TRM11_HUMAN
ID TRM11_HUMAN Reviewed; 463 AA.
AC Q7Z4G4; E1P570; Q5JY11; Q6PGQ5; Q9HC13;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=tRNA (guanine(10)-N2)-methyltransferase homolog;
DE EC=2.1.1.-;
DE AltName: Full=tRNA guanosine-2'-O-methyltransferase TRM11 homolog;
GN Name=TRMT11; Synonyms=C6orf75; ORFNames=MDS024;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Chen Y., Huang C.-H.;
RT "Molecular identification and conserved evolution of a novel RNA methylase
RT protein gene in higher eukaryotic organisms.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Hematopoietic stem cell;
RA Huang C., Qian B., Tu Y., Gu W., Wang Y., Han Z., Chen Z.;
RT "Novel genes expressed in hematopoietic stem/progenitor cells from
RT myelodysplastic syndrome patients.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLN-230.
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [9]
RP INTERACTION WITH TRMT112.
RX PubMed=34948388; DOI=10.3390/ijms222413593;
RA Brumele B., Mutso M., Telanne L., Ounap K., Spunde K., Abroi A., Kurg R.;
RT "Human TRMT112-Methyltransferase Network Consists of Seven Partners
RT Interacting with a Common Co-Factor.";
RL Int. J. Mol. Sci. 22:13593-13593(2021).
CC -!- FUNCTION: Catalytic subunit of an S-adenosyl-L-methionine-dependent
CC tRNA methyltransferase complex that mediates the methylation of the
CC guanosine nucleotide at position 10 (m2G10) in tRNAs. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with TRMT112. {ECO:0000269|PubMed:34948388}.
CC -!- INTERACTION:
CC Q7Z4G4; Q9UHG0: DCDC2; NbExp=3; IntAct=EBI-2515608, EBI-10303987;
CC Q7Z4G4; Q969G2: LHX4; NbExp=3; IntAct=EBI-2515608, EBI-2865388;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q7Z4G4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z4G4-2; Sequence=VSP_017818;
CC Name=3;
CC IsoId=Q7Z4G4-3; Sequence=VSP_017816, VSP_017817;
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. TRM11 methyltransferase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00959}.
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DR EMBL; AF532977; AAQ10284.1; -; mRNA.
DR EMBL; AF182423; AAG14959.1; -; mRNA.
DR EMBL; AL035689; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48125.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48126.1; -; Genomic_DNA.
DR EMBL; BC056878; AAH56878.1; -; mRNA.
DR CCDS; CCDS35496.1; -. [Q7Z4G4-1]
DR RefSeq; NP_001026882.2; NM_001031712.2. [Q7Z4G4-1]
DR AlphaFoldDB; Q7Z4G4; -.
DR SMR; Q7Z4G4; -.
DR BioGRID; 121918; 38.
DR IntAct; Q7Z4G4; 13.
DR STRING; 9606.ENSP00000333934; -.
DR iPTMnet; Q7Z4G4; -.
DR PhosphoSitePlus; Q7Z4G4; -.
DR BioMuta; TRMT11; -.
DR DMDM; 74723330; -.
DR EPD; Q7Z4G4; -.
DR jPOST; Q7Z4G4; -.
DR MassIVE; Q7Z4G4; -.
DR MaxQB; Q7Z4G4; -.
DR PaxDb; Q7Z4G4; -.
DR PeptideAtlas; Q7Z4G4; -.
DR PRIDE; Q7Z4G4; -.
DR ProteomicsDB; 69176; -. [Q7Z4G4-1]
DR ProteomicsDB; 69177; -. [Q7Z4G4-2]
DR ProteomicsDB; 69178; -. [Q7Z4G4-3]
DR Antibodypedia; 32733; 122 antibodies from 25 providers.
DR DNASU; 60487; -.
DR Ensembl; ENST00000334379.11; ENSP00000333934.5; ENSG00000066651.20. [Q7Z4G4-1]
DR Ensembl; ENST00000368332.7; ENSP00000357316.3; ENSG00000066651.20. [Q7Z4G4-2]
DR Ensembl; ENST00000479748.5; ENSP00000433724.1; ENSG00000066651.20. [Q7Z4G4-3]
DR GeneID; 60487; -.
DR KEGG; hsa:60487; -.
DR MANE-Select; ENST00000334379.11; ENSP00000333934.5; NM_001031712.3; NP_001026882.2.
DR UCSC; uc003qam.4; human. [Q7Z4G4-1]
DR CTD; 60487; -.
DR DisGeNET; 60487; -.
DR GeneCards; TRMT11; -.
DR HGNC; HGNC:21080; TRMT11.
DR HPA; ENSG00000066651; Low tissue specificity.
DR neXtProt; NX_Q7Z4G4; -.
DR OpenTargets; ENSG00000066651; -.
DR PharmGKB; PA162407032; -.
DR VEuPathDB; HostDB:ENSG00000066651; -.
DR eggNOG; KOG2671; Eukaryota.
DR GeneTree; ENSGT00390000018131; -.
DR HOGENOM; CLU_029646_1_1_1; -.
DR InParanoid; Q7Z4G4; -.
DR OMA; MWMPTAN; -.
DR OrthoDB; 924753at2759; -.
DR PhylomeDB; Q7Z4G4; -.
DR TreeFam; TF106161; -.
DR PathwayCommons; Q7Z4G4; -.
DR Reactome; R-HSA-6782315; tRNA modification in the nucleus and cytosol.
DR SignaLink; Q7Z4G4; -.
DR BioGRID-ORCS; 60487; 59 hits in 1079 CRISPR screens.
DR ChiTaRS; TRMT11; human.
DR GenomeRNAi; 60487; -.
DR Pharos; Q7Z4G4; Tbio.
DR PRO; PR:Q7Z4G4; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q7Z4G4; protein.
DR Bgee; ENSG00000066651; Expressed in secondary oocyte and 196 other tissues.
DR ExpressionAtlas; Q7Z4G4; baseline and differential.
DR Genevisible; Q7Z4G4; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
DR GO; GO:0004809; F:tRNA (guanine-N2-)-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR000241; RNA_methylase_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016691; tRNA_mtfrase_TRM11.
DR Pfam; PF01170; UPF0020; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
DR PROSITE; PS51627; SAM_MT_TRM11; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Methyltransferase; Reference proteome;
KW RNA-binding; S-adenosyl-L-methionine; Transferase; tRNA processing;
KW tRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..463
FT /note="tRNA (guanine(10)-N2)-methyltransferase homolog"
FT /id="PRO_0000230288"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT VAR_SEQ 254..257
FT /note="GKAT -> ACST (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_017816"
FT VAR_SEQ 258..463
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_017817"
FT VAR_SEQ 416..420
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_017818"
FT VARIANT 230
FT /note="L -> Q (in dbSNP:rs17854915)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_025786"
SQ SEQUENCE 463 AA; 53421 MW; D3DE2AB403F0A84C CRC64;
MALSCTLNRY LLLMAQEHLE FRLPEIKSLL LLFGGQFASS QETYGKSPFW ILSIPSEDIA
RNLMKRTVCA KSIFELWGHG QSPEELYSSL KNYPVEKMVP FLHSDSTYKI KIHTFNKTLT
QEEKIKRIDA LEFLPFEGKV NLKKPQHVFS VLEDYGLDPN CIPENPHNIY FGRWIADGQR
ELIESYSVKK RHFIGNTSMD AGLSFIMANH GKVKENDIVF DPFVGTGGLL IACAHFGAYV
YGTDIDYNTV HGLGKATRKN QKWRGPDENI RANLRQYGLE KYYLDVLVSD ASKPSWRKGT
YFDAIITDPP YGIRESTRRT GSQKEIPKGI EKWEKCPESH VPVSLSYHLS DMFLDLLNFA
AETLVLGGRL VYWLPVYTPE YTEEMVPWHP CLELVSNCEQ KLSSHTSRRL ITMEKVKKFE
NRDQYSHLLS DHFLPYQGHN SFREKYFSGV TKRIAKEEKS TQE
