GZMK
Sign in to saveAlso known as TRYP2, granzyme K
Granzyme K (GrK) is a protein that is encoded by the GZMK gene on chromosome 5 in humans. Granzymes are a family of serine proteases which have various intracellular and extracellular roles. GrK is found in granules of natural killer (NK) cells and cytotoxic T lymphocytes (CTLs), and is traditionally described as being cytotoxic towards targeted foreign, infected, or cancerous cells. NK cells and CTLs can induce apoptosis through the granule secretory pathway, which involves the secretion of granzymes along with perforin at immunological synapses.
Gene data
GZMK- Name
- granzyme K
- Type
- protein-coding
- Aliases
- GrK, TRYP2
This gene product is a member of a group of related serine proteases from the cytoplasmic granules of cytotoxic lymphocytes. Cytolytic T lymphocytes (CTL) and natural killer (NK) cells share the remarkable ability to recognize, bind, and lyse specific target cells. They are thought to protect their host by lysing cells bearing on their surface 'nonself' antigens, usually peptides or proteins resulting from infection by intracellular pathogens. The protein described here lacks consensus sequences for N-glycosylation present in other granzymes. [provided by RefSeq, Jul 2008].
via MyGene.info
Gene · Ensembl
granzyme K
- Symbol
- GZMK
- Biotype
- Protein coding
- Organism
- Homo sapiens
- Location
- 5:55,024,249-55,034,570
- Strand
- Forward (+)
- Assembly
- GRCh38
via Ensembl · EMBL-EBI
Wikidata facts
- Image
- Protein GZMK PDB 1mza.png
Show 5 more facts
- HomoloGene ID
- 20485
- exact match
- identifiers.org/ncbigene/3003
- genomic end
- 54330398
- genomic start
- 55024256
- cytogenetic location
- 5q11.2
Sources (3)
via Wikidata · CC0
~2 min read
Article
2 sectionsContents
- References
- Further reading
Granzyme K (GrK) is a protein that is encoded by the GZMK gene on chromosome 5 in humans. Granzymes are a family of serine proteases which have various intracellular and extracellular roles. GrK is found in granules of natural killer (NK) cells and cytotoxic T lymphocytes (CTLs), and is traditionally described as being cytotoxic towards targeted foreign, infected, or cancerous cells. NK cells and CTLs can induce apoptosis through the granule secretory pathway, which involves the secretion of granzymes along with perforin at immunological synapses.
Intracellularly, GrK may cleave a variety of substrates, such as the nucleosome assembly protein (NAP), HMG2, and Ape1 in the ER-associated SET complex, along with other targets that have downstream cytotoxic effects. Compared to in vitro studies of GrK cytotoxicity in rats and humans, in vitro mouse studies show no cytotoxic potential in the absence of perforin, making the role of GrK controversial. In vitro studies show potential extracellular targets for GrK such as the cleavage and activation of protease activated receptors (PAR)-1 and PAR-2. Grk binds lipopolysaccharides (LPS) in vitro separately from GrK's catalytic activity. Both PAR and LPS activation by GrK induce cytokine production in human in vitro studies.