About Help Definitions Submit Search Analyse Browse Home


Group by :Switch typeMotif classProteinEnzymePathway            Group Index    Colouring Info              Filtered: UNIPROT:Q92731 (4 hits) x
submit


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
LIG_NRBOXMOD_GSK3_1MOD_SUMO_PHOS


ProteinStartEndSwitch TypeSwitch SubtypeSwitch DescriptionInformation

LIG_NRBOX - The nuclear receptor box motif (LXXLL) confers binding to nuclear receptors.
TRXR1_HUMAN4652BinaryPre‑translationalAlternative 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

MOD_GSK3_1 - GSK3 phosphorylation recognition site
ESR2_HUMAN512BinaryPhysicochemical compatibilityThe GSK3-beta binding site at S12 in Estrogen receptor beta (ESR2) is primed by (most likely) RAC-alpha serine/threonine-protein kinase (AKT1). This enhances the binding of SUMO-conjugating enzyme UBC9 (UBE2I) at the adjacent Sumoylation site. This site is also primed at S6 (most likely) by AKT1. The addition of SUMO at K4 stabilises ESR2 as it prevents the ubiquitination at K4 (see switch details
details

MOD_SUMO_PHOS -
ESR2_HUMAN47BinaryPhysicochemical compatibilityThe GSK3-beta binding site at S12 in Estrogen receptor beta (ESR2) is primed by (most likely) RAC-alpha serine/threonine-protein kinase (AKT1). This enhances the binding of SUMO-conjugating enzyme UBC9 (UBE2I) at the adjacent Sumoylation site. This site is also primed at S6 (most likely) by AKT1. The addition of SUMO at K4 stabilises ESR2 as it prevents the ubiquitination at K4 (see switch details)
details
ESR2_HUMAN47BinaryPhysicochemical compatibilitySumoylation of K4 in Estrogen receptor beta (ESR2) is inhibited by ubiquitination K4. This destabilises ESR2 increasing its turnover (see also switch details)
details
           
Please send any suggestions/comments to: switches@elm.eu.org