LIG_CORNRBOX - The corepressor nuclear receptor box motif confers binding to nuclear receptors. |
NCOR1_HUMAN | 2051 | 2059 | Binary | Allostery | Binding of the all-trans-retinoic acid ligand to the nuclear Retinoic acid receptor alpha (RARA) makes the binding site for the CORNRBOX motif of Nuclear receptor corepressor 1 (NCOR1) inaccessible. | details |
NCOR1_HUMAN | 2263 | 2271 | Binary | Allostery | Binding of the all-trans-retinoic acid ligand to the nuclear Retinoic acid receptor alpha (RARA) makes the binding site for the CORNRBOX motif of Nuclear receptor corepressor 1 (NCOR1) inaccessible. | details |
NCOR2_HUMAN | 2143 | 2151 | Binary | Allostery | Binding of the leukotriene D4 ligand to the nuclear Peroxisome proliferator-activated receptor alpha (PPARA) makes the binding site for the CORNRBOX motif of Nuclear receptor corepressor 2 (NCOR2) inaccessible. | details |
NCOR2_HUMAN | 2350 | 2358 | Binary | Allostery | Binding of the leukotriene D4 ligand to the nuclear Peroxisome proliferator-activated receptor alpha (PPARA) makes the binding site for the CORNRBOX motif of Nuclear receptor corepressor 2 (NCOR2) inaccessible. | details |
LIG_NRBOX - The nuclear receptor box motif (LXXLL) confers binding to nuclear receptors. |
NRIP1_HUMAN | 132 | 138 | Binary | Allostery | Binding of the estrogen ligand to the nuclear Estrogen receptor (ESR1) makes the binding site for the NRBOX motif of Nuclear receptor-interacting protein 1 (NRIP1) accessible. | details |
NRIP1_HUMAN | 184 | 190 | Binary | Allostery | Binding of the estrogen ligand to the nuclear Estrogen receptor (ESR1) makes the binding site for the NRBOX motif of Nuclear receptor-interacting protein 1 (NRIP1) accessible. | details |
NRIP1_HUMAN | 20 | 26 | Binary | Allostery | Binding of the estrogen ligand to the nuclear Estrogen receptor (ESR1) makes the binding site for the NRBOX motif of Nuclear receptor-interacting protein 1 (NRIP1) accessible. | details |
NRIP1_HUMAN | 265 | 271 | Binary | Allostery | Binding of the estrogen ligand to the nuclear Estrogen receptor (ESR1) makes the binding site for the NRBOX motif of Nuclear receptor-interacting protein 1 (NRIP1) accessible. | details |
NRIP1_HUMAN | 379 | 385 | Binary | Allostery | Binding of the estrogen ligand to the nuclear Estrogen receptor (ESR1) makes the binding site for the NRBOX motif of Nuclear receptor-interacting protein 1 (NRIP1) accessible. | details |
NRIP1_HUMAN | 499 | 505 | Binary | Allostery | Binding of the estrogen ligand to the nuclear Estrogen receptor (ESR1) makes the binding site for the NRBOX motif of Nuclear receptor-interacting protein 1 (NRIP1) accessible. | details |
NRIP1_HUMAN | 500 | 506 | Binary | Allostery | Binding of the estrogen ligand to the nuclear Estrogen receptor (ESR1) makes the binding site for the NRBOX motif of Nuclear receptor-interacting protein 1 (NRIP1) accessible. | details |
NRIP1_HUMAN | 712 | 718 | Binary | Allostery | Binding of the estrogen ligand to the nuclear Estrogen receptor (ESR1) makes the binding site for the NRBOX motif of Nuclear receptor-interacting protein 1 (NRIP1) accessible. | details |
NRIP1_HUMAN | 818 | 824 | Binary | Allostery | Binding of the estrogen ligand to the nuclear Estrogen receptor (ESR1) makes the binding site for the NRBOX motif of Nuclear receptor-interacting protein 1 (NRIP1) accessible. | details |
NRIP1_HUMAN | 935 | 941 | Binary | Allostery | Binding of the estrogen ligand to the nuclear Estrogen receptor (ESR1) makes the binding site for the NRBOX motif of Nuclear receptor-interacting protein 1 (NRIP1) accessible. | details |
NCOA2_HUMAN | 640 | 646 | Binary | Allostery | Binding of the glucocorticoid ligand to the nuclear Glucocorticoid receptor (NR3C1) makes the binding site for the NRBOX motif of Nuclear receptor coactivator 2 (NCOA2) accessible. | details |
NCOA2_HUMAN | 689 | 695 | Binary | Allostery | Binding of the glucocorticoid ligand to the nuclear Glucocorticoid receptor (NR3C1) makes the binding site for the NRBOX motif of Nuclear receptor coactivator 2 (NCOA2) accessible. | details |
NCOA2_HUMAN | 744 | 750 | Binary | Allostery | Binding of the glucocorticoid ligand to the nuclear Glucocorticoid receptor (NR3C1) makes the binding site for the NRBOX motif of Nuclear receptor coactivator 2 (NCOA2) accessible. | details |
MED1_HUMAN | 603 | 609 | Binary | Allostery | Binding of the 3,3',5-triiodo-L-thyronine ligand to the nuclear Thyroid hormone receptor alpha (THRA) makes the binding site for the NRBOX motif of Mediator of RNA polymerase II transcription subunit 1 (MED1) accessible. | details |
MED1_HUMAN | 644 | 650 | Binary | Allostery | Binding of the 3,3',5-triiodo-L-thyronine ligand to the nuclear Thyroid hormone receptor alpha (THRA) makes the binding site for the NRBOX motif of Mediator of RNA polymerase II transcription subunit 1 (MED1) accessible. | details |
NCOA6_MOUSE | 1494 | 1500 | Binary | Allostery | Binding of the 15-deoxy-Delta(12,14)-prostaglandin J2 ligand to the nuclear Peroxisome proliferator-activated receptor gamma (Pparg) makes the binding site for the NRBOX motif of Nuclear receptor coactivator 6 (Ncoa6) accessible. | details |
TRXR1_HUMAN | 46 | 52 | Binary | Pre‑translational | Alternative 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_HUMAN | 46 | 52 | Binary | Pre‑translational | Alternative 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 |