UniProt Accession

 RL4_HUMAN; P36578; A8K502; P39029; Q4VBR0; Q969Z9 

Genbank Protein ID

 L20868; D23660; AB061820; AK291117; AK291859; CH471082; BC001365; BC005817; BC007748; BC007996; BC009888; BC010151; BC014653; BC066925; BC095427 

Genbank Nucleotide ID

 AAA60281.2; BAA04887.1; BAB79458.1; BAF83806.1; BAF84548.1; EAW77776.1; AAH01365.1; AAH05817.1; AAH07748.1; AAH07996.1; AAH09888.1; AAH10151.1; AAH14653.1; AAH66925.1; AAH95427.1 

Protein Name

 60S ribosomal protein L4 

Protein Synonyms/Alias

 60S ribosomal protein L1 

Gene Name

 RPL4 

Gene Synonyms/Alias

 RPL1 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
14	LISVYSEKGESSGKN	acetylation	[1]
14	LISVYSEKGESSGKN	ubiquitination	[2, 3, 4, 5, 6]
20	EKGESSGKNVTLPAV	ubiquitination	[4, 5, 6, 7, 8]
29	VTLPAVFKAPIRPDI	ubiquitination	[4]
46	FVHTNLRKNNRQPYA	ubiquitination	[4]
106	GRMFAPTKTWRRWHR	acetylation	[1]
106	GRMFAPTKTWRRWHR	ubiquitination	[2, 3, 4, 5, 6, 7, 8]
120	RRVNTTQKRYAICSA	ubiquitination	[8]
140	LPALVMSKGHRIEEV	ubiquitination	[2, 3, 4, 6]
157	LPLVVEDKVEGYKKT	ubiquitination	[2, 3, 4, 5, 6, 8]
162	EDKVEGYKKTKEAVL	ubiquitination	[2, 4, 5, 6, 8]
163	DKVEGYKKTKEAVLL	ubiquitination	[4]
165	VEGYKKTKEAVLLLK	ubiquitination	[2, 3, 4, 5, 6, 8]
172	KEAVLLLKKLKAWND	ubiquitination	[3, 4, 5, 8]
173	EAVLLLKKLKAWNDI	ubiquitination	[4]
175	VLLLKKLKAWNDIKK	ubiquitination	[2, 4, 6, 8]
181	LKAWNDIKKVYASQR	ubiquitination	[2, 4, 6, 8]
182	KAWNDIKKVYASQRM	ubiquitination	[4]
219	NEDNGIIKAFRNIPG	ubiquitination	[2, 4, 6, 7, 8, 9]
234	ITLLNVSKLNILKLA	ubiquitination	[2, 4, 5, 6, 7]
239	VSKLNILKLAPGGHV	ubiquitination	[2, 4, 6, 8, 9]
259	WTESAFRKLDELYGT	ubiquitination	[2, 4, 6, 8]
269	ELYGTWRKAASLKSN	ubiquitination	[4]
274	WRKAASLKSNYNLPM	ubiquitination	[2, 4, 5, 6, 7, 8]
283	NYNLPMHKMINTDLS	ubiquitination	[2, 3, 4, 5, 6, 7, 8]
294	TDLSRILKSPEIQRA	ubiquitination	[2, 3, 4, 5, 6, 7, 8, 9]
315	KIHRRVLKKNPLKNL	ubiquitination	[4]
320	VLKKNPLKNLRIMLK	ubiquitination	[2, 4, 5, 6, 8]
327	KNLRIMLKLNPYAKT	ubiquitination	[2, 3, 4, 5, 6, 7, 8, 9]
333	LKLNPYAKTMRRNTI	acetylation	[1]
333	LKLNPYAKTMRRNTI	ubiquitination	[2, 3, 4, 5, 6, 7, 8]
353	NHKLRVDKAAAAAAA	ubiquitination	[2, 3, 4, 5, 6, 7, 8]
364	AAAALQAKSDEKAAV	ubiquitination	[3, 4, 5, 8]
368	LQAKSDEKAAVAGKK	ubiquitination	[3, 5, 8]
374	EKAAVAGKKPVVGKK	ubiquitination	[4]

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] 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]
 [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] 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]
 [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] 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]
 [7] 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]
 [8] 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]
 [9] 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] 

Functional Description

  

Sequence Annotation

 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 14 14 N6-acetyllysine.
 MOD_RES 106 106 N6-acetyllysine.
 MOD_RES 295 295 Phosphoserine.
 MOD_RES 333 333 N6-acetyllysine.
 MOD_RES 365 365 Phosphoserine.  

Keyword

 3D-structure; Acetylation; Complete proteome; Direct protein sequencing; Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 427 AA 

Protein Sequence

Gene Ontology

 GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
 GO:0005730; C:nucleolus; IDA:HPA.
 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: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

 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