UniProt Accession

 CALR_HUMAN; P27797; Q6IAT4; Q9UDG2 

Genbank Protein ID

 M32294; M84739; AY047586; AB451408; BT007448; CR457070; AD000092; CH471106; BC002500; BC007911; BC020493 

Genbank Nucleotide ID

 AAA36582.1; AAA51916.1; AAL13126.1; BAG70222.1; AAP36116.1; CAG33351.1; AAB51176.1; EAW84331.1; AAH02500.1; AAH07911.1; AAH20493.1 

Protein Name

 Calreticulin 

Protein Synonyms/Alias

 CRP55; Calregulin; Endoplasmic reticulum resident protein 60; ERp60; HACBP; grp60 

Gene Name

 CALR 

Gene Synonyms/Alias

 CRTC 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
48	KHKSDFGKFVLSSGK	acetylation	[1, 2]
48	KHKSDFGKFVLSSGK	ubiquitination	[3, 4, 5, 6]
55	KFVLSSGKFYGDEEK	ubiquitination	[3, 4, 6, 7]
62	KFYGDEEKDKGLQTS	acetylation	[1]
64	YGDEEKDKGLQTSQD	acetylation	[1]
142	DICGPGTKKVHVIFN	ubiquitination	[5]
143	ICGPGTKKVHVIFNY	ubiquitination	[5, 7]
151	VHVIFNYKGKNVLIN	ubiquitination	[4, 5]
153	VIFNYKGKNVLINKD	acetylation	[1]
153	VIFNYKGKNVLINKD	ubiquitination	[3, 5, 6, 7]
159	GKNVLINKDIRCKDD	acetylation	[1, 2]
159	GKNVLINKDIRCKDD	ubiquitination	[3, 4, 5, 6, 7]
206	DWDFLPPKKIKDPDA	acetylation	[1]
206	DWDFLPPKKIKDPDA	ubiquitination	[7]
207	WDFLPPKKIKDPDAS	acetylation	[1]
207	WDFLPPKKIKDPDAS	ubiquitination	[5]
209	FLPPKKIKDPDASKP	acetylation	[1, 2]
209	FLPPKKIKDPDASKP	ubiquitination	[5]
238	SKPEDWDKPEHIPDP	acetylation	[1]

Reference

 [1] Autoacetylation of purified calreticulin transacetylase utilizing acetoxycoumarin as the acetyl group donor.
 Bansal S, Ponnan P, Raj HG, Weintraub ST, Chopra M, Kumari R, Saluja D, Kumar A, Tyagi TK, Singh P, Prasad AK, Saso L, Rastogi RC, Parmar VS.
 Appl Biochem Biotechnol. 2009 May;157(2):285-98. [PMID: 18795239]
 [2] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [5] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [6] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [7] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983] 

Functional Description

 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). 

Sequence Annotation

 REPEAT 191 202 1-1.
 REPEAT 210 221 1-2.
 REPEAT 227 238 1-3.
 REPEAT 244 255 1-4.
 REPEAT 259 269 2-1.
 REPEAT 273 283 2-2.
 REPEAT 287 297 2-3.
 REGION 18 197 N-domain.
 REGION 191 255 4 X approximate repeats.
 REGION 198 308 P-domain.
 REGION 259 297 3 X approximate repeats.
 REGION 309 417 C-domain.
 MOTIF 414 417 Prevents secretion from ER.
 METAL 26 26 Calcium; via carbonyl oxygen.
 METAL 62 62 Calcium; via carbonyl oxygen.
 METAL 64 64 Calcium; via carbonyl oxygen.
 METAL 328 328 Calcium.
 BINDING 109 109 Carbohydrate (By similarity).
 BINDING 111 111 Carbohydrate (By similarity).
 BINDING 128 128 Carbohydrate (By similarity).
 BINDING 135 135 Carbohydrate (By similarity).
 BINDING 317 317 Carbohydrate (By similarity).
 MOD_RES 48 48 N6-acetyllysine.
 MOD_RES 159 159 N6-acetyllysine.
 MOD_RES 209 209 N6-acetyllysine.
 CARBOHYD 344 344 N-linked (GlcNAc...).
 DISULFID 105 137  

Keyword

 3D-structure; Acetylation; Calcium; Chaperone; Complete proteome; Cytoplasm; Direct protein sequencing; Disulfide bond; Endoplasmic reticulum; Extracellular matrix; Glycoprotein; Lectin; Metal-binding; Reference proteome; Repeat; Sarcoplasmic reticulum; Secreted; Signal; Zinc. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 417 AA 

Protein Sequence

Gene Ontology

 GO:0001669; C:acrosomal vesicle; IEA:Compara.
 GO:0009986; C:cell surface; TAS:BHF-UCL.
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0005788; C:endoplasmic reticulum lumen; IDA:UniProtKB.
 GO:0009897; C:external side of plasma membrane; IEA:Compara.
 GO:0005615; C:extracellular space; IDA:BHF-UCL.
 GO:0005794; C:Golgi apparatus; IEA:Compara.
 GO:0071556; C:integral to lumenal side of endoplasmic reticulum membrane; TAS:Reactome.
 GO:0042824; C:MHC class I peptide loading complex; ISS:BHF-UCL.
 GO:0005634; C:nucleus; IDA:BHF-UCL.
 GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
 GO:0005844; C:polysome; ISS:BHF-UCL.
 GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell.
 GO:0033018; C:sarcoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
 GO:0050681; F:androgen receptor binding; IDA:BHF-UCL.
 GO:0005509; F:calcium ion binding; ISS:UniProtKB.
 GO:0030246; F:carbohydrate binding; TAS:BHF-UCL.
 GO:0051087; F:chaperone binding; TAS:BHF-UCL.
 GO:0001849; F:complement component C1q binding; TAS:BHF-UCL.
 GO:0003677; F:DNA binding; NAS:UniProtKB.
 GO:0042562; F:hormone binding; IEA:Compara.
 GO:0005506; F:iron ion binding; IEA:Compara.
 GO:0003729; F:mRNA binding; IDA:BHF-UCL.
 GO:0042277; F:peptide binding; IEA:Compara.
 GO:0044183; F:protein binding involved in protein folding; TAS:BHF-UCL.
 GO:0051082; F:unfolded protein binding; TAS:BHF-UCL.
 GO:0008270; F:zinc ion binding; TAS:BHF-UCL.
 GO:0006987; P:activation of signaling protein activity involved in unfolded protein response; TAS:Reactome.
 GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
 GO:0055007; P:cardiac muscle cell differentiation; IEA:Compara.
 GO:0007050; P:cell cycle arrest; IGI:BHF-UCL.
 GO:0071285; P:cellular response to lithium ion; IEA:Compara.
 GO:0090398; P:cellular senescence; IGI:BHF-UCL.
 GO:0030866; P:cortical actin cytoskeleton organization; IEA:Compara.
 GO:0042921; P:glucocorticoid receptor signaling pathway; TAS:BHF-UCL.
 GO:0033144; P:negative regulation of intracellular steroid hormone receptor signaling pathway; IDA:BHF-UCL.
 GO:0045665; P:negative regulation of neuron differentiation; IDA:BHF-UCL.
 GO:0048387; P:negative regulation of retinoic acid receptor signaling pathway; IDA:BHF-UCL.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
 GO:0017148; P:negative regulation of translation; ISS:BHF-UCL.
 GO:0002502; P:peptide antigen assembly with MHC class I protein complex; ISS:BHF-UCL.
 GO:0045787; P:positive regulation of cell cycle; IGI:BHF-UCL.
 GO:0008284; P:positive regulation of cell proliferation; IGI:BHF-UCL.
 GO:2000510; P:positive regulation of dendritic cell chemotaxis; IMP:UniProtKB.
 GO:0045740; P:positive regulation of DNA replication; IGI:BHF-UCL.
 GO:0010628; P:positive regulation of gene expression; IEA:Compara.
 GO:0050766; P:positive regulation of phagocytosis; ISS:BHF-UCL.
 GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IMP:UniProtKB.
 GO:0043687; P:post-translational protein modification; TAS:Reactome.
 GO:0006611; P:protein export from nucleus; IDA:UniProtKB.
 GO:0034504; P:protein localization to nucleus; IDA:UniProtKB.
 GO:0022417; P:protein maturation by protein folding; TAS:BHF-UCL.
 GO:0018279; P:protein N-linked glycosylation via asparagine; TAS:Reactome.
 GO:0050821; P:protein stabilization; ISS:UniProtKB.
 GO:0042981; P:regulation of apoptotic process; TAS:UniProtKB.
 GO:0040020; P:regulation of meiosis; IEA:Compara.
 GO:0042493; P:response to drug; IEA:Compara.
 GO:0032355; P:response to estradiol stimulus; IEA:Compara.
 GO:0033574; P:response to testosterone stimulus; IEA:Compara.
 GO:0051208; P:sequestering of calcium ion; TAS:BHF-UCL.
 GO:0007283; P:spermatogenesis; IEA:Compara. 

Interpro

 IPR001580; Calret/calnex.
 IPR018124; Calret/calnex_CS.
 IPR009169; Calreticulin.
 IPR008985; ConA-like_lec_gl_sf.
 IPR013320; ConA-like_subgrp. 

Pfam

 PF00262; Calreticulin 

SMART

  

PROSITE

 PS00803; CALRETICULIN_1
 PS00804; CALRETICULIN_2
 PS00805; CALRETICULIN_REPEAT
 PS00014; ER_TARGET 

PRINTS

 PR00626; CALRETICULIN.