CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022339
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 tRNA (guanine(26)-N(2))-dimethyltransferase 
Protein Synonyms/Alias
 tRNA 2,2-dimethylguanosine-26 methyltransferase; tRNA(guanine-26,N(2)-N(2)) methyltransferase; tRNA(m(2,2)G26)dimethyltransferase 
Gene Name
 TRMT1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
100ARIQLGAKGIQIKVPubiquitination[1]
105GAKGIQIKVPGEKDTubiquitination[2]
130EEEKVELKESENLASubiquitination[2]
283KYGAMALKSRACHEMubiquitination[1]
371GVPSGRAKFSAACGPubiquitination[1]
483VSLSHACKNAVKTDAubiquitination[1, 3]
487HACKNAVKTDAPASAubiquitination[1, 2, 3, 4, 5, 6]
504DIMRCWEKECPVKREubiquitination[1]
570PRARPGGKAADEAMEubiquitination[1]
588RLLQNKRKEPPEDVAubiquitination[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] 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]
 [3] 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]
 [4] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [5] 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]
 [6] 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
 Dimethylates a single guanine residue at position 26 of most tRNAs using S-adenosyl-L-methionine as donor of the methyl groups. 
Sequence Annotation
 ZN_FING 600 627 C3H1-type.
 MOD_RES 120 120 Phosphoserine (By similarity).
 MOD_RES 625 625 Phosphoserine.
 MOD_RES 628 628 Phosphothreonine.
 MOD_RES 646 646 Phosphothreonine.  
Keyword
 Alternative splicing; Complete proteome; Metal-binding; Methyltransferase; Phosphoprotein; Reference proteome; S-adenosyl-L-methionine; Transferase; tRNA processing; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 659 AA 
Protein Sequence
MQGSSLWLSL TFRSARVLSR ARFFEWQSPG LPNTAAMENG TGPYGEERPR EVQETTVTEG 60
AAKIAFPSAN EVFYNPVQEF NRDLTCAVIT EFARIQLGAK GIQIKVPGEK DTQKVVVDLS 120
EQEEEKVELK ESENLASGDQ PRTAAVGEIC EEGLHVLEGL AASGLRSIRF ALEVPGLRSV 180
VANDASTRAV DLIRRNVQLN DVAHLVQPSQ ADARMLMYQH QRVSERFDVI DLDPYGSPAT 240
FLDAAVQAVS EGGLLCVTCT DMAVLAGNSG ETCYSKYGAM ALKSRACHEM ALRIVLHSLD 300
LRANCYQRFV VPLLSISADF YVRVFVRVFT GQAKVKASAS KQALVFQCVG CGAFHLQRLG 360
KASGVPSGRA KFSAACGPPV TPECEHCGQR HQLGGPMWAE PIHDLDFVGR VLEAVSANPG 420
RFHTSERIRG VLSVITEELP DVPLYYTLDQ LSSTIHCNTP SLLQLRSALL HADFRVSLSH 480
ACKNAVKTDA PASALWDIMR CWEKECPVKR ERLSETSPAF RILSVEPRLQ ANFTIREDAN 540
PSSRQRGLKR FQANPEANWG PRPRARPGGK AADEAMEERR RLLQNKRKEP PEDVAQRAAR 600
LKTFPCKRFK EGTCQRGDQC CYSHSPPTPR VSADAAPDCP ETSNQTPPGP GAAAGPGID 659 
Gene Ontology
 GO:0003723; F:RNA binding; IEA:InterPro.
 GO:0004809; F:tRNA (guanine-N2-)-methyltransferase activity; IEA:InterPro.
 GO:0008270; F:zinc ion binding; IEA:InterPro. 
Interpro
 IPR002905; TRM1.
 IPR000571; Znf_CCCH. 
Pfam
 PF02005; TRM
 PF00642; zf-CCCH 
SMART
 SM00356; ZnF_C3H1 
PROSITE
 PS50103; ZF_C3H1 
PRINTS