ID TGS1_MOUSE Reviewed; 853 AA.
AC Q923W1; A2AJF7; Q6DI60; Q6PEA7; Q8R0W9;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 27-MAR-2024, entry version 155.
DE RecName: Full=Trimethylguanosine synthase;
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q96RS0};
DE AltName: Full=Nuclear receptor coactivator 6-interacting protein;
DE AltName: Full=PRIP-interacting protein with methyltransferase motif;
DE Short=PIMT;
DE Short=PIPMT;
GN Name=Tgs1; Synonyms=Ncoa6ip, Pimt;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH NCOA6, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Spleen;
RX PubMed=11517327; DOI=10.1073/pnas.181347498;
RA Zhu Y.-J., Qi C., Cao W.-Q., Yeldandi A.V., Rao M.S., Reddy J.K.;
RT "Cloning and characterization of PIMT, a protein with a methyltransferase
RT domain, which interacts with and enhances nuclear receptor coactivator PRIP
RT function.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:10380-10385(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Limb, Liver, and Mammary tumor;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152 AND SER-431, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, and
RC Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalyzes the 2 serial methylation steps for the conversion
CC of the 7-monomethylguanosine (m(7)G) caps of snRNAs and snoRNAs to a
CC 2,2,7-trimethylguanosine (m(2,2,7)G) cap structure. The enzyme is
CC specific for guanine, and N7 methylation must precede N2 methylation.
CC Hypermethylation of the m7G cap of U snRNAs leads to their
CC concentration in nuclear foci, their colocalization with coilin and the
CC formation of canonical Cajal bodies (CBs). Plays a role in
CC transcriptional regulation (By similarity).
CC {ECO:0000250|UniProtKB:Q96RS0, ECO:0000269|PubMed:11517327}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside
CC in mRNA + S-adenosyl-L-methionine = a 5'-end (N(2),N(7)-dimethyl 5'-
CC triphosphoguanosine)-ribonucleoside in mRNA + H(+) + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:67620, Rhea:RHEA-COMP:17167, Rhea:RHEA-
CC COMP:17315, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:156461, ChEBI:CHEBI:172880;
CC Evidence={ECO:0000250|UniProtKB:Q96RS0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67621;
CC Evidence={ECO:0000250|UniProtKB:Q96RS0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (N(2),N(7)-dimethyl 5'-triphosphoguanosine)-
CC ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end
CC (N(2),N(2),N(7)-trimethyl 5'-triphosphoguanosine)-(ribonucleoside) in
CC mRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67624,
CC Rhea:RHEA-COMP:17171, Rhea:RHEA-COMP:17315, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:167623,
CC ChEBI:CHEBI:172880; Evidence={ECO:0000250|UniProtKB:Q96RS0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67625;
CC Evidence={ECO:0000250|UniProtKB:Q96RS0};
CC -!- SUBUNIT: May form homooligomers. Interacts with CREBBP/CBP, EED/WAIT1,
CC EP300/P300, NCOA6/PRIP, PPARBP/PBP and SMN (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96RS0}.
CC Nucleus, Cajal body {ECO:0000269|PubMed:11517327}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q96RS0}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:11517327}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC Trimethylguanosine synthase family. {ECO:0000305}.
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DR EMBL; AF389908; AAK84355.1; -; mRNA.
DR EMBL; AL732617; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC026368; AAH26368.1; -; mRNA.
DR EMBL; BC058183; AAH58183.1; -; mRNA.
DR EMBL; BC075728; AAH75728.1; -; mRNA.
DR CCDS; CCDS17938.1; -.
DR RefSeq; NP_473430.3; NM_054089.4.
DR AlphaFoldDB; Q923W1; -.
DR SMR; Q923W1; -.
DR BioGRID; 228104; 24.
DR IntAct; Q923W1; 21.
DR STRING; 10090.ENSMUSP00000054112; -.
DR iPTMnet; Q923W1; -.
DR PhosphoSitePlus; Q923W1; -.
DR SwissPalm; Q923W1; -.
DR EPD; Q923W1; -.
DR jPOST; Q923W1; -.
DR MaxQB; Q923W1; -.
DR PaxDb; 10090-ENSMUSP00000054112; -.
DR PeptideAtlas; Q923W1; -.
DR ProteomicsDB; 262906; -.
DR Pumba; Q923W1; -.
DR Antibodypedia; 11709; 182 antibodies from 26 providers.
DR DNASU; 116940; -.
DR Ensembl; ENSMUST00000052712.6; ENSMUSP00000054112.6; ENSMUSG00000028233.7.
DR GeneID; 116940; -.
DR KEGG; mmu:116940; -.
DR UCSC; uc008rwi.2; mouse.
DR AGR; MGI:2151797; -.
DR CTD; 96764; -.
DR MGI; MGI:2151797; Tgs1.
DR VEuPathDB; HostDB:ENSMUSG00000028233; -.
DR eggNOG; KOG2730; Eukaryota.
DR GeneTree; ENSGT00390000018056; -.
DR HOGENOM; CLU_016892_0_0_1; -.
DR InParanoid; Q923W1; -.
DR OMA; GWETYWA; -.
DR OrthoDB; 5473515at2759; -.
DR PhylomeDB; Q923W1; -.
DR TreeFam; TF313065; -.
DR Reactome; R-MMU-191859; snRNP Assembly.
DR Reactome; R-MMU-400206; Regulation of lipid metabolism by PPARalpha.
DR Reactome; R-MMU-9707564; Cytoprotection by HMOX1.
DR BioGRID-ORCS; 116940; 23 hits in 83 CRISPR screens.
DR ChiTaRS; Tgs1; mouse.
DR PRO; PR:Q923W1; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q923W1; Protein.
DR Bgee; ENSMUSG00000028233; Expressed in optic fissure and 260 other cell types or tissues.
DR Genevisible; Q923W1; MM.
DR GO; GO:0015030; C:Cajal body; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0071164; F:RNA trimethylguanosine synthase activity; ISO:MGI.
DR GO; GO:0036261; P:7-methylguanosine cap hypermethylation; ISO:MGI.
DR GO; GO:0009452; P:7-methylguanosine RNA capping; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR019012; RNA_cap_Gua-N2-MeTrfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR14741; S-ADENOSYLMETHIONINE-DEPENDENT METHYLTRANSFERASE RELATED; 1.
DR PANTHER; PTHR14741:SF32; TRIMETHYLGUANOSINE SYNTHASE; 1.
DR Pfam; PF09445; Methyltransf_15; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Methyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW Transferase.
FT CHAIN 1..853
FT /note="Trimethylguanosine synthase"
FT /id="PRO_0000204469"
FT REGION 54..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 523..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..426
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..544
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 711
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT MOD_RES 61
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96RS0"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96RS0"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96RS0"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96RS0"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96RS0"
FT MOD_RES 144
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q96RS0"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 405
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96RS0"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 572
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96RS0"
FT CONFLICT 512
FT /note="F -> L (in Ref. 3; AAH75728)"
FT /evidence="ECO:0000305"
FT CONFLICT 633
FT /note="V -> G (in Ref. 1; AAK84355)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 853 AA; 96790 MW; A69974BE660DA3AF CRC64;
MCCEKWNHVA EMLLFIEDRE EEYKILCLCS RAFVEDRKLY NLGLKGYYVK SSGNNAGDQG
TEEEEDGHSN GTAESHSPNE SDLDSEAKLM RSMGLPIQFG RMSSHENFEM SMNARNKAKV
KQKRRKHQKR YLDEMVRESW RNDYEEDDLV VSDDPSSVEH CENNRTCEIQ SKAGSEVENL
PVENTLAPKL EVPENWEKYW NEYGEGLLWQ SWQEKYPDQT LSSEPWNLPD TKEEWEQHYS
QLYWYYLEQF QYWEAQGWTF TASQNCDKDV YTSHTEVDQN AESSLKADVM TFSSSPNIVE
DEIPGSNDND HNEIITAINN ITVSAEKVEQ SQLDSSQHCD EPLSEITGKE CPASGGSDSC
NGTPKENDIS ENRSSDQPAK ELQESSGTNK GKHRPHHNGA DGHESDDDPP EHKPSKVKRS
HELDVDENPD SEVDDNGFLL GFKHGSGQKY GGIPNFSHRQ VRYLEKNVKY KSKYLDLRKQ
MPVKSKHILF TEDSGKPFVV CKSKVRSKVE KFLKWVNERV DEETSQDSLS QNKMQDTCTS
SDSEEQDMSL EKADNLMETR DPEPEKCQII SSATELEAEK SEVGSLVATV PENCSTEEIP
NSPHAETEVE IKKKKKKNKN KKINDLPPEI ASVPELAKYW AQRYRLFSRF DDGIKLDKEG
WFSVTPEKIA EHIAGRVSQA FRCDVVVDAF CGVGGNTIQF ALTGKRVIAI DIDPVKIDLA
RNNAEVYGIA DKIEFICGDF LLLAPCLKAD VVFLSPPWGG PDYATAETFD IRTMMSPDGF
EIFRLSQKIT NNIVYFLPRN ADIDQVASLA GLGGQVEIEQ NFLNNKLKTI TAYFGDLIRR
PALLKTSTSE AEV
//
