CPLM-004650

Genbank Nucleotide ID

60S ribosomal protein L7

Protein Synonyms/Alias

Homo sapiens (Human)

Position	Peptide	Type	References
7	*MEGVEEKKKEVPAV	ubiquitination	[1, 2]
8	MEGVEEKKKEVPAVP	ubiquitination	[1, 2, 3]
9	EGVEEKKKEVPAVPE	ubiquitination	[1]
19	PAVPETLKKKRRNFA	acetylation	[4]
19	PAVPETLKKKRRNFA	ubiquitination	[1, 5, 6, 7]
20	AVPETLKKKRRNFAE	ubiquitination	[1, 2]
29	RRNFAELKIKRLRKK	acetylation	[4]
29	RRNFAELKIKRLRKK	ubiquitination	[1, 2, 5, 6, 7, 8]
40	LRKKFAQKMLRKARR	ubiquitination	[1, 2, 5, 7, 8, 9]
48	MLRKARRKLIYEKAK	ubiquitination	[1]
53	RRKLIYEKAKHYHKE	ubiquitination	[1, 5, 7, 9]
55	KLIYEKAKHYHKEYR	ubiquitination	[1]
77	RMARMARKAGNFYVP	ubiquitination	[1, 5, 7, 8]
88	FYVPAEPKLAFVIRI	ubiquitination	[1, 5, 8]
104	GINGVSPKVRKVLQL	ubiquitination	[1, 5, 7, 8]
107	GVSPKVRKVLQLLRL	ubiquitination	[1, 8]
124	IFNGTFVKLNKASIN	acetylation	[10]
124	IFNGTFVKLNKASIN	ubiquitination	[1, 5, 7, 8, 9]
127	GTFVKLNKASINMLR	ubiquitination	[1, 5, 7, 8, 9, 11]
148	AWGYPNLKSVNELIY	ubiquitination	[1, 5, 7, 11, 12, 13]
156	SVNELIYKRGYGKIN	ubiquitination	[1, 3, 5, 7, 8, 11]
161	IYKRGYGKINKKRIA	acetylation	[10]
181	LIARSLGKYGIICME	ubiquitination	[1]
199	HEIYTVGKRFKEANN	ubiquitination	[1, 5]
202	YTVGKRFKEANNFLW	ubiquitination	[1, 3, 5, 7, 9]
212	NNFLWPFKLSSPRGG	ubiquitination	[1, 5, 7, 9]
223	PRGGMKKKTTHFVEG	ubiquitination	[1, 5, 7]

[1] 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]
[2] 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]
[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] 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] 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]
[6] 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]
[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] 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] 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]
[10] 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]
[11] 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]
[12] 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]
[13] 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]

Functional Description

Binds to G-rich structures in 28S rRNA and in mRNAs. Plays a regulatory role in the translation apparatus; inhibits cell-free translation of mRNAs.

REPEAT 7 18 1.
REPEAT 19 30 2.
REPEAT 31 42 3.
REPEAT 43 54 4.
REGION 7 54 4 X 12 AA tandem repeats.
MOD_RES 1 1 N-acetylmethionine.
MOD_RES 124 124 N6-acetyllysine.
MOD_RES 139 139 Phosphotyrosine.

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

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
GO:0003677; F:DNA binding; IDA:MGI.
GO:0003729; F:mRNA binding; IDA:MGI.
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.

IPR018038; Ribosomal_L30_CS.
IPR016082; Ribosomal_L30_ferredoxin-like.
IPR012988; Ribosomal_L30_N.
IPR005998; Ribosomal_L7_euk.

PF00327; Ribosomal_L30
PF08079; Ribosomal_L30_N

PS00634; RIBOSOMAL_L30