CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004213
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Calreticulin 
Protein Synonyms/Alias
 CRP55; Calregulin; Endoplasmic reticulum resident protein 60; ERp60; HACBP 
Gene Name
 Calr 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
43RWVESKHKSDFGKFVacetylation[1]
48KHKSDFGKFVLSSGKacetylation[1, 2]
55KFVLSSGKFYGDLEKacetylation[1, 2]
55KFVLSSGKFYGDLEKsuccinylation[2]
55KFVLSSGKFYGDLEKubiquitination[3]
62KFYGDLEKDKGLQTSacetylation[1, 2, 4]
62KFYGDLEKDKGLQTSubiquitination[3]
64YGDLEKDKGLQTSQDacetylation[2]
64YGDLEKDKGLQTSQDsuccinylation[2]
80RFYALSAKFEPFSNKacetylation[1, 5]
80RFYALSAKFEPFSNKubiquitination[3]
98LVVQFTVKHEQNIDCacetylation[1]
111DCGGGYVKLFPSGLDacetylation[6]
143ICGPGTKKVHVIFNYacetylation[1]
151VHVIFNYKGKNVLINacetylation[4]
153VIFNYKGKNVLINKDacetylation[1, 2]
153VIFNYKGKNVLINKDsuccinylation[2]
159GKNVLINKDIRCKDDacetylation[1, 2]
164INKDIRCKDDEFTHLacetylation[7, 8]
207WDFLPPKKIKDPDAAacetylation[1]
209FLPPKKIKDPDAAKPacetylation[1, 2, 4, 7, 9]
209FLPPKKIKDPDAAKPsuccinylation[2]
215IKDPDAAKPEDWDERacetylation[4, 7]
232IDDPTDSKPEDWDKPacetylation[4, 7]
238SKPEDWDKPEHIPDPacetylation[2, 4]
248HIPDPDAKKPEDWDEacetylation[4]
360AEKQMKDKQDEEQRLacetylation[4, 7]
368QDEEQRLKEEEEDKKacetylation[7]
374LKEEEEDKKRKEEEEacetylation[4, 7]
Reference
 [1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [2] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [3] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [4] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [5] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [6] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
 [7] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [8] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [9] The fasted/fed mouse metabolic acetylome: N6-acetylation differences suggest acetylation coordinates organ-specific fuel switching.
 Yang L, Vaitheesvaran B, Hartil K, Robinson AJ, Hoopmann MR, Eng JK, Kurland IJ, Bruce JE.
 J Proteome Res. 2011 Sep 2;10(9):4134-49. [PMID: 21728379] 
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 309 416 C-domain.
 MOTIF 413 416 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.
 BINDING 111 111 Carbohydrate.
 BINDING 128 128 Carbohydrate.
 BINDING 135 135 Carbohydrate.
 BINDING 317 317 Carbohydrate.
 MOD_RES 48 48 N6-acetyllysine (By similarity).
 MOD_RES 159 159 N6-acetyllysine (By similarity).
 MOD_RES 209 209 N6-acetyllysine (By similarity).
 DISULFID 105 137  
Keyword
 3D-structure; Acetylation; Calcium; Chaperone; Complete proteome; Direct protein sequencing; Disulfide bond; Endoplasmic reticulum; Lectin; Metal-binding; Reference proteome; Repeat; Sarcoplasmic reticulum; Signal; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 416 AA 
Protein Sequence
MLLSVPLLLG LLGLAAADPA IYFKEQFLDG DAWTNRWVES KHKSDFGKFV LSSGKFYGDL 60
EKDKGLQTSQ DARFYALSAK FEPFSNKGQT LVVQFTVKHE QNIDCGGGYV KLFPSGLDQK 120
DMHGDSEYNI MFGPDICGPG TKKVHVIFNY KGKNVLINKD IRCKDDEFTH LYTLIVRPDN 180
TYEVKIDNSQ VESGSLEDDW DFLPPKKIKD PDAAKPEDWD ERAKIDDPTD SKPEDWDKPE 240
HIPDPDAKKP EDWDEEMDGE WEPPVIQNPE YKGEWKPRQI DNPDYKGTWI HPEIDNPEYS 300
PDANIYAYDS FAVLGLDLWQ VKSGTIFDNF LITNDEAYAE EFGNETWGVT KAAEKQMKDK 360
QDEEQRLKEE EEDKKRKEEE EAEDKEDDDD RDEDEDEEDE KEEDEEESPG QAKDEL 416 
Gene Ontology
 GO:0001669; C:acrosomal vesicle; IEA:Compara.
 GO:0005829; C:cytosol; IEA:Compara.
 GO:0009897; C:external side of plasma membrane; IDA:MGI.
 GO:0031012; C:extracellular matrix; IEA:Compara.
 GO:0005615; C:extracellular space; IDA:MGI.
 GO:0005794; C:Golgi apparatus; IEA:Compara.
 GO:0042824; C:MHC class I peptide loading complex; IMP:BHF-UCL.
 GO:0005634; C:nucleus; IEA:Compara.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:Compara.
 GO:0045335; C:phagocytic vesicle; TAS:Reactome.
 GO:0005844; C:polysome; IDA:BHF-UCL.
 GO:0033018; C:sarcoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
 GO:0005509; F:calcium ion binding; IDA:UniProtKB.
 GO:0030246; F:carbohydrate binding; IDA: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:0055007; P:cardiac muscle cell differentiation; IEA:Compara.
 GO:0007050; P:cell cycle arrest; IEA:Compara.
 GO:0071285; P:cellular response to lithium ion; IEA:Compara.
 GO:0071310; P:cellular response to organic substance; IEA:Compara.
 GO:0090398; P:cellular senescence; IMP:BHF-UCL.
 GO:0030866; P:cortical actin cytoskeleton organization; IDA:MGI.
 GO:0033144; P:negative regulation of intracellular steroid hormone receptor signaling pathway; IEA:Compara.
 GO:0045665; P:negative regulation of neuron differentiation; IEA:Compara.
 GO:0048387; P:negative regulation of retinoic acid receptor signaling pathway; IEA:Compara.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Compara.
 GO:0017148; P:negative regulation of translation; IEA:Compara.
 GO:0002502; P:peptide antigen assembly with MHC class I protein complex; IMP:BHF-UCL.
 GO:0045787; P:positive regulation of cell cycle; IMP:BHF-UCL.
 GO:0008284; P:positive regulation of cell proliferation; IEA:Compara.
 GO:2000510; P:positive regulation of dendritic cell chemotaxis; IEA:Compara.
 GO:0045740; P:positive regulation of DNA replication; IEA:Compara.
 GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
 GO:0050766; P:positive regulation of phagocytosis; IMP:BHF-UCL.
 GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IEA:Compara.
 GO:0006611; P:protein export from nucleus; IEA:Compara.
 GO:0006457; P:protein folding; IEA:InterPro.
 GO:0034504; P:protein localization to nucleus; IMP:UniProtKB.
 GO:0050821; P:protein stabilization; IDA:UniProtKB.
 GO:0040020; P:regulation of meiosis; IDA:MGI.
 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: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.