Gene Ontology annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Gene Ontology annotation based on curation of immunofluorescence data
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Calreticulin is expressed on the cell surface of activated human peripheral blood T lymphocytes in association with major histocompatibility complex class I molecules.
-
Calreticulin is an ER-resident chaperone that is also displayed on the surface of activated T cells in association with MHC class I.
"the 60-kDa calreticulin was labeled by cell surface biotinylation and precipitated from the surface of activated T cells"
Calreticulin functions in vitro as a molecular chaperone for both glycosylated and non-glycosylated proteins.
-
Calreticulin acts as a molecular chaperone in vitro for both glycosylated and non-glycosylated substrates.
"Calreticulin functions in vitro as a molecular chaperone for both glycosylated and non-glycosylated proteins."
HLA-F is a predominantly empty, intracellular, TAP-associated MHC class Ib protein with a restricted expression pattern.
Calreticulin Is a receptor for nuclear export.
Assembly and antigen-presenting function of MHC class I molecules in cells lacking the ER chaperone calreticulin.
-
Cells lacking calreticulin have impaired MHC class I assembly and antigen presentation.
"Assembly and antigen-presenting function of MHC class I molecules in cells lacking the ER chaperone calreticulin"
Cooperation of C1q receptors and integrins in C1q-mediated endothelial cell adhesion and spreading.
Calreticulin interacts with C/EBPalpha and C/EBPbeta mRNAs and represses translation of C/EBP proteins.
Competition of CUGBP1 and calreticulin for the regulation of p21 translation determines cell fate.
Major histocompatibility complex class I molecules expressed with monoglucosylated N-linked glycans bind calreticulin independently of their assembly status.
-
Calreticulin binds MHC class I molecules in a monoglucosylated N-glycan-dependent manner.
"Major histocompatibility complex class I molecules expressed with monoglucosylated N-linked glycans bind calreticulin"
Calreticulin, a Ca2+-binding chaperone of the endoplasmic reticulum.
-
Calreticulin is a Ca2+-binding ER chaperone involved in calcium homeostasis, ER calcium storage, and secretory-pathway quality control.
"The protein is involved in the regulation of intracellular Ca2+ homeostasis and endoplasmic reticulum (ER) Ca2+ storage capacity."
In cerebrospinal fluid ER chaperones ERp57 and calreticulin bind beta-amyloid.
Calreticulin signals upstream of calcineurin and MEF2C in a critical Ca(2+)-dependent signaling cascade.
Proteomics of human umbilical vein endothelial cells applied to etoposide-induced apoptosis.
Chemotaxis of human monocyte-derived dendritic cells to complement component C1q is mediated by the receptors gC1qR and cC1qR.
Human colostrum: identification of minor proteins in the aqueous phase by proteomics.
Redox regulation facilitates optimal peptide selection by MHC class I during antigen processing.
Purification and identification of G protein-coupled receptor protein complexes under native conditions.
Calreticulin and Hsp90 stabilize the human insulin receptor and promote its mobility in the endoplasmic reticulum.
-
Calreticulin controls early maturation and stability of the human insulin receptor in the ER.
"both CRT and Hsp90 control expression of hIR at its earliest maturation stages and modulate its movement within the ER"
Identification of calreticulin as a ligand of GABARAP by phage display screening of a peptide library.
The chaperone and potential mannan-binding lectin (MBL) co-receptor calreticulin interacts with MBL through the binding site for MBL-associated serine proteases.
Structural framework of the GABARAP-calreticulin interface--implications for substrate binding to endoplasmic reticulum chaperones.
Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT).
Defining the membrane proteome of NK cells.
Network organization of the human autophagy system.
Distinct functions for the glycans of tapasin and heavy chains in the assembly of MHC class I molecules.
Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for β-Pix in negative regulation of focal adhesion maturation.
Calreticulin-2 is localized in the lumen of the endoplasmic reticulum but is not a Ca2+ -binding protein.
Proteomic characterization of the human sperm nucleus.
Characterization of unique signature sequences in the divergent maternal protein Bcl2l10.
A directed protein interaction network for investigating intracellular signal transduction.
The unfolded protein response: integrating stress signals through the stress sensor IRE1α.
Calreticulin has opposing effects on the migration of human trophoblast and myometrial endothelial cells.
Sensitive detection of idiotypic platelet-reactive alloantibodies by an electrical protein chip.
Insights into RNA biology from an atlas of mammalian mRNA-binding proteins.
ORMDL3 is an inducible lung epithelial gene regulating metalloproteases, chemokines, OAS, and ATF6.
Tmem64 modulates calcium signaling during RANKL-mediated osteoclast differentiation.
Somatic mutations of calreticulin in myeloproliferative neoplasms.
-
Somatic +1 frameshift insertions/deletions in CALR exon 9 are recurrent driver mutations in essential thrombocythemia and primary myelofibrosis, are mutually exclusive with JAK2 and MPL mutations, and generate a novel mutant C-terminal peptide; these are neomorphic disease mutations rather than a function of wild-type calreticulin.
Somatic CALR mutations in myeloproliferative neoplasms with nonmutated JAK2.
-
CALR exon 9 +1 base-pair frameshift mutations are found in the majority of JAK2/MPL-nonmutated myeloproliferative neoplasms, arise in hematopoietic stem/progenitor cells as an initiating lesion, and produce a mutant calreticulin with a novel C-terminus that removes the normal Ca2+-binding tail and KDEL motif.
Using an in situ proximity ligation assay to systematically profile endogenous protein-protein interactions in a pathway network.
The functional landscape of Hsp27 reveals new cellular processes such as DNA repair and alternative splicing and proposes novel anticancer targets.
Protein interactome mining defines melatonin MT1 receptors as integral component of presynaptic protein complexes of neurons.
Calreticulin-mutant proteins induce megakaryocytic signaling to transform hematopoietic cells and undergo accelerated degradation and Golgi-mediated secretion.
-
Mutant calreticulin drives megakaryocytic transformation through the thrombopoietin receptor MPL, producing constitutive STAT3/STAT5, ERK1/2 and AKT activation and cytokine-independent growth; the mutant protein undergoes accelerated degradation and Golgi-mediated secretion, distinguishing the oncogenic neomorphic activity from the wild-type ER chaperone function.
Systematic protein-protein interaction mapping for clinically relevant human GPCRs.
Comprehensive evaluation of coding region point mutations in microsatellite-unstable colorectal cancer.
Deletion of Tmtc4 activates the unfolded protein response and causes postnatal hearing loss.
A reference map of the human binary protein interactome.
Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains.
Type I but Not Type II Calreticulin Mutations Activate the IRE1α/XBP1 Pathway of the Unfolded Protein Response to Drive Myeloproliferative Neoplasms.
-
Type 1 calreticulin mutants lose more acidic Ca2+-binding residues than type 2 mutants, directly impairing Ca2+ binding and depleting ER Ca2+, which selectively activates the IRE1α/XBP1 arm of the unfolded protein response; this mechanistically links calreticulin's high-capacity ER Ca2+-buffering function to mutation-type-specific oncogenic signaling.
Molecular basis of MHC I quality control in the peptide loading complex.
-
Calreticulin is a central chaperone of the MHC class I peptide loading complex, engulfing the monoglucosylated MHC I glycan and coupling epitope selection to glycan processing.
"peptide-receptive MHC I molecules are stabilized by multivalent chaperone interactions including the calreticulin-engulfed mono-glucosylated MHC I glycan"
Calreticulin mutations affect its chaperone function and perturb the glycoproteome.
-
Disease-associated calreticulin mutations impair its chaperone function and broadly perturb the cellular glycoproteome.
"Calreticulin mutations affect its chaperone function and perturb the glycoproteome."
Human placental calreticulin: purification, characterization and association with other proteins.
Modulation of gene expression by calreticulin binding to the glucocorticoid receptor.
Inhibition of nuclear hormone receptor activity by calreticulin.
The calcium-binding protein calreticulin is a major constituent of lytic granules in cytolytic T lymphocytes.
Calreticulin binds hYRNA and the 52-kDa polypeptide component of the Ro/SS-A ribonucleoprotein autoantigen.
Calreticulin associates with non-HLA-A,-B class I proteins in the human choriocarcinoma cell lines JEG-3 and BeWo.
Evidence that C1q binds specifically to CH2-like immunoglobulin gamma motifs present in the autoantigen calreticulin and interferes with complement activation.
-
C1q binds specifically to calreticulin, supporting calreticulin's role as a C1q-binding protein relevant to complement.
"C1q binds specifically to CH2-like immunoglobulin gamma motifs present in the autoantigen calreticulin"
In vitro interaction of a polypeptide homologous to human Ro/SS-A antigen (calreticulin) with a highly conserved amino acid sequence in the cytoplasmic domain of integrin alpha subunits.
-
Calreticulin binds the conserved KLGFFKR motif in the cytoplasmic tail of integrin alpha subunits in vitro.
"a highly conserved motif in the cytoplasmic domain adjacent to the transmembrane domain of the alpha subunit of integrins"
Expression of Calreticulin
SCARF1:ligand is endocytosed
MSR1:ligand (SCARA1:ligand, SR-A:ligand) is endocytosed
Binding of calnexin/calreticulin to the unfolded protein
Removal of the third glucose by glucosidase II and release from the chaperone
SEC22B, CALR, STX4, TAP and TAPBP bind
Transport of SEC22B, TAP and PLC from ER to ERGIC
Loading of antigenic peptides on to class I MHC
CALR, TAP, TAPBP dissociate from SEC22B:STX4
Formation of peptide loading complex (PLC)
Dissociation of the Antigenic peptide:MHC:B2M peptide loading complex
CALR UniProtKB record (P27797)
Manual CALR curation notes