CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-030798
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Calnexin 
Protein Synonyms/Alias
 cDNA FLJ55574, highly similar to Calnexin 
Gene Name
 CANX 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
96SSPKVTYKAPVPTGEubiquitination[1]
122LSGWILSKAKKDDTDubiquitination[2, 3, 4]
138EIAKYDGKWEVEEMKubiquitination[1, 2, 4]
153ESKLPGDKGLVLMSRubiquitination[2, 4, 5, 6]
172AISAKLNKPFLFDTKubiquitination[2, 4, 5]
205AYVKLLSKTPELNLDubiquitination[2, 4, 5, 6]
217NLDQFHDKTPYTIMFubiquitination[2, 4, 6]
234DKCGEDYKLHFIFRHubiquitination[6]
262KRPDADLKTYFTDKKubiquitination[1, 2, 3, 4, 6]
268LKTYFTDKKTHLYTLubiquitination[1, 6]
269KTYFTDKKTHLYTLIubiquitination[6]
415VIDNPNYKGKWKPPMubiquitination[3, 6]
417DNPNYKGKWKPPMIDubiquitination[6]
433PSYQGIWKPRKIPNPubiquitination[1, 2, 4, 6, 7]
436QGIWKPRKIPNPDFFubiquitination[1, 2, 4, 6, 8, 9]
493ANDGWGLKKAADGAAubiquitination[1, 3, 6, 7, 9]
494NDGWGLKKAADGAAEubiquitination[6]
550QTSGMEYKKTDAPQPubiquitination[2, 4]
551TSGMEYKKTDAPQPDubiquitination[1]
560DAPQPDVKEEEEEKEubiquitination[1]
566VKEEEEEKEEEKDKGacetylation[10]
572EKEEEKDKGDEEEEGubiquitination[1]
582EEEEGEEKLEEKQKSubiquitination[1, 7]
Reference
 [1] 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]
 [2] 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]
 [3] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [8] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [9] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [10] 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
Functional Description
  
Sequence Annotation
  
Keyword
 Chaperone; Complete proteome; Endoplasmic reticulum; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 627 AA 
Protein Sequence
MADRRTPTPF AGCRLPRQRR ARDASQVSAP GTRRIMEGKW LLCMLLVLGT AIVEAHDGHD 60
DDVIDIEDDL DDVIEEVEDS KPDTTAPPSS PKVTYKAPVP TGEVYFADSF DRGTLSGWIL 120
SKAKKDDTDD EIAKYDGKWE VEEMKESKLP GDKGLVLMSR AKHHAISAKL NKPFLFDTKP 180
LIVQYEVNFQ NGIECGGAYV KLLSKTPELN LDQFHDKTPY TIMFGPDKCG EDYKLHFIFR 240
HKNPKTGIYE EKHAKRPDAD LKTYFTDKKT HLYTLILNPD NSFEILVDQS VVNSGNLLND 300
MTPPVNPSRE IEDPEDRKPE DWDERPKIPD PEAVKPDDWD EDAPAKIPDE EATKPEGWLD 360
DEPEYVPDPD AEKPEDWDED MDGEWEAPQI ANPRCESAPG CGVWQRPVID NPNYKGKWKP 420
PMIDNPSYQG IWKPRKIPNP DFFEDLEPFR MTPFSAIGLE LWSMTSDIFF DNFIICADRR 480
IVDDWANDGW GLKKAADGAA EPGVVGQMIE AAEERPWLWV VYILTVALPV FLVILFCCSG 540
KKQTSGMEYK KTDAPQPDVK EEEEEKEEEK DKGDEEEEGE EKLEEKQKSD AEEDGGTVSQ 600
EEEDRKPKAE EDEILNRSPR NRKPRRE 627 
Gene Ontology
 GO:0005783; C:endoplasmic reticulum; IDA:HPA.
 GO:0005509; F:calcium ion binding; IEA:InterPro.
 GO:0006457; P:protein folding; IEA:InterPro. 
Interpro
 IPR001580; Calret/calnex.
 IPR018124; Calret/calnex_CS.
 IPR009033; Calreticulin/calnexin_P_dom.
 IPR008985; ConA-like_lec_gl_sf.
 IPR013320; ConA-like_subgrp. 
Pfam
 PF00262; Calreticulin 
SMART
  
PROSITE
 PS00803; CALRETICULIN_1
 PS00804; CALRETICULIN_2
 PS00805; CALRETICULIN_REPEAT 
PRINTS
 PR00626; CALRETICULIN.