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P14211

- CALR_MOUSE

UniProt

P14211 - CALR_MOUSE

Protein

Calreticulin

Gene

Calr

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 160 (01 Oct 2014)
      Sequence version 1 (01 Jan 1990)
      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 oxygen1 Publication
    Metal bindingi62 – 621Calcium; via carbonyl oxygen1 Publication
    Metal bindingi64 – 641Calcium; via carbonyl oxygen1 Publication
    Binding sitei109 – 1091Carbohydrate
    Binding sitei111 – 1111Carbohydrate
    Binding sitei128 – 1281Carbohydrate
    Binding sitei135 – 1351Carbohydrate
    Binding sitei317 – 3171Carbohydrate
    Metal bindingi328 – 3281Calcium1 Publication

    GO - Molecular functioni

    1. calcium ion binding Source: UniProtKB
    2. carbohydrate binding Source: UniProtKB
    3. hormone binding Source: Ensembl
    4. iron ion binding Source: Ensembl
    5. mRNA binding Source: BHF-UCL
    6. peptide binding Source: Ensembl
    7. protein binding Source: IntAct

    GO - Biological processi

    1. cardiac muscle cell differentiation Source: Ensembl
    2. cell cycle arrest Source: Ensembl
    3. cellular response to lithium ion Source: Ensembl
    4. cellular response to organic substance Source: Ensembl
    5. cellular senescence Source: BHF-UCL
    6. chaperone-mediated protein folding Source: Ensembl
    7. cortical actin cytoskeleton organization Source: MGI
    8. negative regulation of intracellular steroid hormone receptor signaling pathway Source: Ensembl
    9. negative regulation of neuron differentiation Source: Ensembl
    10. negative regulation of retinoic acid receptor signaling pathway Source: Ensembl
    11. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
    12. negative regulation of translation Source: Ensembl
    13. peptide antigen assembly with MHC class I protein complex Source: BHF-UCL
    14. positive regulation of cell cycle Source: BHF-UCL
    15. positive regulation of cell proliferation Source: Ensembl
    16. positive regulation of dendritic cell chemotaxis Source: Ensembl
    17. positive regulation of DNA replication Source: Ensembl
    18. positive regulation of gene expression Source: UniProtKB
    19. positive regulation of phagocytosis Source: BHF-UCL
    20. positive regulation of substrate adhesion-dependent cell spreading Source: Ensembl
    21. protein export from nucleus Source: Ensembl
    22. protein localization to nucleus Source: UniProtKB
    23. protein stabilization Source: UniProtKB
    24. regulation of meiosis Source: MGI
    25. response to drug Source: Ensembl
    26. response to estradiol Source: Ensembl
    27. response to testosterone Source: Ensembl
    28. spermatogenesis Source: Ensembl

    Keywords - Molecular functioni

    Chaperone

    Keywords - Ligandi

    Calcium, Lectin, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_196581. Scavenging by Class A Receptors.
    REACT_196603. Scavenging by Class F Receptors.
    REACT_197102. ER-Phagosome pathway.
    REACT_198616. Calnexin/calreticulin cycle.
    REACT_199105. ER-Phagosome pathway.
    REACT_32838. ATF6-alpha activates chaperone genes.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Calreticulin
    Alternative name(s):
    CRP55
    Calregulin
    Endoplasmic reticulum resident protein 60
    Short name:
    ERp60
    HACBP
    Gene namesi
    Name:Calr
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 8

    Organism-specific databases

    MGIiMGI:88252. Calr.

    Subcellular locationi

    Endoplasmic reticulum lumen 1 PublicationPROSITE-ProRule annotation. Cytoplasmic granule 1 Publication. Sarcoplasmic reticulum lumen By similarity
    Note: Associated with the lytic granules in the cytolytic T-lymphocytes.

    GO - Cellular componenti

    1. acrosomal vesicle Source: Ensembl
    2. cytosol Source: Ensembl
    3. endoplasmic reticulum Source: MGI
    4. endoplasmic reticulum lumen Source: MGI
    5. external side of plasma membrane Source: MGI
    6. extracellular matrix Source: Ensembl
    7. extracellular region Source: Reactome
    8. extracellular space Source: MGI
    9. Golgi apparatus Source: Ensembl
    10. MHC class I peptide loading complex Source: BHF-UCL
    11. nucleus Source: Ensembl
    12. perinuclear region of cytoplasm Source: Ensembl
    13. phagocytic vesicle Source: Reactome
    14. polysome Source: BHF-UCL
    15. sarcoplasmic reticulum lumen Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Endoplasmic reticulum, Sarcoplasmic reticulum

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 17172 PublicationsAdd
    BLAST
    Chaini18 – 416399CalreticulinPRO_0000004174Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei48 – 481N6-acetyllysineBy similarity
    Disulfide bondi105 ↔ 1372 Publications
    Modified residuei159 – 1591N6-acetyllysineBy similarity
    Modified residuei209 – 2091N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Disulfide bond

    Proteomic databases

    MaxQBiP14211.
    PaxDbiP14211.
    PRIDEiP14211.

    2D gel databases

    COMPLUYEAST-2DPAGEP14211.
    REPRODUCTION-2DPAGEIPI00123639.
    P14211.
    SWISS-2DPAGEP14211.

    PTM databases

    PhosphoSiteiP14211.

    Expressioni

    Gene expression databases

    ArrayExpressiP14211.
    BgeeiP14211.
    CleanExiMM_CALR.
    GenevestigatoriP14211.

    Interactioni

    Subunit structurei

    Monomer. Interacts with GABARAP, NR3C1, PDIA3/ERp57 and TRIM21 By similarity. Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5. Interacts with PPIB.By similarity4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AppP120234EBI-644340,EBI-78814
    NcstnP577162EBI-644340,EBI-998934
    Psen1P497693EBI-644340,EBI-990067

    Protein-protein interaction databases

    BioGridi198458. 5 interactions.
    IntActiP14211. 14 interactions.
    MINTiMINT-1679870.

    Structurei

    Secondary structure

    1
    416
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi21 – 255
    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 – 1379
    Turni138 – 1403
    Beta strandi141 – 15010
    Beta strandi153 – 1564
    Beta strandi166 – 17611
    Beta strandi180 – 1867
    Beta strandi189 – 1957
    Helixi196 – 1994
    Beta strandi206 – 2094
    Beta strandi293 – 2953
    Turni303 – 3064
    Beta strandi311 – 32212
    Beta strandi326 – 3349
    Helixi336 – 34510
    Helixi347 – 36014

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3O0VX-ray2.30A18-206[»]
    A301-368[»]
    3O0WX-ray1.95A18-206[»]
    A301-368[»]
    3O0XX-ray2.01A/B18-206[»]
    A/B301-368[»]
    3RG0X-ray2.57A18-238[»]
    A273-368[»]
    ProteinModelPortaliP14211.
    SMRiP14211. Positions 18-367.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ3TVD2.

    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 PPIBAdd
    BLAST
    Regioni259 – 297393 X approximate repeatsAdd
    BLAST
    Regioni309 – 416108C-domainAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi413 – 4164Prevents secretion from ER

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi351 – 40757Asp/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 By similarity.By similarity
    The interaction with glycans occurs through a binding site in the globular lectin domain.By similarity
    The zinc binding sites are localized to the N-domain.By similarity
    Associates with PDIA3 through the tip of the extended arm formed by the P-domain.By similarity

    Sequence similaritiesi

    Belongs to the calreticulin family.Curated

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG305105.
    GeneTreeiENSGT00430000030841.
    HOGENOMiHOG000192435.
    HOVERGENiHBG005407.
    InParanoidiP14211.
    KOiK08057.
    OMAiPEDWEDE.
    OrthoDBiEOG77126Z.
    PhylomeDBiP14211.
    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. 2 hits.
    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.

    P14211-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLLSVPLLLG LLGLAAADPA IYFKEQFLDG DAWTNRWVES KHKSDFGKFV    50
    LSSGKFYGDL EKDKGLQTSQ DARFYALSAK FEPFSNKGQT LVVQFTVKHE 100
    QNIDCGGGYV KLFPSGLDQK DMHGDSEYNI MFGPDICGPG TKKVHVIFNY 150
    KGKNVLINKD IRCKDDEFTH LYTLIVRPDN TYEVKIDNSQ VESGSLEDDW 200
    DFLPPKKIKD PDAAKPEDWD ERAKIDDPTD SKPEDWDKPE HIPDPDAKKP 250
    EDWDEEMDGE WEPPVIQNPE YKGEWKPRQI DNPDYKGTWI HPEIDNPEYS 300
    PDANIYAYDS FAVLGLDLWQ VKSGTIFDNF LITNDEAYAE EFGNETWGVT 350
    KAAEKQMKDK QDEEQRLKEE EEDKKRKEEE EAEDKEDDDD RDEDEDEEDE 400
    KEEDEEESPG QAKDEL 416
    Length:416
    Mass (Da):47,995
    Last modified:January 1, 1990 - v1
    Checksum:i24C03B00913408D8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti272 – 2721K → R in BAE35687. (PubMed:16141072)Curated
    Sequence conflicti407 – 4071E → Q in BAE35687. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14926 mRNA. Translation: CAA33053.1.
    M92988 mRNA. Translation: AAA37569.1.
    AK075605 mRNA. Translation: BAC35852.1.
    AK160197 mRNA. Translation: BAE35687.1.
    BC003453 mRNA. Translation: AAH03453.1.
    CCDSiCCDS22479.1.
    PIRiS06763.
    RefSeqiNP_031617.1. NM_007591.3.
    UniGeneiMm.1971.
    Mm.467043.

    Genome annotation databases

    EnsembliENSMUST00000003912; ENSMUSP00000003912; ENSMUSG00000003814.
    GeneIDi12317.
    KEGGimmu:12317.
    UCSCiuc009mnp.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14926 mRNA. Translation: CAA33053.1 .
    M92988 mRNA. Translation: AAA37569.1 .
    AK075605 mRNA. Translation: BAC35852.1 .
    AK160197 mRNA. Translation: BAE35687.1 .
    BC003453 mRNA. Translation: AAH03453.1 .
    CCDSi CCDS22479.1.
    PIRi S06763.
    RefSeqi NP_031617.1. NM_007591.3.
    UniGenei Mm.1971.
    Mm.467043.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3O0V X-ray 2.30 A 18-206 [» ]
    A 301-368 [» ]
    3O0W X-ray 1.95 A 18-206 [» ]
    A 301-368 [» ]
    3O0X X-ray 2.01 A/B 18-206 [» ]
    A/B 301-368 [» ]
    3RG0 X-ray 2.57 A 18-238 [» ]
    A 273-368 [» ]
    ProteinModelPortali P14211.
    SMRi P14211. Positions 18-367.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198458. 5 interactions.
    IntActi P14211. 14 interactions.
    MINTi MINT-1679870.

    PTM databases

    PhosphoSitei P14211.

    2D gel databases

    COMPLUYEAST-2DPAGE P14211.
    REPRODUCTION-2DPAGE IPI00123639.
    P14211.
    SWISS-2DPAGE P14211.

    Proteomic databases

    MaxQBi P14211.
    PaxDbi P14211.
    PRIDEi P14211.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000003912 ; ENSMUSP00000003912 ; ENSMUSG00000003814 .
    GeneIDi 12317.
    KEGGi mmu:12317.
    UCSCi uc009mnp.1. mouse.

    Organism-specific databases

    CTDi 811.
    MGIi MGI:88252. Calr.

    Phylogenomic databases

    eggNOGi NOG305105.
    GeneTreei ENSGT00430000030841.
    HOGENOMi HOG000192435.
    HOVERGENi HBG005407.
    InParanoidi P14211.
    KOi K08057.
    OMAi PEDWEDE.
    OrthoDBi EOG77126Z.
    PhylomeDBi P14211.
    TreeFami TF338438.

    Enzyme and pathway databases

    Reactomei REACT_196581. Scavenging by Class A Receptors.
    REACT_196603. Scavenging by Class F Receptors.
    REACT_197102. ER-Phagosome pathway.
    REACT_198616. Calnexin/calreticulin cycle.
    REACT_199105. ER-Phagosome pathway.
    REACT_32838. ATF6-alpha activates chaperone genes.

    Miscellaneous databases

    ChiTaRSi CALR. mouse.
    EvolutionaryTracei Q3TVD2.
    NextBioi 280884.
    PROi P14211.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P14211.
    Bgeei P14211.
    CleanExi MM_CALR.
    Genevestigatori P14211.

    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. 2 hits.
    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. "Multiple zones in the sequence of calreticulin (CRP55, calregulin, HACBP), a major calcium binding ER/SR protein."
      Smith M.J., Koch G.L.E.
      EMBO J. 8:3581-3586(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 18-48 AND 129-161.
      Strain: BALB/c.
      Tissue: Liver.
    2. "Determination of the sequence of an expressible cDNA clone encoding ERp60/calregulin by the use of a novel nested set method."
      Mazzarella R.A., Gold P., Cunningham M., Green M.
      Gene 120:217-225(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Brain and Liver.
    4. "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].
      Strain: FVB/N-3.
      Tissue: Mammary gland.
    5. "Separation and sequencing of familiar and novel murine proteins using preparative two-dimensional gel electrophoresis."
      Merrick B.A., Patterson R.M., Wichter L.L., He C., Selkirk J.K.
      Electrophoresis 15:735-745(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 18-38.
      Tissue: Fibroblast.
    6. Lubec G., Kang S.U., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 25-36; 56-64; 74-151; 154-159; 163-222; 225-272; 323-351; 341-357 AND 392-413, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6 and OF1.
      Tissue: Brain and Hippocampus.
    7. "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: SUBCELLULAR LOCATION.
    8. "Age-specific CUGBP1-eIF2 complex increases translation of CCAAT/enhancer-binding protein beta in old liver."
      Timchenko L.T., Salisbury E., Wang G.-L., Nguyen H., Albrecht J.H., Hershey J.W., Timchenko N.A.
      J. Biol. Chem. 281:32806-32819(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN AN EIF2 COMPLEX WITH EIF2S1; EIF2S2; CELF1; CALR3; HSPA5 AND HSP90B1.
    9. Cited for: INTERACTION WITH PPIB.
    10. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-209, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    11. Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 18-368 IN COMPLEX WITH CALCIUM AND TETRASACCHARIDE, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, DISULFIDE BOND.
    12. "Structural and functional relationships between the lectin and arm domains of calreticulin."
      Pocanschi C.L., Kozlov G., Brockmeier U., Brockmeier A., Williams D.B., Gehring K.
      J. Biol. Chem. 286:27266-27277(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.57 ANGSTROMS) OF 18-368 IN COMPLEX WITH CALCIUM IONS, FUNCTION, DISULFIDE BOND.

    Entry informationi

    Entry nameiCALR_MOUSE
    AccessioniPrimary (citable) accession number: P14211
    Secondary accession number(s): Q3TVD2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: January 1, 1990
    Last modified: October 1, 2014
    This is version 160 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

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

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3