CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012541
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Poly(rC)-binding protein 1 
Protein Synonyms/Alias
 Alpha-CP1; Heterogeneous nuclear ribonucleoprotein E1; hnRNP E1; Nucleic acid-binding protein SUB2.3 
Gene Name
 PCBP1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
23IRLLMHGKEVGSIIGubiquitination[1, 2, 3]
31EVGSIIGKKGESVKRubiquitination[1, 3]
32VGSIIGKKGESVKRIubiquitination[1]
115QCGSLIGKGGCKIKEubiquitination[1, 2, 3, 4, 5]
119LIGKGGCKIKEIRESubiquitination[3, 5]
237ISPLDLAKLNQVARQubiquitination[3, 4, 5, 6]
314QMSGAQIKIANPVEGubiquitination[1, 2, 3, 4, 5, 6, 7, 8, 9, 10]
351NARLSSEKGMGCS**acetylation[5]
351NARLSSEKGMGCS**ubiquitination[1, 2, 3, 4, 5, 6, 9]
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] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] 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
Functional Description
 Single-stranded nucleic acid binding protein that binds preferentially to oligo dC. 
Sequence Annotation
 DOMAIN 13 75 KH 1.
 DOMAIN 97 162 KH 2.
 DOMAIN 279 343 KH 3.
 MOD_RES 173 173 Phosphoserine.
 MOD_RES 190 190 Phosphoserine.  
Keyword
 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein; RNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 356 AA 
Protein Sequence
MDAGVTESGL NVTLTIRLLM HGKEVGSIIG KKGESVKRIR EESGARINIS EGNCPERIIT 60
LTGPTNAIFK AFAMIIDKLE EDINSSMTNS TAASRPPVTL RLVVPATQCG SLIGKGGCKI 120
KEIRESTGAQ VQVAGDMLPN STERAITIAG VPQSVTECVK QICLVMLETL SQSPQGRVMT 180
IPYQPMPASS PVICAGGQDR CSDAAGYPHA THDLEGPPLD AYSIQGQHTI SPLDLAKLNQ 240
VARQQSHFAM MHGGTGFAGI DSSSPEVKGY WASLDASTQT THELTIPNNL IGCIIGRQGA 300
NINEIRQMSG AQIKIANPVE GSSGRQVTIT GSAASISLAQ YLINARLSSE KGMGCS 356 
Gene Ontology
 GO:0005737; C:cytoplasm; NAS:UniProtKB.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0030529; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
 GO:0003723; F:RNA binding; IDA:UniProtKB.
 GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
 GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome. 
Interpro
 IPR004087; KH_dom.
 IPR004088; KH_dom_type_1. 
Pfam
 PF00013; KH_1 
SMART
 SM00322; KH 
PROSITE
 PS50084; KH_TYPE_1 
PRINTS