TM10B_HUMAN
ID TM10B_HUMAN Reviewed; 316 AA.
AC Q6PF06; B7Z216; B7Z3D3; Q05DJ4; Q5QP83; Q8NAG2; Q96N36;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=tRNA methyltransferase 10 homolog B;
DE EC=2.1.1.221 {ECO:0000269|PubMed:23042678};
DE AltName: Full=RNA (guanine-9-)-methyltransferase domain-containing protein 3;
DE AltName: Full=tRNA (guanine(9)-N(1))-methyltransferase TRMT10B;
GN Name=TRMT10B; Synonyms=RG9MTD3;
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 [LARGE SCALE MRNA] (ISOFORMS 1; 2; 4 AND 5).
RC TISSUE=Amygdala, Hippocampus, Neuroblastoma, and Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Eye, and Placenta;
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 [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=23042678; DOI=10.1093/nar/gks910;
RA Vilardo E., Nachbagauer C., Buzet A., Taschner A., Holzmann J.,
RA Rossmanith W.;
RT "A subcomplex of human mitochondrial RNase P is a bifunctional
RT methyltransferase--extensive moonlighting in mitochondrial tRNA
RT biogenesis.";
RL Nucleic Acids Res. 40:11583-11593(2012).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent guanine N(1)-
CC methyltransferase that catalyzes the formation of N(1)-methylguanine at
CC position 9 (m1G9) in tRNAs (PubMed:23042678). Probably not able to
CC catalyze formation of N(1)-methyladenine at position 9 (m1A9) in tRNAs
CC (PubMed:23042678). {ECO:0000269|PubMed:23042678}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(9) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-
CC methylguanosine(9) in tRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43156, Rhea:RHEA-COMP:10367, Rhea:RHEA-COMP:10368,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:73542, ChEBI:CHEBI:74269; EC=2.1.1.221;
CC Evidence={ECO:0000269|PubMed:23042678};
CC -!- INTERACTION:
CC Q6PF06; P32243-2: OTX2; NbExp=3; IntAct=EBI-3923391, EBI-9087860;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q6PF06-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PF06-2; Sequence=VSP_029519;
CC Name=5;
CC IsoId=Q6PF06-5; Sequence=VSP_055735, VSP_054653;
CC Name=3;
CC IsoId=Q6PF06-3; Sequence=VSP_029520, VSP_029521;
CC Name=4;
CC IsoId=Q6PF06-4; Sequence=VSP_054652, VSP_054653;
CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC superfamily. TRM10 family. {ECO:0000255|PROSITE-ProRule:PRU01012}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB71074.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK056017; BAB71074.1; ALT_SEQ; mRNA.
DR EMBL; AK092718; BAC03957.1; -; mRNA.
DR EMBL; AK294219; BAH11702.1; -; mRNA.
DR EMBL; AK295733; BAH12169.1; -; mRNA.
DR EMBL; AL138752; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL591470; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471071; EAW58267.1; -; Genomic_DNA.
DR EMBL; CH471071; EAW58268.1; -; Genomic_DNA.
DR EMBL; CH471071; EAW58269.1; -; Genomic_DNA.
DR EMBL; BC012175; AAH12175.1; -; mRNA.
DR EMBL; BC057774; AAH57774.1; -; mRNA.
DR CCDS; CCDS43804.1; -. [Q6PF06-1]
DR CCDS; CCDS69598.1; -. [Q6PF06-5]
DR CCDS; CCDS69600.1; -. [Q6PF06-4]
DR CCDS; CCDS69601.1; -. [Q6PF06-2]
DR RefSeq; NP_001273879.1; NM_001286950.1. [Q6PF06-5]
DR RefSeq; NP_001273880.1; NM_001286951.1. [Q6PF06-2]
DR RefSeq; NP_001273881.1; NM_001286952.1. [Q6PF06-4]
DR RefSeq; NP_001273882.1; NM_001286953.1.
DR RefSeq; NP_001273883.1; NM_001286954.1.
DR RefSeq; NP_659401.2; NM_144964.3. [Q6PF06-1]
DR AlphaFoldDB; Q6PF06; -.
DR SMR; Q6PF06; -.
DR BioGRID; 127659; 41.
DR ComplexPortal; CPX-6124; TIM22 mitochondrial inner membrane twin-pore carrier translocase complex.
DR IntAct; Q6PF06; 33.
DR STRING; 9606.ENSP00000297994; -.
DR iPTMnet; Q6PF06; -.
DR PhosphoSitePlus; Q6PF06; -.
DR BioMuta; TRMT10B; -.
DR DMDM; 74749176; -.
DR EPD; Q6PF06; -.
DR MassIVE; Q6PF06; -.
DR PaxDb; Q6PF06; -.
DR PeptideAtlas; Q6PF06; -.
DR PRIDE; Q6PF06; -.
DR ProteomicsDB; 6511; -.
DR ProteomicsDB; 67098; -. [Q6PF06-1]
DR ProteomicsDB; 67099; -. [Q6PF06-2]
DR ProteomicsDB; 67100; -. [Q6PF06-3]
DR Antibodypedia; 5730; 111 antibodies from 18 providers.
DR DNASU; 158234; -.
DR Ensembl; ENST00000297994.4; ENSP00000297994.3; ENSG00000165275.10. [Q6PF06-1]
DR Ensembl; ENST00000377753.6; ENSP00000366982.2; ENSG00000165275.10. [Q6PF06-4]
DR Ensembl; ENST00000377754.6; ENSP00000366983.2; ENSG00000165275.10. [Q6PF06-2]
DR Ensembl; ENST00000488673.6; ENSP00000437395.1; ENSG00000165275.10. [Q6PF06-3]
DR Ensembl; ENST00000537911.5; ENSP00000444997.1; ENSG00000165275.10. [Q6PF06-5]
DR GeneID; 158234; -.
DR KEGG; hsa:158234; -.
DR MANE-Select; ENST00000297994.4; ENSP00000297994.3; NM_144964.4; NP_659401.2.
DR UCSC; uc004aai.5; human. [Q6PF06-1]
DR CTD; 158234; -.
DR DisGeNET; 158234; -.
DR GeneCards; TRMT10B; -.
DR HGNC; HGNC:26454; TRMT10B.
DR HPA; ENSG00000165275; Low tissue specificity.
DR neXtProt; NX_Q6PF06; -.
DR OpenTargets; ENSG00000165275; -.
DR PharmGKB; PA134938884; -.
DR VEuPathDB; HostDB:ENSG00000165275; -.
DR eggNOG; KOG2967; Eukaryota.
DR GeneTree; ENSGT00530000063169; -.
DR HOGENOM; CLU_034384_8_0_1; -.
DR InParanoid; Q6PF06; -.
DR OMA; ALQAWFP; -.
DR OrthoDB; 1396299at2759; -.
DR PhylomeDB; Q6PF06; -.
DR TreeFam; TF330972; -.
DR BRENDA; 2.1.1.218; 2681.
DR PathwayCommons; Q6PF06; -.
DR SignaLink; Q6PF06; -.
DR SIGNOR; Q6PF06; -.
DR BioGRID-ORCS; 158234; 8 hits in 1074 CRISPR screens.
DR ChiTaRS; TRMT10B; human.
DR GenomeRNAi; 158234; -.
DR Pharos; Q6PF06; Tdark.
DR PRO; PR:Q6PF06; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q6PF06; protein.
DR Bgee; ENSG00000165275; Expressed in right uterine tube and 101 other tissues.
DR ExpressionAtlas; Q6PF06; baseline and differential.
DR Genevisible; Q6PF06; HS.
DR GO; GO:0005829; C:cytosol; IDA:CAFA.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0042721; C:TIM22 mitochondrial import inner membrane insertion complex; IPI:ComplexPortal.
DR GO; GO:0052905; F:tRNA (guanine(9)-N(1))-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009019; F:tRNA (guanine-N1-)-methyltransferase activity; IDA:CAFA.
DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR GO; GO:0045039; P:protein insertion into mitochondrial inner membrane; IDA:ComplexPortal.
DR GO; GO:0002939; P:tRNA N1-guanine methylation; IBA:GO_Central.
DR Gene3D; 3.40.1280.30; -; 1.
DR InterPro; IPR028564; MT_TRM10-typ.
DR InterPro; IPR038459; MT_TRM10-typ_sf.
DR InterPro; IPR007356; tRNA_m1G_MeTrfase_euk.
DR InterPro; IPR016009; tRNA_MeTrfase_TRMD/TRM10.
DR PANTHER; PTHR13563; PTHR13563; 1.
DR Pfam; PF01746; tRNA_m1G_MT; 1.
DR PROSITE; PS51675; SAM_MT_TRM10; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..316
FT /note="tRNA methyltransferase 10 homolog B"
FT /id="PRO_0000311321"
FT DOMAIN 113..310
FT /note="SAM-dependent MTase TRM10-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01012"
FT REGION 77..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 73..97
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..98
FT /note="MDWKLEGSTQKVESPVLQGQEGILEETGEDGLPEGFQLLQIDAEGECQEGEI
FT LATGSTAWCSKNVQRKQRHWEKIVAAKKSKRKQEKERRKANRAENP -> MVL (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_029519"
FT VAR_SEQ 63..140
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054652"
FT VAR_SEQ 141..191
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055735"
FT VAR_SEQ 141..174
FT /note="ELSRLAGQIRRLYGSNKKADRPFWICLTGFTTDS -> VEHPLSLEFLLAMR
FT EAQKGTAFRRIWSTPASGIP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029520"
FT VAR_SEQ 175..316
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029521"
FT VAR_SEQ 282..290
FT /note="Missing (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054653"
FT VARIANT 234
FT /note="V -> G (in dbSNP:rs36023446)"
FT /id="VAR_037224"
FT VARIANT 242
FT /note="V -> A (in dbSNP:rs12337034)"
FT /id="VAR_037225"
FT CONFLICT 106
FT /note="K -> E (in Ref. 1; BAC03957)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 316 AA; 36124 MW; E65D2C5F89FCB8C5 CRC64;
MDWKLEGSTQ KVESPVLQGQ EGILEETGED GLPEGFQLLQ IDAEGECQEG EILATGSTAW
CSKNVQRKQR HWEKIVAAKK SKRKQEKERR KANRAENPGI CPQHSKRFLR ALTKDKLLEA
KHSGPRLCID LSMTHYMSKK ELSRLAGQIR RLYGSNKKAD RPFWICLTGF TTDSPLYEEC
VRMNDGFSSY LLDITEEDCF SLFPLETLVY LTPDSEHALE DVDLNKVYIL GGLVDESIQK
KVTFQKAREY SVKTARLPIQ EYMVRNQNGK NYHSEILAIN QVFDILSTYL ETHNWPEALK
KGVSSGKGYI LRNSVE
