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P27797

- CALR_HUMAN

UniProt

P27797 - CALR_HUMAN

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Protein

Calreticulin

Gene

CALR

Organism
Homo sapiens (Human)
Status
Reviewed - 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 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 involved in protein folding Source: BHF-UCL
  15. ubiquitin protein ligase binding Source: UniProtKB
  16. unfolded protein binding Source: BHF-UCL
  17. 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
Complete GO annotation...

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. focal adhesion Source: UniProtKB
  13. Golgi apparatus Source: Ensembl
  14. integral component of lumenal side of endoplasmic reticulum membrane Source: Reactome
  15. intracellular Source: UniProtKB
  16. membrane Source: UniProtKB
  17. MHC class I peptide loading complex Source: BHF-UCL
  18. nucleus Source: BHF-UCL
  19. perinuclear region of cytoplasm Source: BHF-UCL
  20. polysome Source: BHF-UCL
  21. proteinaceous extracellular matrix Source: UniProtKB-KW
  22. sarcoplasmic reticulum Source: UniProtKB-KW
Complete GO annotation...

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

BgeeiP27797.
CleanExiHS_CALR.
ExpressionAtlasiP27797. baseline and differential.
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. 85 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.
IPR013320. ConA-like_dom.
[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

        10         20         30         40         50
MLLSVPLLLG LLGLAVAEPA VYFKEQFLDG DGWTSRWIES KHKSDFGKFV
60 70 80 90 100
LSSGKFYGDE EKDKGLQTSQ DARFYALSAS FEPFSNKGQT LVVQFTVKHE
110 120 130 140 150
QNIDCGGGYV KLFPNSLDQT DMHGDSEYNI MFGPDICGPG TKKVHVIFNY
160 170 180 190 200
KGKNVLINKD IRCKDDEFTH LYTLIVRPDN TYEVKIDNSQ VESGSLEDDW
210 220 230 240 250
DFLPPKKIKD PDASKPEDWD ERAKIDDPTD SKPEDWDKPE HIPDPDAKKP
260 270 280 290 300
EDWDEEMDGE WEPPVIQNPE YKGEWKPRQI DNPDYKGTWI HPEIDNPEYS
310 320 330 340 350
PDPSIYAYDN FGVLGLDLWQ VKSGTIFDNF LITNDEAYAE EFGNETWGVT
360 370 380 390 400
KAAEKQMKDK QDEEQRLKEE EEDKKRKEEE EAEDKEDDED KDEDEEDEED
410
KEEDEEEDVP GQAKDEL
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. 85 interactions.
DIPi DIP-104N.
IntActi P27797. 28 interactions.
MINTi MINT-101756.
STRINGi 9606.ENSP00000320866.

Chemistry

DrugBanki DB00025. Antihemophilic Factor.
DB01065. Melatonin.
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

Bgeei P27797.
CleanExi HS_CALR.
ExpressionAtlasi P27797. baseline and differential.
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.
IPR013320. ConA-like_dom.
[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

« Hide 'large scale' publications
  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 29, 2014
This is version 180 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