CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021533
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Queuine tRNA-ribosyltransferase subunit QTRTD1 
Protein Synonyms/Alias
 Queuine tRNA-ribosyltransferase domain-containing protein 1 
Gene Name
 QTRTD1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
128RVEMTVSKFMAIQKAubiquitination[1]
134SKFMAIQKALQPDWFubiquitination[1]
152SDGEVSCKEATSIKRubiquitination[1]
186EESEVLQKSVIIGVIubiquitination[2]
211RSARETAKRPVGGFLubiquitination[1, 3, 4, 5, 6, 7]
247TAELPEDKPRLISGVubiquitination[1, 4, 8]
339EINLKEKKYQEDFNPubiquitination[1, 4]
402REALKSDKLAQLKELubiquitination[4]
407SDKLAQLKELIHRQAubiquitination[4]
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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] 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
 Interacts with QTRT1 to form an active queuine tRNA- ribosyltransferase. This enzyme exchanges queuine for the guanine at the wobble position of tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), thereby forming the hypermodified nucleoside queuosine (Q) (7-(((4,5-cis-dihydroxy-2-cyclopenten-1- yl)amino)methyl)-7-deazaguanosine) (By similarity). 
Sequence Annotation
 ACT_SITE 272 272 Nucleophile (By similarity).
 METAL 351 351 Zinc (By similarity).
 METAL 353 353 Zinc (By similarity).
 METAL 356 356 Zinc (By similarity).
 METAL 382 382 Zinc (By similarity).  
Keyword
 Alternative splicing; Complete proteome; Cytoplasm; Glycosyltransferase; Metal-binding; Mitochondrion; Queuosine biosynthesis; Reference proteome; Transferase; tRNA processing; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 415 AA 
Protein Sequence
MKLSLTKVVN GCRLGKIKNL GKTGDHTMDI PGCLLYTKTG SAPHLTHHTL HNIHGVPAMA 60
QLTLSSLAEH HEVLTEYKEG VGKFIGMPES LLYCSLHDPV SPCPAGYVTN KSVSVWSVAG 120
RVEMTVSKFM AIQKALQPDW FQCLSDGEVS CKEATSIKRV RKSVDRSLLF LDNCLRLQEE 180
SEVLQKSVII GVIEGGDVME ERLRSARETA KRPVGGFLLD GFQGNPTTLE ARLRLLSSVT 240
AELPEDKPRL ISGVSRPDEV LECIERGVDL FESFFPYQVT ERGCALTFSF DYQPNPEETL 300
LQQNGTQEEI KCMDQIKKIE TTGCNQEITS FEINLKEKKY QEDFNPLVRG CSCYCCKNHT 360
RAYIHHLLVT NELLAGVLLM MHNFEHYFGF FHYIREALKS DKLAQLKELI HRQAS 415 
Gene Ontology
 GO:0005739; C:mitochondrion; ISS:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0008479; F:queuine tRNA-ribosyltransferase activity; IEA:EC.
 GO:0008616; P:queuosine biosynthetic process; ISS:UniProtKB. 
Interpro
 IPR002616; tRNA_ribo_trans-like. 
Pfam
 PF01702; TGT 
SMART
  
PROSITE
  
PRINTS