UniProt Accession

 RL35A_HUMAN; P18077; Q08ES9; Q9BVN7 

Genbank Protein ID

 X52966; AY871273; CH471252; BC001037; BC010949; BC017093; BC061890; X94619 

Genbank Nucleotide ID

 CAA37138.1; AAX11429.1; EAW92249.1; AAH01037.1; AAH10949.1; AAH17093.1; AAH61890.1; CAA64325.1 

Protein Name

 60S ribosomal protein L35a 

Protein Synonyms/Alias

 Cell growth-inhibiting gene 33 protein 

Gene Name

 RPL35A 

Gene Synonyms/Alias

 GIG33 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
8	MSGRLWSKAIFAGYK	acetylation	[1]
8	MSGRLWSKAIFAGYK	ubiquitination	[2, 3, 4, 5, 6]
15	KAIFAGYKRGLRNQR	acetylation	[7]
15	KAIFAGYKRGLRNQR	ubiquitination	[4]
29	REHTALLKIEGVYAR	ubiquitination	[4]
45	ETEFYLGKRCAYVYK	ubiquitination	[2, 3, 4, 5, 6, 8, 9]
52	KRCAYVYKAKNNTVT	ubiquitination	[4]
54	CAYVYKAKNNTVTPG	ubiquitination	[4]
63	NTVTPGGKPNKTRVI	ubiquitination	[4, 8]
66	TPGGKPNKTRVIWGK	ubiquitination	[4]
73	KTRVIWGKVTRAHGN	ubiquitination	[4, 8, 9]
95	FRSNLPAKAIGHRIR	ubiquitination	[2, 3, 4, 5, 6, 8, 10, 11]

Reference

 [1] 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]
 [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] 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]
 [4] 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]
 [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] 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]
 [7] 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]
 [8] 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]
 [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] 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]
 [11] 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] 

Functional Description

 Required for the proliferation and viability of hematopoietic cells. Plays a role in 60S ribosomal subunit formation. The protein was found to bind to both initiator and elongator tRNAs and consequently was assigned to the P site or P and A site. 

Sequence Annotation

 MOD_RES 8 8 N6-acetyllysine.  

Keyword

 3D-structure; Acetylation; Complete proteome; Diamond-Blackfan anemia; Disease mutation; Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding; tRNA-binding. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 110 AA 

Protein Sequence

Gene Ontology

 GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
 GO:0003735; F:structural constituent of ribosome; NAS:UniProtKB.
 GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
 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. 

Interpro

 IPR001780; Ribosomal_L35A.
 IPR018266; Ribosomal_L35Ae_CS.
 IPR009000; Transl_elong_init/rib_B-barrel. 

Pfam

 PF01247; Ribosomal_L35Ae 

SMART

  

PROSITE

 PS01105; RIBOSOMAL_L35AE 

PRINTS