Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9UBP6 (TRMB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 111. 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·Alt products·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
Synonyms:C12orf1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length276 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. Ref.6

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.

Subcellular location

Nucleus Ref.7.

Tissue specificity

Ubiquitous. Ref.1

Post-translational modification

Phosphorylation at Ser-27 inactivates its catalytic activity but does not affect the interaction with WDR4. HAMAP-Rule MF_03055

Sequence similarities

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

Sequence caution

The sequence CAA65470.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UBP6-1)

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: Q9UBP6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     92-155: VELSPLFPDT...PNFFYKGQLT → ADKDVLPLPR...VHSFRRAPTV
     156-276: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 276275tRNA (guanine-N(7)-)-methyltransferase HAMAP-Rule MF_03055
PRO_0000171431

Regions

Region107 – 1082S-adenosyl-L-methionine binding HAMAP-Rule MF_03055
Region140 – 1412S-adenosyl-L-methionine binding HAMAP-Rule MF_03055
Region238 – 2403S-adenosyl-L-methionine binding HAMAP-Rule MF_03055

Sites

Active site1631 By similarity
Binding site841S-adenosyl-L-methionine; via carbonyl oxygen
Binding site1601S-adenosyl-L-methionine; via carbonyl oxygen

Amino acid modifications

Modified residue21N-acetylalanine Ref.8
Modified residue271Phosphoserine; by PKB and RPS6KA3 Ref.7

Natural variations

Alternative sequence92 – 15564VELSP…KGQLT → ADKDVLPLPRPTFQADKAQV ANHQSHPASRICLRAKSWGA GVYHNRCAGATRLDVHSFRR APTV in isoform 2.
VSP_044671
Alternative sequence156 – 276121Missing in isoform 2.
VSP_044672

Experimental info

Mutagenesis271S → A: Able to complement a trm8-delta mutant yeast. Ref.7
Mutagenesis271S → D or E: Abolishes ability to complement a trm8-delta mutant yeast. Ref.7
Sequence conflict181K → R in BAD96922. Ref.3

Secondary structure

........................................ 276
Helix Strand Turn

Details...

Sequences

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

Last modified May 1, 2000. Version 1.
Checksum: 715AE85A18632892

FASTA27631,471
        10         20         30         40         50         60 
MAAETRNVAG AEAPPPQKRY YRQRAHSNPM ADHTLRYPVK PEEMDWSELY PEFFAPLTQN 

        70         80         90        100        110        120 
QSHDDPKDKK EKRAQAQVEF ADIGCGYGGL LVELSPLFPD TLILGLEIRV KVSDYVQDRI 

       130        140        150        160        170        180 
RALRAAPAGG FQNIACLRSN AMKHLPNFFY KGQLTKMFFL FPDPHFKRTK HKWRIISPTL 

       190        200        210        220        230        240 
LAEYAYVLRV GGLVYTITDV LELHDWMCTH FEEHPLFERV PLEDLSEDPV VGHLGTSTEE 

       250        260        270 
GKKVLRNGGK NFPAIFRRIQ DPVLQAVTSQ TSLPGH 

« Hide

Isoform 2 [UniParc].

Checksum: CFC2A730BA85E8D4
Show »

FASTA15517,423

References

« Hide 'large scale' references
[1]"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 [GENOMIC DNA / MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
Tissue: Brain.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]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] (ISOFORM 2).
Tissue: Kidney proximal tubule.
[4]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] (ISOFORM 1).
Tissue: Brain.
[6]"Two proteins that form a complex are required for 7-methylguanosine modification of yeast tRNA."
Alexandrov A., Martzen M.R., Phizicky E.M.
RNA 8:1253-1266(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH WDR4.
[7]"The tRNA methylase METTL1 is phosphorylated and inactivated by PKB and RSK in vitro and in cells."
Cartlidge R.A., Knebel A., Peggie M., Alexandrov A., Phizicky E.M., Cohen P.
EMBO J. 24:1696-1705(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH WDR4, PHOSPHORYLATION AT SER-27, MUTAGENESIS OF SER-27.
[8]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[9]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Crystal structure of human methyltransferase-like protein 1."
Structural genomics consortium (SGC)
Submitted (APR-2008) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 32-265 IN COMPLEX WITH S-ADENOSYL-L-METHIONINE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y18643 mRNA. Translation: CAA77239.1.
Y18642 Genomic DNA. Translation: CAA77238.1.
X96698 mRNA. Translation: CAA65470.1. Different initiation.
AK314851 mRNA. Translation: BAG37368.1.
AK223202 mRNA. Translation: BAD96922.1.
AC025165 Genomic DNA. No translation available.
BC000550 mRNA. Translation: AAH00550.1.
RefSeqNP_005362.3. NM_005371.5.
NP_075422.3. NM_023033.3.
UniGeneHs.42957.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3CKKX-ray1.55A32-265[»]
ProteinModelPortalQ9UBP6.
SMRQ9UBP6. Positions 37-265.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110392. 30 interactions.
IntActQ9UBP6. 1 interaction.
MINTMINT-1440834.
STRING9606.ENSP00000314441.

PTM databases

PhosphoSiteQ9UBP6.

Polymorphism databases

DMDM32171926.

Proteomic databases

PaxDbQ9UBP6.
PRIDEQ9UBP6.

Protocols and materials databases

DNASU4234.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000257848; ENSP00000257848; ENSG00000037897. [Q9UBP6-2]
ENST00000324871; ENSP00000314441; ENSG00000037897. [Q9UBP6-1]
GeneID4234.
KEGGhsa:4234.
UCSCuc010ssd.2. human. [Q9UBP6-1]

Organism-specific databases

CTD4234.
GeneCardsGC12M058170.
HGNCHGNC:7030. METTL1.
HPAHPA020914.
HPA050450.
MIM604466. gene.
neXtProtNX_Q9UBP6.
PharmGKBPA30766.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0220.
HOGENOMHOG000260965.
HOVERGENHBG044569.
InParanoidQ9UBP6.
KOK03439.
OMARAHSNPI.
OrthoDBEOG7PS1GC.
PhylomeDBQ9UBP6.
TreeFamTF314083.

Enzyme and pathway databases

UniPathwayUPA00989.

Gene expression databases

ArrayExpressQ9UBP6.
BgeeQ9UBP6.
CleanExHS_METTL1.
GenevestigatorQ9UBP6.

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

EvolutionaryTraceQ9UBP6.
GeneWikiMETTL1.
GenomeRNAi4234.
NextBio16693.
PROQ9UBP6.
SOURCESearch...

Entry information

Entry nameTRMB_HUMAN
AccessionPrimary (citable) accession number: Q9UBP6
Secondary accession number(s): B2RBX1 expand/collapse secondary AC list , H7BXF2, Q14105, Q53FS9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 111 of the entry and version 1 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM