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Protein

Calreticulin

Gene

Calr

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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. androgen receptor binding Source: MGI
  2. calcium ion binding Source: UniProtKB
  3. carbohydrate binding Source: UniProtKB
  4. glycoprotein binding Source: MGI
  5. hormone binding Source: Ensembl
  6. integrin binding Source: MGI
  7. iron ion binding Source: Ensembl
  8. mRNA binding Source: BHF-UCL
  9. peptide binding Source: Ensembl
  10. poly(A) RNA binding Source: MGI
  11. ubiquitin protein ligase binding Source: MGI

GO - Biological processi

  1. cardiac muscle cell differentiation Source: Ensembl
  2. cell cycle arrest Source: MGI
  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: MGI
  9. negative regulation of neuron differentiation Source: MGI
  10. negative regulation of retinoic acid receptor signaling pathway Source: MGI
  11. negative regulation of transcription, DNA-templated Source: MGI
  12. negative regulation of transcription from RNA polymerase II promoter Source: MGI
  13. negative regulation of translation Source: Ensembl
  14. peptide antigen assembly with MHC class I protein complex Source: BHF-UCL
  15. positive regulation of cell cycle Source: BHF-UCL
  16. positive regulation of cell proliferation Source: MGI
  17. positive regulation of dendritic cell chemotaxis Source: MGI
  18. positive regulation of DNA replication Source: MGI
  19. positive regulation of gene expression Source: UniProtKB
  20. positive regulation of phagocytosis Source: BHF-UCL
  21. positive regulation of substrate adhesion-dependent cell spreading Source: MGI
  22. protein export from nucleus Source: MGI
  23. protein localization to nucleus Source: UniProtKB
  24. protein stabilization Source: UniProtKB
  25. regulation of meiosis Source: MGI
  26. response to drug Source: Ensembl
  27. response to estradiol Source: Ensembl
  28. response to testosterone Source: Ensembl
  29. spermatogenesis Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

Calcium, Lectin, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_280759. Scavenging by Class F Receptors.
REACT_285184. Calnexin/calreticulin cycle.
REACT_308964. ER-Phagosome pathway.
REACT_339401. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
REACT_341075. ER-Phagosome pathway.
REACT_346699. Scavenging by Class A Receptors.

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 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:88252. Calr.

Subcellular locationi

Endoplasmic reticulum lumen PROSITE-ProRule annotation1 Publication. 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. cytoplasm Source: MGI
  3. cytosol Source: MGI
  4. endoplasmic reticulum Source: MGI
  5. endoplasmic reticulum lumen Source: MGI
  6. external side of plasma membrane Source: MGI
  7. extracellular matrix Source: Ensembl
  8. extracellular region Source: Reactome
  9. extracellular space Source: MGI
  10. extracellular vesicular exosome Source: MGI
  11. focal adhesion Source: MGI
  12. Golgi apparatus Source: Ensembl
  13. membrane Source: MGI
  14. MHC class I peptide loading complex Source: BHF-UCL
  15. nucleus Source: MGI
  16. perinuclear region of cytoplasm Source: MGI
  17. phagocytic vesicle Source: Reactome
  18. polysome Source: BHF-UCL
  19. sarcoplasmic reticulum lumen Source: UniProtKB-SubCell
  20. smooth endoplasmic reticulum Source: Ensembl
Complete GO annotation...

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

BgeeiP14211.
CleanExiMM_CALR.
ExpressionAtlasiP14211. baseline and differential.
GenevestigatoriP14211.

Interactioni

Subunit structurei

Monomer. Interacts with GABARAP, NR3C1, PDIA3/ERp57, C9orf9 homolog 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 similarity5 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi198458. 6 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 – 255Combined sources
Helixi30 – 356Combined sources
Beta strandi37 – 393Combined sources
Beta strandi42 – 443Combined sources
Beta strandi49 – 524Combined sources
Turni60 – 634Combined sources
Beta strandi65 – 684Combined sources
Beta strandi70 – 8415Combined sources
Beta strandi91 – 988Combined sources
Beta strandi104 – 1074Combined sources
Beta strandi110 – 1134Combined sources
Helixi119 – 1213Combined sources
Beta strandi129 – 1379Combined sources
Turni138 – 1403Combined sources
Beta strandi141 – 15010Combined sources
Beta strandi153 – 1564Combined sources
Beta strandi166 – 17611Combined sources
Beta strandi180 – 1867Combined sources
Beta strandi189 – 1957Combined sources
Helixi196 – 1994Combined sources
Beta strandi206 – 2094Combined sources
Beta strandi293 – 2953Combined sources
Turni303 – 3064Combined sources
Beta strandi311 – 32212Combined sources
Beta strandi326 – 3349Combined sources
Helixi336 – 34510Combined sources
Helixi347 – 36014Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

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.
OMAiDDFSNKG.
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.
IPR013320. ConA-like_dom.
[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

        10         20         30         40         50
MLLSVPLLLG LLGLAAADPA IYFKEQFLDG DAWTNRWVES KHKSDFGKFV
60 70 80 90 100
LSSGKFYGDL EKDKGLQTSQ DARFYALSAK FEPFSNKGQT LVVQFTVKHE
110 120 130 140 150
QNIDCGGGYV KLFPSGLDQK DMHGDSEYNI MFGPDICGPG TKKVHVIFNY
160 170 180 190 200
KGKNVLINKD IRCKDDEFTH LYTLIVRPDN TYEVKIDNSQ VESGSLEDDW
210 220 230 240 250
DFLPPKKIKD PDAAKPEDWD ERAKIDDPTD SKPEDWDKPE HIPDPDAKKP
260 270 280 290 300
EDWDEEMDGE WEPPVIQNPE YKGEWKPRQI DNPDYKGTWI HPEIDNPEYS
310 320 330 340 350
PDANIYAYDS FAVLGLDLWQ VKSGTIFDNF LITNDEAYAE EFGNETWGVT
360 370 380 390 400
KAAEKQMKDK QDEEQRLKEE EEDKKRKEEE EAEDKEDDDD RDEDEDEEDE
410
KEEDEEESPG QAKDEL
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi198458. 6 interactions.
IntActiP14211. 14 interactions.
MINTiMINT-1679870.

PTM databases

PhosphoSiteiP14211.

2D gel databases

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

Proteomic databases

MaxQBiP14211.
PaxDbiP14211.
PRIDEiP14211.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi811.
MGIiMGI:88252. Calr.

Phylogenomic databases

eggNOGiNOG305105.
GeneTreeiENSGT00430000030841.
HOGENOMiHOG000192435.
HOVERGENiHBG005407.
InParanoidiP14211.
KOiK08057.
OMAiDDFSNKG.
OrthoDBiEOG77126Z.
PhylomeDBiP14211.
TreeFamiTF338438.

Enzyme and pathway databases

ReactomeiREACT_280759. Scavenging by Class F Receptors.
REACT_285184. Calnexin/calreticulin cycle.
REACT_308964. ER-Phagosome pathway.
REACT_339401. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
REACT_341075. ER-Phagosome pathway.
REACT_346699. Scavenging by Class A Receptors.

Miscellaneous databases

ChiTaRSiCalr. mouse.
NextBioi280884.
PROiP14211.
SOURCEiSearch...

Gene expression databases

BgeeiP14211.
CleanExiMM_CALR.
ExpressionAtlasiP14211. baseline and differential.
GenevestigatoriP14211.

Family and domain databases

Gene3Di2.60.120.200. 2 hits.
InterProiIPR001580. Calret/calnex.
IPR018124. Calret/calnex_CS.
IPR009169. Calreticulin.
IPR009033. Calreticulin/calnexin_P_dom.
IPR013320. ConA-like_dom.
[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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1988) [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(1991) [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(2004) [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(2003) [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(1993) [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 (DEC-2008) 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(1992) [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(2005) [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. "A mouse protein that localizes to acrosome and sperm tail is regulated by Y-chromosome."
    Bhattacharya R., Devi M.S., Dhople V.M., Jesudasan R.A.
    BMC Cell Biol. 14:50-50(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH C9ORF9 HOMOLOG.
  11. "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(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-209, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  12. Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 18-368 IN COMPLEX WITH CALCIUM AND TETRASACCHARIDE, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, DISULFIDE BOND.
  13. "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(2010) [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: April 1, 2015
This is version 166 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.