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Protein / target

Calreticulin

Encoded byCALRP27797Homo sapiensSwiss-Prot
UniProt: P27797Ensembl: ENSG00000179218HGNC: HGNC:1455NCBI Gene: 811
Small-molecule tractable
Druggability
Structure with Ligand
2
Research papers

Protein at a glance

Biological role

Complement component C1q complex binding

Strongest disease association

Neoplasms

Via encoding gene CALR · Genetic evidence · score 0.91

Research activity

Emerging research

2 papers · latest 2024

Derived from structured UniProt, Open Targets and literature data on this page.

Protein profile

UniProt 2026_02

Canonical identity and biological annotation from UniProt.

Function overview

Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle.

View complete UniProt function annotation

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 synthesized in the ER (PubMed:7876246). Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export (PubMed:11149926). Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis (By similarity). 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 (By similarity)

Subcellular location

Endoplasmic reticulum lumenCytoplasm, cytosolSecreted, extracellular space, extracellular matrixCell surfaceSarcoplasmic reticulum lumenCytoplasmic vesicle, secretory vesicle, Cortical granuleCytolytic granule
Domains and Gene Ontology detail (87)

Gene Ontology

  • Cacrosomal vesicle
  • Ccell surface
  • Ccortical granule
  • Ccytolytic granule
  • Ccytoplasm
  • Ccytosol
  • Cendocytic vesicle lumen
  • Cendoplasmic reticulum
  • Cendoplasmic reticulum lumen
  • Cendoplasmic reticulum membrane
  • Cendoplasmic reticulum quality control compartment
  • Cendoplasmic reticulum-Golgi intermediate compartment membrane

417 aa · 48 kDa

Biological roles

What this protein does, drawn together from its UniProt function, Gene Ontology terms and Reactome pathways.

Cell migrationGONuclear receptor signallingGOCell proliferation & survivalGOTranscriptional regulationUniProt · GOImmune signallingGO
View supporting evidence

Cell migration

  • ·negative regulation of trophoblast cell migration
  • ·positive regulation of dendritic cell chemotaxis
  • ·positive regulation of endothelial cell migration

Nuclear receptor signalling

  • ·negative regulation of intracellular steroid hormone receptor signaling pathway
  • ·nuclear receptor-mediated glucocorticoid signaling pathway

Cell proliferation & survival

  • ·positive regulation of cell population proliferation

Transcriptional regulation

  • ·Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control…
  • ·negative regulation of DNA-templated transcription
  • ·negative regulation of transcription by RNA polymerase II
  • ·positive regulation of gene expression

Immune signalling

  • ·negative regulation of trophoblast cell migration
  • ·peptide antigen assembly with MHC class I protein complex
  • ·positive regulation of substrate adhesion-dependent cell spreading

Concepts derived from UniProt GO Reactome — each badge above shows which sources supported that role.

Translational evidence

Open Targets 26

Why this target matters therapeutically, strongest evidence first. Disease associations are gene-level (via the gene that encodes this protein) and open into the full confidence synthesis; the development universe, tractability and safety annotations are target-level, from Open Targets.

Strongest disease associations · via encoding gene CALR

Gene-level evidence surfaced through the gene CALRthat encodes this protein — not a direct protein–disease relationship. Ranked by Forefront's causal-directness weighting, so genetically- and clinically-evidenced diseases lead over ones that merely share the literature.

Neoplasms
0.93Well supported

Genetic evidence dominant · Open Targets 0.58

Myeloproliferative disorder
0.89Well supported

Genetic evidence dominant · Open Targets 0.58

Primary myelofibrosis
0.82Well supported

Genetic evidence dominant · Open Targets 0.56

Hemorrhagic disease
0.71Moderately supported

Genetic evidence dominant · Open Targets 0.54

Neurodegenerative Diseases
0.35Preliminary

Pathway evidence dominant · Open Targets 0.52 · no direct causal or clinical evidence

View evidence synthesis (5)
NeoplasmsWell supported
0.93
agreement 0.79–1.00
Genetic86%Literature14%

Open Targets aggregate 0.58 · 2 independent evidence families

Myeloproliferative disorderWell supported
0.89
agreement 0.77–1.00
Genetic59%Somatic mutation30%Literature11%

Open Targets aggregate 0.58 · 3 independent evidence families

Primary myelofibrosisWell supported
0.82
agreement 0.71–0.94
Genetic65%Somatic mutation31%Literature4%Genetic literaturedup

Open Targets aggregate 0.56 · 3 independent evidence families · 1 not counted as duplicate

Hemorrhagic diseaseModerately supported
0.71
agreement 0.59–0.83
Genetic100%

Open Targets aggregate 0.54 · 1 independent evidence family

Neurodegenerative DiseasesPreliminary
0.35
agreement 0.17–0.53
Pathway97%Literature3%

Open Targets aggregate 0.52 · 2 independent evidence families · no direct causal or clinical evidence

The evidence agreement range shows how closely the independent evidence families agree — it is not a statistical confidence interval, and nothing here is fitted to outcome data. Derived from Open Targets evidence types under Forefront weighting; the per-type scores above show the calculation.

Show all associations
Neoplasms0.58
Myeloproliferative disorder0.58
Primary myelofibrosis0.56
Hemorrhagic disease0.54
Neurodegenerative Diseases0.52
Alzheimer's Disease0.43
Parkinson's Disease0.43
Multiple Sclerosis0.42

Tractability

Small molecules — Emerging

Feasibility evidence (structure with ligand) — no clinical-stage drug of this modality recorded.

Antibodies — Emerging

Feasibility evidence (uniprot loc high conf and go cc high conf) — no clinical-stage drug of this modality recorded.

Protein degraders — Emerging

Feasibility evidence (database ubiquitination and half-life data) — no clinical-stage drug of this modality recorded.

View underlying tractability evidence (6)
SM · Structure with LigandAB · UniProt loc high confAB · GO CC high confAB · UniProt SigP or TMHMMPR · Database UbiquitinationPR · Half-life Data

Raw Open Targets tractability assessment buckets, by modality.

Research activity

2 papers · to 2024

Papers linked directly to this protein. This is the protein's own literature — descriptor-derived papers are kept separate below.

Most cited

Tipping the immunostimulatory and inhibitory DAMP balance to harness immunogenic cell death.205 cites

Hayashi K · Nature communications · 2020

Integrity of neural extracellular matrix is required for microglia-mediated synaptic remodeling.15 cites

Cangalaya C · Glia · 2024

Recent

Integrity of neural extracellular matrix is required for microglia-mediated synaptic remodeling.

Cangalaya C · Glia · 2024

Tipping the immunostimulatory and inhibitory DAMP balance to harness immunogenic cell death.

Hayashi K · Nature communications · 2020

Europe PMC papers linked directly to this protein.