CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021360
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 CUE domain-containing protein 2 
Protein Synonyms/Alias
  
Gene Name
 CUEDC2 
Gene Synonyms/Alias
 C10orf66; HOYS6 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
82TIGDMMQKLSGQLSDubiquitination[1, 2, 3, 4]
121LQRPEMLKEETRSSAubiquitination[5, 6]
186VQMLVEGKEEGPAAWubiquitination[2, 4, 5, 6, 7]
209RRLRGPQKDELKSFIubiquitination[2, 4, 6]
213GPQKDELKSFILQKYubiquitination[1, 2, 3, 4, 5, 6, 8]
219LKSFILQKYMMVDSAubiquitination[1, 2, 3, 4, 5, 6, 7, 8, 9, 10]
230VDSAEDQKIHRPMAPubiquitination[1, 2, 3, 4, 5]
256DNQVVSTKGERFKDVubiquitination[1, 2, 3, 4, 5, 6, 7, 9, 10, 11]
261STKGERFKDVRNPEAubiquitination[2]
272NPEAEEMKATYINLKubiquitination[1, 2, 3, 4, 5, 8]
279KATYINLKPARKYRFacetylation[12]
279KATYINLKPARKYRFubiquitination[1, 2, 3, 4, 5, 6, 8, 10]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [10] 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]
 [11] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [12] 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
 Down-regulates ESR1 protein levels through the ubiquitination-proteasome pathway, regardless of the presence of 17 beta-estradiol. Also involved in 17 beta-estradiol-induced ESR1 degradation. Controls PGR protein levels through a similar mechanism. 
Sequence Annotation
 DOMAIN 144 187 CUE.
 MOD_RES 110 110 Phosphoserine.  
Keyword
 Complete proteome; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation pathway. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 287 AA 
Protein Sequence
MELERIVSAA LLAFVQTHLP EADLSGLDEV IFSYVLGVLE DLGPSGPSEE NFDMEAFTEM 60
MEAYVPGFAH IPRGTIGDMM QKLSGQLSDA RNKENLQPQS SGVQGQVPIS PEPLQRPEML 120
KEETRSSAAA AADTQDEATG AEEELLPGVD VLLEVFPTCS VEQAQWVLAK ARGDLEEAVQ 180
MLVEGKEEGP AAWEGPNQDL PRRLRGPQKD ELKSFILQKY MMVDSAEDQK IHRPMAPKEA 240
PKKLIRYIDN QVVSTKGERF KDVRNPEAEE MKATYINLKP ARKYRFH 287 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005634; C:nucleus; IDA:HPA. 
Interpro
 IPR003892; CUE. 
Pfam
 PF02845; CUE 
SMART
  
PROSITE
 PS51140; CUE 
PRINTS