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Q9Z120 (TRMB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
tRNA (guanine-N(7)-)-methyltransferase

EC=2.1.1.33
Alternative name(s):
Methyltransferase-like protein 1
tRNA (guanine(46)-N(7))-methyltransferase
tRNA(m7G46)-methyltransferase
Gene names
Name:Mettl1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length268 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA By similarity. HAMAP-Rule MF_03055

Catalytic activity

S-adenosyl-L-methionine + guanine46 in tRNA = S-adenosyl-L-homocysteine + N(7)-methylguanine46 in tRNA. HAMAP-Rule MF_03055

Pathway

tRNA modification; N(7)-methylguanine-tRNA biosynthesis. HAMAP-Rule MF_03055

Subunit structure

Forms a complex with WDR4 By similarity. HAMAP-Rule MF_03055

Subcellular location

Nucleus By similarity HAMAP-Rule MF_03055.

Post-translational modification

Phosphorylation at Ser-21 inactivates its catalytic activity but does not affect the interaction with WDR4 By similarity. HAMAP-Rule MF_03055

Sequence similarities

Belongs to the class I-like SAM-binding methyltransferase superfamily. TrmB family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 268268tRNA (guanine-N(7)-)-methyltransferase HAMAP-Rule MF_03055
PRO_0000171432

Regions

Region101 – 1022S-adenosyl-L-methionine binding By similarity
Region134 – 1352S-adenosyl-L-methionine binding By similarity
Region232 – 2343S-adenosyl-L-methionine binding By similarity

Sites

Active site1571 By similarity
Binding site781S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site1541S-adenosyl-L-methionine; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue211Phosphoserine; by PKB and RPS6KA3 By similarity

Experimental info

Sequence conflict521I → N in AAH12649. Ref.4
Sequence conflict561S → N in AAH12649. Ref.4
Sequence conflict2131R → C in AAH12649. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q9Z120 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 1DAE1EEAA4A07627

FASTA26830,603
        10         20         30         40         50         60 
MMAGAEAPQP QKRYYRQRAH SNPMADHTLR YPVKPEEMDW SELYPEFFAP LIQNKSHDDP 

        70         80         90        100        110        120 
KDEKEKHSGA QVEFADIGCG YGGLLVALSP LFPDTLILGL EIRVKVSDYV QDRIRALRAA 

       130        140        150        160        170        180 
PGGGFQNIAC LRSNAMKHLP NFFRKGQLAK MFFLFPDPHF KRTKHKWRII SPTLLAEYAY 

       190        200        210        220        230        240 
VLRVGGLVYT VTDVPELHEW MCTHFEEHPL FERVPLEELS EDPIVEHLGS STEEGKKVLR 

       250        260 
NGGKNFPAVF RRIQDPLLQA VTPNPTLP 

« Hide

References

« Hide 'large scale' references
[1]"Methyltransferase related protein."
Tamura M., Nashimoto M., Kaspar R.L.
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Extraembryonic tissue and Placenta.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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].
[5]"Molecular analysis of METTL1, a novel human methyltransferase-like gene with a high degree of phylogenetic conservation."
Bahr A., Hankeln T., Fiedler T., Hegemann J., Schmidt E.R.
Genomics 57:424-428(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-268.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB023619 mRNA. Translation: BAA75230.1.
AK160914 mRNA. Translation: BAE36088.1.
CH466578 Genomic DNA. Translation: EDL24462.1.
BC012649 mRNA. Translation: AAH12649.1.
Y18644 mRNA. Translation: CAA77240.1.
RefSeqNP_034922.1. NM_010792.1.
UniGeneMm.251593.

3D structure databases

ProteinModelPortalQ9Z120.
SMRQ9Z120. Positions 31-259.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ9Z120.

Proteomic databases

PaxDbQ9Z120.
PRIDEQ9Z120.

Protocols and materials databases

DNASU17299.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000006915; ENSMUSP00000006915; ENSMUSG00000006732.
GeneID17299.
KEGGmmu:17299.
UCSCuc007hhq.1. mouse.

Organism-specific databases

CTD4234.
MGIMGI:1339986. Mettl1.

Phylogenomic databases

eggNOGCOG0220.
GeneTreeENSGT00390000017840.
HOGENOMHOG000260965.
HOVERGENHBG044569.
InParanoidQ3TU83.
KOK03439.
OMARAHSNPI.
PhylomeDBQ9Z120.
TreeFamTF314083.

Enzyme and pathway databases

UniPathwayUPA00989.

Gene expression databases

ArrayExpressQ9Z120.
BgeeQ9Z120.
CleanExMM_METTL1.
GenevestigatorQ9Z120.

Family and domain databases

HAMAPMF_03055. tRNA_methyltr_TrmB_euk.
InterProIPR025763. Trm8_euk.
IPR003358. tRNA_(Gua-N-7)_MeTrfase.
[Graphical view]
PfamPF02390. Methyltransf_4. 1 hit.
[Graphical view]
TIGRFAMsTIGR00091. TIGR00091. 1 hit.
PROSITEPS51625. SAM_MT_TRMB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio291830.
PROQ9Z120.
SOURCESearch...

Entry information

Entry nameTRMB_MOUSE
AccessionPrimary (citable) accession number: Q9Z120
Secondary accession number(s): Q3TU83, Q921G5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: May 1, 1999
Last modified: April 16, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot