1MOD_SUMOTRG_NLS_MonoExtN_4


ProteinStartEndSwitch TypeSwitch SubtypeSwitch DescriptionInformation

MOD_GSK3_1 - GSK3 phosphorylation recognition site
NFAC1_HUMAN287294BinaryPhysicochemical compatibilityPhosphorylation of S294 adjacent to the NLS of Nuclear factor of activated T-cells, cytoplasmic 1 (NFATC1) by cAMP subfamily primes Nuclear factor of activated T-cells, cytoplasmic 1 (NFATC1) for subsequent phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which results in inhibition of nuclear import of Nuclear factor of activated T-cells, cytoplasmic 1 (NFATC1).
details
NFAC1_HUMAN238245BinaryPhysicochemical compatibilityPhosphorylation of S245 adjacent to the NLS of Nuclear factor of activated T-cells, cytoplasmic 1 (NFATC1) by cAMP subfamily primes Nuclear factor of activated T-cells, cytoplasmic 1 (NFATC1) for subsequent phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which results in inhibition of nuclear import of Nuclear factor of activated T-cells, cytoplasmic 1 (NFATC1).
details

MOD_SUMO - Motif recognised for modification by SUMO-1
NFAC1_HUMAN701704BinaryPre‑translationalAlternative splicing removes the Sumoylation motif (SIM) of Nuclear factor of activated T-cells, cytoplasmic 1 (NFATC1), preventing the sumolyation of Isoform A-alpha of Nuclear factor of activated T-cells, cytoplasmic 1 (NFATC1). Both the Isoform C-alpha of Nuclear factor of activated T-cells, cytoplasmic 1 (NFATC1) and Isoform A-alpha of Nuclear factor of activated T-cells, cytoplasmic 1 (NFATC1) exert a differential effect upon IL-2 expression. However, the longer isoform, Isoform C-alpha of Nuclear factor of activated T-cells, cytoplasmic 1 (NFATC1), has a sumoylation motif and is therefore negatively regulated in a sumolyation-dependent manner.
details
NFAC1_HUMAN913916BinaryPre‑translationalAlternative splicing removes the Sumoylation motif (SIM) of Nuclear factor of activated T-cells, cytoplasmic 1 (NFATC1), preventing the sumolyation of Isoform A-alpha of Nuclear factor of activated T-cells, cytoplasmic 1 (NFATC1). Both the Isoform C-alpha of Nuclear factor of activated T-cells, cytoplasmic 1 (NFATC1) and Isoform A-alpha of Nuclear factor of activated T-cells, cytoplasmic 1 (NFATC1) exert a differential effect upon IL-2 expression. However, the longer isoform, Isoform C-alpha of Nuclear factor of activated T-cells, cytoplasmic 1 (NFATC1), has a sumoylation motif and is therefore negatively regulated in a sumolyation-dependent manner.
details

TRG_NLS_MonoExtN_4 - Monopartite variant of the classical basically charged NLS. N-extended version.
NFAC1_HUMAN262269BinaryPhysicochemical compatibilityPhosphorylation of S241 and S290 adjacent to the NLS of Nuclear factor of activated T-cells, cytoplasmic 1 (NFATC1) by Glycogen synthase kinase-3 beta (GSK3B) and Glycogen synthase kinase-3 beta (GSK3B) inhibits nuclear import of Nuclear factor of activated T-cells, cytoplasmic 1 (NFATC1) by disrupting its interaction with Importin subunit alpha-2 (KPNA2). Calcium-dependent dephosphorylation by calcineurin promotes nuclear import.
details
           
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