CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020395
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 39S ribosomal protein L37, mitochondrial 
Protein Synonyms/Alias
 L37mt; MRP-L37; 39S ribosomal protein L2, mitochondrial; L2mt; MRP-L2 
Gene Name
 MRPL37 
Gene Synonyms/Alias
 MRPL2; RPML2; HSPC235 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
127ALWLTKTKLIEGLPEacetylation[1]
127ALWLTKTKLIEGLPEubiquitination[2]
135LIEGLPEKVLSLVDDubiquitination[2, 3, 4]
172QTTEEIPKRETYCPVubiquitination[4, 5, 6]
189DNLIQLCKSQILKHPubiquitination[7]
233GGARLSTKDPLPTIAubiquitination[4]
334LLYGNDAKVLEQPVVubiquitination[2, 4, 8]
407PVGPVGFKPETFRKFubiquitination[4, 8]
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] 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]
 [3] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
 [4] 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]
 [5] 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]
 [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] 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] 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
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Mitochondrion; Polymorphism; Reference proteome; Ribonucleoprotein; Ribosomal protein; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 423 AA 
Protein Sequence
MALASGPARR ALAGSGQLGL GGFGAPRRGA YEWGVRSTRK SEPPPLDRVY EIPGLEPITF 60
AGKMHFVPWL ARPIFPPWDR GYKDPRFYRS PPLHEHPLYK DQACYIFHHR CRLLEGVKQA 120
LWLTKTKLIE GLPEKVLSLV DDPRNHIENQ DECVLNVISH ARLWQTTEEI PKRETYCPVI 180
VDNLIQLCKS QILKHPSLAR RICVQNSTFS ATWNRESLLL QVRGSGGARL STKDPLPTIA 240
SREEIEATKN HVLETFYPIS PIIDLHECNI YDVKNDTGFQ EGYPYPYPHT LYLLDKANLR 300
PHRLQPDQLR AKMILFAFGS ALAQARLLYG NDAKVLEQPV VVQSVGTDGR VFHFLVFQLN 360
TTDLDCNEGV KNLAWVDSDQ LLYQHFWCLP VIKKRVVVEP VGPVGFKPET FRKFLALYLH 420
GAA 423 
Gene Ontology
 GO:0005761; C:mitochondrial ribosome; NAS:UniProtKB.
 GO:0003735; F:structural constituent of ribosome; NAS:UniProtKB.
 GO:0006412; P:translation; NAS:UniProtKB. 
Interpro
 IPR010793; Ribosomal_L37/S30. 
Pfam
 PF07147; PDCD9 
SMART
  
PROSITE
  
PRINTS