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Protein

tRNA (guanine(26)-N(2))-dimethyltransferase

Gene

TRMT1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

2 S-adenosyl-L-methionine + guanine(26) in tRNA = 2 S-adenosyl-L-homocysteine + N(2)-dimethylguanine(26) in tRNA.PROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri600 – 62728C3H1-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

Metal-binding, RNA-binding, S-adenosyl-L-methionine, tRNA-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-6782315. tRNA modification in the nucleus and cytosol.

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA (guanine(26)-N(2))-dimethyltransferase (EC:2.1.1.216)
Alternative name(s):
tRNA 2,2-dimethylguanosine-26 methyltransferase
tRNA(guanine-26,N(2)-N(2)) methyltransferase
tRNA(m(2,2)G26)dimethyltransferase
Gene namesi
Name:TRMT1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:25980. TRMT1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134867808.

Polymorphism and mutation databases

BioMutaiTRMT1.
DMDMi12643821.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 659659tRNA (guanine(26)-N(2))-dimethyltransferasePRO_0000147671Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei120 – 1201PhosphoserineBy similarity
Modified residuei625 – 6251PhosphoserineCombined sources
Modified residuei628 – 6281PhosphothreonineCombined sources
Modified residuei646 – 6461PhosphothreonineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9NXH9.
MaxQBiQ9NXH9.
PaxDbiQ9NXH9.
PRIDEiQ9NXH9.

PTM databases

iPTMnetiQ9NXH9.
PhosphoSiteiQ9NXH9.

Expressioni

Gene expression databases

BgeeiQ9NXH9.
CleanExiHS_TRMT1.
ExpressionAtlasiQ9NXH9. baseline and differential.
GenevisibleiQ9NXH9. HS.

Organism-specific databases

HPAiHPA041130.
HPA041380.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
MAGEA11P43364-23EBI-748900,EBI-10178634
TERF1P542742EBI-748900,EBI-710997

Protein-protein interaction databases

BioGridi120760. 53 interactions.
IntActiQ9NXH9. 2 interactions.
MINTiMINT-1465402.
STRINGi9606.ENSP00000350352.

Structurei

3D structure databases

ProteinModelPortaliQ9NXH9.
SMRiQ9NXH9. Positions 156-491.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini55 – 499445Trm1 methyltransferasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.PROSITE-ProRule annotation
Contains 1 C3H1-type zinc finger.PROSITE-ProRule annotation
Contains 1 Trm1 methyltransferase domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri600 – 62728C3H1-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG1253. Eukaryota.
COG1867. LUCA.
GeneTreeiENSGT00530000063646.
HOGENOMiHOG000177995.
HOVERGENiHBG000477.
InParanoidiQ9NXH9.
KOiK00555.
OMAiESHANRH.
OrthoDBiEOG7ZD1V0.
PhylomeDBiQ9NXH9.
TreeFamiTF300851.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
4.10.1000.10. 1 hit.
InterProiIPR029063. SAM-dependent_MTases.
IPR002905. Trm1.
IPR000571. Znf_CCCH.
[Graphical view]
PANTHERiPTHR10631. PTHR10631. 1 hit.
PfamiPF02005. TRM. 1 hit.
PF00642. zf-CCCH. 1 hit.
[Graphical view]
SMARTiSM00356. ZnF_C3H1. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 3 hits.
SSF90229. SSF90229. 1 hit.
TIGRFAMsiTIGR00308. TRM1. 1 hit.
PROSITEiPS51626. SAM_MT_TRM1. 1 hit.
PS50103. ZF_C3H1. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q9NXH9-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MQGSSLWLSL TFRSARVLSR ARFFEWQSPG LPNTAAMENG TGPYGEERPR
60 70 80 90 100
EVQETTVTEG AAKIAFPSAN EVFYNPVQEF NRDLTCAVIT EFARIQLGAK
110 120 130 140 150
GIQIKVPGEK DTQKVVVDLS EQEEEKVELK ESENLASGDQ PRTAAVGEIC
160 170 180 190 200
EEGLHVLEGL AASGLRSIRF ALEVPGLRSV VANDASTRAV DLIRRNVQLN
210 220 230 240 250
DVAHLVQPSQ ADARMLMYQH QRVSERFDVI DLDPYGSPAT FLDAAVQAVS
260 270 280 290 300
EGGLLCVTCT DMAVLAGNSG ETCYSKYGAM ALKSRACHEM ALRIVLHSLD
310 320 330 340 350
LRANCYQRFV VPLLSISADF YVRVFVRVFT GQAKVKASAS KQALVFQCVG
360 370 380 390 400
CGAFHLQRLG KASGVPSGRA KFSAACGPPV TPECEHCGQR HQLGGPMWAE
410 420 430 440 450
PIHDLDFVGR VLEAVSANPG RFHTSERIRG VLSVITEELP DVPLYYTLDQ
460 470 480 490 500
LSSTIHCNTP SLLQLRSALL HADFRVSLSH ACKNAVKTDA PASALWDIMR
510 520 530 540 550
CWEKECPVKR ERLSETSPAF RILSVEPRLQ ANFTIREDAN PSSRQRGLKR
560 570 580 590 600
FQANPEANWG PRPRARPGGK AADEAMEERR RLLQNKRKEP PEDVAQRAAR
610 620 630 640 650
LKTFPCKRFK EGTCQRGDQC CYSHSPPTPR VSADAAPDCP ETSNQTPPGP

GAAAGPGID
Length:659
Mass (Da):72,234
Last modified:October 1, 2000 - v1
Checksum:iE4F0F2B740B44387
GO
Isoform 2 (identifier: Q9NXH9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     340-368: Missing.

Note: No experimental confirmation available.
Show »
Length:630
Mass (Da):69,306
Checksum:i2CE1AF04EED60391
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti500 – 5034RCWE → Q in AAC33150 (PubMed:15057824).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei340 – 36829Missing in isoform 2. 1 PublicationVSP_016720Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS12293.1. [Q9NXH9-1]
CCDS45997.1. [Q9NXH9-2]
RefSeqiNP_001129507.1. NM_001136035.2. [Q9NXH9-1]
NP_001136026.1. NM_001142554.1. [Q9NXH9-2]
NP_060192.1. NM_017722.3. [Q9NXH9-1]
XP_005260040.1. XM_005259983.1. [Q9NXH9-2]
UniGeneiHs.515169.

Genome annotation databases

EnsembliENST00000221504; ENSP00000221504; ENSG00000104907. [Q9NXH9-2]
ENST00000357720; ENSP00000350352; ENSG00000104907. [Q9NXH9-1]
ENST00000437766; ENSP00000416149; ENSG00000104907. [Q9NXH9-1]
ENST00000592062; ENSP00000466967; ENSG00000104907. [Q9NXH9-1]
GeneIDi55621.
KEGGihsa:55621.
UCSCiuc002mwj.3. human. [Q9NXH9-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS12293.1. [Q9NXH9-1]
CCDS45997.1. [Q9NXH9-2]
RefSeqiNP_001129507.1. NM_001136035.2. [Q9NXH9-1]
NP_001136026.1. NM_001142554.1. [Q9NXH9-2]
NP_060192.1. NM_017722.3. [Q9NXH9-1]
XP_005260040.1. XM_005259983.1. [Q9NXH9-2]
UniGeneiHs.515169.

3D structure databases

ProteinModelPortaliQ9NXH9.
SMRiQ9NXH9. Positions 156-491.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120760. 53 interactions.
IntActiQ9NXH9. 2 interactions.
MINTiMINT-1465402.
STRINGi9606.ENSP00000350352.

PTM databases

iPTMnetiQ9NXH9.
PhosphoSiteiQ9NXH9.

Polymorphism and mutation databases

BioMutaiTRMT1.
DMDMi12643821.

Proteomic databases

EPDiQ9NXH9.
MaxQBiQ9NXH9.
PaxDbiQ9NXH9.
PRIDEiQ9NXH9.

Protocols and materials databases

DNASUi55621.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000221504; ENSP00000221504; ENSG00000104907. [Q9NXH9-2]
ENST00000357720; ENSP00000350352; ENSG00000104907. [Q9NXH9-1]
ENST00000437766; ENSP00000416149; ENSG00000104907. [Q9NXH9-1]
ENST00000592062; ENSP00000466967; ENSG00000104907. [Q9NXH9-1]
GeneIDi55621.
KEGGihsa:55621.
UCSCiuc002mwj.3. human. [Q9NXH9-1]

Organism-specific databases

CTDi55621.
GeneCardsiTRMT1.
HGNCiHGNC:25980. TRMT1.
HPAiHPA041130.
HPA041380.
MIMi611669. gene.
neXtProtiNX_Q9NXH9.
PharmGKBiPA134867808.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1253. Eukaryota.
COG1867. LUCA.
GeneTreeiENSGT00530000063646.
HOGENOMiHOG000177995.
HOVERGENiHBG000477.
InParanoidiQ9NXH9.
KOiK00555.
OMAiESHANRH.
OrthoDBiEOG7ZD1V0.
PhylomeDBiQ9NXH9.
TreeFamiTF300851.

Enzyme and pathway databases

ReactomeiR-HSA-6782315. tRNA modification in the nucleus and cytosol.

Miscellaneous databases

GenomeRNAii55621.
PROiQ9NXH9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NXH9.
CleanExiHS_TRMT1.
ExpressionAtlasiQ9NXH9. baseline and differential.
GenevisibleiQ9NXH9. HS.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
4.10.1000.10. 1 hit.
InterProiIPR029063. SAM-dependent_MTases.
IPR002905. Trm1.
IPR000571. Znf_CCCH.
[Graphical view]
PANTHERiPTHR10631. PTHR10631. 1 hit.
PfamiPF02005. TRM. 1 hit.
PF00642. zf-CCCH. 1 hit.
[Graphical view]
SMARTiSM00356. ZnF_C3H1. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 3 hits.
SSF90229. SSF90229. 1 hit.
TIGRFAMsiTIGR00308. TRM1. 1 hit.
PROSITEiPS51626. SAM_MT_TRM1. 1 hit.
PS50103. ZF_C3H1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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.
    , 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] (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.
    , 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].
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-646, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-625; THR-628 AND THR-646, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTRM1_HUMAN
AccessioniPrimary (citable) accession number: Q9NXH9
Secondary accession number(s): O76103, Q548Y5, Q8WVA6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: October 1, 2000
Last modified: June 8, 2016
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.