BAIT

MAPR3

ARABIDOPSIS THALIANA MEMBRANE-ASSOCIATED PROGESTERONE BINDING PROTEIN 3, ATMAPR3, ATMP2, MEMBRANE STEROID BINDING PROTEIN 2, MSBP2, membrane-associated progesterone binding protein 3, AT3G48890
membrane-associated progesterone binding protein 3
GO Process (0)
GO Function (0)
GO Component (4)

Gene Ontology Cellular Component

Arabidopsis thaliana (Columbia)
PREY

UBQ10

C17L7.240, C17L7_240, polyubiquitin 10, AT4G05320
polyubiquitin 10
GO Process (3)
GO Function (0)
GO Component (0)

Gene Ontology Biological Process

Arabidopsis thaliana (Columbia)

Reconstituted Complex

An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator.

Publication

E3-independent ubiquitination of AtMAPR/MSBP1.

Kao AL, Lin YH, Chen RP, Huang YY, Chen CC, Yang CC

AtMAPR5/MSBP1 and its homologs can be ubiquitinated in the absence of E3 ligase in in vitro ubiquitination assays. Ubiquitinated AtMAPR3, AtMAPR5/MSBP1, and AtMAPR2 were identified using LC-MS/MS. Analysis of trypsin-released signature peptides showed that this E3-independent ubiquitination of AtMAPR3, AtMAPR5/MSBP1, and AtMAPR2 was dominated by mono-ubiquitination at multiple sites. Unlike AtUBC8-type E2s, AtUBC36 was not able to transfer ubiquitin to ... [more]

Phytochemistry Jun. 01, 2012; 78(0);7-19 [Pubmed: 22513011]

Throughput

  • Low Throughput

Curated By

  • BioGRID