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P27797

- CALR_HUMAN

UniProt

P27797 - CALR_HUMAN

Protein

Calreticulin

Gene

CALR

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 179 (01 Oct 2014)
      Sequence version 1 (01 Aug 1992)
      Previous versions | rss
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    Functioni

    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.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi26 – 261Calcium; via carbonyl oxygen
    Metal bindingi62 – 621Calcium; via carbonyl oxygen
    Metal bindingi64 – 641Calcium; via carbonyl oxygen
    Binding sitei109 – 1091CarbohydrateBy similarity
    Binding sitei111 – 1111CarbohydrateBy similarity
    Binding sitei128 – 1281CarbohydrateBy similarity
    Binding sitei135 – 1351CarbohydrateBy similarity
    Binding sitei317 – 3171CarbohydrateBy similarity
    Metal bindingi328 – 3281Calcium

    GO - Molecular functioni

    1. androgen receptor binding Source: BHF-UCL
    2. calcium ion binding Source: UniProtKB
    3. carbohydrate binding Source: BHF-UCL
    4. chaperone binding Source: BHF-UCL
    5. complement component C1q binding Source: BHF-UCL
    6. DNA binding Source: UniProtKB
    7. glycoprotein binding Source: UniProt
    8. hormone binding Source: Ensembl
    9. integrin binding Source: BHF-UCL
    10. iron ion binding Source: Ensembl
    11. mRNA binding Source: BHF-UCL
    12. peptide binding Source: Ensembl
    13. poly(A) RNA binding Source: UniProtKB
    14. protein binding Source: IntAct
    15. protein binding involved in protein folding Source: BHF-UCL
    16. ubiquitin protein ligase binding Source: UniProtKB
    17. unfolded protein binding Source: BHF-UCL
    18. zinc ion binding Source: BHF-UCL

    GO - Biological processi

    1. activation of signaling protein activity involved in unfolded protein response Source: Reactome
    2. antigen processing and presentation of exogenous peptide antigen via MHC class I Source: Reactome
    3. antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent Source: Reactome
    4. antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
    5. cardiac muscle cell differentiation Source: Ensembl
    6. cell cycle arrest Source: BHF-UCL
    7. cellular calcium ion homeostasis Source: UniProtKB
    8. cellular protein metabolic process Source: Reactome
    9. cellular response to lithium ion Source: Ensembl
    10. cellular senescence Source: BHF-UCL
    11. chaperone-mediated protein folding Source: Ensembl
    12. cortical actin cytoskeleton organization Source: Ensembl
    13. endoplasmic reticulum unfolded protein response Source: Reactome
    14. glucocorticoid receptor signaling pathway Source: BHF-UCL
    15. negative regulation of intracellular steroid hormone receptor signaling pathway Source: BHF-UCL
    16. negative regulation of neuron differentiation Source: BHF-UCL
    17. negative regulation of retinoic acid receptor signaling pathway Source: BHF-UCL
    18. negative regulation of transcription, DNA-templated Source: BHF-UCL
    19. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    20. negative regulation of translation Source: BHF-UCL
    21. peptide antigen assembly with MHC class I protein complex Source: BHF-UCL
    22. positive regulation of cell cycle Source: BHF-UCL
    23. positive regulation of cell proliferation Source: BHF-UCL
    24. positive regulation of dendritic cell chemotaxis Source: UniProtKB
    25. positive regulation of DNA replication Source: BHF-UCL
    26. positive regulation of gene expression Source: Ensembl
    27. positive regulation of phagocytosis Source: BHF-UCL
    28. positive regulation of substrate adhesion-dependent cell spreading Source: UniProtKB
    29. post-translational protein modification Source: Reactome
    30. protein export from nucleus Source: UniProtKB
    31. protein folding Source: BHF-UCL
    32. protein localization to nucleus Source: UniProtKB
    33. protein maturation by protein folding Source: BHF-UCL
    34. protein N-linked glycosylation via asparagine Source: Reactome
    35. protein stabilization Source: UniProtKB
    36. regulation of apoptotic process Source: UniProtKB
    37. regulation of meiosis Source: Ensembl
    38. regulation of transcription, DNA-templated Source: ProtInc
    39. response to drug Source: Ensembl
    40. response to estradiol Source: Ensembl
    41. response to testosterone Source: Ensembl
    42. sequestering of calcium ion Source: BHF-UCL
    43. spermatogenesis Source: Ensembl

    Keywords - Molecular functioni

    Chaperone

    Keywords - Ligandi

    Calcium, Lectin, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_111178. ER-Phagosome pathway.
    REACT_163699. Scavenging by Class A Receptors.
    REACT_163813. Scavenging by Class F Receptors.
    REACT_18423. ATF6-alpha activates chaperone genes.
    REACT_23810. Calnexin/calreticulin cycle.
    REACT_6277. Assembly of Viral Components at the Budding Site.
    REACT_75795. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Calreticulin
    Alternative name(s):
    CRP55
    Calregulin
    Endoplasmic reticulum resident protein 60
    Short name:
    ERp60
    HACBP
    grp60
    Gene namesi
    Name:CALR
    Synonyms:CRTC
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:1455. CALR.

    Subcellular locationi

    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.

    GO - Cellular componenti

    1. acrosomal vesicle Source: Ensembl
    2. cell surface Source: BHF-UCL
    3. cytoplasm Source: BHF-UCL
    4. cytosol Source: UniProtKB
    5. endocytic vesicle lumen Source: Reactome
    6. endoplasmic reticulum Source: UniProtKB
    7. endoplasmic reticulum lumen Source: UniProtKB
    8. external side of plasma membrane Source: Ensembl
    9. extracellular region Source: Reactome
    10. extracellular space Source: BHF-UCL
    11. extracellular vesicular exosome Source: UniProt
    12. Golgi apparatus Source: Ensembl
    13. integral component of lumenal side of endoplasmic reticulum membrane Source: Reactome
    14. intracellular Source: UniProtKB
    15. membrane Source: UniProtKB
    16. MHC class I peptide loading complex Source: BHF-UCL
    17. nucleus Source: BHF-UCL
    18. perinuclear region of cytoplasm Source: BHF-UCL
    19. polysome Source: BHF-UCL
    20. proteinaceous extracellular matrix Source: UniProtKB-SubCell
    21. sarcoplasmic reticulum lumen Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum, Extracellular matrix, Sarcoplasmic reticulum, Secreted

    Pathology & Biotechi

    Organism-specific databases

    Orphaneti3318. Essential thrombocythemia.
    824. Myelofibrosis with myeloid metaplasia.
    PharmGKBiPA26046.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 17177 PublicationsAdd
    BLAST
    Chaini18 – 417400CalreticulinPRO_0000004173Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei48 – 481N6-acetyllysine1 Publication
    Disulfide bondi105 ↔ 1372 Publications
    Modified residuei159 – 1591N6-acetyllysine1 Publication
    Modified residuei209 – 2091N6-acetyllysine1 Publication
    Glycosylationi344 – 3441N-linked (GlcNAc...)1 Publication

    Keywords - PTMi

    Acetylation, Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP27797.
    PaxDbiP27797.
    PRIDEiP27797.

    2D gel databases

    DOSAC-COBS-2DPAGEP27797.
    OGPiP27797.
    REPRODUCTION-2DPAGEIPI00020599.
    SWISS-2DPAGEP27797.
    UCD-2DPAGEP27797.

    PTM databases

    PhosphoSiteiP27797.

    Expressioni

    Gene expression databases

    ArrayExpressiP27797.
    BgeeiP27797.
    CleanExiHS_CALR.
    GenevestigatoriP27797.

    Organism-specific databases

    HPAiCAB001513.
    CAB019952.
    HPA002242.

    Interactioni

    Subunit structurei

    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.By similarity5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    APPP050672EBI-1049597,EBI-77613
    GABARAPO951664EBI-1049597,EBI-712001
    TAP1Q035182EBI-1049597,EBI-747259

    Protein-protein interaction databases

    BioGridi107262. 83 interactions.
    DIPiDIP-104N.
    IntActiP27797. 28 interactions.
    MINTiMINT-101756.
    STRINGi9606.ENSP00000320866.

    Structurei

    Secondary structure

    1
    417
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi20 – 256
    Helixi30 – 356
    Beta strandi37 – 393
    Beta strandi42 – 443
    Beta strandi49 – 524
    Turni60 – 634
    Beta strandi65 – 684
    Beta strandi70 – 8415
    Beta strandi91 – 988
    Beta strandi104 – 1074
    Beta strandi110 – 1134
    Helixi119 – 1213
    Beta strandi129 – 13810
    Beta strandi142 – 1509
    Beta strandi153 – 1564
    Beta strandi166 – 17611
    Beta strandi180 – 1867
    Beta strandi189 – 1957
    Helixi196 – 1994
    Beta strandi201 – 2033
    Beta strandi311 – 32212
    Beta strandi326 – 3349
    Helixi336 – 34510
    Helixi347 – 36620

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CLRX-ray2.00C/F1-10[»]
    3DOWX-ray2.30B195-205[»]
    3POSX-ray1.65A/B/C18-204[»]
    A/B/C302-368[»]
    3POWX-ray1.55A18-204[»]
    A302-368[»]
    DisProtiDP00333.
    ProteinModelPortaliP27797.
    SMRiP27797. Positions 18-367.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP27797.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati191 – 202121-1Add
    BLAST
    Repeati210 – 221121-2Add
    BLAST
    Repeati227 – 238121-3Add
    BLAST
    Repeati244 – 255121-4Add
    BLAST
    Repeati259 – 269112-1Add
    BLAST
    Repeati273 – 283112-2Add
    BLAST
    Repeati287 – 297112-3Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni18 – 197180N-domainAdd
    BLAST
    Regioni191 – 255654 X approximate repeatsAdd
    BLAST
    Regioni198 – 308111P-domainAdd
    BLAST
    Regioni237 – 27034Interaction with PPIBBy similarityAdd
    BLAST
    Regioni259 – 297393 X approximate repeatsAdd
    BLAST
    Regioni309 – 417109C-domainAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi414 – 4174Prevents secretion from ER

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi351 – 40858Asp/Glu/Lys-richAdd
    BLAST

    Domaini

    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 similaritiesi

    Belongs to the calreticulin family.Curated

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG305105.
    HOGENOMiHOG000192435.
    HOVERGENiHBG005407.
    InParanoidiP27797.
    KOiK08057.
    OMAiVKLFPDG.
    OrthoDBiEOG77126Z.
    PhylomeDBiP27797.
    TreeFamiTF338438.

    Family and domain databases

    Gene3Di2.60.120.200. 2 hits.
    InterProiIPR001580. 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]
    PANTHERiPTHR11073. PTHR11073. 1 hit.
    PfamiPF00262. Calreticulin. 1 hit.
    [Graphical view]
    PIRSFiPIRSF002356. Calreticulin. 1 hit.
    PRINTSiPR00626. CALRETICULIN.
    SUPFAMiSSF49899. SSF49899. 1 hit.
    SSF63887. SSF63887. 1 hit.
    PROSITEiPS00803. CALRETICULIN_1. 1 hit.
    PS00804. CALRETICULIN_2. 1 hit.
    PS00805. CALRETICULIN_REPEAT. 3 hits.
    PS00014. ER_TARGET. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P27797-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLLSVPLLLG LLGLAVAEPA VYFKEQFLDG DGWTSRWIES KHKSDFGKFV    50
    LSSGKFYGDE EKDKGLQTSQ DARFYALSAS FEPFSNKGQT LVVQFTVKHE 100
    QNIDCGGGYV KLFPNSLDQT DMHGDSEYNI MFGPDICGPG TKKVHVIFNY 150
    KGKNVLINKD IRCKDDEFTH LYTLIVRPDN TYEVKIDNSQ VESGSLEDDW 200
    DFLPPKKIKD PDASKPEDWD ERAKIDDPTD SKPEDWDKPE HIPDPDAKKP 250
    EDWDEEMDGE WEPPVIQNPE YKGEWKPRQI DNPDYKGTWI HPEIDNPEYS 300
    PDPSIYAYDN FGVLGLDLWQ VKSGTIFDNF LITNDEAYAE EFGNETWGVT 350
    KAAEKQMKDK QDEEQRLKEE EEDKKRKEEE EAEDKEDDED KDEDEEDEED 400
    KEEDEEEDVP GQAKDEL 417
    Length:417
    Mass (Da):48,142
    Last modified:August 1, 1992 - v1
    Checksum:iBC37C3C0F1054FB2
    GO

    Mass spectrometryi

    Molecular mass is 46879 Da from positions 18 - 417. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS12288.1.
    PIRiA42330. A37047.
    RefSeqiNP_004334.1. NM_004343.3.
    UniGeneiHs.515162.

    Genome annotation databases

    EnsembliENST00000316448; ENSP00000320866; ENSG00000179218.
    GeneIDi811.
    KEGGihsa:811.
    UCSCiuc002mvu.2. human.

    Polymorphism databases

    DMDMi117501.

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Calreticulin entry

    Functional Glycomics Gateway - Glycan Binding

    Calreticulin

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS12288.1.
    PIRi A42330. A37047.
    RefSeqi NP_004334.1. NM_004343.3.
    UniGenei Hs.515162.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2CLR X-ray 2.00 C/F 1-10 [» ]
    3DOW X-ray 2.30 B 195-205 [» ]
    3POS X-ray 1.65 A/B/C 18-204 [» ]
    A/B/C 302-368 [» ]
    3POW X-ray 1.55 A 18-204 [» ]
    A 302-368 [» ]
    DisProti DP00333.
    ProteinModelPortali P27797.
    SMRi P27797. Positions 18-367.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107262. 83 interactions.
    DIPi DIP-104N.
    IntActi P27797. 28 interactions.
    MINTi MINT-101756.
    STRINGi 9606.ENSP00000320866.

    Chemistry

    DrugBanki DB00009. Alteplase.
    DB00029. Anistreplase.
    DB00025. Antihemophilic Factor.
    DB00015. Reteplase.
    DB00031. Tenecteplase.

    PTM databases

    PhosphoSitei P27797.

    Polymorphism databases

    DMDMi 117501.

    2D gel databases

    DOSAC-COBS-2DPAGE P27797.
    OGPi P27797.
    REPRODUCTION-2DPAGE IPI00020599.
    SWISS-2DPAGE P27797.
    UCD-2DPAGE P27797.

    Proteomic databases

    MaxQBi P27797.
    PaxDbi P27797.
    PRIDEi P27797.

    Protocols and materials databases

    DNASUi 811.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000316448 ; ENSP00000320866 ; ENSG00000179218 .
    GeneIDi 811.
    KEGGi hsa:811.
    UCSCi uc002mvu.2. human.

    Organism-specific databases

    CTDi 811.
    GeneCardsi GC19P013049.
    HGNCi HGNC:1455. CALR.
    HPAi CAB001513.
    CAB019952.
    HPA002242.
    MIMi 109091. gene.
    neXtProti NX_P27797.
    Orphaneti 3318. Essential thrombocythemia.
    824. Myelofibrosis with myeloid metaplasia.
    PharmGKBi PA26046.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG305105.
    HOGENOMi HOG000192435.
    HOVERGENi HBG005407.
    InParanoidi P27797.
    KOi K08057.
    OMAi VKLFPDG.
    OrthoDBi EOG77126Z.
    PhylomeDBi P27797.
    TreeFami TF338438.

    Enzyme and pathway databases

    Reactomei REACT_111178. ER-Phagosome pathway.
    REACT_163699. Scavenging by Class A Receptors.
    REACT_163813. Scavenging by Class F Receptors.
    REACT_18423. ATF6-alpha activates chaperone genes.
    REACT_23810. Calnexin/calreticulin cycle.
    REACT_6277. Assembly of Viral Components at the Budding Site.
    REACT_75795. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

    Miscellaneous databases

    ChiTaRSi CALR. human.
    EvolutionaryTracei P27797.
    GeneWikii Calreticulin.
    GenomeRNAii 811.
    NextBioi 3292.
    PROi P27797.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P27797.
    Bgeei P27797.
    CleanExi HS_CALR.
    Genevestigatori P27797.

    Family and domain databases

    Gene3Di 2.60.120.200. 2 hits.
    InterProi IPR001580. 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 ]
    PANTHERi PTHR11073. PTHR11073. 1 hit.
    Pfami PF00262. Calreticulin. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF002356. Calreticulin. 1 hit.
    PRINTSi PR00626. CALRETICULIN.
    SUPFAMi SSF49899. SSF49899. 1 hit.
    SSF63887. SSF63887. 1 hit.
    PROSITEi PS00803. CALRETICULIN_1. 1 hit.
    PS00804. CALRETICULIN_2. 1 hit.
    PS00805. CALRETICULIN_REPEAT. 3 hits.
    PS00014. ER_TARGET. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.
      , 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. 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. 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. Cited for: INTERACTION WITH PPIB.
    28. 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.

    Entry informationi

    Entry nameiCALR_HUMAN
    AccessioniPrimary (citable) accession number: P27797
    Secondary accession number(s): Q6IAT4, Q9UDG2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: August 1, 1992
    Last modified: October 1, 2014
    This is version 179 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Caution

    Was originally thought to be the 52 kDa Ro autoantigen.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3