MRM1_HUMAN
ID MRM1_HUMAN Reviewed; 353 AA.
AC Q6IN84; A8K8E2; Q96GK2; Q9H664;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=rRNA methyltransferase 1, mitochondrial {ECO:0000303|PubMed:24036117};
DE EC=2.1.1.- {ECO:0000305|PubMed:25074936};
DE AltName: Full=16S rRNA (guanosine(1145)-2'-O)-methyltransferase {ECO:0000303|PubMed:25074936};
DE AltName: Full=16S rRNA [Gm1145] 2'-O-methyltransferase {ECO:0000303|PubMed:25074936};
DE Flags: Precursor;
GN Name=MRM1 {ECO:0000303|PubMed:24036117};
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 AND 2).
RC TISSUE=Small intestine, and Testis;
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 MRNA] (ISOFORM 2).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Kidney, and Skin;
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 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 [6]
RP SUBCELLULAR LOCATION.
RX PubMed=24036117; DOI=10.1074/jbc.m113.515692;
RA Lee K.W., Okot-Kotber C., LaComb J.F., Bogenhagen D.F.;
RT "Mitochondrial ribosomal RNA (rRNA) methyltransferase family members are
RT positioned to modify nascent rRNA in foci near the mitochondrial DNA
RT nucleoid.";
RL J. Biol. Chem. 288:31386-31399(2013).
RN [7]
RP FUNCTION.
RX PubMed=25074936; DOI=10.1074/jbc.c114.581868;
RA Lee K.W., Bogenhagen D.F.;
RT "Assignment of 2'-O-methyltransferases to modification sites on the
RT mammalian mitochondrial large subunit 16S rRNA.";
RL J. Biol. Chem. 289:24936-24942(2014).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=25009282; DOI=10.1091/mbc.e14-01-0014;
RA Rorbach J., Boesch P., Gammage P.A., Nicholls T.J., Pearce S.F., Patel D.,
RA Hauser A., Perocchi F., Minczuk M.;
RT "MRM2 and MRM3 are involved in biogenesis of the large subunit of the
RT mitochondrial ribosome.";
RL Mol. Biol. Cell 25:2542-2555(2014).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent 2'-O-ribose
CC methyltransferase that catalyzes the formation of 2'-O-methylguanosine
CC at position 1145 (Gm1145) in the 16S mitochondrial large subunit
CC ribosomal RNA (mtLSU rRNA), a universally conserved modification in the
CC peptidyl transferase domain of the mtLSU rRNA.
CC {ECO:0000269|PubMed:25074936}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(1145) in 16S rRNA + S-adenosyl-L-methionine = 2'-O-
CC methylguanosine(1145) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:47776, Rhea:RHEA-COMP:11909, Rhea:RHEA-COMP:11910,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74269, ChEBI:CHEBI:74445;
CC Evidence={ECO:0000305|PubMed:25074936};
CC -!- INTERACTION:
CC Q6IN84; Q15848: ADIPOQ; NbExp=3; IntAct=EBI-5454865, EBI-10827839;
CC Q6IN84; Q6RW13: AGTRAP; NbExp=3; IntAct=EBI-5454865, EBI-741181;
CC Q6IN84; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-5454865, EBI-11522760;
CC Q6IN84; P29972: AQP1; NbExp=3; IntAct=EBI-5454865, EBI-745213;
CC Q6IN84; P41181: AQP2; NbExp=3; IntAct=EBI-5454865, EBI-12701138;
CC Q6IN84; Q92482: AQP3; NbExp=3; IntAct=EBI-5454865, EBI-2808854;
CC Q6IN84; Q6PL45-2: BRICD5; NbExp=3; IntAct=EBI-5454865, EBI-12244618;
CC Q6IN84; P13236: CCL4; NbExp=3; IntAct=EBI-5454865, EBI-2873970;
CC Q6IN84; Q8NHW4: CCL4L2; NbExp=3; IntAct=EBI-5454865, EBI-10271156;
CC Q6IN84; Q9UFW8: CGGBP1; NbExp=4; IntAct=EBI-5454865, EBI-723153;
CC Q6IN84; Q96MX0: CMTM3; NbExp=3; IntAct=EBI-5454865, EBI-7247651;
CC Q6IN84; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-5454865, EBI-11522780;
CC Q6IN84; O95406: CNIH1; NbExp=3; IntAct=EBI-5454865, EBI-12172273;
CC Q6IN84; Q8NI60: COQ8A; NbExp=3; IntAct=EBI-5454865, EBI-745535;
CC Q6IN84; Q96LL9: DNAJC30; NbExp=3; IntAct=EBI-5454865, EBI-8639143;
CC Q6IN84; Q9UKR5: ERG28; NbExp=3; IntAct=EBI-5454865, EBI-711490;
CC Q6IN84; P62508-3: ESRRG; NbExp=5; IntAct=EBI-5454865, EBI-12001340;
CC Q6IN84; Q9Y680: FKBP7; NbExp=3; IntAct=EBI-5454865, EBI-3918971;
CC Q6IN84; P11215: ITGAM; NbExp=3; IntAct=EBI-5454865, EBI-2568251;
CC Q6IN84; Q96E93: KLRG1; NbExp=3; IntAct=EBI-5454865, EBI-750770;
CC Q6IN84; Q9UBY5: LPAR3; NbExp=3; IntAct=EBI-5454865, EBI-12033434;
CC Q6IN84; Q969L2: MAL2; NbExp=3; IntAct=EBI-5454865, EBI-944295;
CC Q6IN84; Q14696: MESD; NbExp=3; IntAct=EBI-5454865, EBI-6165891;
CC Q6IN84; O14880: MGST3; NbExp=3; IntAct=EBI-5454865, EBI-724754;
CC Q6IN84; Q8IXM6: NRM; NbExp=3; IntAct=EBI-5454865, EBI-10262547;
CC Q6IN84; Q969Y0: NXPE3; NbExp=3; IntAct=EBI-5454865, EBI-17973370;
CC Q6IN84; Q6NTF9-3: RHBDD2; NbExp=3; IntAct=EBI-5454865, EBI-17589229;
CC Q6IN84; Q5GAN6: RNASE10; NbExp=3; IntAct=EBI-5454865, EBI-12423312;
CC Q6IN84; Q9Y6D0: SELENOK; NbExp=3; IntAct=EBI-5454865, EBI-9679163;
CC Q6IN84; Q9BT56: SPX; NbExp=3; IntAct=EBI-5454865, EBI-17975052;
CC Q6IN84; P02808: STATH; NbExp=3; IntAct=EBI-5454865, EBI-738687;
CC Q6IN84; O15400: STX7; NbExp=3; IntAct=EBI-5454865, EBI-3221827;
CC Q6IN84; P08247: SYP; NbExp=3; IntAct=EBI-5454865, EBI-9071725;
CC Q6IN84; Q9BQG1: SYT3; NbExp=3; IntAct=EBI-5454865, EBI-17284568;
CC Q6IN84; P17152: TMEM11; NbExp=3; IntAct=EBI-5454865, EBI-723946;
CC Q6IN84; Q9BU79: TMEM243; NbExp=3; IntAct=EBI-5454865, EBI-12887458;
CC Q6IN84; Q69YG0: TMEM42; NbExp=3; IntAct=EBI-5454865, EBI-12038591;
CC Q6IN84; Q5BJF2: TMEM97; NbExp=3; IntAct=EBI-5454865, EBI-12111910;
CC Q6IN84; P49638: TTPA; NbExp=3; IntAct=EBI-5454865, EBI-10210710;
CC Q6IN84; A5PKU2: TUSC5; NbExp=3; IntAct=EBI-5454865, EBI-11988865;
CC Q6IN84; Q8N0U8: VKORC1L1; NbExp=3; IntAct=EBI-5454865, EBI-11337915;
CC Q6IN84; Q6UX27-3: VSTM1; NbExp=3; IntAct=EBI-5454865, EBI-12190699;
CC Q6IN84-2; P55212: CASP6; NbExp=3; IntAct=EBI-25835707, EBI-718729;
CC Q6IN84-2; P28329-3: CHAT; NbExp=3; IntAct=EBI-25835707, EBI-25837549;
CC Q6IN84-2; P22607: FGFR3; NbExp=3; IntAct=EBI-25835707, EBI-348399;
CC Q6IN84-2; Q14957: GRIN2C; NbExp=3; IntAct=EBI-25835707, EBI-8285963;
CC Q6IN84-2; P06396: GSN; NbExp=3; IntAct=EBI-25835707, EBI-351506;
CC Q6IN84-2; P30519: HMOX2; NbExp=3; IntAct=EBI-25835707, EBI-712096;
CC Q6IN84-2; P13473-2: LAMP2; NbExp=3; IntAct=EBI-25835707, EBI-21591415;
CC Q6IN84-2; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-25835707, EBI-5280197;
CC Q6IN84-2; P62826: RAN; NbExp=3; IntAct=EBI-25835707, EBI-286642;
CC Q6IN84-2; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-25835707, EBI-741480;
CC Q6IN84-2; Q9Y649; NbExp=3; IntAct=EBI-25835707, EBI-25900580;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:24036117,
CC ECO:0000269|PubMed:25009282}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6IN84-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6IN84-2; Sequence=VSP_022494;
CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC superfamily. RNA methyltransferase TrmH family. {ECO:0000305}.
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DR EMBL; AK026231; BAB15401.1; -; mRNA.
DR EMBL; AK292307; BAF84996.1; -; mRNA.
DR EMBL; CR457357; CAG33638.1; -; mRNA.
DR EMBL; CH471199; EAW57571.1; -; Genomic_DNA.
DR EMBL; BC009416; AAH09416.2; -; mRNA.
DR EMBL; BC072411; AAH72411.1; -; mRNA.
DR CCDS; CCDS32631.1; -. [Q6IN84-1]
DR RefSeq; NP_079140.2; NM_024864.4. [Q6IN84-1]
DR AlphaFoldDB; Q6IN84; -.
DR SMR; Q6IN84; -.
DR BioGRID; 122999; 372.
DR IntAct; Q6IN84; 86.
DR MINT; Q6IN84; -.
DR STRING; 9606.ENSP00000481559; -.
DR GlyGen; Q6IN84; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q6IN84; -.
DR PhosphoSitePlus; Q6IN84; -.
DR BioMuta; MRM1; -.
DR DMDM; 74736506; -.
DR EPD; Q6IN84; -.
DR jPOST; Q6IN84; -.
DR MassIVE; Q6IN84; -.
DR MaxQB; Q6IN84; -.
DR PaxDb; Q6IN84; -.
DR PeptideAtlas; Q6IN84; -.
DR PRIDE; Q6IN84; -.
DR ProteomicsDB; 66442; -. [Q6IN84-1]
DR ProteomicsDB; 66443; -. [Q6IN84-2]
DR Antibodypedia; 72774; 123 antibodies from 21 providers.
DR DNASU; 79922; -.
DR Ensembl; ENST00000611231.2; ENSP00000478520.1; ENSG00000274853.2. [Q6IN84-1]
DR Ensembl; ENST00000614766.5; ENSP00000481559.1; ENSG00000278619.5. [Q6IN84-1]
DR GeneID; 79922; -.
DR KEGG; hsa:79922; -.
DR MANE-Select; ENST00000614766.5; ENSP00000481559.1; NM_024864.5; NP_079140.2.
DR UCSC; uc002hne.4; human. [Q6IN84-1]
DR CTD; 79922; -.
DR DisGeNET; 79922; -.
DR GeneCards; MRM1; -.
DR HGNC; HGNC:26202; MRM1.
DR HPA; ENSG00000278619; Low tissue specificity.
DR neXtProt; NX_Q6IN84; -.
DR OpenTargets; ENSG00000278619; -.
DR PharmGKB; PA142671338; -.
DR VEuPathDB; HostDB:ENSG00000278619; -.
DR eggNOG; KOG0838; Eukaryota.
DR GeneTree; ENSGT00390000018761; -.
DR HOGENOM; CLU_021322_5_1_1; -.
DR InParanoid; Q6IN84; -.
DR OMA; QVPPYEY; -.
DR OrthoDB; 1412032at2759; -.
DR PhylomeDB; Q6IN84; -.
DR TreeFam; TF315167; -.
DR BRENDA; 2.1.1.B125; 2681.
DR PathwayCommons; Q6IN84; -.
DR Reactome; R-HSA-6793080; rRNA modification in the mitochondrion.
DR SignaLink; Q6IN84; -.
DR BioGRID-ORCS; 79922; 19 hits in 1068 CRISPR screens.
DR GenomeRNAi; 79922; -.
DR Pharos; Q6IN84; Tbio.
DR PRO; PR:Q6IN84; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q6IN84; protein.
DR Bgee; ENSG00000278619; Expressed in mucosa of transverse colon and 92 other tissues.
DR ExpressionAtlas; Q6IN84; baseline and differential.
DR Genevisible; Q6IN84; HS.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0016435; F:rRNA (guanine) methyltransferase activity; IBA:GO_Central.
DR GO; GO:0070039; F:rRNA (guanosine-2'-O-)-methyltransferase activity; IMP:FlyBase.
DR GO; GO:0000451; P:rRNA 2'-O-methylation; TAS:Reactome.
DR GO; GO:0000154; P:rRNA modification; IBA:GO_Central.
DR Gene3D; 3.30.1330.30; -; 1.
DR Gene3D; 3.40.1280.10; -; 1.
DR InterPro; IPR029028; Alpha/beta_knot_MTases.
DR InterPro; IPR029064; L30e-like.
DR InterPro; IPR004441; rRNA_MeTrfase_TrmH.
DR InterPro; IPR001537; SpoU_MeTrfase.
DR InterPro; IPR013123; SpoU_subst-bd.
DR InterPro; IPR029026; tRNA_m1G_MTases_N.
DR Pfam; PF00588; SpoU_methylase; 1.
DR Pfam; PF08032; SpoU_sub_bind; 1.
DR SMART; SM00967; SpoU_sub_bind; 1.
DR SUPFAM; SSF55315; SSF55315; 1.
DR SUPFAM; SSF75217; SSF75217; 1.
DR TIGRFAMs; TIGR00186; rRNA_methyl_3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Methyltransferase; Mitochondrion; Reference proteome;
KW rRNA processing; S-adenosyl-L-methionine; Transferase; Transit peptide.
FT TRANSIT 1..20
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 21..353
FT /note="rRNA methyltransferase 1, mitochondrial"
FT /id="PRO_0000273202"
FT REGION 311..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..198
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_022494"
FT VARIANT 98
FT /note="P -> S (in dbSNP:rs60978234)"
FT /id="VAR_061906"
SQ SEQUENCE 353 AA; 38638 MW; D47B4B147523D07D CRC64;
MALLSTVRGA TWGRLVTRHF SHAARHGERP GGEELSRLLL DDLVPTSRLE LLFGMTPCLL
ALQAARRSVA RLLLQAGKAG LQGKRAELLR MAEARDIPVL RPRRQKLDTM CRYQVHQGVC
MEVSPLRPRP WREAGEASPG DDPQQLWLVL DGIQDPRNFG AVLRSAHFLG VDKVITSRRN
SCPLTPVVSK SSAGAMEVMD VFSTDDLTGF LQTKAQQGWL VAGTVGCPST EDPQSSEIPI
MSCLEFLWER PTLLVLGNEG SGLSQEVQAS CQLLLTILPR RQLPPGLESL NVSVAAGILL
HSICSQRKGF PTEGERRQLL QDPQEPSARS EGLSMAQHPG LSSGPEKERQ NEG
