P27797 (CALR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Calreticulin

Alternative name(s):
CRP55
Calregulin
Endoplasmic reticulum resident protein 60
Short name=ERp60
HACBP
grp60

Gene names

Name:	CALR
Synonyms:	CRTC

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	417 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the 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. Ref.20 Ref.23
Subunit structure	Monomer. Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5. Interacts with PDIA3/ERp57 By similarity. Interacts with NR3C1 and TRIM21. Interacts with GABARAP. Ref.21 Ref.23 Ref.28
Subcellular location	Endoplasmic reticulum lumen. Cytoplasm › cytosol. Secreted › extracellular space › extracellular matrix. Cell surface. Note: Also found in cell surface (T cells), cytosol and extracellular matrix. Associated with the lytic granules in the cytolytic T-lymphocytes. Ref.18 Ref.22 Ref.23
Domain	Can be divided into a N-terminal globular domain, a proline-rich P-domain forming an elongated arm-like structure and a C-terminal acidic domain. The P-domain binds one molecule of calcium with high affinity, whereas the acidic C-domain binds multiple calcium ions with low affinity. The interaction with glycans occurs through a binding site in the globular lectin domain. The zinc binding sites are localized to the N-domain. Associates with PDIA3 through the tip of the extended arm formed by the P-domain.
Sequence similarities	Belongs to the calreticulin family.
Caution	Was originally (Ref.1) thought to be the 52 kDa Ro autoantigen.
Mass spectrometry	Molecular mass is 46879 Da from positions 18 - 417. Determined by MALDI. Ref.23

Ontologies

Keywords
Cellular component	Cytoplasm Endoplasmic reticulum Extracellular matrix Secreted
Domain	Repeat Signal
Ligand	Calcium Lectin Metal-binding Zinc
Molecular function	Chaperone
PTM	Acetylation Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	cell cycle arrest Inferred from genetic interaction. Source: BHF-UCL cellular senescence Inferred from genetic interaction. Source: BHF-UCL glucocorticoid receptor signaling pathway Traceable author statement. Source: BHF-UCL negative regulation of intracellular steroid hormone receptor signaling pathway Inferred from direct assay. Source: BHF-UCL negative regulation of neuron differentiation Inferred from direct assay. Source: BHF-UCL negative regulation of retinoic acid receptor signaling pathway Inferred from direct assay. Source: BHF-UCL negative regulation of transcription from RNA polymerase II promoter Inferred from direct assay. Source: BHF-UCL negative regulation of translation Inferred from sequence or structural similarity. Source: BHF-UCL peptide antigen assembly with MHC class I protein complex Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of DNA replication Inferred from genetic interaction. Source: BHF-UCL positive regulation of cell cycle Inferred from genetic interaction. Source: BHF-UCL positive regulation of cell proliferation Inferred from genetic interaction. Source: BHF-UCL positive regulation of phagocytosis Inferred from sequence or structural similarity. Source: BHF-UCL post-translational protein modification Traceable author statement. Source: Reactome protein N-linked glycosylation via asparagine Traceable author statement. Source: Reactome protein export from nucleus Inferred from direct assay Ref.23. Source: UniProtKB protein localization to nucleus Inferred from direct assay. Source: UniProtKB protein maturation by protein folding Traceable author statement. Source: BHF-UCL protein stabilization Inferred from sequence or structural similarity. Source: UniProtKB regulation of apoptotic process Traceable author statement. Source: UniProtKB sequestering of calcium ion Traceable author statement. Source: BHF-UCL
Cellular component	MHC class I peptide loading complex Inferred from sequence or structural similarity. Source: BHF-UCL cytosol Inferred from direct assay Ref.23. Source: UniProtKB endoplasmic reticulum lumen Inferred from direct assay Ref.23. Source: UniProtKB extracellular space Inferred from direct assay. Source: BHF-UCL integral to lumenal side of endoplasmic reticulum membrane Traceable author statement. Source: Reactome nucleus Inferred from direct assay. Source: BHF-UCL perinuclear region of cytoplasm Inferred from direct assay Ref.13. Source: BHF-UCL polysome Inferred from sequence or structural similarity. Source: BHF-UCL proteinaceous extracellular matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	DNA binding Non-traceable author statement Ref.23. Source: UniProtKB androgen receptor binding Inferred from direct assay. Source: BHF-UCL calcium ion binding Inferred from sequence or structural similarity. Source: UniProtKB chaperone binding Traceable author statement. Source: BHF-UCL complement component C1q binding Traceable author statement. Source: BHF-UCL integrin binding Inferred from physical interaction Ref.13. Source: BHF-UCL mRNA binding Inferred from direct assay. Source: BHF-UCL protein binding involved in protein folding Traceable author statement. Source: BHF-UCL sugar binding Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin protein ligase binding Inferred from physical interaction Ref.21. Source: UniProtKB unfolded protein binding Traceable author statement. Source: BHF-UCL zinc ion binding Traceable author statement. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TAP1	Q03518	2	EBI-1049597,EBI-747259

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 17

17

Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.18 Ref.19

Chain

18 – 417

400

Calreticulin

PRO_0000004173

Regions

Repeat

191 – 202

12

1-1

Repeat

210 – 221

12

1-2

Repeat

227 – 238

12

1-3

Repeat

244 – 255

12

1-4

Repeat

259 – 269

11

2-1

Repeat

273 – 283

11

2-2

Repeat

287 – 297

11

2-3

Region

18 – 197

180

N-domain

Region

191 – 255

65

4 X approximate repeats

Region

198 – 308

111

P-domain

Region

259 – 297

39

3 X approximate repeats

Region

309 – 417

109

C-domain

Motif

414 – 417

4

Prevents secretion from ER

Compositional bias

351 – 408

58

Asp/Glu/Lys-rich

Sites

Metal binding

26

1

Calcium; via carbonyl oxygen

Metal binding

62

1

Calcium; via carbonyl oxygen

Metal binding

64

1

Calcium; via carbonyl oxygen

Metal binding

328

1

Calcium

Amino acid modifications

Modified residue

48

1

N6-acetyllysine Ref.26

Modified residue

159

1

N6-acetyllysine Ref.26

Modified residue

209

1

N6-acetyllysine Ref.26

Glycosylation

344

1

N-linked (GlcNAc...) Ref.25

Disulfide bond

105 ↔ 137

Ref.24 Ref.29

Secondary structure

1

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417

Helix Strand Turn

Details...

Beta strand

20 – 25

6

Turn

34 – 36

3

Beta strand

37 – 39

3

Beta strand

42 – 44

3

Turn

60 – 63

4

Beta strand

70 – 84

15

Beta strand

91 – 98

8

Beta strand

110 – 112

3

Helix

119 – 121

3

Beta strand

129 – 132

4

Beta strand

147 – 149

3

Beta strand

154 – 156

3

Beta strand

166 – 176

11

Beta strand

182 – 186

5

Beta strand

189 – 192

4

Helix

196 – 199

4

Beta strand

316 – 321

6

Beta strand

326 – 334

9

Helix

336 – 341

6

Helix

351 – 366

16

Sequences

	Sequence		Length	Mass (Da)
	P27797 [UniParc]. Last modified August 1, 1992. Version 1. Checksum: BC37C3C0F1054FB2	FASTA	417	48,142
	10 20 30 40 50 60 MLLSVPLLLG LLGLAVAEPA VYFKEQFLDG DGWTSRWIES KHKSDFGKFV LSSGKFYGDE 70 80 90 100 110 120 EKDKGLQTSQ DARFYALSAS FEPFSNKGQT LVVQFTVKHE QNIDCGGGYV KLFPNSLDQT 130 140 150 160 170 180 DMHGDSEYNI MFGPDICGPG TKKVHVIFNY KGKNVLINKD IRCKDDEFTH LYTLIVRPDN 190 200 210 220 230 240 TYEVKIDNSQ VESGSLEDDW DFLPPKKIKD PDASKPEDWD ERAKIDDPTD SKPEDWDKPE 250 260 270 280 290 300 HIPDPDAKKP EDWDEEMDGE WEPPVIQNPE YKGEWKPRQI DNPDYKGTWI HPEIDNPEYS 310 320 330 340 350 360 PDPSIYAYDN FGVLGLDLWQ VKSGTIFDNF LITNDEAYAE EFGNETWGVT KAAEKQMKDK 370 380 390 400 410 QDEEQRLKEE EEDKKRKEEE EAEDKEDDED KDEDEEDEED KEEDEEEDVP GQAKDEL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning, expression, and chromosome 19 localization of a human Ro/SS-A autoantigen." McCauliffe D.P., Lux F.A., Lieu T.S., Sanz I., Hanke J., Newkirk M.M., Bachinski L.L., Itoh Y., Siciliano M.J., Reichlin M., Sontheimer R.D., Capra J.D. J. Clin. Invest. 85:1379-1391(1990) [PubMed: 2332496] [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: 1919005] [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: 1733953] [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: 19054851] [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: 15057824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [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: 7841019] [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: 3260607] [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: 1911778] [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: 2400400] [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: 1286669] [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, 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: 1286667] [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: 8418194] [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: 9150948] [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: 7876246] [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: 8666824] [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: 10358038] [Abstract] Cited for: SUBCELLULAR LOCATION.
[23]	"Calreticulin is a receptor for nuclear export." Holaska J.M., Black B.E., Love D.C., Hanover J.A., Leszyk J., Paschal B.M. J. Cell Biol. 152:127-140(2001) [PubMed: 11149926] [Abstract] Cited for: FUNCTION, INTERACTION WITH NR3C1, SUBCELLULAR LOCATION, MASS SPECTROMETRY.
[24]	"Human placental calreticulin characterization of domain structure and post-translational modifications." Hoejrup P., Roepstorff P., Houen G. Eur. J. Biochem. 268:2558-2565(2001) [PubMed: 11322874] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, MASS SPECTROMETRY, DISULFIDE BOND. 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: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-344, MASS SPECTROMETRY. 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., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-48; LYS-159 AND LYS-209, MASS SPECTROMETRY.
[27]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]	"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: 19154346] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 195-205 IN COMPLEX WITH GABARAP, INTERACTION WITH GABARAP.
[29]	"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: 21423620] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 18-368 IN COMPLEX WITH CALCIUM IONS, DISULFIDE BOND.
+	Additional computationally mapped references.

Web resources

Wikipedia

Calreticulin entry

Functional Glycomics Gateway - Glycan Binding

Calreticulin

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M32294 mRNA. Translation: AAA36582.1.
M84739 mRNA. Translation: AAA51916.1.
AY047586 mRNA. Translation: AAL13126.1.
AB451408 mRNA. Translation: BAG70222.1.
BT007448 mRNA. Translation: AAP36116.1.
CR457070 mRNA. Translation: CAG33351.1.
AD000092 Genomic DNA. Translation: AAB51176.1.
CH471106 Genomic DNA. Translation: EAW84331.1.
BC002500 mRNA. Translation: AAH02500.1.
BC007911 mRNA. Translation: AAH07911.1.
BC020493 mRNA. Translation: AAH20493.1.

IPI

IPI00020599.

PIR

A37047. A42330.

RefSeq

NP_004334.1. NM_004343.3.

UniGene

Hs.515162.

3D structure databases

PDBe
RCSB PDB
PDBj

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	18-368	[»]
3POW	X-ray	1.55	A	18-368	[»]

ProteinModelPortal

P27797.

SMR

P27797. Positions 18-367.

DisProt

DP00333.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-104N.

IntAct

P27797. 12 interactions.

MINT

MINT-101756.

STRING

P27797.

PTM databases

PhosphoSite

P27797.

Polymorphism databases

DMDM

117501.

2D gel databases

SWISS-2DPAGE

P27797.

Aarhus/Ghent-2DPAGE

9401. IEF.

DOSAC-COBS-2DPAGE

P27797.

OGP

P27797.

PHCI-2DPAGE

P27797.

PMMA-2DPAGE

P27797.

REPRODUCTION-2DPAGE

IPI00020599.

Siena-2DPAGE

P27797.

UCD-2DPAGE

P27797.

Proteomic databases

PRIDE

P27797.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000316448; ENSP00000320866; ENSG00000179218.

GeneID

811.

KEGG

hsa:811.

UCSC

uc002mvu.1. human.

Organism-specific databases

CTD

811.

GeneCards

GC19P013049.

H-InvDB

HIX0014813.

HGNC

HGNC:1455. CALR.

HPA

CAB001513.
CAB019952.
HPA002242.

MIM

109091. gene.

neXtProt

NX_P27797.

PharmGKB

PA26046.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG13293.

HOGENOM

HBG444251.

HOVERGEN

HBG005407.

InParanoid

P27797.

OMA

DSNIYAY.

OrthoDB

EOG41JZCD.

PhylomeDB

P27797.

Enzyme and pathway databases

Reactome

REACT_15380. Diabetes pathways.
REACT_17015. Metabolism of proteins.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P27797.

Bgee

P27797.

CleanEx

HS_CALR.

Genevestigator

P27797.

GermOnline

ENSG00000179218. Homo sapiens.

Family and domain databases

InterPro

IPR001580. Calret/calnex.
IPR018124. Calret/calnex_CS.
IPR009169. Calreticulin.
IPR008985. ConA-like_lec_gl.
IPR013320. ConA-like_subgrp.
[Graphical view]

Gene3D

G3DSA:2.60.120.200. ConA_like_subgrp. 2 hits.

KO

K08057.

PANTHER

PTHR11073. Calret/calnex. 1 hit.

Pfam

PF00262. Calreticulin. 1 hit.
[Graphical view]

PIRSF

PIRSF002356. Calreticulin. 1 hit.

PRINTS

PR00626. CALRETICULIN.

SUPFAM

SSF49899. ConA_like_lec_gl. 2 hits.

PROSITE

PS00803. CALRETICULIN_1. 1 hit.
PS00804. CALRETICULIN_2. 1 hit.
PS00805. CALRETICULIN_REPEAT. 3 hits.
PS00014. ER_TARGET. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

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

NextBio

3292.

SOURCE

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Entry information

Entry name

CALR_HUMAN

Accession

Primary (citable) accession number: P27797
Secondary accession number(s): Q6IAT4, Q9UDG2

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	January 25, 2012
This is version 150 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.