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Q32P41 (TRM5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 74. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
tRNA (guanine(37)-N1)-methyltransferase

EC=2.1.1.228
Alternative name(s):
M1G-methyltransferase
tRNA [GM37] methyltransferase
tRNA methyltransferase 5 homolog
Gene names
Name:TRMT5
Synonyms:KIAA1393, TRM5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length509 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Specifically methylates the N1 position of guanosine-37 in various cytoplasmic and mitochondrial tRNAs. Methylation is not dependent on the nature of the nucleoside 5' of the target nucleoside. This is the first step in the biosynthesis of wybutosine (yW), a modified base adjacent to the anticodon of tRNAs and required for accurate decoding. HAMAP-Rule MF_03152

Catalytic activity

S-adenosyl-L-methionine + guanine37 in tRNA = S-adenosyl-L-homocysteine + N(1)-methylguanine37 in tRNA. Ref.6

Subunit structure

Monomer. Ref.6

Subcellular location

Mitochondrion matrix By similarity. Nucleus By similarity. Cytoplasm By similarity. Note: Predominantly in the mitochondria and in the nucleus By similarity. HAMAP-Rule MF_03152

Sequence similarities

Belongs to the class I-like SAM-binding methyltransferase superfamily. TRM5/TYW2 family.

Ontologies

Keywords
   Biological processtRNA processing
   Cellular componentCytoplasm
Mitochondrion
Nucleus
   Coding sequence diversityPolymorphism
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functiontRNA (guanine(37)-N(1))-methyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 509509tRNA (guanine(37)-N1)-methyltransferase HAMAP-Rule MF_03152
PRO_0000256513

Regions

Region327 – 3282S-adenosyl-L-methionine binding By similarity
Region355 – 3562S-adenosyl-L-methionine binding By similarity

Sites

Binding site2891S-adenosyl-L-methionine By similarity
Binding site3871S-adenosyl-L-methionine By similarity

Natural variations

Natural variant2171S → P. Ref.1 Ref.3 Ref.4 Ref.5
Corresponds to variant rs7142228 [ dbSNP | Ensembl ].
VAR_028898
Natural variant2551L → P.
Corresponds to variant rs2882686 [ dbSNP | Ensembl ].
VAR_028899
Natural variant2941E → A.
Corresponds to variant rs2296928 [ dbSNP | Ensembl ].
VAR_028900

Experimental info

Sequence conflict3941E → K in BAA92631. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q32P41 [UniParc].

Last modified April 17, 2007. Version 2.
Checksum: 4BCF6A00EBACD4FB

FASTA50958,246
        10         20         30         40         50         60 
MVLWILWRPF GFSGRFLKLE SHSITESKSL IPVAWTSLTQ MLLEAPGIFL LGQRKRFSTM 

        70         80         90        100        110        120 
PETETHERET ELFSPPSDVR GMTKLDRTAF KKTVNIPVLK VRKEIVSKLM RSLKRAALQR 

       130        140        150        160        170        180 
PGIRRVIEDP EDKESRLIML DPYKIFTHDS FEKAELSVLE QLNVSPQISK YNLELTYEHF 

       190        200        210        220        230        240 
KSEEILRAVL PEGQDVTSGF SRIGHIAHLN LRDHQLSFKH LIGQVMIDKN PGITSAVNKI 

       250        260        270        280        290        300 
NNIDNMYRNF QMEVLSGEQN MMTKVRENNY TYEFDFSKVY WNPRLSTEHS RITELLKPGD 

       310        320        330        340        350        360 
VLFDVFAGVG PFAIPVAKKN CTVFANDLNP ESHKWLLYNC KLNKVDQKVK VFNLDGKDFL 

       370        380        390        400        410        420 
QGPVKEELMQ LLGLSKERKP SVHVVMNLPA KAIEFLSAFK WLLDGQPCSS EFLPIVHCYS 

       430        440        450        460        470        480 
FSKDANPAED VRQRAGAVLG ISLEACSSVH LVRNVAPNKE MLCITFQIPA SVLYKNQTRN 

       490        500 
PENHEDPPLK RQRTAEAFSD EKTQIVSNT 

« Hide

References

« Hide 'large scale' references
[1]"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], VARIANT PRO-217.
[2]"The DNA sequence and analysis of human chromosome 14."
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. expand/collapse author list , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT PRO-217.
[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], VARIANT PRO-217.
Tissue: Bone.
[5]"Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 10-509, VARIANT PRO-217.
Tissue: Brain.
[6]"Isolation and characterization of the human tRNA-(N1G37) methyltransferase (TRM5) and comparison to the Escherichia coli TrmD protein."
Brule H., Elliott M., Redlak M., Zehner Z.E., Holmes W.M.
Biochemistry 43:9243-9255(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, SUBUNIT.
[7]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK293158 mRNA. Translation: BAG56703.1.
AL160236 Genomic DNA. No translation available.
CH471061 Genomic DNA. Translation: EAW80792.1.
BC108284 mRNA. Translation: AAI08285.1.
BC136606 mRNA. Translation: AAI36607.1.
BC136607 mRNA. Translation: AAI36608.1.
AB037814 mRNA. Translation: BAA92631.1.
RefSeqNP_065861.2. NM_020810.2.
UniGeneHs.380159.

3D structure databases

ProteinModelPortalQ32P41.
SMRQ32P41. Positions 97-470.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121623. 1 interaction.
STRING9606.ENSP00000261249.

PTM databases

PhosphoSiteQ32P41.

Polymorphism databases

DMDM145559536.

Proteomic databases

PaxDbQ32P41.
PRIDEQ32P41.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261249; ENSP00000261249; ENSG00000126814.
GeneID57570.
KEGGhsa:57570.
UCSCuc001xff.4. human.

Organism-specific databases

CTD57570.
GeneCardsGC14M061438.
H-InvDBHIX0011715.
HGNCHGNC:23141. TRMT5.
HPAHPA000943.
MIM611023. gene.
neXtProtNX_Q32P41.
PharmGKBPA134952106.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2520.
HOGENOMHOG000195270.
HOVERGENHBG094093.
InParanoidQ32P41.
KOK15429.
OMAVNKLMRS.
OrthoDBEOG7VDXP0.
PhylomeDBQ32P41.
TreeFamTF315073.

Enzyme and pathway databases

SABIO-RKQ32P41.

Gene expression databases

ArrayExpressQ32P41.
BgeeQ32P41.
CleanExHS_TRMT5.
GenevestigatorQ32P41.

Family and domain databases

HAMAPMF_03152. TRM5.
InterProIPR025792. tRNA_Gua_MeTrfase_euk.
IPR003402. tRNA_Trfase_Trm5/Tyw2.
[Graphical view]
PfamPF02475. Met_10. 1 hit.
[Graphical view]
PROSITEPS51684. SAM_MT_TRM5_TYW2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTRMT5. human.
GenomeRNAi57570.
NextBio64090.
PROQ32P41.
SOURCESearch...

Entry information

Entry nameTRM5_HUMAN
AccessionPrimary (citable) accession number: Q32P41
Secondary accession number(s): B2RN19, Q9P2F4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: April 17, 2007
Last modified: March 19, 2014
This is version 74 of the entry and version 2 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

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM