| BRAG | BRAG (B cell associated protein), GALNAC4S-6ST |
| Molecule Type | Antigen Expression | Molecular Weight Min / Max |
| Non-lineage Restricted Molecule Type 2 glycoprotein | B Cell Spleen Lymph Node Tonsil Leukocyte Bone Marrow Peripheral blood |
Expression | ||||||||||||||
| BRAG is expressed by Northern blot analysis in all B cell lines and enriched tissues, little of no expression was detected in several nonlymphoid cell lines and no expression in T cells. Expression was in bone marrow but not in heart, thymus or placenta. RNA dot blot analysis detected high levels of expresssion in fetal or adult spleen, lymph node and peripheral blood leukocytes, moderate expression in heart, ovary, stomach and brain putamen and low levels of expression in bone marrow and several other tissues. Zoo blot analysis showed that BRAG is conserved across eukaryotes. | ||||||||||||||
Structure | ||||||||||||||
| MOLECULAR FAMILY NAME: Belongs to the sulfotransferase family. BRAG is a single-pass type-2 glycoprotein. It contains a 405 aa extracellular domain which contains a C terminus containing 4 putative N-linked glycosylation sites , a transmembrane and an 81 aa cytoplasmic domain which contains a C terminus containing a putative palmitoylation site and several phosphorylation sites. BRAG is determined to be a membrane-integrated glycoprotein that is expressed as adisulfide-linker dimer in B cells. In pro-B and mature B-cell lines, it colocalizes with RAG1. RAG1 (recombination activating gene 1) is involved in recognition of DNA substrate. MOLECULAR MASS POST-TRANSCRIPTIONAL MODIFICATION Alternative splicing yields 2 different isoforms. POST-TRANSLATIONAL MODIFICATION BRAG has 4 putative N-linked glycoslation sites. | ||||||||||||||
Ligands | ||||||||||||||
| LIGANDS AND MOLECULES ASSOCIATED WITH BRAG: No information. | ||||||||||||||
Function | ||||||||||||||
Sulfotransferase transfers sulfate to yield a highly sulfated structure similar to the structure found in thrombomodulin chondroitin sulfate. BRAG may act as a B cell receptor involved in BCR ligation-mediated early activation that mediate regulatory signals key to B cell development and/or regulation of B cell specific RAG1 expression. BRAG associates with phosphorylated proteins in unstimulated mature B cells but not in B cell activated through B cell receptor cross-linking. Evidence presented shows that BRAG functions as a cell surface receptor cabable of cell signaling. | ||||||||||||||
Comments | ||||||||||||||
| MOLECULAR INTERACTION- PROTEINS AND DNA ELEMENTS WHICH REGULATE TRANSCRIPTION OF BRAG: No information. SUBSTRATES: No information. ENZYMES WHICH MODIFY BRAG: No information. | ||||||||||||||
Database accession numbers | ||||||||||||||
Revised June 25, 2008
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