Q9BXR0 (TGT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	403 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
Catalytic activity	Guanine34 in tRNA + queuine = queuosine34 in tRNA + guanine.
Cofactor	Binds 1 zinc ion per subunit By similarity.
Pathway	tRNA modification; tRNA-queuosine biosynthesis.
Subunit structure	Interacts with QTRTD1 By similarity.
Subcellular location	Cytoplasm By similarity. Mitochondrion By similarity. Nucleus By similarity. Note: Weakly associates with mitochondria, possibly via QTRTD1 By similarity.
Sequence similarities	Belongs to the queuine tRNA-ribosyltransferase family.
Sequence caution	The sequence AAH15350.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Queuosine biosynthesis tRNA processing
Cellular component	Cytoplasm Mitochondrion Nucleus
Ligand	Metal-binding Zinc
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	queuosine biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell ribosome Non-traceable author statement. Source: UniProtKB
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW queuine tRNA-ribosyltransferase activity Traceable author statement Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 403	403	Queuine tRNA-ribosyltransferase		PRO_0000135565
Sites
	Active site	279	1	Nucleophile By similarity
	Metal binding	317	1	Zinc By similarity
	Metal binding	319	1	Zinc By similarity
	Metal binding	322	1	Zinc By similarity
	Metal binding	348	1	Zinc By similarity
	Binding site	106	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9BXR0 [UniParc]. Last modified June 16, 2009. Version 3. Checksum: 1E30F3C7BF47A106	FASTA	403	44,048
	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

References

	« Hide 'large scale' referencesShow '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. , 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].
+	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.
IPI	IPI00215974.
RefSeq	NP_112486.1. NM_031209.2.
UniGene	Hs.631638.
3D structure databases
ProteinModelPortal	Q9BXR0.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9BXR0. 7 interactions.
MINT	MINT-4656737.
STRING	9606.ENSP00000250237.
PTM databases
PhosphoSite	Q9BXR0.
Polymorphism databases
DMDM	239938842.
Proteomic databases
PaxDb	Q9BXR0.
PRIDE	Q9BXR0.
Protocols and materials databases
DNASU	81890.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000250237; ENSP00000250237; ENSG00000213339.
GeneID	81890.
KEGG	hsa:81890.
UCSC	uc002mpr.3. human.
Organism-specific databases
CTD	81890.
GeneCards	GC19P010812.
HGNC	HGNC:23797. QTRT1.
HPA	HPA048651. HPA049440.
MIM	609615. gene.
neXtProt	NX_Q9BXR0.
PharmGKB	PA134963074.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0343.
HOGENOM	HOG000223473.
HOVERGEN	HBG101131.
InParanoid	Q9BXR0.
KO	K00773.
OMA	MSPERSI.
OrthoDB	EOG4THVT7.
PhylomeDB	Q9BXR0.
Enzyme and pathway databases
UniPathway	UPA00392.
Gene expression databases
ArrayExpress	Q9BXR0.
Bgee	Q9BXR0.
CleanEx	HS_QTRT1.
Genevestigator	Q9BXR0.
GermOnline	ENSG00000079805. Homo sapiens.
Family and domain databases
Gene3D	3.20.20.105. 1 hit.
InterPro	IPR004803. Queuine_tRNA-ribosylTrfase. IPR002616. tRNA_ribo_trans-like. [Graphical view]
PANTHER	PTHR11962. PTHR11962. 1 hit.
Pfam	PF01702. TGT. 1 hit. [Graphical view]
SUPFAM	SSF51713. tRNA_ribo_trans. 1 hit.
TIGRFAMs	TIGR00430. Q_tRNA_tgt. 1 hit. TIGR00449. tgt_general. 1 hit.
ProtoNet	Search...
Other
BindingDB	Q9BXR0.
ChEMBL	CHEMBL6004.
ChiTaRS	QTRT1. human.
GenomeRNAi	81890.
NextBio	72242.
SOURCE	Search...

Entry information

Entry name

TGT_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 106 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.