Stromal interaction molecule 1 (STIM1), a transmembrane protein with growth suppressor activity, contains an extracellular SAM domain modified by N-linked glycosylation

Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

Volumn 1596, Issue 1, 2002, Pages 131-137

  Williams, Richard T ^a   Senior, Paul V ^a   Van Stekelenburg, Leonie ^a   Layton, Judith E ^b   Smith, Peter J ^a   Dziadek, Marie A ^a,c  

^a UNIVERSITY OF MELBOURNE   (Australia)

^b LUDWIG INSTITUTE FOR CANCER RESEARCH   (Australia)

^c UNIVERSITY OF AUCKLAND   (New Zealand)

Author keywords

Glycosylation; Oligomerization; Sterile alpha motif domain; Stromal interaction molecule 1; Tunicamycin

Indexed keywords

AMINO ACID; MEMBRANE PROTEIN; OLIGOSACCHARIDE; STROMAL INTERACTION MOLECULE 1; UNCLASSIFIED DRUG;

ARTICLE; CELL SURFACE; CONTROLLED STUDY; CYTOSOL; ENDOPLASMIC RETICULUM; EXTRACELLULAR SPACE; GOLGI COMPLEX; HUMAN; HUMAN CELL; MEMBRANE TRANSPORT; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN GLYCOSYLATION; PROTEIN LOCALIZATION; PROTEIN MODIFICATION; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTEIN TRANSPORT;

CLONING, MOLECULAR; CYTOPLASM; EXTRACELLULAR SPACE; GENE EXPRESSION REGULATION; GLYCOSYLATION; GRANULOCYTE COLONY-STIMULATING FACTOR; HUMANS; IMMUNOBLOTTING; MEMBRANE PROTEINS; MUTAGENESIS, SITE-DIRECTED; NEOPLASM PROTEINS; TRANSFECTION;

EID: 0036537823     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(02)00211-X     Document Type: Article

References (27)