SEC23/YPR181C Literature Guide Help

Other names published for SEC23: YPR181C

SEC23 - Protein Sequence Features (10)

ReferenceOther Genes Addressed
Helbig AO, et al.  (2010) Perturbation of the yeast N-acetyltransferase NatB induces elevation of protein phosphorylation levels. BMC Genomics 11(1):685
Ma L, et al.  (2010) Proteins deleterious on overexpression are associated with high intrinsic disorder, specific interaction domains, and low abundance. J Proteome Res 9(3):1218-25
Marino SM, et al.  (2010) Characterization of Surface-Exposed Reactive Cysteine Residues in Saccharomyces cerevisiae. Biochemistry 49(35):7709-21
Ossareh-Nazari B, et al.  (2010) The Rsp5 ubiquitin ligase and the AAA-ATPase Cdc48 control the ubiquitin-mediated degradation of the COPII component Sec23. Exp Cell Res 316(20):3351-7
Zhang KX and Ouellette BF  (2009) GAIA: a gram-based interaction analysis tool--an approach for identifying interacting domains in yeast. BMC Bioinformatics 10 Suppl 1:S60
Tartaglia GG and Caflisch A  (2007) Computational analysis of the S. cerevisiae proteome reveals the function and cellular localization of the least and most amyloidogenic proteins. Proteins 68(1):273-8
Jothi R, et al.  (2006) Co-evolutionary Analysis of Domains in Interacting Proteins Reveals Insights into Domain-Domain Interactions Mediating Protein-Protein Interactions. J Mol Biol 362(4):861-75
Giraudo CG and Maccioni HJ  (2003) Endoplasmic reticulum export of glycosyltransferases depends on interaction of a cytoplasmic dibasic motif with Sar1. Mol Biol Cell 14(9):3753-66
Miller EA, et al.  (2003) Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles. Cell 114(4):497-509
Bi X, et al.  (2002) Structure of the Sec23/24-Sar1 pre-budding complex of the COPII vesicle coat. Nature 419(6904):271-7