UniProt Accession

 RL11_HUMAN; P62913; P25121; P39026; Q8TDH2; Q9Y674 

Genbank Protein ID

 X79234; L05092; AF101385; BC018970; AF432212; AB007171 

Genbank Nucleotide ID

 CAA55816.1; AAC15856.1; AAD20460.3; AAH18970.1; AAL99919.1; BAA25831.1 

Protein Name

 60S ribosomal protein L11 

Protein Synonyms/Alias

 CLL-associated antigen KW-12 

Gene Name

 RPL11 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
8	MAQDQGEKENPMREL	acetylation	[1]
8	MAQDQGEKENPMREL	ubiquitination	[1, 2, 3]
19	MRELRIRKLCLNICV	ubiquitination	[1, 3, 4]
38	DRLTRAAKVLEQLTG	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 8, 9, 10]
52	GQTPVFSKARYTVRS	acetylation	[1, 11, 12, 13]
52	GQTPVFSKARYTVRS	ubiquitination	[1, 2, 3, 4, 6, 7, 8, 9, 10, 14, 15, 16, 17, 18]
67	FGIRRNEKIAVHCTV	acetylation	[1]
67	FGIRRNEKIAVHCTV	ubiquitination	[1, 2, 3]
78	HCTVRGAKAEEILEK	ubiquitination	[1, 2, 3, 4]
85	KAEEILEKGLKVREY	acetylation	[1, 11, 12, 13]
85	KAEEILEKGLKVREY	ubiquitination	[1, 2, 3, 4, 6, 7, 10]
88	EILEKGLKVREYELR	ubiquitination	[3]
144	PGFSIADKKRRTGCI	ubiquitination	[1, 3, 6, 10]
145	GFSIADKKRRTGCIG	ubiquitination	[1, 6, 10]
154	RTGCIGAKHRISKEE	acetylation	[1, 19]
154	RTGCIGAKHRISKEE	ubiquitination	[4]
159	GAKHRISKEEAMRWF	acetylation	[1, 11, 12]
159	GAKHRISKEEAMRWF	ubiquitination	[1, 2, 3, 4]
169	AMRWFQQKYDGIILP	ubiquitination	[2, 3, 4, 5, 6, 8, 9, 10, 16, 17]
178	DGIILPGK*******	ubiquitination	[1, 8, 10, 15, 17]

Reference

 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [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] 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]
 [8] 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]
 [9] 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]
 [10] 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]
 [11] 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]
 [12] 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]
 [13] 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]
 [14] A data set of human endogenous protein ubiquitination sites.
 Shi Y, Chan DW, Jung SY, Malovannaya A, Wang Y, Qin J.
 Mol Cell Proteomics. 2011 May;10(5):M110.002089. [PMID: 20972266]
 [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]
 [16] 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]
 [17] 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]
 [18] 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]
 [19] Monoclonal antibody cocktail as an enrichment tool for acetylome analysis.
 Shaw PG, Chaerkady R, Zhang Z, Davidson NE, Pandey A.
 Anal Chem. 2011 May 15;83(10):3623-6. [PMID: 21466224] 

Functional Description

 Binds to 5S ribosomal RNA (By similarity). Required for rRNA maturation and formation of the 60S ribosomal subunits. Promotes nucleolar location of PML (By similarity). 

Sequence Annotation

 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 44 44 Phosphothreonine.
 MOD_RES 52 52 N6-acetyllysine.
 MOD_RES 85 85 N6-acetyllysine.  

Keyword

 3D-structure; Acetylation; Alternative splicing; Complete proteome; Diamond-Blackfan anemia; Direct protein sequencing; Disease mutation; Nucleus; Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 178 AA 

Protein Sequence

Gene Ontology

 GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
 GO:0005730; C:nucleolus; IDA:UniProtKB.
 GO:0003723; F:RNA binding; TAS:ProtInc.
 GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
 GO:0003735; F:structural constituent of ribosome; NAS:UniProtKB.
 GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
 GO:0034504; P:protein localization to nucleus; ISS:UniProtKB.
 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

 IPR002132; Ribosomal_L5.
 IPR020929; Ribosomal_L5_CS.
 IPR022803; Ribosomal_L5_domain. 

Pfam

 PF00281; Ribosomal_L5
 PF00673; Ribosomal_L5_C 

SMART

  

PROSITE

 PS00358; RIBOSOMAL_L5 

PRINTS