位置:首页 > 蛋白库 > TGS1_MOUSE
TGS1_MOUSE
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   03-AUG-2022, entry version 146.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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; 23.
DR   IntAct; Q923W1; 21.
DR   STRING; 10090.ENSMUSP00000054112; -.
DR   iPTMnet; Q923W1; -.
DR   PhosphoSitePlus; Q923W1; -.
DR   EPD; Q923W1; -.
DR   jPOST; Q923W1; -.
DR   MaxQB; Q923W1; -.
DR   PaxDb; Q923W1; -.
DR   PeptideAtlas; Q923W1; -.
DR   PRIDE; Q923W1; -.
DR   ProteomicsDB; 262906; -.
DR   Antibodypedia; 11709; 167 antibodies from 26 providers.
DR   DNASU; 116940; -.
DR   Ensembl; ENSMUST00000052712; ENSMUSP00000054112; ENSMUSG00000028233.
DR   GeneID; 116940; -.
DR   KEGG; mmu:116940; -.
DR   UCSC; uc008rwi.2; mouse.
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; VNKPMDE; -.
DR   OrthoDB; 176302at2759; -.
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 78 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 257 other 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   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR019012; RNA_cap_Gua-N2-MeTrfase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF09445; Methyltransf_15; 1.
DR   SUPFAM; SSF53335; SSF53335; 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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024