CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005396
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 40S ribosomal protein S2 
Protein Synonyms/Alias
 Omnipotent suppressor protein SUP44; RP12; S4; YS5 
Gene Name
 RPS2 
Gene Synonyms/Alias
 RPS4; SUP38; SUP44; YGL123W; G2893 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
10APEAQQQKRGGFGGRacetylation[1]
33GPRNTEEKGWVPVTKacetylation[1]
33GPRNTEEKGWVPVTKubiquitination[2, 3, 4]
119GLGIKTAKEVAGAIRacetylation[1]
119GLGIKTAKEVAGAIRubiquitination[4]
157QPHSLATKTTGKCGSacetylation[1]
161LATKTTGKCGSVTVRubiquitination[4]
185IVASPAVKKLLQLAGubiquitination[4]
186VASPAVKKLLQLAGVubiquitination[4]
251SDEASAQKKRF****ubiquitination[3]
Reference
 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [2] A perturbed ubiquitin landscape distinguishes between ubiquitin in trafficking and in proteolysis.
 Ziv I, Matiuhin Y, Kirkpatrick DS, Erpapazoglou Z, Leon S, Pantazopoulou M, Kim W, Gygi SP, Haguenauer-Tsapis R, Reis N, Glickman MH, Kleifeld O.
 Mol Cell Proteomics. 2011 May;10(5):M111.009753. [PMID: 21427232]
 [3] Sites of ubiquitin attachment in Saccharomyces cerevisiae.
 Starita LM, Lo RS, Eng JK, von Haller PD, Fields S.
 Proteomics. 2012 Jan;12(2):236-40. [PMID: 22106047]
 [4] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, VillĂ©n J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301
Functional Description
 Important in the assembly and function of the 40S ribosomal subunit. Mutations in this protein affects the control of translational fidelity. Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly. 
Sequence Annotation
 DOMAIN 76 139 S5 DRBM.
 MOD_RES 2 2 N-acetylserine.  
Keyword
 3D-structure; Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; Nucleus; Reference proteome; Ribonucleoprotein; Ribosomal protein; Ribosome biogenesis; rRNA processing. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 254 AA 
Protein Sequence
MSAPEAQQQK RGGFGGRNRG RPNRRGPRNT EEKGWVPVTK LGRLVKAGKI TTIEEIFLHS 60
LPVKEFQIID TLLPGLQDEV MNIKPVQKQT RAGQRTRFKA VVVVGDSNGH VGLGIKTAKE 120
VAGAIRAGII IAKLSVIPIR RGYWGTNLGQ PHSLATKTTG KCGSVTVRLI PAPRGSGIVA 180
SPAVKKLLQL AGVEDVYTQS NGKTRTLENT LKAAFVAIGN TYGFLTPNLW AEQPLPVSPL 240
DIYSDEASAQ KKRF 254 
Gene Ontology
 GO:0022627; C:cytosolic small ribosomal subunit; IDA:SGD.
 GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
 GO:0032040; C:small-subunit processome; IDA:SGD.
 GO:0070181; F:SSU rRNA binding; IDA:SGD.
 GO:0003735; F:structural constituent of ribosome; IDA:SGD.
 GO:0045903; P:positive regulation of translational fidelity; IMP:SGD.
 GO:0006407; P:rRNA export from nucleus; IMP:SGD.
 GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
 GO:0006412; P:translation; IEA:InterPro. 
Interpro
 IPR014720; dsRNA-bd-like_dom.
 IPR000851; Ribosomal_S5.
 IPR005324; Ribosomal_S5_C.
 IPR020568; Ribosomal_S5_D2-typ_fold.
 IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
 IPR005711; Ribosomal_S5_euk/arc.
 IPR013810; Ribosomal_S5_N.
 IPR018192; Ribosomal_S5_N_CS. 
Pfam
 PF00333; Ribosomal_S5
 PF03719; Ribosomal_S5_C 
SMART
  
PROSITE
 PS00585; RIBOSOMAL_S5
 PS50881; S5_DSRBD 
PRINTS