Cell Senescence Entries for CALR

Cell Types
Endometrial glandular epithelial
Cell Lines
EM-E6/E7/TERT-1
Cancer Cell?
No
Method
Knockdown
Type of senescence
Unclear
Senescence Effect
Inhibits
Primary Reference
Kusama et al. (2015) EPAC2-mediated calreticulin regulates LIF and COX2 expression in human endometrial glandular cells. J Mol Endocrinol 54(1)17-24 (PubMed)

CALR Gene Information

HGNC symbol
CALR 
Aliases
cC1qR; CRT; FLJ26680; RO; SSA 
Common name
calreticulin 
Entrez Id
811
Description
Calreticulin is a highly conserved chaperone protein which resides primarily in the endoplasmic reticulum, and is involved in a variety of cellular processes, among them, cell adhesion. Additionally, it functions in protein folding quality control and calcium homeostasis. Calreticulin is also found in the nucleus, suggesting that it may have a role in transcription regulation. Systemic lupus erythematosus is associated with increased autoantibody titers against calreticulin. Recurrent mutations in calreticulin have been linked to various neoplasms, including the myeloproliferative type.[provided by RefSeq, May 2020].

CALR Ontologies

Gene Ontology
Process: GO:6457; protein folding
GO:6874; cellular calcium ion homeostasis
GO:42981; regulation of apoptotic process
GO:30433; ubiquitin-dependent ERAD pathway
GO:50821; protein stabilization
GO:17148; negative regulation of translation
GO:8284; positive regulation of cell population proliferation
GO:2000510; positive regulation of dendritic cell chemotaxis
GO:122; negative regulation of transcription by RNA polymerase II
GO:45892; negative regulation of transcription, DNA-templated
GO:34504; protein localization to nucleus
GO:51208; sequestering of calcium ion
GO:6355; regulation of transcription, DNA-templated
GO:6611; protein export from nucleus
GO:48387; negative regulation of retinoic acid receptor signaling pathway
GO:45787; positive regulation of cell cycle
GO:22417; protein maturation by protein folding
GO:1900026; positive regulation of substrate adhesion-dependent cell spreading
GO:90398; cellular senescence
GO:34975; protein folding in endoplasmic reticulum
GO:2502; peptide antigen assembly with MHC class I protein complex
GO:7283; spermatogenesis
GO:9410; response to xenobiotic stimulus
GO:10033; response to organic substance
GO:10595; positive regulation of endothelial cell migration
GO:10628; positive regulation of gene expression
GO:30866; cortical actin cytoskeleton organization
GO:32355; response to estradiol
GO:33144; negative regulation of intracellular steroid hormone receptor signaling pathway
GO:33574; response to testosterone
GO:40020; regulation of meiotic nuclear division
GO:42921; glucocorticoid receptor signaling pathway
GO:45665; negative regulation of neuron differentiation
GO:50766; positive regulation of phagocytosis
GO:55007; cardiac muscle cell differentiation
GO:71285; cellular response to lithium ion
GO:71310; cellular response to organic substance
GO:1901164; negative regulation of trophoblast cell migration
GO:1901224; positive regulation of NIK/NF-kappaB signaling
Cellular component: GO:5783; endoplasmic reticulum
GO:5788; endoplasmic reticulum lumen
GO:5737; cytoplasm
GO:5634; nucleus
GO:16020; membrane
GO:31410; cytoplasmic vesicle
GO:5576; extracellular region
GO:5925; focal adhesion
GO:5635; nuclear envelope
GO:5829; cytosol
GO:5615; extracellular space
GO:5764; lysosome
GO:9986; cell surface
GO:16529; sarcoplasmic reticulum
GO:33018; sarcoplasmic reticulum lumen
GO:5789; endoplasmic reticulum membrane
GO:70062; extracellular exosome
GO:30670; phagocytic vesicle membrane
GO:48471; perinuclear region of cytoplasm
GO:33116; endoplasmic reticulum-Golgi intermediate compartment membrane
GO:71556; integral component of lumenal side of endoplasmic reticulum membrane
GO:42824; MHC class I peptide loading complex
GO:71682; endocytic vesicle lumen
GO:60473; cortical granule
GO:44194; cytolytic granule
GO:1669; acrosomal vesicle
GO:5790; smooth endoplasmic reticulum
GO:5794; Golgi apparatus
GO:5844; polysome
GO:9897; external side of plasma membrane
GO:32991; protein-containing complex
GO:43231; intracellular membrane-bounded organelle
GO:44322; endoplasmic reticulum quality control compartment
GO:62023; collagen-containing extracellular matrix
Function: GO:5509; calcium ion binding
GO:51082; unfolded protein binding
GO:5515; protein binding
GO:3723; RNA binding
GO:46872; metal ion binding
GO:30246; carbohydrate binding
GO:3677; DNA binding
GO:31625; ubiquitin protein ligase binding
GO:51087; chaperone binding
GO:50681; androgen receptor binding
GO:8270; zinc ion binding
GO:1849; complement component C1q complex binding
GO:5178; integrin binding
GO:44183; protein folding chaperone
GO:3729; mRNA binding
GO:5506; iron ion binding
GO:42277; peptide binding
GO:42562; hormone binding
Hide GO terms

Homologs of CALR in Model Organisms

Caenorhabditis elegans
crt-1
Danio rerio
calrl2
Drosophila melanogaster
Crc
Mus musculus
Calr
Rattus norvegicus
Calr
Saccharomyces cerevisiae
CNE1

External links

OMIM
109091
Ensembl
ENSG00000179218
Entrez Gene
811
UniGene
515162
1000 Genomes
1000 Genomes
HPRD
GenAtlas
CALR
GeneCards
CALR