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Protein Page:
Calreticulin (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
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: Secreted, signal peptide; Nuclear receptor co-regulator; Calcium-binding; Motility/polarity/chemotaxis; Secreted
Chromosomal Location of Human Ortholog: 19p13.3-p13.2
Cellular Component: acrosome; cell surface; cytoplasm; cytosol; endoplasmic reticulum; endoplasmic reticulum lumen; external side of plasma membrane; extracellular region; extracellular space; focal adhesion; Golgi apparatus; intracellular; membrane; nucleus; perinuclear region of cytoplasm; polysome; proteinaceous extracellular matrix; sarcoplasmic reticulum lumen; smooth endoplasmic reticulum
Molecular Function: androgen receptor binding; calcium ion binding; carbohydrate binding; chaperone binding; complement component C1q binding; DNA binding; glycoprotein binding; hormone binding; integrin binding; iron ion binding; mRNA binding; peptide binding; protein binding; ubiquitin protein ligase binding; unfolded protein binding; zinc ion binding
Biological Process: antigen processing and presentation of peptide antigen via MHC class I; cardiac muscle cell differentiation; cell cycle arrest; cellular calcium ion homeostasis; cortical actin cytoskeleton organization and biogenesis; glucocorticoid receptor signaling pathway; negative regulation of neuron differentiation; negative regulation of retinoic acid receptor signaling pathway; negative regulation of steroid hormone receptor signaling pathway; negative regulation of transcription from RNA polymerase II promoter; negative regulation of transcription, DNA-dependent; negative regulation of translation; peptide antigen assembly with MHC class I protein complex; positive regulation of cell cycle; positive regulation of cell proliferation; positive regulation of DNA replication; positive regulation of phagocytosis; protein export from nucleus; protein folding; protein maturation via protein folding; protein stabilization; receptor-mediated endocytosis; regulation of apoptosis; regulation of meiosis; regulation of transcription, DNA-dependent; response to drug; response to estradiol stimulus; response to testosterone stimulus; sequestering of calcium ion; spermatogenesis
Disease: Myelofibrosis; Thrombocythemia 1
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
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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


 LTP 

LTP: 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.


 HTP 

HTP: 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 T34‑p FLDGDGWtsRWIESK
0 1 S35‑p LDGDGWtsRWIESKH
0 1 K41 tsRWIESKHksDFGk
0 1 K43 RWIESKHKsDFGkFV
0 1 K43‑sc RWIESKHksDFGkFV
0 1 S44‑p WIESKHksDFGkFVL
1 3 K48‑ac KHksDFGkFVLssGk
0 3 K48‑ub KHksDFGkFVLssGk
0 1 K48‑sc KHksDFGkFVLssGk
0 3 S52‑p DFGkFVLssGkFyGD
0 2 S53‑p FGkFVLssGkFyGDE
0 1 K55 kFVLssGKFyGDEEk
0 3 K55‑ub kFVLssGkFyGDEEk
0 1 K55‑sc kFVLssGkFyGDEEk
0 1 Y57‑p VLssGkFyGDEEkDk
1 2 K62‑ac kFyGDEEkDkGLQTS
0 4 K62‑ub kFyGDEEkDkGLQTS
0 1 K62‑sc kFyGDEEkDkGLQTS
1 0 K64‑ac yGDEEkDkGLQTSQD
0 3 Y75‑p TSQDARFyALsAsFE
0 1 S78‑p DARFyALsAsFEPFs
0 1 S80‑p RFyALsAsFEPFsNK
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 2 K151 VHVIFNyKGkNVLIN
0 2 K151‑ub VHVIFNykGkNVLIN
0 1 K151‑sc VHVIFNykGkNVLIN
1 0 K153‑ac VIFNykGkNVLINkD
0 5 K153‑ub VIFNykGkNVLINkD
1 5 K159‑ac GkNVLINkDIRCKDD
0 13 K159‑ub GkNVLINkDIRCKDD
0 1 K159‑sc GkNVLINkDIRCKDD
0 1 T169‑p RCKDDEFtHLyTLIV
0 1 Y172‑p DDEFtHLyTLIVRPD
0 1 T181‑p LIVRPDNtyEVKIDN
0 1 Y182‑p IVRPDNtyEVKIDNS
0 1 S195‑p NSQVESGsLEDDWDF
1 1 K206‑ac DWDFLPPkkIkDPDA
0 2 K206‑ub DWDFLPPkkIkDPDA
0 1 K206 DWDFLPPKkIkDPDA
1 0 K207‑ac WDFLPPkkIkDPDAs
1 4 K209‑ac FLPPkkIkDPDAsKP
0 3 S214‑p kIkDPDAsKPEDWDE
0 1 K215 IkDPDAsKPEDWDER
0 1 T229‑p RAKIDDPtDsKPEDW
0 2 S231‑p KIDDPtDsKPEDWDk
0 1 K232 IDDPtDsKPEDWDkP
1 2 K238‑ac sKPEDWDkPEHIPDP
0 1 Y271‑p PVIQNPEyKGEWKPR
0 2 Y285‑p RQIDNPDyKGTWIHP
0 1 Y299‑p PEIDNPEysPDPSIY
0 1 S300‑p EIDNPEysPDPSIYA
0 1 T333‑p IFDNFLItNDEAYAE
0 1 Y338 LItNDEAYAEEFGNE
0 1 K360 AEKQMKDKQDEEQRL
0 1 K368 QDEEQRLKEEEEDKK
0 1 K368 QDEEQRLKEEEEDKK
0 4 K374 LKEEEEDKKRKEEEE
0 13 K375 KEEEEDKKRKEEEEA
  mouse

 
Y22 AAADPAIYFKEQFLD
K24 ADPAIYFKEQFLDGD
T34 FLDGDAWTNRWVESK
N35 LDGDAWTNRWVESKH
K41 TNRWVESKHkSDFGk
K43‑ac RWVESKHkSDFGkFV
K43 RWVESKHKSDFGkFV
S44 WVESKHkSDFGkFVL
K48 KHkSDFGKFVLSSGk
K48 KHkSDFGKFVLSSGk
K48‑sc KHkSDFGkFVLSSGk
S52 DFGkFVLSSGkFYGD
S53 FGkFVLSSGkFYGDL
K55 kFVLSSGKFYGDLEk
K55‑ub kFVLSSGkFYGDLEk
K55‑sc kFVLSSGkFYGDLEk
Y57 VLSSGkFYGDLEkDK
K62‑ac kFYGDLEkDKGLQTS
K62‑ub kFYGDLEkDKGLQTS
K62‑sc kFYGDLEkDKGLQTS
K64 YGDLEkDKGLQTSQD
Y75 TSQDARFYALSAkFE
S78 DARFYALSAkFEPFS
K80 RFYALSAKFEPFSNK
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
T169 RCKDDEFTHLYTLIV
Y172 DDEFTHLYTLIVRPD
T181 LIVRPDNTYEVKIDN
Y182 IVRPDNTYEVKIDNS
S195 NSQVESGSLEDDWDF
K206 DWDFLPPKKIkDPDA
K206 DWDFLPPKKIkDPDA
K206‑sc DWDFLPPkKIkDPDA
K207 WDFLPPkKIkDPDAA
K209‑ac FLPPkKIkDPDAAKP
A214 KIkDPDAAKPEDWDE
K215 IkDPDAAKPEDWDER
T229 RAKIDDPTDsKPEDW
S231‑p KIDDPTDsKPEDWDk
K232 IDDPTDsKPEDWDkP
K238‑ac sKPEDWDkPEHIPDP
Y271 PVIQNPEYKGEWKPR
Y285 RQIDNPDYKGTWIHP
Y299 PEIDNPEYSPDANIY
S300 EIDNPEYSPDANIYA
T333 IFDNFLITNDEAyAE
Y338‑p LITNDEAyAEEFGNE
K360‑sc AEKQMKDkQDEEQRL
K368 QDEEQRLKEEEEDkk
K368‑sc QDEEQRLkEEEEDkk
K374‑ac LkEEEEDkkRKEEEE
K375‑ac kEEEEDkkRKEEEEA
  rat

 
Y22 AAADPAIYFKEQFLD
K24 ADPAIYFKEQFLDGD
T34 FLDGDAWTNRWVESk
N35 LDGDAWTNRWVESkH
K41‑ac TNRWVESkHKSDFGk
K43 RWVESkHKSDFGkFV
K43 RWVESkHKSDFGkFV
S44 WVESkHKSDFGkFVL
K48‑ac kHKSDFGkFVLSSGk
K48 kHKSDFGKFVLSSGk
K48 kHKSDFGKFVLSSGk
S52 DFGkFVLSSGkFYGD
S53 FGkFVLSSGkFYGDQ
K55‑ac kFVLSSGkFYGDQEk
K55 kFVLSSGKFYGDQEk
K55 kFVLSSGKFYGDQEk
Y57 VLSSGkFYGDQEkDK
K62‑ac kFYGDQEkDKGLQTS
K62 kFYGDQEKDKGLQTS
K62 kFYGDQEKDKGLQTS
K64 YGDQEkDKGLQTSQD
Y75 TSQDARFYALSARFE
S78 DARFYALSARFEPFS
R80 RFYALSARFEPFSNK
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
T169 RCKDDEFTHLYTLIV
Y172 DDEFTHLYTLIVRPD
T181 LIVRPDNTYEVKIDN
Y182 IVRPDNTYEVKIDNS
S195 NSQVESGSLEDDWDF
K206 DWDFLPPKKIkDPDA
K206 DWDFLPPKKIkDPDA
K206 DWDFLPPKKIkDPDA
K207 WDFLPPKKIkDPDAA
K209‑ac FLPPKKIkDPDAAkP
A214 KIkDPDAAkPEDWDE
K215‑ac IkDPDAAkPEDWDER
T229 RAKIDDPTDSkPEDW
S231 KIDDPTDSkPEDWDk
K232‑ac IDDPTDSkPEDWDkP
K238‑ac SkPEDWDkPEHIPDP
Y271 PVIQNPEYKGEWKPR
Y285 RQIDNPDYKGTWIHP
Y299 PEIDNPEYSPDANIY
S300 EIDNPEYSPDANIYA
T333 IFDNFLITNDEAYAE
Y338 LITNDEAYAEEFGNE
K360 AEKQMKDKQDEEQRL
K368‑ac QDEEQRLkEEEEDKK
K368 QDEEQRLKEEEEDKK
K374 LkEEEEDKKRKEEEE
K375 kEEEEDKKRKEEEEA
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