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Switch #:
SWTI000316
Switch type:
Specificity
Switch subtype:
Motif hiding

Description:
Inhibition of nuclear import of DNA polymerase processivity factor (UL44) by phosphorylation-dependent (T427) binding of BRCA1-associated protein (BRAP).

Participants:
(1) DNA polymerase processivity factor (UL44)
(2) BRCA1-associated protein (BRAP)
(3) Importin subunit alpha-1 (KPNA1)

Interactions
Interaction #1 UL44 - BRAP

Is mutually exclusive with Interaction #2 UL44 - KPNA1

Interfaces
(1) TRG_NLS_MonoExtN_4 motif (425PNTKKQKC432) in DNA polymerase processivity factor (UL44)
(2) BRCA1-associated protein (BRAP)

Interaction Regulation
PTM-dependent Induction (Phosphorylation of T427 on DNA polymerase processivity factor (UL44)) of the DNA polymerase processivity factor (UL44) TRG_NLS_MonoExtN_4 motif - BRCA1-associated protein (BRAP) interaction

Interaction #2 UL44 - KPNA1

Is mutually exclusive with Interaction #1 UL44 - BRAP

Interfaces
(3) TRG_NLS_MonoExtN_4 motif (425PNTKKQKC432) in DNA polymerase processivity factor (UL44)
(4) Armadillo/beta-catenin-like repeat (115-451) in Importin subunit alpha-1 (KPNA1)

Interaction Regulation
Effector binding Abrogation (BRCA1-associated protein (BRAP)) of the DNA polymerase processivity factor (UL44) TRG_NLS_MonoExtN_4 motif - Importin subunit alpha-1 (KPNA1) Armadillo/beta-catenin-like repeat interaction

Context
References

(1) The BRCA-1 binding protein BRAP2 is a novel, negative regulator of nuclear import of viral proteins, dependent on phosphorylation flanking the nuclear localization signal.
Fulcher et al. FASEB J. (2010)

(2) Identification of a novel cytoplasmic protein that specifically binds to nuclear localization signal motifs.
Li et al. J. Biol. Chem. (1998)

See also

Other switches involving participants
BRCA1-associated protein (BRAP) - 1 more (view)
Importin subunit alpha-1 (KPNA1) - 9 more (view)

Other switches involving interfaces
TRG_NLS_MonoExtN_4 - 10 more (view)
Armadillo/beta-catenin-like repeat - 16 more (view)
coiled_coil;PFAM:Pfam-B_17154 - 1 more (view)




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