Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q9NXH9 (TRM1_HUMAN)

Last modified July 7, 2009. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    N(2),N(2)-dimethylguanosine tRNA methyltransferase
    EC=2.1.1.32
Alternative name(s):
    tRNA(guanine-26,N(2)-N(2)) methyltransferase
    tRNA 2,2-dimethylguanosine-26 methyltransferase
    tRNA(m(2,2)G26)dimethyltransferase
Gene names
Name: TRMT1
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length659 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Dimethylates a single guanine residue at position 26 of most tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Catalytic activity

S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing N(2)-methylguanine.

Sequence similarities

Contains 1 C3H1-type zinc finger.

Ontologies

Keywords
   Biological processtRNA processing
   Coding sequence diversityAlternative splicing
   DomainZinc-finger
   LigandMetal-binding
S-adenosyl-L-methionine
Zinc
   Molecular functionMethyltransferase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processtRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionRNA binding

Inferred from electronic annotation. Source: InterPro

tRNA (guanine-N2-)-methyltransferase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NXH9-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9NXH9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     340-368: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 659659N(2),N(2)-dimethylguanosine tRNA methyltransferase
PRO_0000147671

Regions

Zinc finger600 – 62728C3H1-type

Amino acid modifications

Modified residue1201Phosphoserine By similarity
Modified residue6251Phosphoserine Ref.7
Modified residue6281Phosphothreonine Ref.7 Ref.6
Modified residue6461Phosphothreonine Ref.7 Ref.5

Natural variations

Alternative sequence340 – 36829Missing in isoform 2.
VSP_016720

Experimental info

Sequence conflict500 – 5034RCWE → Q in AAC33150. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: E4F0F2B740B44387

FASTA65972,234
        10         20         30         40         50         60 
MQGSSLWLSL TFRSARVLSR ARFFEWQSPG LPNTAAMENG TGPYGEERPR EVQETTVTEG 

        70         80         90        100        110        120 
AAKIAFPSAN EVFYNPVQEF NRDLTCAVIT EFARIQLGAK GIQIKVPGEK DTQKVVVDLS 

       130        140        150        160        170        180 
EQEEEKVELK ESENLASGDQ PRTAAVGEIC EEGLHVLEGL AASGLRSIRF ALEVPGLRSV 

       190        200        210        220        230        240 
VANDASTRAV DLIRRNVQLN DVAHLVQPSQ ADARMLMYQH QRVSERFDVI DLDPYGSPAT 

       250        260        270        280        290        300 
FLDAAVQAVS EGGLLCVTCT DMAVLAGNSG ETCYSKYGAM ALKSRACHEM ALRIVLHSLD 

       310        320        330        340        350        360 
LRANCYQRFV VPLLSISADF YVRVFVRVFT GQAKVKASAS KQALVFQCVG CGAFHLQRLG 

       370        380        390        400        410        420 
KASGVPSGRA KFSAACGPPV TPECEHCGQR HQLGGPMWAE PIHDLDFVGR VLEAVSANPG 

       430        440        450        460        470        480 
RFHTSERIRG VLSVITEELP DVPLYYTLDQ LSSTIHCNTP SLLQLRSALL HADFRVSLSH 

       490        500        510        520        530        540 
ACKNAVKTDA PASALWDIMR CWEKECPVKR ERLSETSPAF RILSVEPRLQ ANFTIREDAN 

       550        560        570        580        590        600 
PSSRQRGLKR FQANPEANWG PRPRARPGGK AADEAMEERR RLLQNKRKEP PEDVAQRAAR 

       610        620        630        640        650 
LKTFPCKRFK EGTCQRGDQC CYSHSPPTPR VSADAAPDCP ETSNQTPPGP GAAAGPGID 

« Hide

Isoform 2.

Checksum: 2CE1AF04EED60391
Show »

FASTA63069,306

References

« Hide 'large scale' references
[1]"The human tRNA(m22G26)dimethyltransferase: functional expression and characterization of a cloned hTRM1 gene."
Liu J., Straby K.B.
Nucleic Acids Res. 28:3445-3451(2000) [PubMed: 10982862] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Placenta.
[2]"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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Colon mucosa.
[3]"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: 15057824] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Brain, Cervix and Colon.
[5]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-646, MASS SPECTROMETRY.
Tissue: Epithelium.
[6]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-628, MASS SPECTROMETRY.
[7]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-625; THR-628 AND THR-646, MASS SPECTROMETRY.
[8]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.

Cross-references

Sequence databases

AF196479 mRNA. Translation: AAG28495.1.
AK000251 mRNA. Translation: BAA91031.1.
AC005546 Genomic DNA. Translation: AAC33150.1.
BC002492 mRNA. Translation: AAH02492.1.
BC018302 mRNA. Translation: AAH18302.1.
BC040126 mRNA. Translation: AAH40126.1.
IPIIPI00020508.
IPI00178861.
RefSeqNP_001129507.1.
NP_001136026.1.
NP_060192.1.
UniGeneHs.515169

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActQ9NXH9. 1 interaction.

PTM databases

PhosphoSiteQ9NXH9.

Proteomic databases

PRIDEQ9NXH9.

Genome annotation databases

EnsemblENSG00000104907. Homo sapiens. [Contig view]
GeneID55621.
KEGGhsa:55621.
UCSCuc002mwj.1. human.
uc002mwk.1. human.

Organism-specific databases

GeneCardsGC19M013077.
H-InvDBHIX0014819.
HGNCHGNC:25980. TRMT1.
MIM611669. gene.
PharmGKBPA134867808.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ9NXH9.
HOVERGENQ9NXH9.
OMAQ9NXH9. AAMENGT.

Enzyme and pathway databases

BRENDA2.1.1.32. 247.

Gene expression databases

ArrayExpressQ9NXH9.
BgeeQ9NXH9.
CleanExHS_TRMT1.
GermOnlineENSG00000104907. Homo sapiens.

Family and domain databases

InterProIPR002905. TRM_MeTrfase.
IPR000571. Znf_CCCH.
[Graphical view]
PANTHERPTHR10631. TRM_mtfrase. 1 hit.
PfamPF02005. TRM. 1 hit.
PF00642. zf-CCCH. 1 hit.
[Graphical view]
SMARTSM00356. ZnF_C3H1. 1 hit.
[Graphical view]
TIGRFAMsTIGR00308. TRM1. 1 hit.
PROSITEPS50103. ZF_C3H1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio60228.
SOURCESearch...

Entry information

Entry nameTRM1_HUMAN
AccessionPrimary (citable) accession number: Q9NXH9
Secondary accession number(s): O76103, Q548Y5, Q8WVA6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: October 1, 2000
Last modified: July 7, 2009
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant 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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents