CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019985
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 28S ribosomal protein S5, mitochondrial 
Protein Synonyms/Alias
 MRP-S5; S5mt 
Gene Name
 Mrps5 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
367THQHLADKKGLHVVEacetylation[1, 2, 3]
414KLDWQDVKAMQGLKRacetylation[4]
414KLDWQDVKAMQGLKRsuccinylation[4]
Reference
 [1] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [2] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
 [3] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [4] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337
Functional Description
  
Sequence Annotation
 DOMAIN 220 284 S5 DRBM.  
Keyword
 Complete proteome; Mitochondrion; Reference proteome; Ribonucleoprotein; Ribosomal protein. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 432 AA 
Protein Sequence
MAAAVRAAGC LPALCSLQAG HFLSRQLSLN AFPVAATSFL AVKTALSHGS LSSRETRRNH 60
CLTSLSHVLQ TQCCVSSPGN WTGQQCRPYS FFTKLTAEEL WKGALAETGA GARKGRGKRT 120
KKKKRKDLNR GQIIGEGRSG FLWPGLNVPL IKSGVVQNIG QRSKEEQQKV EATMVEQREE 180
WDRKRKIKVK RERGWSGNTW GGVSIGPPDP GPNGETYEDF DTRILEVRNV FNMTAKEGRK 240
KSVRVLVAVG NGNGAAGFAI GKAADRGDAF RKAKNRAIHY LHYIERYEGH TIFHDISLRF 300
KRTQIRMKKQ PRGYGLRCHR AIITICRLIG IKDMYARVTG SMNMLNLTRG LFHGLARQET 360
HQHLADKKGL HVVEFREECG PLPIVVASPH GALSKEPEPE PEVPDTKLDW QDVKAMQGLK 420
RSVWFNLKRP AT 432 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0005840; C:ribosome; IEA:UniProtKB-KW.
 GO:0003723; F:RNA binding; IEA:InterPro.
 GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
 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.
 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