UniProt Accession

 RS24_HUMAN; P62847; E7EPK6; P16632; Q5T0P7; Q5T0P8; Q7Z3D1 

Genbank Protein ID

 M31520; U12202; U12202; BX336465; AK311776; AK311910; BX537975; AL512628; AL512628; CH471083; CH471083; BC000523; BC003149; BC071926 

Genbank Nucleotide ID

 AAA36588.1; AAB08007.1; AAB08006.1; BAG34719.1; BAG34851.1; CAD97939.1; CAI16467.1; CAI16468.1; EAW54623.1; EAW54625.1; AAH00523.1; AAH71926.1 

Protein Name

 40S ribosomal protein S24 

Protein Synonyms/Alias

  

Gene Name

 RPS24 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
21	TNRLLQRKQMVIDVL	ubiquitination	[1]
32	IDVLHPGKATVPKTE	ubiquitination	[1]
37	PGKATVPKTEIREKL	acetylation	[2]
37	PGKATVPKTEIREKL	ubiquitination	[1, 3]
49	EKLAKMYKTTPDVIF	ubiquitination	[4]
68	RTHFGGGKTTGFGMI	ubiquitination	[1, 3, 4, 5, 6, 7, 8]
83	YDSLDYAKKNEPKHR	ubiquitination	[1, 3, 4, 7, 8]
84	DSLDYAKKNEPKHRL	ubiquitination	[7]
88	YAKKNEPKHRLARHG	ubiquitination	[7]
99	ARHGLYEKKKTSRKQ	ubiquitination	[3]
115	KERKNRMKKVRGTAK	acetylation	[2]

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] 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]
 [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] 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]
 [6] 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]
 [7] 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]
 [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] 

Functional Description

 Required for processing of pre-rRNA and maturation of 40S ribosomal subunits. 

Sequence Annotation

 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 9 9 Phosphothreonine.
 MOD_RES 81 81 Phosphotyrosine (By similarity).  

Keyword

 3D-structure; Acetylation; Alternative splicing; Complete proteome; Diamond-Blackfan anemia; Direct protein sequencing; Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 133 AA 

Protein Sequence

Gene Ontology

 GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
 GO:0005730; C:nucleolus; IBA:RefGenome.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0003735; F:structural constituent of ribosome; NAS:UniProtKB.
 GO:0031369; F:translation initiation factor binding; ISS:UniProtKB.
 GO:0034101; P:erythrocyte homeostasis; IMP:UniProtKB.
 GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:RefGenome.
 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. 

Interpro

 IPR012677; Nucleotide-bd_a/b_plait.
 IPR012678; Ribosomal_L23/L15e_core_dom.
 IPR001976; Ribosomal_S24e.
 IPR018098; Ribosomal_S24e_CS. 

Pfam

 PF01282; Ribosomal_S24e 

SMART

  

PROSITE

 PS00529; RIBOSOMAL_S24E 

PRINTS