CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012019
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Heterogeneous nuclear ribonucleoprotein A0 
Protein Synonyms/Alias
 hnRNP A0 
Gene Name
 HNRNPA0 
Gene Synonyms/Alias
 HNRPA0 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
8MENSQLCKLFIGGLNubiquitination[1, 2]
45VVVNPQTKRSRCFGFubiquitination[1, 2, 3]
80DGNTVELKRAVSREDubiquitination[1, 2, 4, 5]
96ARPGAHAKVKKLFVGacetylation[6]
99GAHAKVKKLFVGGLKubiquitination[2, 6, 7, 8]
106KLFVGGLKGDVAEGDubiquitination[1, 2, 3]
126SQFGTVEKAEIIADKubiquitination[2]
133KAEIIADKQSGKKRGacetylation[6]
133KAEIIADKQSGKKRGubiquitination[1, 2, 3, 5, 6]
137IADKQSGKKRGFGFVubiquitination[1]
154QNHDAADKAAVVKFHubiquitination[1, 2, 6]
159ADKAAVVKFHPIQGHubiquitination[2, 6]
172GHRVEVKKAVPKEDIubiquitination[1, 2]
176EVKKAVPKEDIYSGGubiquitination[2, 6]
Reference
 [1] 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]
 [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] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [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] 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
Functional Description
 mRNA-binding component of ribonucleosomes. Specifically binds AU-rich element (ARE)-containing mRNAs. Involved in post- transcriptional regulation of cytokines mRNAs. 
Sequence Annotation
 DOMAIN 7 86 RRM 1.
 DOMAIN 98 175 RRM 2.
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 84 84 Phosphoserine; by MAPKAPK2.
 MOD_RES 188 188 Phosphoserine.
 MOD_RES 291 291 Dimethylated arginine.  
Keyword
 Acetylation; Complete proteome; Direct protein sequencing; Methylation; Nucleus; Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein; RNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 305 AA 
Protein Sequence
MENSQLCKLF IGGLNVQTSE SGLRGHFEAF GTLTDCVVVV NPQTKRSRCF GFVTYSNVEE 60
ADAAMAASPH AVDGNTVELK RAVSREDSAR PGAHAKVKKL FVGGLKGDVA EGDLIEHFSQ 120
FGTVEKAEII ADKQSGKKRG FGFVYFQNHD AADKAAVVKF HPIQGHRVEV KKAVPKEDIY 180
SGGGGGGSRS SRGGRGGRGR GGGRDQNGLS KGGGGGYNSY GGYGGGGGGG YNAYGGGGGG 240
SSYGGSDYGN GFGGFGSYSQ HQSSYGPMKS GGGGGGGGSS WGGRSNSGPY RGGYGGGGGY 300
GGSSF 305 
Gene Ontology
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0030529; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
 GO:0017091; F:AU-rich element binding; IDA:UniProtKB.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0070935; P:3'-UTR-mediated mRNA stabilization; ISS:UniProtKB.
 GO:0006954; P:inflammatory response; ISS:UniProtKB.
 GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
 GO:0032496; P:response to lipopolysaccharide; ISS:UniProtKB. 
Interpro
 IPR012677; Nucleotide-bd_a/b_plait.
 IPR000504; RRM_dom. 
Pfam
 PF00076; RRM_1 
SMART
 SM00360; RRM 
PROSITE
 PS50102; RRM 
PRINTS