CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-031195
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 cDNA FLJ50195, highly similar to mRNA capping enzyme 
Protein Synonyms/Alias
 mRNA-capping enzyme 
Gene Name
 RNGTT 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
21YDRNDIEKEGIKYIKubiquitination[1]
25DIEKEGIKYIKLQCKubiquitination[1]
32KYIKLQCKGHGECPTubiquitination[1, 2]
111IYKGDYLKELFRRYGubiquitination[1, 3, 4]
189TQVTTQPKLGEVQQKubiquitination[1]
227NIKLLDLKPYKVSWKubiquitination[1]
230LLDLKPYKVSWKADGubiquitination[1]
234KPYKVSWKADGTRYMubiquitination[1]
337SPRHEKMKTGLIDKTubiquitination[1]
343MKTGLIDKTQEPFSVubiquitination[1, 4]
353EPFSVRNKPFFDICTubiquitination[1]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [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] 
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Hydrolase; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 514 AA 
Protein Sequence
MGLLVDLTNT SRFYDRNDIE KEGIKYIKLQ CKGHGECPTT ENTETFIRLC ERFNERNPPE 60
LIGVHCTHGF NRTGFLICAF LVEKMDWSIE AAVATFAQAR PPGIYKGDYL KELFRRYGDI 120
EEAPPPPLLP DWCFEDDEDE DEDEDGKKES EPGSSASFGK RRKERLKLGA IFLEGVTVKG 180
VTQVTTQPKL GEVQQKCHQF CGWEGSGFPG AQPVSMDKQN IKLLDLKPYK VSWKADGTRY 240
MMLIDGTNEV FMIDRDNSVF HVSNLEFPFR KDLRMHLSNT LLDGEMIIDR VNGQAVPRYL 300
IYDIIKFNSQ PVGDCDFNVR LQCIEREIIS PRHEKMKTGL IDKTQEPFSV RNKPFFDICT 360
SRKKYKPGRC DDILKWKPPS LNSVDFRLKI TRMGGEGLLP QNVGLLYVGG YERPFAQIKV 420
TKELKQYDNK IIECKFENNS WVFMRQRTDK SFPNAYNTAM AVCNSISNPV TKEMLFEFID 480
RCTAASQGQK RKHHLDPDTE LMPPPPPKRP RPLT 514 
Gene Ontology
 GO:0005634; C:nucleus; IEA:InterPro.
 GO:0004484; F:mRNA guanylyltransferase activity; IEA:InterPro.
 GO:0004651; F:polynucleotide 5'-phosphatase activity; IEA:InterPro.
 GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
 GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
 GO:0006370; P:7-methylguanosine mRNA capping; IEA:InterPro.
 GO:0035335; P:peptidyl-tyrosine dephosphorylation; IEA:GOC. 
Interpro
 IPR000340; Dual-sp_phosphatase_cat-dom.
 IPR017074; mRNA_cap_enz_bifunc.
 IPR001339; mRNA_cap_enzyme.
 IPR013846; mRNA_cap_enzyme_C.
 IPR012340; NA-bd_OB-fold.
 IPR000387; Tyr/Dual-sp_Pase.
 IPR016130; Tyr_Pase_AS. 
Pfam
 PF00782; DSPc
 PF03919; mRNA_cap_C
 PF01331; mRNA_cap_enzyme 
SMART
  
PROSITE
 PS00383; TYR_PHOSPHATASE_1
 PS50056; TYR_PHOSPHATASE_2 
PRINTS