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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

B-cell receptor-associated protein 29

Bap29
Top mentioned proteins: BAP31, p22, MHC, PrP, caspase-8
Papers on Bap29
A disulfide polymerized protein crystal.
Quistgaard, Stockholm, Sweden. In Chem Commun (camb), 2015
The vDED coiled coil domain from human BAP29 was crystallized in dimeric and tetrameric forms.
Structural and biophysical characterization of the cytoplasmic domains of human BAP29 and BAP31.
Nordlund et al., Stockholm, Sweden. In Plos One, 2012
Two members of the B-cell associated 31 (BAP31) family are found in humans; BAP29 and BAP31.
Yet1p-Yet3p interacts with Scs2p-Opi1p to regulate ER localization of the Opi1p repressor.
Barlowe et al., United States. In Mol Biol Cell, 2011
We recently reported that Yet1p and Yet3p, the yeast homologues of BAP29 and BAP31, are required for normal growth in the absence of inositol.
Yet1p and Yet3p, the yeast homologs of BAP29 and BAP31, interact with the endoplasmic reticulum translocation apparatus and are required for inositol prototrophy.
Barlowe et al., United States. In J Biol Chem, 2010
The mammalian B-cell receptor-associated proteins of 29 and 31 kDa (BAP29 and BAP31) are conserved integral membrane proteins that have reported roles in endoplasmic reticulum (ER) quality control, ER export of secretory cargo, and programmed cell death.
Monoclonal antibodies against human BAP31 for immunocytochemistry.
Jin et al., Xi'an, China. In Hybridoma (larchmt), 2009
Human BAP31 is a 28 kDa polytopic integral protein of the ER and part of a large BAP hetero-oligomeric complex that includes the related BAP29 protein and connections to actomyosin.
Interaction of Bap31 and MHC class I molecules and their traffic out of the endoplasmic reticulum.
Edidin et al., Baltimore, United States. In J Immunol, 2009
The increased forward traffic is blocked by overexpression of Bap29, a partner protein for Bap31, which localizes to the ER.
Bap29varP, a variant of Bap29, influences the cell surface expression of the human P-glycoprotein.
GeneRIF
Rao et al., Amarillo, United States. In Int J Oncol, 2008
Bap29varP acts as an essential chaperone, influencing the processing and trafficking of Pgp to the cell surface.
Bap31 enhances the endoplasmic reticulum export and quality control of human class I MHC molecules.
Edidin et al., Baltimore, United States. In J Immunol, 2006
Overexpression of the Bap31 homolog, Bap29, decreases surface class levels in HeLa, indicating that it does not substitute for Bap31.
Bap29/31 influences the intracellular traffic of MHC class I molecules.
GeneRIF
Williams et al., Toronto, Canada. In J Immunol, 2004
results are consistent with the view that class I molecules are largely recruited to ER exit sites by Bap29/31, and that Bap29/31 is a cargo receptor for MHC class I molecules
A high-molecular-weight complex of membrane proteins BAP29/BAP31 is involved in the retention of membrane-bound IgD in the endoplasmic reticulum.
GeneRIF
Reth et al., Freiburg, Germany. In Proc Natl Acad Sci U S A, 2003
A high-molecular-weight complex of membrane proteins BAP29/BAP31 is involved in the retention of membrane-bound IgD in the endoplasmic reticulum.
The procaspase-8 isoform, procaspase-8L, recruited to the BAP31 complex at the endoplasmic reticulum.
Shore et al., Montréal, Canada. In Proc Natl Acad Sci U S A, 2002
Gene deletion identified BAP31 and related BAP29 as required for processing of procaspase-8L in response to E1A, by a FADD-independent mechanism that was blocked by BCL-2.
The specificity of association of the IgD molecule with the accessory proteins BAP31/BAP29 lies in the IgD transmembrane sequence.
Reth et al., Freiburg, Germany. In Embo J, 1996
Recently two proteins of 29 and 31 kDa (BAP29 and BAP31) have been described that are preferentially associated with membrane IgD but only weakly with membrane IgM.
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