CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008340
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 60S ribosomal protein L14 
Protein Synonyms/Alias
 CAG-ISL 7 
Gene Name
 RPL14 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
23SFGPHAGKLVAIVDVubiquitination[1, 2, 3]
53RRQAMPFKCMQLTDFubiquitination[2]
63QLTDFILKFPHSAHQubiquitination[2, 3]
71FPHSAHQKYVRQAWQacetylation[4]
71FPHSAHQKYVRQAWQubiquitination[1, 2]
79YVRQAWQKADINTKWacetylation[4]
79YVRQAWQKADINTKWubiquitination[1, 2, 3]
85QKADINTKWAATRWAacetylation[4]
85QKADINTKWAATRWAubiquitination[1, 2, 3, 5, 6]
101KIEARERKAKMTDFDubiquitination[1, 2]
103EARERKAKMTDFDRFubiquitination[1, 2]
124KMRNRIIKNEVKKLQubiquitination[2, 7]
129IIKNEVKKLQKAALLubiquitination[2, 8]
132NEVKKLQKAALLKASubiquitination[2, 8]
137LQKAALLKASPKKAPubiquitination[2, 5, 7, 8]
165AAKVPAKKITAASKKubiquitination[5]
187AQKATGQKAAPAPKAacetylation[9]
193QKAAPAPKAQKGQKAacetylation[9]
196APAPKAQKGQKAPAQacetylation[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] 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] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786
Functional Description
  
Sequence Annotation
 REPEAT 171 175 1-1.
 REPEAT 176 180 1-2.
 REPEAT 181 185 1-3.
 REPEAT 186 190 1-4.
 REPEAT 193 195 2-1.
 REPEAT 196 198 2-2.
 REGION 171 190 4 X 5 AA tandem repeats of Q-K-A-[PAS]-X.
 REGION 193 198 2 X 3 AA tandem repeats of K-[GA]-Q.
 MOD_RES 79 79 N6-acetyllysine.
 MOD_RES 85 85 N6-acetyllysine.
 MOD_RES 139 139 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Complete proteome; Direct protein sequencing; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Ribonucleoprotein; Ribosomal protein; Triplet repeat expansion. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 215 AA 
Protein Sequence
MVFRRFVEVG RVAYVSFGPH AGKLVAIVDV IDQNRALVDG PCTQVRRQAM PFKCMQLTDF 60
ILKFPHSAHQ KYVRQAWQKA DINTKWAATR WAKKIEARER KAKMTDFDRF KVMKAKKMRN 120
RIIKNEVKKL QKAALLKASP KKAPGTKGTA AAAAAAAAAK VPAKKITAAS KKAPAQKVPA 180
QKATGQKAAP APKAQKGQKA PAQKAPAPKA SGKKA 215 
Gene Ontology
 GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
 GO:0003723; F:RNA binding; TAS:ProtInc.
 GO:0003735; F:structural constituent of ribosome; NAS:UniProtKB.
 GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
 GO:0042273; P:ribosomal large subunit biogenesis; IMP:UniProtKB.
 GO:0006364; P:rRNA processing; IMP:UniProtKB.
 GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; TAS:Reactome.
 GO:0006414; P:translational elongation; TAS:Reactome.
 GO:0006413; P:translational initiation; TAS:Reactome.
 GO:0006415; P:translational termination; TAS:Reactome.
 GO:0019083; P:viral transcription; TAS:Reactome. 
Interpro
 IPR014722; Rib_L2_dom2.
 IPR002784; Ribosomal_L14. 
Pfam
 PF01929; Ribosomal_L14e 
SMART
  
PROSITE
  
PRINTS