CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005101
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Heterogeneous nuclear ribonucleoproteins A2/B1 
Protein Synonyms/Alias
 hnRNP A2/B1 
Gene Name
 HNRNPA2B1 
Gene Synonyms/Alias
 HNRPA2B1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
3*****MEKTLETVPLacetylation[1, 2]
3*****MEKTLETVPLubiquitination[2, 3, 4, 5]
22REKEQFRKLFIGGLSubiquitination[2, 4, 6, 7]
46NYYEQWGKLTDCVVMacetylation[2]
46NYYEQWGKLTDCVVMubiquitination[2, 3, 4, 5, 6, 7, 8, 9]
59VMRDPASKRSRGFGFacetylation[2]
59VMRDPASKRSRGFGFubiquitination[2, 3, 4, 5, 7, 10]
104VAREESGKPGAHVTVmethylation[11]
104VAREESGKPGAHVTVubiquitination[2, 4, 5, 7, 10]
112PGAHVTVKKLFVGGIacetylation[2]
112PGAHVTVKKLFVGGIubiquitination[7]
113GAHVTVKKLFVGGIKubiquitination[2, 5]
120KLFVGGIKEDTEEHHacetylation[2, 12]
120KLFVGGIKEDTEEHHubiquitination[2, 4, 5, 6, 7]
137DYFEEYGKIDTIEIIubiquitination[7, 13]
168DDHDPVDKIVLQKYHacetylation[1, 2, 12, 14]
168DDHDPVDKIVLQKYHubiquitination[2, 3, 4, 5, 7, 10, 15]
173VDKIVLQKYHTINGHacetylation[1, 2, 14]
173VDKIVLQKYHTINGHubiquitination[2, 4, 5, 6, 7]
Reference
 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
 [9] 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]
 [10] 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]
 [11] Update on activities at the Universal Protein Resource (UniProt) in 2013.
 e="String">UniProt Consortium.
 Nucleic Acids Res. 2013 Jan;41(Database issue):D43-7. [PMID: 23161681]
 [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]
 [13] 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]
 [14] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [15] 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
Functional Description
 Involved with pre-mRNA processing. Forms complexes (ribonucleosomes) with at least 20 other different hnRNP and heterogeneous nuclear RNA in the nucleus. 
Sequence Annotation
 DOMAIN 21 104 RRM 1.
 DOMAIN 112 191 RRM 2.
 REGION 308 347 Nuclear targeting sequence (By
 MOTIF 9 15 Nuclear localization signal (Potential).
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 85 85 Phosphoserine.
 MOD_RES 104 104 N6,N6-dimethyllysine.
 MOD_RES 149 149 Phosphoserine.
 MOD_RES 168 168 N6-acetyllysine.
 MOD_RES 173 173 N6-acetyllysine.
 MOD_RES 203 203 Dimethylated arginine; alternate.
 MOD_RES 203 203 Omega-N-methylarginine; alternate.
 MOD_RES 212 212 Phosphoserine.
 MOD_RES 213 213 Dimethylated arginine; alternate.
 MOD_RES 213 213 Omega-N-methylarginine; alternate.
 MOD_RES 225 225 Phosphoserine.
 MOD_RES 231 231 Phosphoserine.
 MOD_RES 236 236 Phosphoserine.
 MOD_RES 259 259 Phosphoserine.
 MOD_RES 324 324 Phosphoserine.
 MOD_RES 331 331 Phosphotyrosine.
 MOD_RES 341 341 Phosphoserine.
 MOD_RES 344 344 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Complete proteome; Cytoplasm; Direct protein sequencing; Methylation; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein; RNA-binding; Spliceosome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 353 AA 
Protein Sequence
MEKTLETVPL ERKKREKEQF RKLFIGGLSF ETTEESLRNY YEQWGKLTDC VVMRDPASKR 60
SRGFGFVTFS SMAEVDAAMA ARPHSIDGRV VEPKRAVARE ESGKPGAHVT VKKLFVGGIK 120
EDTEEHHLRD YFEEYGKIDT IEIITDRQSG KKRGFGFVTF DDHDPVDKIV LQKYHTINGH 180
NAEVRKALSR QEMQEVQSSR SGRGGNFGFG DSRGGGGNFG PGPGSNFRGG SDGYGSGRGF 240
GDGYNGYGGG PGGGNFGGSP GYGGGRGGYG GGGPGYGNQG GGYGGGYDNY GGGNYGSGNY 300
NDFGNYNQQP SNYGPMKSGN FGGSRNMGGP YGGGNYGPGG SGGSGGYGGR SRY 353 
Gene Ontology
 GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005730; C:nucleolus; IDA:HPA.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0097157; F:pre-mRNA intronic binding; IEA:Compara.
 GO:0003723; F:RNA binding; IDA:HGNC.
 GO:0043047; F:single-stranded telomeric DNA binding; IDA:HGNC.
 GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB.
 GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; IEA:Compara.
 GO:0050658; P:RNA transport; IDA:HGNC. 
Interpro
 IPR012677; Nucleotide-bd_a/b_plait.
 IPR000504; RRM_dom. 
Pfam
 PF00076; RRM_1 
SMART
 SM00360; RRM 
PROSITE
 PS50102; RRM 
PRINTS