UniProt Accession

 RL7A_HUMAN; P62424; P11518; Q5T8U4 

Genbank Protein ID

 X06705; X52138; X61923; M36072; AK291123; AK311743; AL158826; CH471090; BC005128; BC021979; BC023594; BC023624; BC071900; BC071901; BC073802; BC105290 

Genbank Nucleotide ID

 CAA29889.1; CAA36383.1; CAA43925.1; AAA60282.1; BAF83812.1; BAG34686.1; CAI12832.1; EAW88063.1; AAH05128.1; AAH21979.1; AAH23594.1; AAH23624.1; AAH71900.1; AAH71901.1; AAH73802.1; AAI05291.1 

Protein Name

 60S ribosomal protein L7a 

Protein Synonyms/Alias

 PLA-X polypeptide; Surfeit locus protein 3 

Gene Name

 RPL7A 

Gene Synonyms/Alias

 SURF-3; SURF3 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
11	GKKAKGKKVAPAPAV	ubiquitination	[1, 2]
20	APAPAVVKKQEAKKV	ubiquitination	[2, 3, 4, 5]
21	PAPAVVKKQEAKKVV	ubiquitination	[1, 2]
26	VKKQEAKKVVNPLFE	ubiquitination	[1, 2, 6, 7]
34	VVNPLFEKRPKNFGI	acetylation	[2, 8, 9, 10]
34	VVNPLFEKRPKNFGI	ubiquitination	[2, 3, 5, 6, 7]
37	PLFEKRPKNFGIGQD	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 11, 12, 13]
48	IGQDIQPKRDLTRFV	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 13]
56	RDLTRFVKWPRYIRL	ubiquitination	[1, 3]
72	RQRAILYKRLKVPPA	ubiquitination	[11]
75	AILYKRLKVPPAINQ	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 11, 12, 13, 14]
97	QTATQLLKLAHKYRP	acetylation	[2, 8, 9]
97	QTATQLLKLAHKYRP	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 13]
101	QLLKLAHKYRPETKQ	acetylation	[2]
101	QLLKLAHKYRPETKQ	methylation	[15]
101	QLLKLAHKYRPETKQ	ubiquitination	[3, 4]
125	AEKKAAGKGDVPTKR	ubiquitination	[2, 3, 5, 11]
131	GKGDVPTKRPPVLRA	ubiquitination	[1, 2, 3, 6, 7, 11, 13, 16]
150	VTTLVENKKAQLVVI	ubiquitination	[1, 3, 4, 5, 11]
151	TTLVENKKAQLVVIA	acetylation	[17]
151	TTLVENKKAQLVVIA	ubiquitination	[2]
176	FLPALCRKMGVPYCI	ubiquitination	[1, 13]
185	GVPYCIIKGKARLGR	ubiquitination	[1, 11]
187	PYCIIKGKARLGRLV	ubiquitination	[1]
197	LGRLVHRKTCTTVAF	ubiquitination	[1]
212	TQVNSEDKGALAKLV	acetylation	[2, 10]
212	TQVNSEDKGALAKLV	ubiquitination	[1, 2, 4]
217	EDKGALAKLVEAIRT	acetylation	[8, 9]
217	EDKGALAKLVEAIRT	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 11, 13, 16, 18]
245	GGNVLGPKSVARIAK	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 11, 12, 13]
259	KLEKAKAKELATKLG	ubiquitination	[1, 3, 5, 11]
264	KAKELATKLG*****	ubiquitination	[1, 2, 3, 4, 5, 11, 12]

Reference

 [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] 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] 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]
 [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] 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] 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]
 [8] 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]
 [9] 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]
 [10] 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]
 [11] 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]
 [12] 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]
 [13] 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]
 [14] 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]
 [15] Mass spectrometry-based identification and characterisation of lysine and arginine methylation in the human proteome.
 Bremang M, Cuomo A, Agresta AM, Stugiewicz M, Spadotto V, Bonaldi T.
 Mol Biosyst. 2013 Jul 30;9(9):2231-47. [PMID: 23748837]
 [16] 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]
 [17] 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]
 [18] 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] 

Functional Description

  

Sequence Annotation

 MOD_RES 34 34 N6-acetyllysine.
 MOD_RES 97 97 N6-acetyllysine.
 MOD_RES 217 217 N6-acetyllysine.  

Keyword

 3D-structure; Acetylation; Chromosomal rearrangement; Complete proteome; Polymorphism; Reference proteome; Ribonucleoprotein; Ribosomal protein. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 266 AA 

Protein Sequence

Gene Ontology

 GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
 GO:0016020; C:membrane; IDA:BHF-UCL.
 GO:0042788; C:polysomal ribosome; IDA:HGNC.
 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:0042254; P:ribosome biogenesis; IEA:InterPro.
 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

 IPR001921; Ribosomal_L7A/L8.
 IPR004038; Ribosomal_L7Ae/L30e/S12e/Gad45.
 IPR018492; Ribosomal_L7Ae/L8/Nhp2.
 IPR004037; Ribosomal_L7Ae_CS. 

Pfam

 PF01248; Ribosomal_L7Ae 

SMART

  

PROSITE

 PS01082; RIBOSOMAL_L7AE 

PRINTS

 PR00881; L7ARS6FAMILY.
 PR00882; RIBOSOMALL7A.