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P27797 (CALR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 174. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Calreticulin
Alternative name(s):
CRP55
Calregulin
Endoplasmic reticulum resident protein 60
Short name=ERp60
HACBP
grp60
Gene names
Name:CALR
Synonyms:CRTC
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length417 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 By similarity. Ref.20 Ref.23

Subunit structure

Monomer. Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5. Interacts with PDIA3/ERp57 By similarity. Interacts with NR3C1 and TRIM21. Interacts with GABARAP. Interacts with PPIB. Ref.21 Ref.23 Ref.27 Ref.29

Subcellular location

Endoplasmic reticulum lumen. Cytoplasmcytosol. Secretedextracellular spaceextracellular matrix. Cell surface. Sarcoplasmic reticulum lumen By similarity. Note: Also found in cell surface (T cells), cytosol and extracellular matrix. Associated with the lytic granules in the cytolytic T-lymphocytes. Ref.18 Ref.22 Ref.23

Domain

Can be divided into a N-terminal globular domain, a proline-rich P-domain forming an elongated arm-like structure and a C-terminal acidic domain. The P-domain binds one molecule of calcium with high affinity, whereas the acidic C-domain binds multiple calcium ions with low affinity.

The interaction with glycans occurs through a binding site in the globular lectin domain.

The zinc binding sites are localized to the N-domain.

Associates with PDIA3 through the tip of the extended arm formed by the P-domain.

Sequence similarities

Belongs to the calreticulin family.

Caution

Was originally (Ref.1) thought to be the 52 kDa Ro autoantigen.

Mass spectrometry

Molecular mass is 46879 Da from positions 18 - 417. Determined by MALDI. Ref.23

Ontologies

Keywords
   Cellular componentCytoplasm
Endoplasmic reticulum
Extracellular matrix
Sarcoplasmic reticulum
Secreted
   DomainRepeat
Signal
   LigandCalcium
Lectin
Metal-binding
Zinc
   Molecular functionChaperone
   PTMAcetylation
Disulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of signaling protein activity involved in unfolded protein response

Traceable author statement. Source: Reactome

antigen processing and presentation of exogenous peptide antigen via MHC class I

Traceable author statement. Source: Reactome

antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent

Traceable author statement. Source: Reactome

antigen processing and presentation of peptide antigen via MHC class I

Traceable author statement. Source: Reactome

cardiac muscle cell differentiation

Inferred from electronic annotation. Source: Ensembl

cell cycle arrest

Inferred from genetic interaction PubMed 14726956. Source: BHF-UCL

cellular calcium ion homeostasis

Traceable author statement Ref.23. Source: UniProtKB

cellular protein metabolic process

Traceable author statement. Source: Reactome

cellular response to lithium ion

Inferred from electronic annotation. Source: Ensembl

cellular senescence

Inferred from genetic interaction PubMed 14726956. Source: BHF-UCL

chaperone-mediated protein folding

Inferred from electronic annotation. Source: Ensembl

cortical actin cytoskeleton organization

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum unfolded protein response

Traceable author statement. Source: Reactome

glucocorticoid receptor signaling pathway

Traceable author statement PubMed 8107809. Source: BHF-UCL

negative regulation of intracellular steroid hormone receptor signaling pathway

Inferred from direct assay PubMed 8107809. Source: BHF-UCL

negative regulation of neuron differentiation

Inferred from direct assay PubMed 8107809. Source: BHF-UCL

negative regulation of retinoic acid receptor signaling pathway

Inferred from direct assay PubMed 8107809. Source: BHF-UCL

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 8107809. Source: BHF-UCL

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 8107809. Source: BHF-UCL

negative regulation of translation

Inferred from sequence or structural similarity PubMed 14726956. Source: BHF-UCL

peptide antigen assembly with MHC class I protein complex

Inferred from sequence or structural similarity PubMed 11825569. Source: BHF-UCL

positive regulation of DNA replication

Inferred from genetic interaction PubMed 14726956. Source: BHF-UCL

positive regulation of cell cycle

Inferred from genetic interaction PubMed 14726956. Source: BHF-UCL

positive regulation of cell proliferation

Inferred from genetic interaction PubMed 14726956. Source: BHF-UCL

positive regulation of dendritic cell chemotaxis

Inferred from mutant phenotype PubMed 16140380. Source: UniProtKB

positive regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

positive regulation of phagocytosis

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of substrate adhesion-dependent cell spreading

Inferred from mutant phenotype PubMed 11859136. Source: UniProtKB

post-translational protein modification

Traceable author statement. Source: Reactome

protein N-linked glycosylation via asparagine

Traceable author statement. Source: Reactome

protein export from nucleus

Inferred from direct assay Ref.23. Source: UniProtKB

protein folding

Traceable author statement PubMed 15474971. Source: BHF-UCL

protein localization to nucleus

Inferred from direct assay PubMed 15998798. Source: UniProtKB

protein maturation by protein folding

Traceable author statement PubMed 17563366. Source: BHF-UCL

protein stabilization

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of apoptotic process

Traceable author statement PubMed 16130169. Source: UniProtKB

regulation of meiosis

Inferred from electronic annotation. Source: Ensembl

regulation of transcription, DNA-templated

Traceable author statement PubMed 8107808. Source: ProtInc

response to drug

Inferred from electronic annotation. Source: Ensembl

response to estradiol

Inferred from electronic annotation. Source: Ensembl

response to testosterone

Inferred from electronic annotation. Source: Ensembl

sequestering of calcium ion

Traceable author statement PubMed 15474971. Source: BHF-UCL

spermatogenesis

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

MHC class I peptide loading complex

Inferred from sequence or structural similarity PubMed 11825569. Source: BHF-UCL

acrosomal vesicle

Inferred from electronic annotation. Source: Ensembl

cell surface

Traceable author statement PubMed 15474971. Source: BHF-UCL

cytoplasm

Inferred from direct assay Ref.13. Source: BHF-UCL

cytosol

Inferred from direct assay Ref.23. Source: UniProtKB

endocytic vesicle lumen

Traceable author statement. Source: Reactome

endoplasmic reticulum

Traceable author statement PubMed 16130169. Source: UniProtKB

endoplasmic reticulum lumen

Inferred from direct assay Ref.23. Source: UniProtKB

external side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 20551380. Source: BHF-UCL

extracellular vesicular exosome

Inferred from direct assay PubMed 19199708. Source: UniProt

integral component of lumenal side of endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

intracellular

Traceable author statement Ref.11. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 8107809. Source: BHF-UCL

perinuclear region of cytoplasm

Inferred from direct assay Ref.13. Source: BHF-UCL

polysome

Inferred from sequence or structural similarity PubMed 14726956. Source: BHF-UCL

proteinaceous extracellular matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

sarcoplasmic reticulum lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionDNA binding

Non-traceable author statement Ref.23. Source: UniProtKB

androgen receptor binding

Inferred from direct assay PubMed 8107809. Source: BHF-UCL

calcium ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

carbohydrate binding

Traceable author statement PubMed 15474971. Source: BHF-UCL

chaperone binding

Traceable author statement PubMed 15474971. Source: BHF-UCL

complement component C1q binding

Traceable author statement PubMed 15474971. Source: BHF-UCL

hormone binding

Inferred from electronic annotation. Source: Ensembl

integrin binding

Inferred from physical interaction Ref.13. Source: BHF-UCL

iron ion binding

Inferred from electronic annotation. Source: Ensembl

mRNA binding

Inferred from direct assay PubMed 14726956. Source: BHF-UCL

peptide binding

Inferred from electronic annotation. Source: Ensembl

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

protein binding involved in protein folding

Traceable author statement PubMed 15474971. Source: BHF-UCL

ubiquitin protein ligase binding

Inferred from physical interaction Ref.21. Source: UniProtKB

unfolded protein binding

Traceable author statement PubMed 15474971. Source: BHF-UCL

zinc ion binding

Traceable author statement PubMed 15474971. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TAP1Q035182EBI-1049597,EBI-747259

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.18 Ref.19
Chain18 – 417400Calreticulin
PRO_0000004173

Regions

Repeat191 – 202121-1
Repeat210 – 221121-2
Repeat227 – 238121-3
Repeat244 – 255121-4
Repeat259 – 269112-1
Repeat273 – 283112-2
Repeat287 – 297112-3
Region18 – 197180N-domain
Region191 – 255654 X approximate repeats
Region198 – 308111P-domain
Region237 – 27034Interaction with PPIB By similarity
Region259 – 297393 X approximate repeats
Region309 – 417109C-domain
Motif414 – 4174Prevents secretion from ER
Compositional bias351 – 40858Asp/Glu/Lys-rich

Sites

Metal binding261Calcium; via carbonyl oxygen
Metal binding621Calcium; via carbonyl oxygen
Metal binding641Calcium; via carbonyl oxygen
Metal binding3281Calcium
Binding site1091Carbohydrate By similarity
Binding site1111Carbohydrate By similarity
Binding site1281Carbohydrate By similarity
Binding site1351Carbohydrate By similarity
Binding site3171Carbohydrate By similarity

Amino acid modifications

Modified residue481N6-acetyllysine Ref.26
Modified residue1591N6-acetyllysine Ref.26
Modified residue2091N6-acetyllysine Ref.26
Glycosylation3441N-linked (GlcNAc...) Ref.25
Disulfide bond105 ↔ 137 Ref.24 Ref.30

Secondary structure

................................................ 417
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P27797 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: BC37C3C0F1054FB2

FASTA41748,142
        10         20         30         40         50         60 
MLLSVPLLLG LLGLAVAEPA VYFKEQFLDG DGWTSRWIES KHKSDFGKFV LSSGKFYGDE 

        70         80         90        100        110        120 
EKDKGLQTSQ DARFYALSAS FEPFSNKGQT LVVQFTVKHE QNIDCGGGYV KLFPNSLDQT 

       130        140        150        160        170        180 
DMHGDSEYNI MFGPDICGPG TKKVHVIFNY KGKNVLINKD IRCKDDEFTH LYTLIVRPDN 

       190        200        210        220        230        240 
TYEVKIDNSQ VESGSLEDDW DFLPPKKIKD PDASKPEDWD ERAKIDDPTD SKPEDWDKPE 

       250        260        270        280        290        300 
HIPDPDAKKP EDWDEEMDGE WEPPVIQNPE YKGEWKPRQI DNPDYKGTWI HPEIDNPEYS 

       310        320        330        340        350        360 
PDPSIYAYDN FGVLGLDLWQ VKSGTIFDNF LITNDEAYAE EFGNETWGVT KAAEKQMKDK 

       370        380        390        400        410 
QDEEQRLKEE EEDKKRKEEE EAEDKEDDED KDEDEEDEED KEEDEEEDVP GQAKDEL 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning, expression, and chromosome 19 localization of a human Ro/SS-A autoantigen."
McCauliffe D.P., Lux F.A., Lieu T.S., Sanz I., Hanke J., Newkirk M.M., Bachinski L.L., Itoh Y., Siciliano M.J., Reichlin M., Sontheimer R.D., Capra J.D.
J. Clin. Invest. 85:1379-1391(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Characterization of the autoantigen calreticulin."
Rokeach L.A., Haselby J.A., Meilof J.F., Smeenk R.J., Unnasch T.R., Greene B.M., Hoch S.O.
J. Immunol. 147:3031-3039(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The 5'-flanking region of the human calreticulin gene shares homology with the human GRP78, GRP94, and protein disulfide isomerase promoters."
McCauliffe D.P., Yang Y.S., Wilson J., Sontheimer R.D., Capra J.D.
J. Biol. Chem. 267:2557-2562(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]Liu J., Peng X., Yuan J., Qiang B.
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]"Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B. expand/collapse author list , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[8]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Eye, Pancreas and Skin.
[11]"Human placental calreticulin: purification, characterization and association with other proteins."
Houen G., Koch C.
Acta Chem. Scand. 48:905-911(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 18-48; 65-92; 96-114; 168-205 AND 257-354.
Tissue: Placenta.
[12]"Molecular characterization of human Ro/SS-A antigen. Amino terminal sequence of the protein moiety of human Ro/SS-A antigen and immunological activity of a corresponding synthetic peptide."
Lieu T.-S., Newkirk M.M., Capra J.D., Sontheimer R.D.
J. Clin. Invest. 82:96-101(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 18-41.
[13]"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."
Rojiani M.V., Finlay B.B., Gray V., Dedhar S.
Biochemistry 30:9859-9866(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 18-36.
[14]"Sequence similarity of calreticulin with a Ca2(+)-binding protein that co-purifies with an Ins(1,4,5)P3-sensitive Ca2+ store in HL-60 cells."
Krause K.-H., Simmerman H.K.B., Jones L.R., Campbell K.P.
Biochem. J. 270:545-548(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 18-32.
[15]"Human liver protein map: a reference database established by microsequencing and gel comparison."
Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., Appel R.D., Hughes G.J.
Electrophoresis 13:992-1001(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 18-28.
Tissue: Liver.
[16]Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 25-36; 74-111 AND 208-222, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[17]"Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes."
Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.
Electrophoresis 13:960-969(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-34; 56-62; 208-221 AND 273-278.
Tissue: Keratinocyte.
[18]"The calcium-binding protein calreticulin is a major constituent of lytic granules in cytolytic T lymphocytes."
Dupuis M., Schaerer E., Krause K.-H., Tschopp J.
J. Exp. Med. 177:1-7(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 18-27, SUBCELLULAR LOCATION.
[19]"A two-dimensional gel database of human colon carcinoma proteins."
Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J.
Electrophoresis 18:605-613(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 18-26.
Tissue: Colon carcinoma.
[20]"Calreticulin functions as a molecular chaperone in the biosynthesis of myeloperoxidase."
Nauseef W.M., McCormick S.J., Clark R.A.
J. Biol. Chem. 270:4741-4747(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[21]"Calreticulin binds hYRNA and the 52-kDa polypeptide component of the Ro/SS-A ribonucleoprotein autoantigen."
Cheng S.T., Nguyen T.Q., Yang Y.S., Capra J.D., Sontheimer R.D.
J. Immunol. 156:4484-4491(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRIM21.
[22]"Calreticulin is expressed on the cell surface of activated human peripheral blood T lymphocytes in association with major histocompatibility complex class I molecules."
Arosa F.A., de Jesus O., Porto G., Carmo A.M., de Sousa M.
J. Biol. Chem. 274:16917-16922(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[23]"Calreticulin is a receptor for nuclear export."
Holaska J.M., Black B.E., Love D.C., Hanover J.A., Leszyk J., Paschal B.M.
J. Cell Biol. 152:127-140(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH NR3C1, SUBCELLULAR LOCATION, MASS SPECTROMETRY.
[24]"Human placental calreticulin characterization of domain structure and post-translational modifications."
Hoejrup P., Roepstorff P., Houen G.
Eur. J. Biochem. 268:2558-2565(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, DISULFIDE BOND, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Placenta.
[25]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-344.
Tissue: Liver.
[26]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-48; LYS-159 AND LYS-209, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"Structural basis of cyclophilin B binding by the calnexin/calreticulin P-domain."
Kozlov G., Bastos-Aristizabal S., Maattanen P., Rosenauer A., Zheng F., Killikelly A., Trempe J.F., Thomas D.Y., Gehring K.
J. Biol. Chem. 285:35551-35557(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PPIB.
[28]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[29]"Structural framework of the GABARAP-calreticulin interface --implications for substrate binding to endoplasmic reticulum chaperones."
Thielmann Y., Weiergraber O.H., Mohrluder J., Willbold D.
FEBS J. 276:1140-1152(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 195-205 IN COMPLEX WITH GABARAP, INTERACTION WITH GABARAP.
[30]"X-ray structure of the human calreticulin globular domain reveals a peptide-binding area and suggests a multi-molecular mechanism."
Chouquet A., Paidassi H., Ling W.L., Frachet P., Houen G., Arlaud G.J., Gaboriaud C.
PLoS ONE 6:E17886-E17886(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 18-368 IN COMPLEX WITH CALCIUM IONS, DISULFIDE BOND.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M32294 mRNA. Translation: AAA36582.1.
M84739 mRNA. Translation: AAA51916.1.
AY047586 mRNA. Translation: AAL13126.1.
AB451408 mRNA. Translation: BAG70222.1.
BT007448 mRNA. Translation: AAP36116.1.
CR457070 mRNA. Translation: CAG33351.1.
AD000092 Genomic DNA. Translation: AAB51176.1.
CH471106 Genomic DNA. Translation: EAW84331.1.
BC002500 mRNA. Translation: AAH02500.1.
BC007911 mRNA. Translation: AAH07911.1.
BC020493 mRNA. Translation: AAH20493.1.
PIRA37047. A42330.
RefSeqNP_004334.1. NM_004343.3.
UniGeneHs.515162.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CLRX-ray2.00C/F1-10[»]
3DOWX-ray2.30B195-205[»]
3POSX-ray1.65A/B/C18-368[»]
3POWX-ray1.55A18-368[»]
DisProtDP00333.
ProteinModelPortalP27797.
SMRP27797. Positions 18-367.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107262. 79 interactions.
DIPDIP-104N.
IntActP27797. 26 interactions.
MINTMINT-101756.
STRING9606.ENSP00000320866.

Chemistry

DrugBankDB00009. Alteplase.
DB00029. Anistreplase.
DB00025. Antihemophilic Factor.
DB00015. Reteplase.
DB00031. Tenecteplase.

PTM databases

PhosphoSiteP27797.

Polymorphism databases

DMDM117501.

2D gel databases

DOSAC-COBS-2DPAGEP27797.
OGPP27797.
REPRODUCTION-2DPAGEIPI00020599.
SWISS-2DPAGEP27797.
UCD-2DPAGEP27797.

Proteomic databases

PaxDbP27797.
PRIDEP27797.

Protocols and materials databases

DNASU811.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000316448; ENSP00000320866; ENSG00000179218.
GeneID811.
KEGGhsa:811.
UCSCuc002mvu.2. human.

Organism-specific databases

CTD811.
GeneCardsGC19P013049.
HGNCHGNC:1455. CALR.
HPACAB001513.
CAB019952.
HPA002242.
MIM109091. gene.
neXtProtNX_P27797.
PharmGKBPA26046.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG305105.
HOGENOMHOG000192435.
HOVERGENHBG005407.
InParanoidP27797.
KOK08057.
OMAVKLFPDG.
OrthoDBEOG77126Z.
PhylomeDBP27797.
TreeFamTF338438.

Enzyme and pathway databases

ReactomeREACT_160300. Binding and Uptake of Ligands by Scavenger Receptors.
REACT_17015. Metabolism of proteins.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressP27797.
BgeeP27797.
CleanExHS_CALR.
GenevestigatorP27797.

Family and domain databases

Gene3D2.60.120.200. 2 hits.
InterProIPR001580. Calret/calnex.
IPR018124. Calret/calnex_CS.
IPR009169. Calreticulin.
IPR009033. Calreticulin/calnexin_P_dom.
IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
[Graphical view]
PANTHERPTHR11073. PTHR11073. 1 hit.
PfamPF00262. Calreticulin. 1 hit.
[Graphical view]
PIRSFPIRSF002356. Calreticulin. 1 hit.
PRINTSPR00626. CALRETICULIN.
SUPFAMSSF49899. SSF49899. 1 hit.
SSF63887. SSF63887. 1 hit.
PROSITEPS00803. CALRETICULIN_1. 1 hit.
PS00804. CALRETICULIN_2. 1 hit.
PS00805. CALRETICULIN_REPEAT. 3 hits.
PS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCALR. human.
EvolutionaryTraceP27797.
GeneWikiCalreticulin.
GenomeRNAi811.
NextBio3292.
PROP27797.
SOURCESearch...

Entry information

Entry nameCALR_HUMAN
AccessionPrimary (citable) accession number: P27797
Secondary accession number(s): Q6IAT4, Q9UDG2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: April 16, 2014
This is version 174 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM