CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022288
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Probable tRNA(His) guanylyltransferase 
Protein Synonyms/Alias
 Interphase cytoplasmic foci protein 45; tRNA-histidine guanylyltransferase 
Gene Name
 THG1L 
Gene Synonyms/Alias
 ICF45 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
68NFHRFAEKHNFAKPNacetylation[1]
119KRKTNWFKRRASKFMubiquitination[2, 3]
170YPSNQTLKDYLSWRQubiquitination[4]
252KVDEVMTKEIKLPTEubiquitination[5]
263LPTEMEGKKMAVTRTacetylation[6, 7, 8, 9]
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] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
 Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
 J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330]
 [7] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [8] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [9] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302
Functional Description
 Adds a GMP to the 5'-end of tRNA(His) after transcription and RNase P cleavage. This step is essential for proper recognition of the tRNA and for the fidelity of protein synthesis. 
Sequence Annotation
 NP_BIND 58 63 GTP.
 NP_BIND 104 105 GTP.
 METAL 58 58 Magnesium 1; catalytic.
 METAL 58 58 Magnesium 2; catalytic.
 METAL 59 59 Magnesium 1; via carbonyl oxygen;
 METAL 105 105 Magnesium 1; catalytic.
 METAL 105 105 Magnesium 2; catalytic.
 MOD_RES 251 251 Phosphothreonine (By similarity).  
Keyword
 3D-structure; Complete proteome; Cytoplasm; GTP-binding; Magnesium; Metal-binding; Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein; Polymorphism; Reference proteome; Transferase; tRNA processing. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 298 AA 
Protein Sequence
MWGACKVKVH DSLATISITL RRYLRLGATM AKSKFEYVRD FEADDTCLAH CWVVVRLDGR 60
NFHRFAEKHN FAKPNDSRAL QLMTKCAQTV MEELEDIVIA YGQSDEYSFV FKRKTNWFKR 120
RASKFMTHVA SQFASSYVFY WRDYFEDQPL LYPPGFDGRV VVYPSNQTLK DYLSWRQADC 180
HINNLYNTVF WALIQQSGLT PVQAQGRLQG TLAADKNEIL FSEFNINYNN ELPMYRKGTV 240
LIWQKVDEVM TKEIKLPTEM EGKKMAVTRT RTKPVPLHCD IIGDAFWKEH PEILDEDS 298 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:LIFEdb.
 GO:0005524; F:ATP binding; IDA:BHF-UCL.
 GO:0005525; F:GTP binding; IDA:BHF-UCL.
 GO:0000287; F:magnesium ion binding; IDA:BHF-UCL.
 GO:0000049; F:tRNA binding; TAS:BHF-UCL.
 GO:0008193; F:tRNA guanylyltransferase activity; IDA:UniProtKB.
 GO:0051289; P:protein homotetramerization; IPI:UniProtKB.
 GO:0006400; P:tRNA modification; ISS:UniProtKB. 
Interpro
 IPR025845; Thg1_C_dom.
 IPR024956; tRNAHis_GuaTrfase_cat.
 IPR007537; tRNAHis_GuaTrfase_Thg1. 
Pfam
 PF04446; Thg1
 PF14413; Thg1C 
SMART
  
PROSITE
  
PRINTS