CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009387
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 60S ribosomal protein L37 
Protein Synonyms/Alias
 G1.16 
Gene Name
 RPL37 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
10KGTSSFGKRRNKTHTacetylation[1]
25LCRRCGSKAYHLQKSubiquitination[2]
31SKAYHLQKSTCGKCGubiquitination[2, 3]
36LQKSTCGKCGYPAKRubiquitination[2, 3]
46YPAKRKRKYNWSAKAubiquitination[3]
52RKYNWSAKAKRRNTTubiquitination[3]
54YNWSAKAKRRNTTGTubiquitination[3]
68TGRMRHLKIVYRRFRubiquitination[2, 3, 4, 5]
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] 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]
 [3] 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]
 [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] 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
 Binds to the 23S rRNA (By similarity). 
Sequence Annotation
 ZN_FING 19 37 C4-type (Potential).
 METAL 19 19 Zinc (By similarity).
 METAL 22 22 Zinc (By similarity).
 METAL 34 34 Zinc (By similarity).
 METAL 37 37 Zinc (By similarity).
 MOD_RES 10 10 N6-acetyllysine.
 MOD_RES 96 96 Phosphoserine.
 MOD_RES 97 97 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Complete proteome; Metal-binding; Phosphoprotein; Polymorphism; Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 97 AA 
Protein Sequence
MTKGTSSFGK RRNKTHTLCR RCGSKAYHLQ KSTCGKCGYP AKRKRKYNWS AKAKRRNTTG 60
TGRMRHLKIV YRRFRHGFRE GTTPKPKRAA VAASSSS 97 
Gene Ontology
 GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0003723; F:RNA binding; TAS:UniProtKB.
 GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
 GO:0003735; F:structural constituent of ribosome; NAS:UniProtKB.
 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
 IPR011331; Ribosomal_L37ae/L37e.
 IPR001569; Ribosomal_L37e.
 IPR018267; Ribosomal_L37e_CS.
 IPR011332; Ribosomal_zn-bd_dom. 
Pfam
 PF01907; Ribosomal_L37e 
SMART
  
PROSITE
 PS01077; RIBOSOMAL_L37E 
PRINTS