CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000696
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Heterogeneous nuclear ribonucleoprotein R 
Protein Synonyms/Alias
 hnRNP R 
Gene Name
 HNRNPR 
Gene Synonyms/Alias
 HNRPR 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
41IEAGLPQKVAERLDEubiquitination[1, 2]
103AFLCGVMKTYRQREKacetylation[3]
103AFLCGVMKTYRQREKubiquitination[4, 5]
114QREKQGSKVQESTKGubiquitination[5]
171GTEVFVGKIPRDLYEubiquitination[5, 6, 7]
187ELVPLFEKAGPIWDLubiquitination[6, 7, 8]
224EAAQEAVKLCDSYEIubiquitination[5, 9]
235SYEIRPGKHLGVCISmethylation[10]
255LFVGSIPKNKTKENIubiquitination[1, 2]
257VGSIPKNKTKENILEubiquitination[5]
259SIPKNKTKENILEEFubiquitination[4]
300FLEYEDHKSAAQARRubiquitination[5]
341PEVMAKVKVLFVRNLubiquitination[1, 4, 5]
359VTEEILEKSFSEFGKubiquitination[2, 5, 6, 11]
366KSFSEFGKLERVKKLacetylation[3]
366KSFSEFGKLERVKKLubiquitination[1, 2, 4, 5, 6]
374LERVKKLKDYAFVHFubiquitination[4, 5]
389EDRGAAVKAMDEMNGacetylation[3]
389EDRGAAVKAMDEMNGubiquitination[4, 5, 6]
397AMDEMNGKEIEGEEIacetylation[3]
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] 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]
 [3] 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]
 [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] 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]
 [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] 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] 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]
 [10] Large-scale global identification of protein lysine methylation in vivo.
 Cao XJ, Arnaudo AM, Garcia BA.
 Epigenetics. 2013 May 1;8(5):477-85. [PMID: 23644510]
 [11] 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
 Component of ribonucleosomes, which are complexes of at least 20 other different heterogenious nuclear ribonucleoproteins (hnRNP). hnRNP play an important role in processing of precursor mRNA in the nucleus. 
Sequence Annotation
 DOMAIN 165 244 RRM 1.
 DOMAIN 246 328 RRM 2.
 DOMAIN 341 411 RRM 3.
 REPEAT 462 471 1; approximate.
 REPEAT 472 482 2.
 REPEAT 488 497 3; approximate.
 REGION 447 567 RNA-binding RGG-box.
 REGION 462 497 3 X 11 AA approximate repeats of D-D-Y-Y-
 MOTIF 412 418 Nuclear localization signal (Potential).
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 366 366 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Complete proteome; Cytoplasm; Direct protein sequencing; mRNA processing; mRNA splicing; Nucleus; Reference proteome; Repeat; Ribonucleoprotein; RNA-binding; Spliceosome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 633 AA 
Protein Sequence
MANQVNGNAV QLKEEEEPMD TSSVTHTEHY KTLIEAGLPQ KVAERLDEIF QTGLVAYVDL 60
DERAIDALRE FNEEGALSVL QQFKESDLSH VQNKSAFLCG VMKTYRQREK QGSKVQESTK 120
GPDEAKIKAL LERTGYTLDV TTGQRKYGGP PPDSVYSGVQ PGIGTEVFVG KIPRDLYEDE 180
LVPLFEKAGP IWDLRLMMDP LSGQNRGYAF ITFCGKEAAQ EAVKLCDSYE IRPGKHLGVC 240
ISVANNRLFV GSIPKNKTKE NILEEFSKVT EGLVDVILYH QPDDKKKNRG FCFLEYEDHK 300
SAAQARRRLM SGKVKVWGNV VTVEWADPVE EPDPEVMAKV KVLFVRNLAT TVTEEILEKS 360
FSEFGKLERV KKLKDYAFVH FEDRGAAVKA MDEMNGKEIE GEEIEIVLAK PPDKKRKERQ 420
AARQASRSTA YEDYYYHPPP RMPPPIRGRG RGGGRGGYGY PPDYYGYEDY YDDYYGYDYH 480
DYRGGYEDPY YGYDDGYAVR GRGGGRGGRG APPPPRGRGA PPPRGRAGYS QRGAPLGPPR 540
GSRGGRGGPA QQQRGRGSRG SRGNRGGNVG GKRKADGYNQ PDSKRRQTNN QQNWGSQPIA 600
QQPLQQGGDY SGNYGYNNDN QEFYQDTYGQ QWK 633 
Gene Ontology
 GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005654; C:nucleoplasm; IDA:UniProtKB.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0003723; F:RNA binding; NAS:UniProtKB.
 GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB. 
Interpro
 IPR006535; HnRNP_R/Q_splicing_fac.
 IPR012677; Nucleotide-bd_a/b_plait.
 IPR000504; RRM_dom. 
Pfam
 PF00076; RRM_1 
SMART
 SM00360; RRM 
PROSITE
 PS50102; RRM 
PRINTS