UniProt Accession

 RLA0_HUMAN; P05388; Q9BVK4 

Genbank Protein ID

 M17885; AC004263; BC000087; BC000345; BC000752; BC001127; BC001834; BC003655; BC005863; BC008092; BC008594; BC009867; BC015173; BC015690; AB007187 

Genbank Nucleotide ID

 AAA36470.1; AAC05176.1; AAH00087.1; AAH00345.1; AAH00752.1; AAH01127.1; AAH01834.1; AAH03655.1; AAH05863.1; AAH08092.1; AAH08594.1; AAH09867.1; AAH15173.1; AAH15690.1; BAA25845.1 

Protein Name

 60S acidic ribosomal protein P0 

Protein Synonyms/Alias

 60S ribosomal protein L10E 

Gene Name

 RPLP0 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
10	REDRATWKSNYFLKI	ubiquitination	[1, 2, 3, 4]
16	WKSNYFLKIIQLLDD	ubiquitination	[5]
26	QLLDDYPKCFIVGAD	ubiquitination	[1, 2, 3, 4, 6, 7, 8]
38	GADNVGSKQMQQIRM	ubiquitination	[1, 2, 3, 4, 6, 8]
50	IRMSLRGKAVVLMGK	ubiquitination	[2, 3, 5, 8]
57	KAVVLMGKNTMMRKA	ubiquitination	[1, 3, 4]
77	ENNPALEKLLPHIRG	acetylation	[9]
77	ENNPALEKLLPHIRG	ubiquitination	[1, 3, 4, 5]
92	NVGFVFTKEDLTEIR	ubiquitination	[2, 3, 5, 6, 7, 8]
106	RDMLLANKVPAAARA	ubiquitination	[1, 3, 4, 5, 7, 8, 10]
134	NTGLGPEKTSFFQAL	ubiquitination	[3]
146	QALGITTKISRGTIE	ubiquitination	[3, 7, 8]
162	LSDVQLIKTGDKVGA	ubiquitination	[8]
246	HSIINGYKRVLALSV	ubiquitination	[3]
264	YTFPLAEKVKAFLAD	ubiquitination	[5, 6, 8]
266	FPLAEKVKAFLADPS	ubiquitination	[3, 5, 8]
297	AAAAAPAKVEAKEES	ubiquitination	[3, 5, 8]
301	APAKVEAKEESEESD	ubiquitination	[3]

Reference

 [1] 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]
 [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] 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]
 [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] 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]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] 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] 

Functional Description

 Ribosomal protein P0 is the functional equivalent of E.coli protein L10. 

Sequence Annotation

 MOD_RES 24 24 Phosphotyrosine (By similarity).
 MOD_RES 304 304 Phosphoserine (By similarity).
 MOD_RES 307 307 Phosphoserine (By similarity).  

Keyword

 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; Host-virus interaction; Nucleus; Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 317 AA 

Protein Sequence

Gene Ontology

 GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 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.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 

Interpro

 IPR001790; Ribosomal_L10/acidic_P0.
 IPR001813; Ribosomal_L10/L12. 

Pfam

 PF00428; Ribosomal_60s
 PF00466; Ribosomal_L10 

SMART

  

PROSITE

  

PRINTS