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Q9NWX6 (THG1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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:
Probable tRNA(His) guanylyltransferase

EC=2.7.7.79
Alternative name(s):
Interphase cytoplasmic foci protein 45
tRNA-histidine guanylyltransferase
Gene names
Name:THG1L
Synonyms:ICF45
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length298 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Adds a GMP to the 5'-end of tRNA(His) after transcription and RNase P cleavage. This step is essential for proper recognition of the tRNA and for the fidelity of protein synthesis. Ref.9

Catalytic activity

p-tRNA(His) + ATP + GTP = pppG-P-tRNA(His) + AMP + diphosphate.

Cofactor

Binds 2 magnesium ions per subunit. Ref.9

Subunit structure

Homotetramer. Ref.9

Subcellular location

Cytoplasm. Note: Found near the nuclear membrane. Ref.1

Tissue specificity

Expressed in many tissues. Ref.1

Sequence similarities

Belongs to the tRNA(His) guanylyltransferase family.

Sequence caution

The sequence AAH01523.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAH01852.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 298298Probable tRNA(His) guanylyltransferase
PRO_0000284984

Regions

Nucleotide binding58 – 636GTP
Nucleotide binding104 – 1052GTP

Sites

Metal binding581Magnesium 1; catalytic
Metal binding581Magnesium 2; catalytic
Metal binding591Magnesium 1; via carbonyl oxygen; catalytic
Metal binding1051Magnesium 1; catalytic
Metal binding1051Magnesium 2; catalytic

Natural variations

Natural variant2321L → P. Ref.3 Ref.5 Ref.6 Ref.7
Corresponds to variant rs2270812 [ dbSNP | Ensembl ].
VAR_031871

Experimental info

Mutagenesis581D → A: Reduces activity by 99.5%. Ref.9
Mutagenesis631H → A: Slightly reduced enzyme activity. Ref.9
Mutagenesis1041S → A: Slightly reduced enzyme activity. Ref.9
Mutagenesis1051D → A: Loss of enzyme activity. Ref.9
Mutagenesis1061E → A: Reduces activity by 95%. Ref.9
Mutagenesis1271T → A: Abolishes oligomerization. Loss of enzyme activity. Ref.9
Mutagenesis1811H → A: Loss of enzyme activity. Ref.9
Mutagenesis2161K → A: Reduces activity by 98.5%. Ref.9
Mutagenesis2271N → A: Loss of enzyme activity. Ref.9
Sequence conflict571L → Q in BAD96839. Ref.5

Secondary structure

........................................ 298
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9NWX6 [UniParc].

Last modified May 1, 2007. Version 2.
Checksum: A6C941B75611C448

FASTA29834,831
        10         20         30         40         50         60 
MWGACKVKVH DSLATISITL RRYLRLGATM AKSKFEYVRD FEADDTCLAH CWVVVRLDGR 

        70         80         90        100        110        120 
NFHRFAEKHN FAKPNDSRAL QLMTKCAQTV MEELEDIVIA YGQSDEYSFV FKRKTNWFKR 

       130        140        150        160        170        180 
RASKFMTHVA SQFASSYVFY WRDYFEDQPL LYPPGFDGRV VVYPSNQTLK DYLSWRQADC 

       190        200        210        220        230        240 
HINNLYNTVF WALIQQSGLT PVQAQGRLQG TLAADKNEIL FSEFNINYNN ELPMYRKGTV 

       250        260        270        280        290 
LIWQKVDEVM TKEIKLPTEM EGKKMAVTRT RTKPVPLHCD IIGDAFWKEH PEILDEDS 

« Hide

References

« Hide 'large scale' references
[1]"Identification and characterization of a novel cytoplasm protein ICF45 that is involved in cell cycle regulation."
Guo D., Hu K., Lei Y., Wang Y., Ma T., He D.
J. Biol. Chem. 279:53498-53505(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[2]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT PRO-232.
[4]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT PRO-232.
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT PRO-232.
[7]"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], VARIANT PRO-232.
Tissue: Brain and Muscle.
[8]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"tRNA(His) guanylyltransferase (THG1), a unique 3'-5' nucleotidyl transferase, shares unexpected structural homology with canonical 5'-3' DNA polymerases."
Hyde S.J., Eckenroth B.E., Smith B.A., Eberley W.A., Heintz N.H., Jackman J.E., Doublie S.
Proc. Natl. Acad. Sci. U.S.A. 107:20305-20310(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 30-298 IN COMPLEX WITH MAGNESIUM; TRIPHOSPHATE AND GTP, FUNCTION, COFACTOR, SUBUNIT, MUTAGENESIS OF ASP-58; HIS-63; SER-104; ASP-105; GLU-106; THR-127; HIS-181; LYS-216 AND ASN-227.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY463216 mRNA. Translation: AAS21134.1.
AL136669 mRNA. Translation: CAB66604.1.
AK000553 mRNA. Translation: BAA91249.1.
AK021663 mRNA. Translation: BAB13870.1.
CR533503 mRNA. Translation: CAG38534.1.
AK223119 mRNA. Translation: BAD96839.1.
CH471062 Genomic DNA. Translation: EAW61590.1.
CH471062 Genomic DNA. Translation: EAW61591.1.
BC001523 mRNA. Translation: AAH01523.2. Different initiation.
BC001852 mRNA. Translation: AAH01852.2. Different initiation.
BC023521 mRNA. Translation: AAH23521.1.
RefSeqNP_060342.2. NM_017872.3.
UniGeneHs.353090.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3OTBX-ray2.95A/B30-298[»]
3OTCX-ray3.01A/B30-298[»]
3OTDX-ray2.28A/B30-298[»]
3OTEX-ray2.56A/B30-298[»]
ProteinModelPortalQ9NWX6.
SMRQ9NWX6. Positions 33-296.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120311. 23 interactions.
DIPDIP-59479N.
IntActQ9NWX6. 1 interaction.
MINTMINT-4873002.
STRING9606.ENSP00000231198.

PTM databases

PhosphoSiteQ9NWX6.

Polymorphism databases

DMDM146325755.

Proteomic databases

PaxDbQ9NWX6.
PeptideAtlasQ9NWX6.
PRIDEQ9NWX6.

Protocols and materials databases

DNASU54974.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000231198; ENSP00000231198; ENSG00000113272.
GeneID54974.
KEGGhsa:54974.
UCSCuc003lxd.3. human.

Organism-specific databases

CTD54974.
GeneCardsGC05P157159.
HGNCHGNC:26053. THG1L.
HPAHPA035877.
HPA035878.
neXtProtNX_Q9NWX6.
PharmGKBPA162405691.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4021.
HOGENOMHOG000204890.
HOVERGENHBG054289.
InParanoidQ9NWX6.
KOK10761.
OMAKFEYVRN.
OrthoDBEOG7X0VHR.
PhylomeDBQ9NWX6.
TreeFamTF325119.

Gene expression databases

ArrayExpressQ9NWX6.
BgeeQ9NWX6.
CleanExHS_THG1L.
GenevestigatorQ9NWX6.

Family and domain databases

InterProIPR025845. Thg1_C_dom.
IPR024956. tRNAHis_GuaTrfase_cat.
IPR007537. tRNAHis_GuaTrfase_Thg1.
[Graphical view]
PANTHERPTHR12729. PTHR12729. 1 hit.
PfamPF04446. Thg1. 1 hit.
PF14413. Thg1C. 1 hit.
[Graphical view]
PIRSFPIRSF028980. tRNAHis_guanylyltransferase. 1 hit.
ProtoNetSearch...

Other

ChiTaRSTHG1L. human.
EvolutionaryTraceQ9NWX6.
GeneWikiTHG1L.
GenomeRNAi54974.
NextBio58226.
PROQ9NWX6.

Entry information

Entry nameTHG1_HUMAN
AccessionPrimary (citable) accession number: Q9NWX6
Secondary accession number(s): D3DQJ5 expand/collapse secondary AC list , Q53G12, Q7L5R3, Q9H0S2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: May 1, 2007
Last modified: April 16, 2014
This is version 102 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM