SERPINB9
Sign in to saveAlso known as CAP-3, CAP3, PI-9, PI9, serpin family B member 9
Serpin B9 is a protein that in humans is encoded by the SERPINB9 gene. Serpin B9 is an inhibitor of Granzyme B (GzmB). GzmB is a potent cytotoxic molecule that is secreted by cytotoxic T lymphocytes and natural killer (NK) cells to induce apoptosis in target cells during an immune response. Serpin B9, expressed in the cytosol and nucleus, thus protects from apoptosis by cytotoxic T lymphocytes and NK cells.
Gene data
SERPINB9- Name
- serpin family B member 9
- Type
- protein-coding
- Aliases
- CAP-3, CAP3, PI-9, PI9
This gene encodes a member of the serine protease inhibitor family which are also known as serpins. The encoded protein belongs to a subfamily of intracellular serpins. This protein inhibits the activity of the effector molecule granzyme B. Overexpression of this protein may prevent cytotoxic T-lymphocytes from eliminating certain tumor cells. A pseudogene of this gene is found on chromosome 6. [provided by RefSeq, Mar 2012].
via MyGene.info
Gene · Ensembl
serpin family B member 9
- Symbol
- SERPINB9
- Biotype
- Protein coding
- Organism
- Homo sapiens
- Location
- 6:2,887,169-2,903,318
- Strand
- Reverse (−)
- Assembly
- GRCh38
via Ensembl · EMBL-EBI
Wikidata facts
Show 5 more facts
- HomoloGene ID
- 37888
- exact match
- identifiers.org/ncbigene/5272
- genomic start
- 2887270
- genomic end
- 2903309
- cytogenetic location
- 6p25.2
Sources (4)
via Wikidata · CC0
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Article
4 sectionsContents
- See also
- References
- Further reading
- External links
Serpin B9 is a protein that in humans is encoded by the SERPINB9 gene. Serpin B9 is an inhibitor of Granzyme B (GzmB). GzmB is a potent cytotoxic molecule that is secreted by cytotoxic T lymphocytes and natural killer (NK) cells to induce apoptosis in target cells during an immune response. Serpin B9, expressed in the cytosol and nucleus, thus protects from apoptosis by cytotoxic T lymphocytes and NK cells.
Serpin B9 belongs to the large superfamily of serine proteinase inhibitors (serpins), which bind to and inactivate serine proteinases. These interactions are involved in many cellular processes, including coagulation, fibrinolysis, complement fixation, matrix remodeling, and apoptosis (Sprecher et al., 1995).[supplied by OMIM]