UniProt Accession

 RS19_HUMAN; P39019 

Genbank Protein ID

 M81757; AF092907; AF092906; BC000023; BC007615; BC018616; AB007155 

Genbank Nucleotide ID

 AAA89070.1; AAD13668.1; AAD13668.1; AAH00023.1; AAH07615.1; AAH18616.1; BAA28593.1 

Protein Name

 40S ribosomal protein S19 

Protein Synonyms/Alias

  

Gene Name

 RPS19 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
7	*MPGVTVKDVNQQEF	ubiquitination	[1, 2]
23	RALAAFLKKSGKLKV	acetylation	[3]
23	RALAAFLKKSGKLKV	ubiquitination	[2]
29	LKKSGKLKVPEWVDT	ubiquitination	[2, 4, 5]
38	PEWVDTVKLAKHKEL	ubiquitination	[2, 4]
43	TVKLAKHKELAPYDE	ubiquitination	[2, 4]
77	AGVGSMTKIYGGRQR	acetylation	[3, 6]
77	AGVGSMTKIYGGRQR	ubiquitination	[2, 4, 5, 7, 8, 9]
111	LQALEGLKMVEKDQD	acetylation	[3, 10]
111	LQALEGLKMVEKDQD	ubiquitination	[2, 4, 7, 8, 9, 11]

Reference

 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [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] 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]
 [7] 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]
 [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] 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]
 [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] 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

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

Sequence Annotation

 MOD_RES 23 23 N6-acetyllysine.
 MOD_RES 111 111 N6-acetyllysine.  

Keyword

 3D-structure; Acetylation; Complete proteome; Diamond-Blackfan anemia; Direct protein sequencing; Disease mutation; Nucleus; Reference proteome; Ribonucleoprotein; Ribosomal protein. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 145 AA 

Protein Sequence

Gene Ontology

 GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
 GO:0005730; C:nucleolus; IDA:UniProtKB.
 GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
 GO:0003735; F:structural constituent of ribosome; IDA:UniProtKB.
 GO:0030218; P:erythrocyte differentiation; IMP:HGNC.
 GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:UniProtKB.
 GO:0002548; P:monocyte chemotaxis; IDA:UniProtKB.
 GO:0060266; P:negative regulation of respiratory burst involved in inflammatory response; IDA:UniProtKB.
 GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
 GO:0007000; P:nucleolus organization; IMP:UniProtKB.
 GO:0051272; P:positive regulation of cellular component movement; TAS:HGNC.
 GO:0060265; P:positive regulation of respiratory burst involved in inflammatory response; IDA:UniProtKB.
 GO:0051262; P:protein tetramerization; IDA:UniProtKB.
 GO:0009991; P:response to extracellular stimulus; TAS:HGNC.
 GO:0000028; P:ribosomal small subunit assembly; 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

 IPR001266; Ribosomal_S19e.
 IPR018277; Ribosomal_S19e_CS. 

Pfam

 PF01090; Ribosomal_S19e 

SMART

  

PROSITE

 PS00628; RIBOSOMAL_S19E 

PRINTS