QTRT1

Functionⁱ

Catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GU_N anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine) (PubMed:11255023, PubMed:20354154).

Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming queuine, allowing a nucleophilic attack on the C1' of the ribose to form the product (By similarity).

UniRule annotationBy similarity2 Publications

Catalytic activityⁱ

guanosine³⁴ in tRNA
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
+
queuine
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
=
guanine
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
queuosine³⁴ in tRNA
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
UniRule annotation
Manual assertion according to rulesⁱ
- HAMAP-Rule:MF_03218
1 Publication
Manual assertion based on experiment inⁱ
- Ref.5
  "Characterization of the human tRNA-guanine transglycosylase: confirmation of the heterodimeric subunit structure."
  Chen Y.C., Kelly V.P., Stachura S.V., Garcia G.A.
  RNA 16:958-968(2010) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF ASP-279, IDENTIFICATION BY MASS SPECTROMETRY.
EC:
2.4.2.64
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
- Search reactions for this EC number in Rhea.
UniRule annotation
Manual assertion according to rulesⁱ
- HAMAP-Rule:MF_03218
1 Publication
Manual assertion based on experiment inⁱ
- Ref.5
  "Characterization of the human tRNA-guanine transglycosylase: confirmation of the heterodimeric subunit structure."
  Chen Y.C., Kelly V.P., Stachura S.V., Garcia G.A.
  RNA 16:958-968(2010) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF ASP-279, IDENTIFICATION BY MASS SPECTROMETRY.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
guanosine³⁴ in tRNA
GMP residue
zoom
+
queuine
zoom
=
guanine
zoom
+
queuosine³⁴ in tRNA
queuosine 5'-phosphate residue
zoom

Cofactorⁱ

Zn²⁺UniRule annotation1 Publication

Kineticsⁱ

kcat is 0.0056 sec(-1) with tRNA(Tyr) as substrate and 0.00586 sec(-1) with guanine as substrate.1 Publication

Sites

Feature key	Position(s)	DescriptionActions	Length
Active siteⁱ	105	Proton acceptorUniRule annotation	1
Binding siteⁱ	159	SubstrateUniRule annotationCombined sources1 Publication	1
Binding siteⁱ	202	SubstrateUniRule annotation	1
Binding siteⁱ	229	Substrate; via amide nitrogenUniRule annotationCombined sources1 Publication	1
Active siteⁱ	279	NucleophileUniRule annotation	1
Metal bindingⁱ	317	ZincUniRule annotationCombined sources1 Publication	1
Metal bindingⁱ	319	ZincUniRule annotationCombined sources1 Publication	1
Metal bindingⁱ	322	ZincUniRule annotationCombined sources1 Publication	1
Metal bindingⁱ	348	Zinc; via pros nitrogenUniRule annotationCombined sources1 Publication	1

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Glycosyltransferase, Transferase
Biological process	tRNA processing
Ligand	Metal-binding, Zinc

Enzyme and pathway databases

BioCycⁱ	MetaCyc:HS05270-MONOMER
BRENDAⁱ	2.4.2.29, 2681
PathwayCommonsⁱ	Q9BXR0
Reactomeⁱ	R-HSA-6782315, tRNA modification in the nucleus and cytosol

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Queuine tRNA-ribosyltransferase catalytic subunit 1UniRule annotation (EC:2.4.2.64UniRule annotation1 Publication) Alternative name(s): Guanine insertion enzymeUniRule annotation tRNA-guanine transglycosylaseUniRule annotation
Gene namesⁱ	Name:QTRT1UniRule annotation Synonyms:TGT, TGUT
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 19

Organism-specific databases

Human Gene Nomenclature Database More...HGNCⁱ	HGNC:23797, QTRT1
MIMⁱ	609615, gene
neXtProtⁱ	NX_Q9BXR0
VEuPathDBⁱ	HostDB:ENSG00000213339

Keywords - Cellular componentⁱ

Cytoplasm, Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Mutagenesisⁱ	279	D → N: Loss of transglycosylase activity. 1 Publication		1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	81890
Open Targets More...OpenTargetsⁱ	ENSG00000213339
PharmGKBⁱ	PA134963074

Miscellaneous databases

Pharosⁱ	Q9BXR0, Tbio

Pharosⁱ

Q9BXR0, Tbio

Chemistry databases

ChEMBLⁱ	CHEMBL6004

ChEMBLⁱ

CHEMBL6004

Genetic variation databases

BioMutaⁱ	QTRT1
DMDMⁱ	239938842

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Initiator methionineⁱ		RemovedCombined sources
ChainⁱPRO_0000135565	2 – 403	Queuine tRNA-ribosyltransferase catalytic subunit 1Add BLAST		402

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Modified residueⁱ	2	N-acetylalanineCombined sources		1
Modified residueⁱ	139	PhosphoserineCombined sources		1

Keywords - PTMⁱ

Acetylation, Phosphoprotein

Proteomic databases

EPDⁱ	Q9BXR0
jPOSTⁱ	Q9BXR0
MassIVEⁱ	Q9BXR0
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q9BXR0
PaxDbⁱ	Q9BXR0
PeptideAtlas More...PeptideAtlasⁱ	Q9BXR0
PRIDEⁱ	Q9BXR0
ProteomicsDBⁱ	4060 79483 [Q9BXR0-1]

PTM databases

iPTMnetⁱ	Q9BXR0
PhosphoSitePlusⁱ	Q9BXR0

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSG00000213339, Expressed in body of pancreas and 192 other tissues
ExpressionAtlasⁱ	Q9BXR0, baseline and differential
Genevisibleⁱ	Q9BXR0, HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	ENSG00000213339, Low tissue specificity

HPAⁱ

ENSG00000213339, Low tissue specificity

Interactionⁱ

Subunit structureⁱ

Heterodimer of a catalytic subunit QTRT1 and an accessory subunit QTRT2.

UniRule annotation2 Publications

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGRIDⁱ	123623, 22 interactors
IntActⁱ	Q9BXR0, 17 interactors
STRINGⁱ	9606.ENSP00000250237

Chemistry databases

BindingDBⁱ

Q9BXR0

Miscellaneous databases

RNActⁱ	Q9BXR0, protein

RNActⁱ

Q9BXR0, protein

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	16 – 22	Combined sources	7
Beta strandⁱ	24 – 26	Combined sources	3
Beta strandⁱ	29 – 35	Combined sources	7
Beta strandⁱ	38 – 45	Combined sources	8
Beta strandⁱ	54 – 56	Combined sources	3
Helixⁱ	59 – 64	Combined sources	6
Beta strandⁱ	69 – 71	Combined sources	3
Beta strandⁱ	77 – 82	Combined sources	6
Helixⁱ	91 – 96	Combined sources	6
Beta strandⁱ	100 – 104	Combined sources	5
Helixⁱ	108 – 114	Combined sources	7
Beta strandⁱ	125 – 128	Combined sources	4
Beta strandⁱ	130 – 132	Combined sources	3
Beta strandⁱ	135 – 138	Combined sources	4
Helixⁱ	140 – 150	Combined sources	11
Beta strandⁱ	153 – 156	Combined sources	4
Helixⁱ	169 – 187	Combined sources	19
Turnⁱ	192 – 194	Combined sources	3
Beta strandⁱ	196 – 201	Combined sources	6
Helixⁱ	207 – 217	Combined sources	11
Beta strandⁱ	223 – 227	Combined sources	5
Beta strandⁱ	231 – 233	Combined sources	3
Helixⁱ	236 – 249	Combined sources	14
Beta strandⁱ	256 – 259	Combined sources	4
Helixⁱ	264 – 272	Combined sources	9
Beta strandⁱ	277 – 279	Combined sources	3
Helixⁱ	282 – 288	Combined sources	7
Beta strandⁱ	291 – 294	Combined sources	4
Beta strandⁱ	297 – 300	Combined sources	4
Helixⁱ	304 – 306	Combined sources	3
Helixⁱ	320 – 324	Combined sources	5
Helixⁱ	327 – 336	Combined sources	10
Helixⁱ	338 – 365	Combined sources	28
Helixⁱ	369 – 381	Combined sources	13
Helixⁱ	384 – 386	Combined sources	3
Helixⁱ	389 – 397	Combined sources	9

Show more details

3D structure databases

SMRⁱ	Q9BXR0
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	105 – 109	Substrate bindingUniRule annotationCombined sources1 Publication	5
Regionⁱ	260 – 266	RNA bindingUniRule annotation	7
Regionⁱ	284 – 288	RNA binding; important for wobble base 34 recognitionUniRule annotation	5

Sequence similaritiesⁱ

Belongs to the queuine tRNA-ribosyltransferase family.UniRule annotation

Phylogenomic databases

eggNOGⁱ	KOG3908, Eukaryota
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00530000063679
HOGENOMⁱ	CLU_022060_0_1_1
InParanoidⁱ	Q9BXR0
OMAⁱ	GIDLFDC
PhylomeDBⁱ	Q9BXR0
TreeFamⁱ	TF300732

Family and domain databases

Gene3Dⁱ	3.20.20.105, 1 hit
HAMAPⁱ	MF_00168, Q_tRNA_Tgt, 1 hit
InterProⁱ	View protein in InterPro IPR004803, TGT IPR036511, TGT-like_sf IPR002616, tRNA_ribo_trans-like
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF01702, TGT, 1 hit
SUPFAMⁱ	SSF51713, SSF51713, 1 hit
TIGRFAMsⁱ	TIGR00430, Q_tRNA_tgt, 1 hit TIGR00449, tgt_general, 1 hit

Sequences (2+)ⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 2 described isoforms and 4 potential isoforms that are computationally mapped.Show all Align All

Isoform 1 (identifier: Q9BXR0-1) [UniParc]FASTA Add to basket

This isoform has been chosen as the canonicalⁱ sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAGAATQASL ESAPRIMRLV AECSRSRARA GELWLPHGTV ATPVFMPVGT 
        60         70         80         90        100
QATMKGITTE QLDALGCRIC LGNTYHLGLR PGPELIQKAN GLHGFMNWPH 
       110        120        130        140        150
NLLTDSGGFQ MVSLVSLSEV TEEGVRFRSP YDGNETLLSP EKSVQIQNAL 
       160        170        180        190        200
GSDIIMQLDD VVSSTVTGPR VEEAMYRSIR WLDRCIAAHQ RPDKQNLFAI 
       210        220        230        240        250
IQGGLDADLR ATCLEEMTKR DVPGFAIGGL SGGESKSQFW RMVALSTSRL 
       260        270        280        290        300
PKDKPRYLMG VGYATDLVVC VALGCDMFDC VFPTRTARFG SALVPTGNLQ 
       310        320        330        340        350
LRKKVFEKDF GPIDPECTCP TCQKHSRAFL HALLHSDNTA ALHHLTVHNI 
       360        370        380        390        400
AYQLQLMSAV RTSIVEKRFP DFVRDFMGAM YGDPTLCPTW ATDALASVGI 

TLG

Length:403

Mass (Da):44,048

Last modified:June 16, 2009 - v3

Checksum:ⁱ1E30F3C7BF47A106

GO

Isoform 2 (identifier: Q9BXR0-2) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
178-225: SIRWLDRCIA...EMTKRDVPGF → PLGLVTGALL...AGRRSPGHLP
226-403: Missing.

« Hide

        10         20         30         40         50
MAGAATQASL ESAPRIMRLV AECSRSRARA GELWLPHGTV ATPVFMPVGT 
        60         70         80         90        100
QATMKGITTE QLDALGCRIC LGNTYHLGLR PGPELIQKAN GLHGFMNWPH 
       110        120        130        140        150
NLLTDSGGFQ MVSLVSLSEV TEEGVRFRSP YDGNETLLSP EKSVQIQNAL 
       160        170        180        190        200
GSDIIMQLDD VVSSTVTGPR VEEAMYRPLG LVTGALLQVN PLAGPVHCSP 
       210        220 
SAAGQAEPLR HYPGWAGRRS PGHLP

Show »

Length:225

Mass (Da):24,015

Checksum:ⁱC62B238F305E24A9

GO

Computationally mapped potential isoform sequencesⁱ

There are 4 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

K7EPI1	K7EPI1_HUMAN	Queuine tRNA-ribosyltransferase cat... Queuine tRNA-ribosyltransferase catalytic subunit 1	QTRT1	124	Annotation score:
K7EL95	K7EL95_HUMAN	Queuine tRNA-ribosyltransferase cat... Queuine tRNA-ribosyltransferase catalytic subunit 1	QTRT1	136	Annotation score:
K7ESP6	K7ESP6_HUMAN	Queuine tRNA-ribosyltransferase cat... Queuine tRNA-ribosyltransferase catalytic subunit 1	QTRT1	180	Annotation score:
K7EJ21	K7EJ21_HUMAN	Queuine tRNA-ribosyltransferase cat... Queuine tRNA-ribosyltransferase catalytic subunit 1	QTRT1	203	Annotation score:

Sequence cautionⁱ

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

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_056470	178 – 225	SIRWL…DVPGF → PLGLVTGALLQVNPLAGPVH CSPSAAGQAEPLRHYPGWAG RRSPGHLP in isoform 2. 1 PublicationAdd BLAST		48
Alternative sequenceⁱVSP_056471	226 – 403	Missing in isoform 2. 1 PublicationAdd BLAST		178

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF302783 mRNA Translation: AAG60033.1 AF302784 mRNA Translation: AAG60034.1 AK294166 mRNA Translation: BAG57488.1 AC011475 Genomic DNA No translation available. BC015350 mRNA Translation: AAH15350.1 Different initiation.
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS12248.1 [Q9BXR0-1]
NCBI Reference Sequences More...RefSeqⁱ	NP_112486.1, NM_031209.2 [Q9BXR0-1]

Genome annotation databases

Ensemblⁱ	ENST00000250237; ENSP00000250237; ENSG00000213339 [Q9BXR0-1] ENST00000421333; ENSP00000389126; ENSG00000213339 [Q9BXR0-2]
GeneIDⁱ	81890
KEGGⁱ	hsa:81890
UCSC genome browser More...UCSCⁱ	uc002mpr.4, human [Q9BXR0-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q9BXR0	Queuine tRNA-ribosyltransferase catalytic subunit 1		PANTR		403	UniRef100_Q9BXR0
Queuine tRNA-ribosyltransferase catalytic subunit 1		PANPA		403
Queuine tRNA-ribosyltransferase catalytic subunit 1		PANTR		403
+2
Q9BXR0-2	QTRT1 isoform 1		PANTR		225	UniRef100_A0A2J8LWE6

Protein	Similar proteins		Species	Score	Length	Source
Q9BXR0	Queuine tRNA-ribosyltransferase catalytic subunit 1		PANTR		403	UniRef90_Q9BXR0
Queuine tRNA-ribosyltransferase catalytic subunit 1		PANPA		403
Queuine tRNA-ribosyltransferase catalytic subunit 1		RHIBE		412
Queuine tRNA-ribosyltransferase catalytic subunit 1		RHIRO		403
Queuine tRNA-ribosyltransferase catalytic subunit 1		COLAP		403
+116
Q9BXR0-2	QTRT1 isoform 1		PANTR		225	UniRef90_A0A2J8LWE6
QTRT1 isoform 1		PONAB		225

Protein	Similar proteins		Species	Score	Length	Source
Q9BXR0	Queuine tRNA-ribosyltransferase catalytic subunit 1	)	MOUSE		403	UniRef50_Q9BXR0
Queuine tRNA-ribosyltransferase catalytic subunit 1		RAT		403
Queuine tRNA-ribosyltransferase catalytic subunit 1		DANRE		400
Queuine tRNA-ribosyltransferase catalytic subunit 1		XENTR		396
Queuine tRNA-ribosyltransferase catalytic subunit 1		XENLA		396
+610
Q9BXR0-2	QTRT1 isoform 1		PANTR		225	UniRef50_A0A2J8LWE6
QTRT1 isoform 1		PONAB		225
TGT (Fragment)		blackstripe livebearer		279

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF302783 mRNA Translation: AAG60033.1 AF302784 mRNA Translation: AAG60034.1 AK294166 mRNA Translation: BAG57488.1 AC011475 Genomic DNA No translation available. BC015350 mRNA Translation: AAH15350.1 Different initiation.
CCDSⁱ	CCDS12248.1 [Q9BXR0-1]
RefSeqⁱ	NP_112486.1, NM_031209.2 [Q9BXR0-1]

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	6H42	X-ray	2.45	A/B	11-403	[»]
	6H45	X-ray	2.40	A/B	12-403	[»]
SMRⁱ	Q9BXR0
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

BioGRIDⁱ	123623, 22 interactors
IntActⁱ	Q9BXR0, 17 interactors
STRINGⁱ	9606.ENSP00000250237

Chemistry databases

BindingDBⁱ	Q9BXR0
ChEMBLⁱ	CHEMBL6004

PTM databases

iPTMnetⁱ	Q9BXR0
PhosphoSitePlusⁱ	Q9BXR0

Genetic variation databases

BioMutaⁱ	QTRT1
DMDMⁱ	239938842

Proteomic databases

EPDⁱ	Q9BXR0
jPOSTⁱ	Q9BXR0
MassIVEⁱ	Q9BXR0
MaxQBⁱ	Q9BXR0
PaxDbⁱ	Q9BXR0
PeptideAtlasⁱ	Q9BXR0
PRIDEⁱ	Q9BXR0
ProteomicsDBⁱ	4060 79483 [Q9BXR0-1]

Protocols and materials databases

Antibodypediaⁱ	25490, 155 antibodies
The DNASU plasmid repository More...DNASUⁱ	81890

Genome annotation databases

Ensemblⁱ	ENST00000250237; ENSP00000250237; ENSG00000213339 [Q9BXR0-1] ENST00000421333; ENSP00000389126; ENSG00000213339 [Q9BXR0-2]
GeneIDⁱ	81890
KEGGⁱ	hsa:81890
UCSCⁱ	uc002mpr.4, human [Q9BXR0-1]

Organism-specific databases

CTDⁱ	81890
DisGeNETⁱ	81890
GeneCardsⁱ	QTRT1
HGNCⁱ	HGNC:23797, QTRT1
HPAⁱ	ENSG00000213339, Low tissue specificity
MIMⁱ	609615, gene
neXtProtⁱ	NX_Q9BXR0
OpenTargetsⁱ	ENSG00000213339
PharmGKBⁱ	PA134963074
VEuPathDBⁱ	HostDB:ENSG00000213339
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG3908, Eukaryota
GeneTreeⁱ	ENSGT00530000063679
HOGENOMⁱ	CLU_022060_0_1_1
InParanoidⁱ	Q9BXR0
OMAⁱ	GIDLFDC
PhylomeDBⁱ	Q9BXR0
TreeFamⁱ	TF300732

Enzyme and pathway databases

BioCycⁱ	MetaCyc:HS05270-MONOMER
BRENDAⁱ	2.4.2.29, 2681
PathwayCommonsⁱ	Q9BXR0
Reactomeⁱ	R-HSA-6782315, tRNA modification in the nucleus and cytosol

Miscellaneous databases

BioGRID-ORCSⁱ	81890, 24 hits in 1020 CRISPR screens
ChiTaRSⁱ	QTRT1, human
GenomeRNAiⁱ	81890
Pharosⁱ	Q9BXR0, Tbio
Protein Ontology More...PROⁱ	PR:Q9BXR0
RNActⁱ	Q9BXR0, protein
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000213339, Expressed in body of pancreas and 192 other tissues
ExpressionAtlasⁱ	Q9BXR0, baseline and differential
Genevisibleⁱ	Q9BXR0, HS

Family and domain databases

Gene3Dⁱ	3.20.20.105, 1 hit
HAMAPⁱ	MF_00168, Q_tRNA_Tgt, 1 hit
InterProⁱ	View protein in InterPro IPR004803, TGT IPR036511, TGT-like_sf IPR002616, tRNA_ribo_trans-like
Pfamⁱ	View protein in Pfam PF01702, TGT, 1 hit
SUPFAMⁱ	SSF51713, SSF51713, 1 hit
TIGRFAMsⁱ	TIGR00430, Q_tRNA_tgt, 1 hit TIGR00449, tgt_general, 1 hit
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	TGT_HUMAN
Accessionⁱ	Q9BXR0Primary (citable) accession number: Q9BXR0 Secondary accession number(s): B4DFM7, Q96BQ4, Q9BXQ9
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	May 2, 2002
	Last sequence update:	June 16, 2009
	Last modified:	September 29, 2021
	This is version 172 of the entry and version 3 of the sequence. See complete history.
Entry statusⁱ	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.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Reference proteome

Documents

Human chromosome 19
Human chromosome 19: entries, gene names and cross-references to MIM
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
SIMILARITY comments
Index of protein domains and families

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q9BXR0 (TGT_HUMAN)

Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the 'basket' to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>

Queuine tRNA-ribosyltransferase catalytic subunit 1

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Mitochondrion

Cytoplasm and Cytosol

Mitochondrion

Nucleus

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Organism-specific databases

Miscellaneous databases

Chemistry databases

Genetic variation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

Miscellaneous databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Genetic variation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Your basket is currently empty. ⁱ

Functionⁱ

Catalytic activityⁱ

Kineticsⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequence cautionⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ