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P85107

- TGS1_RAT

UniProt

P85107 - TGS1_RAT

Protein

Trimethylguanosine synthase

Gene

Tgs1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 56 (01 Oct 2014)
      Sequence version 1 (03 Apr 2007)
      Previous versions | rss
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    Functioni

    Catalyzes the 2 serial methylation steps for the conversion of the 7-monomethylguanosine (m7G) caps of snRNAs and snoRNAs to a 2,2,7-trimethylguanosine (m(2,2,7)G) cap structure. The enzyme is specific for guanine, and N7 methylation must precede N2 methylation. Hypermethylation of the m7G cap of U snRNAs leads to their concentration in nuclear foci, their colocalization with coilin and the formation of canonical Cajal bodies (CBs). Plays a role in transcriptional regulation By similarity.By similarity

    Catalytic activityi

    S-adenosyl-L-methionine + m7G(5')pppR-RNA = S-adenosyl-L-homocysteine + m(2,7)G(5')pppR-RNA.
    S-adenosyl-L-methionine + m(2,7)G(5')pppR-RNA = S-adenosyl-L-homocysteine + m(2,2,7)G(5')pppR-RNA.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei713 – 7131S-adenosyl-L-methionineBy similarity

    GO - Molecular functioni

    1. RNA trimethylguanosine synthase activity Source: Ensembl

    GO - Biological processi

    1. 7-methylguanosine RNA capping Source: InterPro
    2. regulation of transcription, DNA-templated Source: UniProtKB-KW
    3. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    S-adenosyl-L-methionine

    Enzyme and pathway databases

    ReactomeiREACT_196405. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
    REACT_196408. PPARA activates gene expression.
    REACT_196852. REV-ERBA represses gene expression.
    REACT_196856. RORA activates circadian gene expression.
    REACT_198613. Activation of gene expression by SREBF (SREBP).
    REACT_198793. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
    REACT_216049. Transcriptional activation of mitochondrial biogenesis.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Trimethylguanosine synthase (EC:2.1.1.-)
    Alternative name(s):
    Nuclear receptor coactivator 6-interacting protein
    PRIP-interacting protein with methyltransferase motif
    Short name:
    PIMT
    Short name:
    PIPMT
    Gene namesi
    Name:Tgs1By similarity
    Synonyms:Ncoa6ipImported, PimtBy similarity
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 5

    Organism-specific databases

    RGDi1309953. Tgs1.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity
    Note: A 90 kDa isoform is found in the nucleus while a 55 kDa isoform is found in the cytoplasm.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 850850Trimethylguanosine synthasePRO_0000283727Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei61 – 611PhosphothreonineBy similarity
    Modified residuei152 – 1521PhosphoserineBy similarity
    Modified residuei431 – 4311PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP85107.
    PRIDEiP85107.

    PTM databases

    PhosphoSiteiP85107.

    Expressioni

    Tissue specificityi

    A 55 kDa isoform is widely expressed while a 90 kDa isoform is detected exclusively in brain and testis (at protein level).1 Publication

    Gene expression databases

    GenevestigatoriP85107.

    Interactioni

    Subunit structurei

    May form homooligomers. Interacts with CREBBP/CBP, EED/WAIT1, EP300/P300, NCOA6/PRIP, PPARBP/PBP and SMN By similarity.By similarity

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000010783.

    Structurei

    3D structure databases

    ProteinModelPortaliP85107.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi611 – 62414Lys-richSequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0500.
    GeneTreeiENSGT00390000018056.
    HOGENOMiHOG000154561.
    HOVERGENiHBG059797.
    InParanoidiP85107.
    KOiK14292.
    OMAiCSRAFVE.
    OrthoDBiEOG70CR73.
    PhylomeDBiP85107.
    TreeFamiTF313065.

    Family and domain databases

    Gene3Di3.40.50.150. 1 hit.
    InterProiIPR019012. RNA_cap_Gua-N2-MeTrfase.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view]
    PfamiPF09445. Methyltransf_15. 1 hit.
    [Graphical view]
    SUPFAMiSSF53335. SSF53335. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P85107-1 [UniParc]FASTAAdd to Basket

    « Hide

    MCCEKWSHVA EMLLFIEDRE EEYKILCLCS RAFVEDRKLY NLGLKGYYVK    50
    SSGNNAGDRV TEEEEDDHSS GTTESHSADE GDLDPEAKLM RSMGLPVRFG 100
    RMSTHGSFEV SMNARNKAKV RQKRRKHRKQ YLDEIVREDW RNDCEEDDLV 150
    VSDDPSSVEH CENNSACEIQ SKTDAEAENL PVENTLAPKL EVTENWEKYW 200
    NEYGEGLLWQ SWQEKYPDQT LSSEPWNLPD TKEEWEQHYS QLYWYYLEQF 250
    QYWEAQGWTF VASQNCDKDV CTSHTQVDQN AESSLKADGT TLSSSPNTAE 300
    DESLGSNDND HNEIIAGINK ITLSAEEVEQ SQLDSSEHCD KPLSEVTGKE 350
    CPASGGSDSC HGTPKESDIS ENRSSDQPAQ ELQESSGTNT SKHRPHHNGT 400
    DGNESEDDPP DHKPSKMKRS HELDIDENPD SEVDDNGFHL GFKHGSGQKY 450
    GGIPNFSRRQ VRYLEKNVKY KSKYLDMRKR MTVKNKHIVF SEESGKPFIR 500
    KSKVRSKVEK FLKWVNEPVD EEISQEPLSH NKMQDTCTSS DSEEQDMSME 550
    KTDGLMETRD PEPENCQTIS SASELEAEKS EGGSLVAAVP ENCSTEGVAN 600
    SPRAEAEVEI KKKKKKKKKN KNKKINGLPP EIASVPELAK YWAQRYRLFS 650
    RFDDGIKLDK EGWFSVTPEK IAEHIAGRVS QSFNCDIIVD AFCGVGGNTI 700
    QFALTGKRVI AIDIDPVKID LARNNAEVYG VADKIEFICG DFLLLAPCLK 750
    ADVVFLSPPW GGPDYATAET FDIRTMMSPD GFEIFRLSQK ITNNIVYFLP 800
    RNADVDQVAS LAGPGGQVEI EQNFLNNKLK TITAYFGDLI RRPALRSAEA 850
    Length:850
    Mass (Da):96,045
    Last modified:April 3, 2007 - v1
    Checksum:i1C47E614F90382DD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AABR03040398 Genomic DNA. No translation available.
    RefSeqiNP_001101374.1. NM_001107904.1.
    UniGeneiRn.48378.

    Genome annotation databases

    EnsembliENSRNOT00000010783; ENSRNOP00000010783; ENSRNOG00000008156.
    GeneIDi312947.
    KEGGirno:312947.
    UCSCiRGD:1309953. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AABR03040398 Genomic DNA. No translation available.
    RefSeqi NP_001101374.1. NM_001107904.1.
    UniGenei Rn.48378.

    3D structure databases

    ProteinModelPortali P85107.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000010783.

    PTM databases

    PhosphoSitei P85107.

    Proteomic databases

    PaxDbi P85107.
    PRIDEi P85107.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000010783 ; ENSRNOP00000010783 ; ENSRNOG00000008156 .
    GeneIDi 312947.
    KEGGi rno:312947.
    UCSCi RGD:1309953. rat.

    Organism-specific databases

    CTDi 96764.
    RGDi 1309953. Tgs1.

    Phylogenomic databases

    eggNOGi COG0500.
    GeneTreei ENSGT00390000018056.
    HOGENOMi HOG000154561.
    HOVERGENi HBG059797.
    InParanoidi P85107.
    KOi K14292.
    OMAi CSRAFVE.
    OrthoDBi EOG70CR73.
    PhylomeDBi P85107.
    TreeFami TF313065.

    Enzyme and pathway databases

    Reactomei REACT_196405. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
    REACT_196408. PPARA activates gene expression.
    REACT_196852. REV-ERBA represses gene expression.
    REACT_196856. RORA activates circadian gene expression.
    REACT_198613. Activation of gene expression by SREBF (SREBP).
    REACT_198793. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
    REACT_216049. Transcriptional activation of mitochondrial biogenesis.

    Miscellaneous databases

    NextBioi 665415.
    PROi P85107.

    Gene expression databases

    Genevestigatori P85107.

    Family and domain databases

    Gene3Di 3.40.50.150. 1 hit.
    InterProi IPR019012. RNA_cap_Gua-N2-MeTrfase.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view ]
    Pfami PF09445. Methyltransf_15. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53335. SSF53335. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
      Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
      , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
      Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Brown Norway1 Publication.
    2. "Different isoforms of PRIP-interacting protein with methyltransferase domain/trimethylguanosine synthase localize to the cytoplasm and nucleus."
      Enuenlue I., Papai G., Cserpan I., Udvardy A., Jeang K.-T., Boros I.
      Biochem. Biophys. Res. Commun. 309:44-51(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiTGS1_RAT
    AccessioniPrimary (citable) accession number: P85107
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 3, 2007
    Last sequence update: April 3, 2007
    Last modified: October 1, 2014
    This is version 56 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3