CPLM-007341

Genbank Nucleotide ID

60S ribosomal protein L13a

Protein Synonyms/Alias

23 kDa highly basic protein

Homo sapiens (Human)

Position	Peptide	Type	References
25	RLAAIVAKQVLLGRK	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 8]
51	SGNFYRNKLKYLAFL	ubiquitination	[2, 3, 8]
53	NFYRNKLKYLAFLRK	ubiquitination	[2, 3, 4, 5, 6, 7, 8]
91	VRGMLPHKTKRGQAA	ubiquitination	[6]
93	GMLPHKTKRGQAALD	ubiquitination	[6]
103	QAALDRLKVFDGIPP	ubiquitination	[2, 5, 8]
114	GIPPPYDKKKRMVVP	ubiquitination	[3, 6, 7, 9]
115	IPPPYDKKKRMVVPA	ubiquitination	[6]
125	MVVPAALKVVRLKPT	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 8, 9]
134	VRLKPTRKFAYLGRL	ubiquitination	[2, 5, 6, 8, 9]
148	LAHEVGWKYQAVTAT	ubiquitination	[2, 3, 5, 6, 7, 8]
159	VTATLEEKRKEKAKI	ubiquitination	[1, 3, 4, 6, 7, 8]
161	ATLEEKRKEKAKIHY	ubiquitination	[6]
188	AEKNVEKKIDKYTEV	acetylation	[10]
188	AEKNVEKKIDKYTEV	ubiquitination	[2, 6, 8]
191	NVEKKIDKYTEVLKT	acetylation	[11]
191	NVEKKIDKYTEVLKT	ubiquitination	[2, 6, 8]
197	DKYTEVLKTHGLLV*	ubiquitination	[5, 6, 7]

[1] 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]
[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] 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]
[4] 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]
[5] 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]
[6] 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]
[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] 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]
[9] 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]
[10] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330]
[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]

Functional Description

Associated with ribosomes but is not required for canonical ribosome function and has extra-ribosomal functions. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma activation and subsequent phosphorylation dissociates from the ribosome and assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation. In the GAIT complex interacts with m7G cap-bound eIF4G at or near the eIF3-binding site and blocks the recruitment of the 43S ribosomal complex. Involved in methylation of rRNA.

MOD_RES 2 2 N-acetylalanine; partial.
MOD_RES 77 77 Phosphoserine; by ZIPK/DAPK3.
MOD_RES 191 191 N6-acetyllysine.

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

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
GO:0003735; F:structural constituent of ribosome; NAS:UniProtKB.
GO:0071346; P:cellular response to interferon-gamma; IDA:UniProtKB.
GO:1901194; P:negative regulation of formation of translation preinitiation complex; IDA:UniProtKB.
GO:0017148; P:negative regulation of translation; IDA: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.

IPR005822; Ribosomal_L13.
IPR023563; Ribosomal_L13_CS.
IPR023564; Ribosomal_L13_dom.
IPR005755; Ribosomal_L13_euk/arc.

PF00572; Ribosomal_L13

PS00783; RIBOSOMAL_L13