CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020869
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 60S ribosomal protein L4 
Protein Synonyms/Alias
  
Gene Name
 Rpl4 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
14LISVYSEKGESSGKNacetylation[1, 2]
29VTLPAVFKAPIRPDIacetylation[3]
106GRMFAPTKTWRRWHRacetylation[1, 2, 4, 5]
106GRMFAPTKTWRRWHRubiquitination[6]
140LPALVMSKGHRIEEVacetylation[1]
157LPLVVEDKVEGYKKTubiquitination[6]
162EDKVEGYKKTKEAVQacetylation[3]
162EDKVEGYKKTKEAVQubiquitination[6]
173EAVQLLKKLKAWNDIubiquitination[6]
175VQLLKKLKAWNDIKKubiquitination[6]
181LKAWNDIKKVYASQRacetylation[5]
219NEDNGIIKAFRNIPGacetylation[1]
234ITLLNVSKLNILKLAacetylation[1, 7]
234ITLLNVSKLNILKLAubiquitination[6]
239VSKLNILKLAPGGHVacetylation[1]
259WTESAFRKLDELYGTacetylation[1, 2]
259WTESAFRKLDELYGTubiquitination[6]
274WRKAASLKSNYNLPMubiquitination[6]
283NYNLPMHKMMNTDLSacetylation[1]
283NYNLPMHKMMNTDLSubiquitination[6]
294TDLSRILKSPEIQRAubiquitination[6]
320VLKKNPLKNLRIMLKubiquitination[6]
327KNLRIMLKLNPYAKTacetylation[2]
327KNLRIMLKLNPYAKTubiquitination[6]
333LKLNPYAKTMRRNTIacetylation[5]
333LKLNPYAKTMRRNTIubiquitination[6]
353NHKLRVKKLEAAATAacetylation[2]
353NHKLRVKKLEAAATAsuccinylation[2]
353NHKLRVKKLEAAATAubiquitination[6]
364AATALATKSEKVVPEacetylation[1, 2]
364AATALATKSEKVVPEubiquitination[6]
367ALATKSEKVVPEKGTacetylation[2]
372SEKVVPEKGTADKKPubiquitination[6]
377PEKGTADKKPAVGKKacetylation[2, 3]
378EKGTADKKPAVGKKGacetylation[3]
Reference
 [1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [2] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [3] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [4] 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]
 [5] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [6] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [7] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758
Functional Description
  
Sequence Annotation
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 14 14 N6-acetyllysine (By similarity).
 MOD_RES 106 106 N6-acetyllysine (By similarity).
 MOD_RES 295 295 Phosphoserine.
 MOD_RES 333 333 N6-acetyllysine (By similarity).
 MOD_RES 365 365 Phosphoserine (By similarity).  
Keyword
 Acetylation; Complete proteome; Direct protein sequencing; Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 419 AA 
Protein Sequence
MACARPLISV YSEKGESSGK NVTLPAVFKA PIRPDIVNFV HTNLRKNNRQ PYAVSELAGH 60
QTSAESWGTG RAVARIPRVR GGGTHRSGQG AFGNMCRGGR MFAPTKTWRR WHRRVNTTQK 120
RYAICSALAA SALPALVMSK GHRIEEVPEL PLVVEDKVEG YKKTKEAVQL LKKLKAWNDI 180
KKVYASQRMR AGKGKMRNRR RIQRRGPCII YNEDNGIIKA FRNIPGITLL NVSKLNILKL 240
APGGHVGRFC IWTESAFRKL DELYGTWRKA ASLKSNYNLP MHKMMNTDLS RILKSPEIQR 300
ALRAPRKKIH RRVLKKNPLK NLRIMLKLNP YAKTMRRNTI LRQARNHKLR VKKLEAAATA 360
LATKSEKVVP EKGTADKKPA VGKKGKKVDA KKQKPAGKKV VAKKPAEKKP TTEEKKPAA 419 
Gene Ontology
 GO:0022625; C:cytosolic large ribosomal subunit; IEA:Compara.
 GO:0005730; C:nucleolus; IEA:Compara.
 GO:0030529; C:ribonucleoprotein complex; ISO:MGI.
 GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
 GO:0006412; P:translation; IEA:InterPro. 
Interpro
 IPR025755; Ribos_L4_C_dom.
 IPR002136; Ribosomal_L4/L1e.
 IPR013000; Ribosomal_L4/L1e_euk/arc_CS.
 IPR023574; Ribosomal_L4_dom. 
Pfam
 PF14374; Ribos_L4_asso_C
 PF00573; Ribosomal_L4 
SMART
  
PROSITE
 PS00939; RIBOSOMAL_L1E 
PRINTS