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Switch #:
SWTI000522
Switch type:
Binary
Switch subtype:
Pre-translational

Description:
Alternative splicing removes the di-lysine ER-retention motif of UDP-galactose translocator (SLC35A2), abrogating binding to Coatomer subunit alpha (COPA). This motif localises Isoform UGT1 of UDP-galactose translocator (SLC35A2) exclusively in the Golgi whereas Isoform UGT2 of UDP-galactose translocator (SLC35A2) shows dual expression in both the Golgi and the ER. This motif is considered a weak retention signal.

Participants:
(1) UDP-galactose translocator (SLC35A2)
(2) Coatomer subunit alpha (COPA)

Interactions
Interaction #1 SLC35A2 - COPA

Interfaces
(1) TRG_ER_diLys_1 motif (392KVKGS396) in UDP-galactose translocator (SLC35A2)
(2) WD domain, G-beta repeat (1-277) in Coatomer subunit alpha (COPA)

Interaction Regulation
Alternative splicing Abrogation of the UDP-galactose translocator (SLC35A2) TRG_ER_diLys_1 motif - Coatomer subunit alpha (COPA) WD domain, G-beta repeat interaction

Context
Switch localisation
ELM curated: rough endoplasmic reticulum, endoplasmic reticulum, COPI coated vesicle membrane, endoplasmic reticulum cisterna, cytosol, endoplasmic reticulum membrane, endoplasmic reticulum membrane, integral protein, ER-Golgi transport vesicle membrane, Golgi-ER transport vesicle membrane
References

(1) Endoplasmic reticulum retention of the large splice variant of the UDP-galactose transporter is caused by a dilysine motif.
Kabuss et al. Glycobiology (2005)

See also

Other switches involving interfaces
WD domain, G-beta repeat - 36 more (view)


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