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Group by :Switch typeMotif classProteinEnzymePathway            Group Index    Colouring Info              Filtered: UNIPROT:Q16881-4 (2 hits) x


x  Coloured by switch type.
  Domain hiding  Altered binding specificity  Motif hiding  Composite binding site formation
  Uncategorised  Rheostatic  Allostery  Avidity-sensing
  Physicochemical compatibility  Pre-translational  Competition

x  Index
Type: Binary Subtype: Pre‑translational


ProteinMotifStartEndSwitch descriptionInformation

Type: Binary Subtype: Pre‑translational
Pre-translational mechanisms such as alternative splicing, alternative promoter-usage and/or RNA editing result in inclusion or removal of exons that contain an entire or partial motif.
TRXR1_HUMANLIG_NRBOX4652Alternative splicing removes the NRBOX motif of Isoform TXNRD1_v2 of Thioredoxin reductase 1, cytoplasmic (TXNRD1), abrogating binding to Estrogen receptor (ESR1). Unlike splice variants without the NRBOX motif, TrxR1b (also known as Isoform TXNRD1_v2 of Thioredoxin reductase 1, cytoplasmic (TXNRD1)) is identified within the nucleus. TrxR1b enhanced the transcriptional activity of the estrogen receptors ESR1 and ESR2, possibly by providing a reduced environment in the immediate vicinity of the ERs.
details
TRXR1_HUMANLIG_NRBOX4652Alternative splicing removes the NRBOX motif of Isoform TXNRD1_v2 of Thioredoxin reductase 1, cytoplasmic (TXNRD1), abrogating binding to Estrogen receptor beta (ESR2). Unlike splice variants without the NRBOX motif, TrxR1b (also known as Isoform TXNRD1_v2 of Thioredoxin reductase 1, cytoplasmic (TXNRD1)) is identified within the nucleus. TrxR1b enhanced the transcriptional activity of the estrogen receptors ESR1 and ESR2, possibly by providing a reduced environment in the immediate vicinity of the ERs.
details
           
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