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UniProtKB/Swiss-Prot entry Q9NXH9


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name TRM1_HUMAN
Primary accession number Q9NXH9
Secondary accession numbers O76103 Q548Y5 Q8WVA6
Integrated into Swiss-Prot on January 11, 2001
Sequence was last modified on October 1, 2000 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 63)
Name and origin of the protein
Protein name N(2),N(2)-dimethylguanosine tRNA methyltransferase
Synonyms EC 2.1.1.32
tRNA(guanine-26,N(2)-N(2)) methyltransferase
tRNA 2,2-dimethylguanosine-26 methyltransferase
tRNA(m(2,2)G26)dimethyltransferase
Gene name
Name: TRMT1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Placenta;
DOI=10.1093/nar/28.18.3445; PubMed=10982862 [NCBI, ExPASy, EBI, Israel, Japan]
Liu J., Straby K.B.;
"The human tRNA(m22G26)dimethyltransferase: functional expression and characterization of a cloned hTRM1 gene.";
Nucleic Acids Res. 28:3445-3451(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Colon mucosa;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02399; PubMed=15057824 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain, Cervix, and Colon;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-646, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1038/nbt1240; PubMed=16964243 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-628, AND MASS SPECTROMETRY.
DOI=10.1021/pr0705441; PubMed=18220336 [NCBI, ExPASy, EBI, Israel, Japan]
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-625; THR-628 AND THR-646, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF196479; AAG28495.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK000251; BAA91031.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC005546; AAC33150.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC002492; AAH02492.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC018302; AAH18302.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC040126; AAH40126.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_060192.1; -.
UniGene Hs.515169
3D structure databases
ModBase Q9NXH9.
Protein-protein interaction databases
IntAct Q9NXH9; -.
PTM databases
PhosphoSite Q9NXH9; -.
Organism-specific databases
H-InvDB HIX0014819; -.
HGNC HGNC:25980; TRMT1.
GenAtlas TRMT1.
MIM 611669; gene. [NCBI / EBI]
PharmGKB PA134867808; -.
GeneCards Q9NXH9.
Gene expression databases
ArrayExpress Q9NXH9; -.
CleanEx HS_TRMT1; -.
GermOnline ENSG00000104907; Homo sapiens.
Ontologies
GO
GO:0003723; Molecular function: RNA binding (inferred from electronic annotation from InterPro).
GO:0004809; Molecular function: tRNA (guanine-N2-)-methyltransferase activity (inferred from electronic annotation from InterPro).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0008033; Biological process: tRNA processing (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR002905; TRM_MeTrfase.
IPR000571; Znf_CCCH.
Graphical view of domain structure.
PANTHER PTHR10631; TRM_mtfrase; 1.
Pfam PF02005; TRM; 1.
PF00642; zf-CCCH; 1.
Pfam graphical view of domain structure.
SMART SM00356; ZnF_C3H1; 1.
SMART graphical view of domain structure.
TIGRFAMs TIGR00308; TRM1; 1.
PROSITE PS50103; ZF_C3H1; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet Q9NXH9.
Genome annotation databases
Ensembl ENSG00000104907; Homo sapiens. [Contig view]
GeneID 55621; -.
KEGG hsa:55621; -.
Phylogenomic databases
HOGENOM Q9NXH9; -.
HOVERGEN Q9NXH9; -.
Other
LinkHub Q9NXH9; -.
NextBio 60228; -.
SOURCE TRMT1; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Metal-binding; Methyltransferase; Phosphoprotein; S-adenosyl-L-methionine; Transferase; tRNA processing; Zinc; Zinc-finger.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   659  659     N(2),N(2)-dimethylguanosine tRNA methyltransferase. PRO_0000147671
ZN_FING   600   627  28     C3H1-type. 
MOD_RES   120   120        Phosphoserine (By similarity). 
MOD_RES   625   625        Phosphoserine. 
MOD_RES   628   628        Phosphothreonine. 
MOD_RES   646   646        Phosphothreonine. 
VAR_SEQ   340   368        Missing (in isoform 2). VSP_016720
CONFLICT   500   503        RCWE -> Q (in Ref. 3; AAC33150). 
Sequence information
Length: 659 AA [This is the length of the unprocessed precursor] Molecular weight: 72234 Da [This is the MW of the unprocessed precursor] CRC64: E4F0F2B740B44387 [This is a checksum on the sequence]
        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 

Q9NXH9 in FASTA format

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