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Q9BXR0 (TGT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Queuine tRNA-ribosyltransferase

EC=2.4.2.29
Alternative name(s):
Guanine insertion enzyme
tRNA-guanine transglycosylase
Gene names
Name:QTRT1
Synonyms:TGT, TGUT
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length403 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Interacts with QTRTD1 to form an active queuine tRNA-ribosyltransferase. This enzyme exchanges queuine for the guanine at the wobble position of tRNAs with GUN 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. HAMAP-Rule MF_00168

Catalytic activity

Guanine34 in tRNA + queuine = queuosine34 in tRNA + guanine. HAMAP-Rule MF_00168

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_00168

Pathway

tRNA modification; tRNA-queuosine biosynthesis. HAMAP-Rule MF_00168

Subunit structure

Interacts with QTRTD1 By similarity. HAMAP-Rule MF_00168

Subcellular location

Cytoplasm By similarity. Mitochondrion By similarity. Nucleus By similarity. Note: Weakly associates with mitochondria, possibly via QTRTD1 By similarity. HAMAP-Rule MF_00168

Sequence similarities

Belongs to the queuine tRNA-ribosyltransferase family.

Sequence caution

The sequence AAH15350.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 403402Queuine tRNA-ribosyltransferase HAMAP-Rule MF_00168
PRO_0000135565

Sites

Active site2791Nucleophile By similarity
Metal binding3171Zinc By similarity
Metal binding3191Zinc By similarity
Metal binding3221Zinc By similarity
Metal binding3481Zinc By similarity
Binding site1061Substrate By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q9BXR0 [UniParc].

Last modified June 16, 2009. Version 3.
Checksum: 1E30F3C7BF47A106

FASTA40344,048
        10         20         30         40         50         60 
MAGAATQASL ESAPRIMRLV AECSRSRARA GELWLPHGTV ATPVFMPVGT QATMKGITTE 

        70         80         90        100        110        120 
QLDALGCRIC LGNTYHLGLR PGPELIQKAN GLHGFMNWPH NLLTDSGGFQ MVSLVSLSEV 

       130        140        150        160        170        180 
TEEGVRFRSP YDGNETLLSP EKSVQIQNAL GSDIIMQLDD VVSSTVTGPR VEEAMYRSIR 

       190        200        210        220        230        240 
WLDRCIAAHQ RPDKQNLFAI IQGGLDADLR ATCLEEMTKR DVPGFAIGGL SGGESKSQFW 

       250        260        270        280        290        300 
RMVALSTSRL PKDKPRYLMG VGYATDLVVC VALGCDMFDC VFPTRTARFG SALVPTGNLQ 

       310        320        330        340        350        360 
LRKKVFEKDF GPIDPECTCP TCQKHSRAFL HALLHSDNTA ALHHLTVHNI AYQLQLMSAV 

       370        380        390        400 
RTSIVEKRFP DFVRDFMGAM YGDPTLCPTW ATDALASVGI TLG 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of cDNA encoding the human tRNA-guanine transglycosylase (TGT) catalytic subunit."
Deshpande K.L., Katze J.R.
Gene 265:205-212(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Spleen.
[2]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-403.
Tissue: Brain.
[4]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[5]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF302783 mRNA. Translation: AAG60033.1.
AF302784 mRNA. Translation: AAG60034.1.
AC011475 Genomic DNA. No translation available.
BC015350 mRNA. Translation: AAH15350.1. Different initiation.
CCDSCCDS12248.1.
RefSeqNP_112486.1. NM_031209.2.
UniGeneHs.631638.

3D structure databases

ProteinModelPortalQ9BXR0.
SMRQ9BXR0. Positions 27-376.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123623. 8 interactions.
IntActQ9BXR0. 7 interactions.
MINTMINT-4656737.
STRING9606.ENSP00000250237.

Chemistry

BindingDBQ9BXR0.
ChEMBLCHEMBL6004.

PTM databases

PhosphoSiteQ9BXR0.

Polymorphism databases

DMDM239938842.

Proteomic databases

MaxQBQ9BXR0.
PaxDbQ9BXR0.
PRIDEQ9BXR0.

Protocols and materials databases

DNASU81890.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000250237; ENSP00000250237; ENSG00000213339.
GeneID81890.
KEGGhsa:81890.
UCSCuc002mpr.3. human.

Organism-specific databases

CTD81890.
GeneCardsGC19P010812.
HGNCHGNC:23797. QTRT1.
HPAHPA048651.
HPA049440.
MIM609615. gene.
neXtProtNX_Q9BXR0.
PharmGKBPA134963074.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0343.
HOGENOMHOG000223473.
HOVERGENHBG101131.
InParanoidQ9BXR0.
KOK00773.
OMASSCCAPF.
OrthoDBEOG7W41BR.
PhylomeDBQ9BXR0.
TreeFamTF300732.

Enzyme and pathway databases

UniPathwayUPA00392.

Gene expression databases

ArrayExpressQ9BXR0.
BgeeQ9BXR0.
CleanExHS_QTRT1.
GenevestigatorQ9BXR0.

Family and domain databases

Gene3D3.20.20.105. 1 hit.
HAMAPMF_00168. Q_tRNA_Tgt.
InterProIPR004803. Queuine_tRNA-ribosylTrfase.
IPR002616. tRNA_ribo_trans-like.
[Graphical view]
PANTHERPTHR11962. PTHR11962. 1 hit.
PfamPF01702. TGT. 1 hit.
[Graphical view]
SUPFAMSSF51713. SSF51713. 1 hit.
TIGRFAMsTIGR00430. Q_tRNA_tgt. 1 hit.
TIGR00449. tgt_general. 1 hit.
ProtoNetSearch...

Other

ChiTaRSQTRT1. human.
GenomeRNAi81890.
NextBio72242.
PROQ9BXR0.
SOURCESearch...

Entry information

Entry nameTGT_HUMAN
AccessionPrimary (citable) accession number: Q9BXR0
Secondary accession number(s): Q96BQ4, Q9BXQ9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: June 16, 2009
Last modified: July 9, 2014
This is version 116 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM