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Protein Page:
Calreticulin (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

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: Calcium-binding protein; Motility/polarity/chemotaxis; Secreted; Secreted, signal peptide; Nuclear receptor co-regulator
Chromosomal Location of Human Ortholog: 19p13.3-p13.2
Cellular Component: Golgi apparatus; extracellular space; cell surface; sarcoplasmic reticulum lumen; endoplasmic reticulum; endoplasmic reticulum lumen; extracellular region; acrosome; cytosol; polysome; proteinaceous extracellular matrix; membrane; 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; integrin binding; mRNA binding; protein binding; androgen receptor binding; DNA binding; chaperone binding; ubiquitin protein ligase binding; iron ion binding; carbohydrate binding; glycoprotein binding
Biological Process: protein maturation via protein folding; protein folding; regulation of meiosis; negative regulation of transcription from RNA polymerase II promoter; cardiac muscle cell differentiation; response to estradiol stimulus; 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; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; positive regulation of cell cycle; 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; unfolded protein response, activation of signaling protein activity; cellular protein metabolic process; negative regulation of translation; sequestering of calcium ion; glucocorticoid receptor signaling pathway; 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 1 Y22-p AVAEPAVyFkEQFLD
0 8 K24-ub AEPAVyFkEQFLDGD
0 1 K43 RWIESKHKSDFGkFV
0 1 K43-sc RWIESKHkSDFGkFV
1 1 K48-ac KHkSDFGkFVLsSGk
0 3 K48-ub KHkSDFGkFVLsSGk
0 1 K48-sc KHkSDFGkFVLsSGk
0 2 S52-p DFGkFVLsSGkFyGD
0 3 K55-ub kFVLsSGkFyGDEEk
0 1 K55-sc kFVLsSGkFyGDEEk
0 1 Y57-p VLsSGkFyGDEEkDk
1 1 K62-ac kFyGDEEkDkGLQTS
0 4 K62-ub kFyGDEEkDkGLQTS
0 1 K62-sc kFyGDEEkDkGLQTS
1 0 K64-ac yGDEEkDkGLQTSQD
0 2 Y75-p TSQDARFyALSASFE
0 4 S80 RFyALSASFEPFsNK
0 1 S80 RFyALSASFEPFsNK
0 1 S80 RFyALSASFEPFsNK
0 1 S85-p SASFEPFsNKGQTLV
0 6 Y109-p NIDCGGGyVKLFPNS
0 5 K142-ac DICGPGTkkVHVIFN
0 2 K143-ub ICGPGTkkVHVIFNy
0 3 Y150-p kVHVIFNykGkNVLI
0 1 K151 VHVIFNyKGkNVLIN
0 2 K151-ub VHVIFNykGkNVLIN
0 1 K151-sc VHVIFNykGkNVLIN
1 0 K153-ac VIFNykGkNVLINkD
0 5 K153-ub VIFNykGkNVLINkD
1 4 K159-ac GkNVLINkDIRCKDD
0 12 K159-ub GkNVLINkDIRCKDD
0 1 K159-sc GkNVLINkDIRCKDD
1 1 K206-ac DWDFLPPkkIkDPDA
0 2 K206-ub DWDFLPPkkIkDPDA
0 1 K206 DWDFLPPKkIkDPDA
1 0 K207-ac WDFLPPkkIkDPDAs
1 2 K209-ac FLPPkkIkDPDAsKP
0 2 S214-p kIkDPDAsKPEDWDE
0 1 T229-p RAKIDDPtDsKPEDW
0 1 S231-p KIDDPtDsKPEDWDk
1 1 K238-ac sKPEDWDkPEHIPDP
0 1 Y299-p PEIDNPEysPDPSIY
0 1 S300-p EIDNPEysPDPSIYA
0 1 Y338 LITNDEAYAEEFGNE
0 1 K360 AEKQMKDKQDEEQRL
0 1 K368 QDEEQRLKEEEEDKK
0 4 K374 LKEEEEDKKRKEEEE
0 13 K375 KEEEEDKKRKEEEEA
  mouse

 
Y22 AAADPAIYFKEQFLD
K24 ADPAIYFKEQFLDGD
K43-ac RWVESKHkSDFGkFV
K43 RWVESKHKSDFGkFV
K48 KHkSDFGKFVLSSGk
K48 KHkSDFGKFVLSSGk
K48-sc KHkSDFGkFVLSSGk
S52 DFGkFVLSSGkFYGD
K55-ub kFVLSSGkFYGDLEk
K55-sc kFVLSSGkFYGDLEk
Y57 VLSSGkFYGDLEkDK
K62-ac kFYGDLEkDKGLQTS
K62-ub kFYGDLEkDKGLQTS
K62-sc kFYGDLEkDKGLQTS
K64 YGDLEkDKGLQTSQD
Y75 TSQDARFYALSAkFE
K80-ac RFYALSAkFEPFSNK
K80-ub RFYALSAkFEPFSNK
K80-sc RFYALSAkFEPFSNK
S85 SAkFEPFSNKGQTLV
Y109 NIDCGGGYVKLFPSG
K142-ac DICGPGTkKVHVIFN
K143 ICGPGTkKVHVIFNy
Y150-p KVHVIFNykGKNVLI
K151-ac VHVIFNykGKNVLIN
K151 VHVIFNyKGKNVLIN
K151-sc VHVIFNykGKNVLIN
K153 VIFNykGKNVLINkD
K153 VIFNykGKNVLINkD
K159-ac GKNVLINkDIRCKDD
K159 GKNVLINKDIRCKDD
K159 GKNVLINKDIRCKDD
K206 DWDFLPPKKIkDPDA
K206 DWDFLPPKKIkDPDA
K206-sc DWDFLPPkKIkDPDA
K207 WDFLPPkKIkDPDAA
K209-ac FLPPkKIkDPDAAKP
A214 KIkDPDAAKPEDWDE
T229 RAKIDDPTDSKPEDW
S231 KIDDPTDSKPEDWDk
K238-ac SKPEDWDkPEHIPDP
Y299 PEIDNPEYSPDANIY
S300 EIDNPEYSPDANIYA
Y338-p LITNDEAyAEEFGNE
K360-sc AEKQMKDkQDEEQRL
K368-sc QDEEQRLkEEEEDkk
K374-ac LkEEEEDkkRKEEEE
K375-ac kEEEEDkkRKEEEEA
  rat

 
Y22 AAADPAIYFKEQFLD
K24 ADPAIYFKEQFLDGD
K43 RWVESKHKSDFGkFV
K43 RWVESKHKSDFGkFV
K48-ac KHKSDFGkFVLSSGK
K48 KHKSDFGKFVLSSGK
K48 KHKSDFGKFVLSSGK
S52 DFGkFVLSSGKFYGD
K55 kFVLSSGKFYGDQEk
K55 kFVLSSGKFYGDQEk
Y57 VLSSGKFYGDQEkDK
K62-ac KFYGDQEkDKGLQTS
K62 KFYGDQEKDKGLQTS
K62 KFYGDQEKDKGLQTS
K64 YGDQEkDKGLQTSQD
Y75 TSQDARFYALSARFE
R80 RFYALSARFEPFSNK
R80 RFYALSARFEPFSNK
R80 RFYALSARFEPFSNK
S85 SARFEPFSNKGQTLV
Y109 NIDCGGGYVKLFPGG
K142 DICGPGTKKVHVIFN
K143 ICGPGTKKVHVIFNY
Y150 KVHVIFNYkGKNVLI
K151-ac VHVIFNYkGKNVLIN
K151 VHVIFNYKGKNVLIN
K151 VHVIFNYKGKNVLIN
K153 VIFNYkGKNVLINkD
K153 VIFNYkGKNVLINkD
K159-ac GKNVLINkDIRCKDD
K159 GKNVLINKDIRCKDD
K159 GKNVLINKDIRCKDD
K206 DWDFLPPKKIkDPDA
K206 DWDFLPPKKIkDPDA
K206 DWDFLPPKKIkDPDA
K207 WDFLPPKKIkDPDAA
K209-ac FLPPKKIkDPDAAKP
A214 KIkDPDAAKPEDWDE
T229 RAKIDDPTDSKPEDW
S231 KIDDPTDSKPEDWDk
K238-ac SKPEDWDkPEHIPDP
Y299 PEIDNPEYSPDANIY
S300 EIDNPEYSPDANIYA
Y338 LITNDEAYAEEFGNE
K360 AEKQMKDKQDEEQRL
K368 QDEEQRLKEEEEDKK
K374 LKEEEEDKKRKEEEE
K375 KEEEEDKKRKEEEEA
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