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Protein Page:
Calreticulin (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
Calreticulin 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. 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. Monomer. Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5. Interacts with PDIA3/ERp57. Interacts with NR3C1 and TRIM21. Interacts with GABARAP. Belongs to the calreticulin family. Note: This description may include information from UniProtKB.
Protein type: Motility/polarity/chemotaxis; Calcium-binding protein; Secreted; Nuclear receptor co-regulator; Secreted, signal peptide
Cellular Component: Golgi apparatus; extracellular space; sarcoplasmic reticulum lumen; cell surface; endoplasmic reticulum; endoplasmic reticulum lumen; extracellular region; acrosome; cytosol; polysome; proteinaceous extracellular matrix; perinuclear region of cytoplasm; cytoplasm; intracellular; nucleus; external side of plasma membrane
Molecular Function: hormone binding; zinc ion binding; complement component C1q binding; unfolded protein binding; calcium ion binding; peptide binding; mRNA binding; integrin binding; protein binding; DNA binding; androgen receptor binding; chaperone binding; ubiquitin protein ligase binding; iron ion binding; glycoprotein binding; carbohydrate binding
Biological Process: protein maturation via protein folding; protein folding; regulation of meiosis; negative regulation of transcription from RNA polymerase II promoter; response to estradiol stimulus; cardiac muscle cell differentiation; regulation of apoptosis; antigen processing and presentation of peptide antigen via MHC class I; regulation of transcription, DNA-dependent; positive regulation of phagocytosis; positive regulation of cell proliferation; antigen processing and presentation of exogenous peptide antigen via MHC class I; protein export from nucleus; cortical actin cytoskeleton organization and biogenesis; cell cycle arrest; response to drug; negative regulation of steroid hormone receptor signaling pathway; protein stabilization; unfolded protein response; positive regulation of cell cycle; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; response to testosterone stimulus; post-translational protein modification; peptide antigen assembly with MHC class I protein complex; cellular calcium ion homeostasis; negative regulation of retinoic acid receptor signaling pathway; negative regulation of neuron differentiation; cellular protein metabolic process; unfolded protein response, activation of signaling protein activity; glucocorticoid receptor signaling pathway; sequestering of calcium ion; negative regulation of translation; spermatogenesis; protein amino acid N-linked glycosylation via asparagine; negative regulation of transcription, DNA-dependent; positive regulation of DNA replication
Reference #:  P27797 (UniProtKB)
Alt. Names/Synonyms: autoantigen Ro; CALR; Calregulin; Calreticulin; calreticulin); cC1qR; CRP55; CRT; CRTC; Endoplasmic reticulum resident protein 60; ERp60; FLJ26680; grp60; HACBP; RO; Sicca syndrome antigen A (autoantigen Ro; SSA
Gene Symbols: CALR
Molecular weight: 48,142 Da
Basal Isoelectric point: 4.29  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

Calreticulin

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 8 K24-u AEPAVYFkEQFLDGD
1 1 K48-a KHKSDFGkFVLSSGk
0 3 K48-u KHKSDFGkFVLSSGk
0 3 K55-u kFVLSSGkFyGDEEk
0 2 Y57-p VLSSGkFyGDEEkDk
1 0 K62-a kFyGDEEkDkGLQTS
0 4 K62-u kFyGDEEkDkGLQTS
1 0 K64-a yGDEEkDkGLQTSQD
0 2 Y75-p TSQDARFyALSASFE
0 3 S80 RFyALSASFEPFSNK
0 1 S80 RFyALSASFEPFSNK
0 7 Y109-p NIDCGGGyVKLFPNS
0 5 K142-a DICGPGTkkVHVIFN
0 2 K143-u ICGPGTkkVHVIFNy
0 3 Y150-p kVHVIFNykGkNVLI
0 2 K151-u VHVIFNykGkNVLIN
1 0 K153-a VIFNykGkNVLINkD
0 5 K153-u VIFNykGkNVLINkD
1 3 K159-a GkNVLINkDIRCKDD
0 12 K159-u GkNVLINkDIRCKDD
1 1 K206-a DWDFLPPkkIkDPDA
0 2 K206-u DWDFLPPkkIkDPDA
1 0 K207-a WDFLPPkkIkDPDAs
1 2 K209-a FLPPkkIkDPDAsKP
0 1 S214-p kIkDPDAsKPEDWDE
1 0 K238-a SKPEDWDkPEHIPDP
0 1 Y338 LITNDEAYAEEFGNE
0 4 K374 LKEEEEDKKRKEEEE
0 13 K375 KEEEEDKKRKEEEEA
  mouse

 
K24 ADPAIYFKEQFLDGD
K48 KHKSDFGKFVLSSGk
K48 KHKSDFGKFVLSSGk
K55-u KFVLSSGkFYGDLEk
Y57 VLSSGkFYGDLEkDK
K62 kFYGDLEKDKGLQTS
K62-u kFYGDLEkDKGLQTS
K64 YGDLEkDKGLQTSQD
Y75 TSQDARFYALSAkFE
K80-a RFYALSAkFEPFSNK
K80-u RFYALSAkFEPFSNK
Y109 NIDCGGGYVKLFPSG
K142-a DICGPGTkKVHVIFN
K143 ICGPGTkKVHVIFNy
Y150-p KVHVIFNyKGKNVLI
K151 VHVIFNyKGKNVLIN
K153 VIFNyKGKNVLINKD
K153 VIFNyKGKNVLINKD
K159 GKNVLINKDIRCKDD
K159 GKNVLINKDIRCKDD
K206 DWDFLPPKKIkDPDA
K206 DWDFLPPKKIkDPDA
K207 WDFLPPKKIkDPDAA
K209-a FLPPKKIkDPDAAKP
A214 KIkDPDAAKPEDWDE
K238 SKPEDWDKPEHIPDP
Y338-p LITNDEAyAEEFGNE
K374-a LKEEEEDkkRKEEEE
K375-a KEEEEDkkRKEEEEA
  rat

 
K24 ADPAIYFKEQFLDGD
K48 KHKSDFGKFVLSSGK
K48 KHKSDFGKFVLSSGK
K55 KFVLSSGKFYGDQEK
Y57 VLSSGKFYGDQEKDK
K62 KFYGDQEKDKGLQTS
K62 KFYGDQEKDKGLQTS
K64 YGDQEKDKGLQTSQD
Y75 TSQDARFYALSARFE
R80 RFYALSARFEPFSNK
R80 RFYALSARFEPFSNK
Y109 NIDCGGGYVKLFPGG
K142 DICGPGTKKVHVIFN
K143 ICGPGTKKVHVIFNY
Y150 KVHVIFNYKGKNVLI
K151 VHVIFNYKGKNVLIN
K153 VIFNYKGKNVLINKD
K153 VIFNYKGKNVLINKD
K159 GKNVLINKDIRCKDD
K159 GKNVLINKDIRCKDD
K206 DWDFLPPKKIKDPDA
K206 DWDFLPPKKIKDPDA
K207 WDFLPPKKIKDPDAA
K209 FLPPKKIKDPDAAKP
A214 KIKDPDAAKPEDWDE
K238 SKPEDWDKPEHIPDP
Y338 LITNDEAYAEEFGNE
K374 LKEEEEDKKRKEEEE
K375 KEEEEDKKRKEEEEA
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