Loading
CALR (Calreticulin) is a gene. The public catalogues list it as a drug target, a biomarker and a fusion partner, and an approved or late-stage drug is recorded against it. Tied to Myeloproliferative neoplasms, Essential thrombocythaemia and Primary myelofibrosis.
Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesised in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export.
CIViC holds 8 clinical evidence items and 0 assertions across 2 variants, naming Peginterferon Alfa-2a. Open Targets scores its association with cancer at 0.79 (direct and indirect evidence; datatypes literature 0.99, genetic association 0.82, somatic mutation 0.87, genetic literature 0.30). In OnCo, 1 product record names it (Ruxolitinib).
In plain words · CALR (Calreticulin) is a gene. The public catalogues list it as a drug target, a biomarker and a fusion partner, and an approved or late-stage drug is recorded against it. Tied to Myeloproliferative neoplasms, Essential thrombocythaemia and Primary myelofibrosis.
CALR (Calreticulin) is a gene. The public catalogues list it as a drug target, a biomarker and a fusion partner, and an approved or late-stage drug is recorded against it. Tied to Myeloproliferative neoplasms, Essential thrombocythaemia and Primary myelofibrosis.
Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle.
No product in this corpus aims at CALR yet. Drugs bind the molecule precisely: to switch it off, flag the cell for the immune system, or deliver a payload.
Broadly expressed or essential: HPA finds the RNA at low tissue specificity; the 1 medicine aimed at it (Ruxolitinib) act on the wild-type protein, so normal tissue is exposed and the therapeutic window comes from the tumour's faster division or its dependence on the protein. HPA CALR: RNA low tissue specificity; high antibody staining in 29 normal tissues; highest cancer staining endometrial cancer (12 of 12 high). Distribution: 1 cancer family in the corpus carries a prevalence row, label threshold or catalogue link for it (Myeloid neoplasms); Open Targets associates it with 2 specific cancer types at or above 0.5 (myeloproliferative disorder, primary myelofibrosis); the corpus evidence decides and the Open Targets list is quoted for comparison. (Rule 7 of scripts/fetch-target-specificity.ts.)
Sources: Human Protein Atlas CALR tissue; Open Targets ENSG00000179218 associations
First described 1988. Earliest sequence paper UniProt cites for the protein: Lieu T.-S. et al, J. Clin. Invest, 1988, "Molecular characterization of human Ro/SS-A antigen. Amino terminal sequence of the protein moiety of human Ro/SS-A antigen and immunological activity of a corresponding synthetic peptide". Source.
Sources: HGNC HGNC:1455 (approved symbol, name, aliases, locus and cross-references (hgnc_complete_set.txt)); UniProt P27797 (protein name, function text, keywords and locations (REST API)); CIViC gene CALR (8 evidence items, 0 assertions, 2 variants; diseases: Myelofibrosis, Essential Thrombocythemia (GraphQL API, CC0)); Open Targets ENSG00000179218 (association with cancer (MONDO_0004992) 0.79; per-cancer scores at or above 0.5: myeloproliferative neoplasm 0.73, primary myelofibrosis 0.56 (GraphQL API, CC0))
Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesised in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export. Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis. Present in the cortical granules of non-activated oocytes, is exocytosed during the cortical reaction in response to oocyte activation and might participate in the block to polyspermy. Location: Endoplasmic reticulum lumen; Cytoplasm, cytosol; Secreted, extracellular space, extracellular matrix; Cell surface (UniProt). Locus 19p13.13 (HGNC).
RNA: low tissue specificity, detected in all normal tissues.
Medium: Adipose tissue, Adrenal gland, Bone marrow, Cervix, Esophagus, Lung, Parathyroid gland, Seminal vesicle.
Medium only: carcinoid.
Human Protein Atlas version 25.1, antibody staining at reliability approved, enhanced or supported; used under CC BY-SA 3.0. Staining counts are patients per level in the atlas cohort, not population prevalence.
Query for this target: (TITLE:"CALR" OR ABSTRACT:"CALR" OR TITLE:"calreticulin" OR ABSTRACT:"calreticulin" OR TITLE:"Calreticulin" OR ABSTRACT:"Calreticulin" OR TITLE:"cC1qR" OR ABSTRACT:"cC1qR" OR TITLE:"FLJ26680" OR ABSTRACT:"FLJ26680" OR TITLE:"CALR1" OR ABSTRACT:"CALR1") AND (cancer OR tumor OR tumour OR oncology OR carcinoma OR lymphoma OR leukemia OR leukaemia OR myeloma OR sarcoma OR melanoma OR glioma). Results are unfiltered search hits about CALR, not a curated reading list.
Shares Essential thrombocythaemia (ET), Ruxolitinib, Primary myelofibrosis, Myeloproliferative neoplasms (PV, ET, myelofibrosis).
Shares Essential thrombocythaemia (ET), Myeloproliferative neoplasms (PV, ET, myelofibrosis), Open Targets Platform.
Shares Essential thrombocythaemia (ET), Myeloproliferative neoplasms (PV, ET, myelofibrosis), Open Targets Platform.
Shares Essential thrombocythaemia (ET), Ruxolitinib, Primary myelofibrosis, Myeloproliferative neoplasms (PV, ET, myelofibrosis).
Shares Ruxolitinib, Primary myelofibrosis, Myeloproliferative neoplasms (PV, ET, myelofibrosis).
Shares Ruxolitinib, Primary myelofibrosis, Myeloproliferative neoplasms (PV, ET, myelofibrosis).
Shares Ruxolitinib, Primary myelofibrosis, Myeloproliferative neoplasms (PV, ET, myelofibrosis).
Shares Ruxolitinib, Primary myelofibrosis, Myeloproliferative neoplasms (PV, ET, myelofibrosis).