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Protein

Trimethylguanosine synthase

Gene

TGS1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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.4 Publications

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.

Kineticsi

  1. KM=30 µM for m7GDP1 Publication
  2. KM=5 µM for S-adenosyl-L-methionine1 Publication

    pH dependencei

    Optimum pH is 8.5-9.5.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei719 – 7191S-adenosyl-L-methionineBy similarity
    Binding sitei766 – 76617-methylguanosine1 Publication

    GO - Molecular functioni

    • RNA trimethylguanosine synthase activity Source: BHF-UCL

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    S-adenosyl-L-methionine

    Enzyme and pathway databases

    ReactomeiREACT_11066. snRNP Assembly.
    REACT_111118. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
    REACT_116145. PPARA activates gene expression.
    REACT_118659. RORA activates gene expression.
    REACT_118713. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
    REACT_147904. Activation of gene expression by SREBF (SREBP).
    REACT_19241. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
    REACT_24941. Circadian Clock.
    REACT_264212. Transcriptional activation of mitochondrial biogenesis.
    REACT_27161. Transcriptional regulation of white adipocyte differentiation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Trimethylguanosine synthase (EC:2.1.1.-)
    Alternative name(s):
    CLL-associated antigen KW-2
    Cap-specific guanine-N2 methyltransferase
    Hepatocellular carcinoma-associated antigen 137
    Nuclear receptor coactivator 6-interacting protein
    PRIP-interacting protein with methyltransferase motif
    Short name:
    PIMT
    Short name:
    PIPMT
    Gene namesi
    Name:TGS1
    Synonyms:HCA137, NCOA6IP, PIMT
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:17843. TGS1.

    Subcellular locationi

    • Cytoplasm
    • NucleusCajal body

    • Note: A 90 kDa isoform is found in the nucleus while a 55 kDa isoform is found in the cytoplasm and colocalizes with the tubulin network.

    GO - Cellular componenti

    • Cajal body Source: UniProtKB-SubCell
    • cytoplasm Source: HPA
    • cytosol Source: Reactome
    • extracellular space Source: UniProtKB
    • nucleoplasm Source: HPA
    • nucleus Source: HPA
    • small nuclear ribonucleoprotein complex Source: BHF-UCL
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi655 – 6551F → A: Loss of catalytic activity. 1 Publication
    Mutagenesisi673 – 6731T → A: Decreases catalytic activity to 13 percent of wild type. 1 Publication
    Mutagenesisi696 – 6961D → A: Loss of catalytic activity. 1 Publication
    Mutagenesisi704 – 7041N → A: Decreases catalytic activity to 5 percent of wild type. 1 Publication
    Mutagenesisi719 – 7191D → A: Loss of catalytic activity. 1 Publication
    Mutagenesisi731 – 7311N → A: Decreases catalytic activity to 4 percent of wild type. 1 Publication
    Mutagenesisi763 – 7631S → A: Decreases catalytic activity to 26 percent of wild type. 2 Publications
    Mutagenesisi766 – 7661W → A: Loss of catalytic activity. 2 Publications
    Mutagenesisi807 – 8071R → A: Decreases catalytic activity to 6 percent of wild type. 1 Publication
    Mutagenesisi808 – 8081N → A: Decreases catalytic activity to 11 percent of wild type. 1 Publication

    Organism-specific databases

    PharmGKBiPA162405660.

    Polymorphism and mutation databases

    BioMutaiTGS1.
    DMDMi317373500.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 853853Trimethylguanosine synthasePRO_0000204468Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei55 – 551Phosphoserine2 Publications
    Modified residuei60 – 601Phosphothreonine2 Publications
    Modified residuei85 – 851Phosphoserine1 Publication
    Modified residuei89 – 891Phosphoserine3 Publications
    Modified residuei154 – 1541Phosphoserine2 Publications
    Modified residuei438 – 4381Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ96RS0.
    PaxDbiQ96RS0.
    PRIDEiQ96RS0.

    PTM databases

    PhosphoSiteiQ96RS0.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed. High expression in heart, skeletal muscle, kidney, liver and placenta.1 Publication

    Gene expression databases

    BgeeiQ96RS0.
    CleanExiHS_TGS1.
    ExpressionAtlasiQ96RS0. baseline and differential.
    GenevisibleiQ96RS0. HS.

    Organism-specific databases

    HPAiHPA025024.
    HPA029824.

    Interactioni

    Subunit structurei

    May form homooligomers. Interacts with CREBBP/CBP, EED/WAIT1, EP300/P300, NCOA6/PRIP, PPARBP/PBP and SMN.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NOP58Q9Y2X32EBI-949244,EBI-395469

    Protein-protein interaction databases

    BioGridi125179. 12 interactions.
    DIPiDIP-49970N.
    IntActiQ96RS0. 7 interactions.
    MINTiMINT-2878093.
    STRINGi9606.ENSP00000260129.

    Structurei

    Secondary structure

    1
    853
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi636 – 6405Combined sources
    Helixi642 – 6443Combined sources
    Helixi645 – 6495Combined sources
    Helixi651 – 6544Combined sources
    Helixi658 – 6603Combined sources
    Helixi666 – 6716Combined sources
    Helixi675 – 68814Combined sources
    Beta strandi692 – 6965Combined sources
    Helixi703 – 7108Combined sources
    Beta strandi714 – 7207Combined sources
    Helixi722 – 73413Combined sources
    Helixi738 – 7403Combined sources
    Beta strandi741 – 7466Combined sources
    Helixi748 – 7514Combined sources
    Helixi752 – 7543Combined sources
    Beta strandi758 – 7625Combined sources
    Helixi769 – 7735Combined sources
    Beta strandi774 – 7774Combined sources
    Turni779 – 7813Combined sources
    Beta strandi782 – 7854Combined sources
    Helixi787 – 79711Combined sources
    Beta strandi801 – 8066Combined sources
    Helixi811 – 8166Combined sources
    Beta strandi824 – 8318Combined sources
    Beta strandi834 – 8429Combined sources
    Helixi843 – 8453Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3EGIX-ray2.21A/B/C/D653-853[»]
    3GDHX-ray2.00A/B/C618-853[»]
    ProteinModelPortaliQ96RS0.
    SMRiQ96RS0. Positions 634-844.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ96RS0.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni631 – 846216Sufficient for catalytic activityAdd
    BLAST

    Compositional bias

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

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0500.
    GeneTreeiENSGT00390000018056.
    HOGENOMiHOG000154561.
    HOVERGENiHBG059797.
    InParanoidiQ96RS0.
    KOiK14292.
    OMAiMNTRNKV.
    OrthoDBiEOG70CR73.
    PhylomeDBiQ96RS0.
    TreeFamiTF313065.

    Family and domain databases

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

    Sequencei

    Sequence statusi: Complete.

    Q96RS0-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MCCEKWSRVA EMFLFIEERE DCKILCLCSR AFVEDRKLYN LGLKGYYIRD
    60 70 80 90 100
    SGNNSGDQAT EEEEGGYSCG TAESHDSKGI GLDESELDSE AELMRSMGLP
    110 120 130 140 150
    LQFGRITAHK DFEVSMNTRN KVKIKKKKHQ KKYLDEIVQE SWRKEYEEDD
    160 170 180 190 200
    ILASDDPSSI EQYENTRTYE LQSKKDTETE NPPVENTLSP KLEITEKWEK
    210 220 230 240 250
    YWNEYGGGLL WQSWQEKHPG QALSSEPWNF PDTKEEWEQH YSQLYWYYLE
    260 270 280 290 300
    QFQYWEAQGW TFDASQSCDT DTYTSKTEAD DKNDEKCMKV DLVSFPSSPI
    310 320 330 340 350
    MVDNDSSGTS DKDHSEILDG ISNIKLNSEE VTQSQLDSCT SHDGHQQLSE
    360 370 380 390 400
    VSSKRECPAS GQSEPRNGGT NEESNSSGNT NTDPPAEDSQ KSSGANTSKD
    410 420 430 440 450
    RPHASGTDGD ESEEDPPEHK PSKLKRSHEL DIDENPASDF DDSGSLLGFK
    460 470 480 490 500
    YGSGQKYGGI PNFSHRQVRY LEKNVKLKSK YLDMRRQIKM KNKHIFFTKE
    510 520 530 540 550
    SEKPFFKKSK ILSKVEKFLT WVNKPMDEEA SQESSSHDNV HDASTSSDSE
    560 570 580 590 600
    EQDMSVKKGD DLLETNNPEP EKCQSVSSAG ELETENYERD SLLATVPDEQ
    610 620 630 640 650
    DCVTQEVPDS RQAETEAEVK KKKNKKKNKK VNGLPPEIAA VPELAKYWAQ
    660 670 680 690 700
    RYRLFSRFDD GIKLDREGWF SVTPEKIAEH IAGRVSQSFK CDVVVDAFCG
    710 720 730 740 750
    VGGNTIQFAL TGMRVIAIDI DPVKIALARN NAEVYGIADK IEFICGDFLL
    760 770 780 790 800
    LASFLKADVV FLSPPWGGPD YATAETFDIR TMMSPDGFEI FRLSKKITNN
    810 820 830 840 850
    IVYFLPRNAD IDQVASLAGP GGQVEIEQNF LNNKLKTITA YFGDLIRRPA

    SET
    Length:853
    Mass (Da):96,620
    Last modified:January 11, 2011 - v3
    Checksum:iFF670AFBE0979443
    GO

    Sequence cautioni

    The sequence AAH11999.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence BAB15516.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti566 – 5661Missing in AAK27730 (PubMed:11517327).Curated
    Sequence conflicti624 – 6241N → T in AAK83025 (PubMed:12097419).Curated
    Sequence conflicti628 – 6281N → T in AAK83025 (PubMed:12097419).Curated
    Sequence conflicti681 – 6811I → F in AAK27730 (PubMed:11517327).Curated
    Sequence conflicti771 – 7711Y → H in AAL99922 (PubMed:12200376).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti16 – 161I → T.3 Publications
    Corresponds to variant rs1818 [ dbSNP | Ensembl ].
    VAR_024734
    Natural varianti160 – 1601I → V.
    Corresponds to variant rs3213971 [ dbSNP | Ensembl ].
    VAR_024735
    Natural varianti299 – 2991P → S.
    Corresponds to variant rs11986329 [ dbSNP | Ensembl ].
    VAR_056241
    Natural varianti511 – 5111I → T.
    Corresponds to variant rs10100659 [ dbSNP | Ensembl ].
    VAR_024736
    Natural varianti576 – 5761V → I.
    Corresponds to variant rs16922259 [ dbSNP | Ensembl ].
    VAR_024737
    Natural varianti595 – 5951T → A.
    Corresponds to variant rs10109493 [ dbSNP | Ensembl ].
    VAR_056242
    Natural varianti754 – 7541F → C.
    Corresponds to variant rs7823773 [ dbSNP | Ensembl ].
    VAR_024738

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY028423 mRNA. Translation: AAK27730.1.
    AF432215 mRNA. Translation: AAL99922.1.
    AF286340 mRNA. Translation: AAK83025.1.
    AC100817 Genomic DNA. No translation available.
    AY534911 mRNA. Translation: AAT02709.1.
    BC011999 mRNA. Translation: AAH11999.1. Different initiation.
    AK026648 mRNA. Translation: BAB15516.1. Different initiation.
    CCDSiCCDS34894.1.
    RefSeqiNP_079107.6. NM_024831.6.
    UniGeneiHs.335068.

    Genome annotation databases

    EnsembliENST00000260129; ENSP00000260129; ENSG00000137574.
    GeneIDi96764.
    KEGGihsa:96764.
    UCSCiuc003xsj.4. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY028423 mRNA. Translation: AAK27730.1.
    AF432215 mRNA. Translation: AAL99922.1.
    AF286340 mRNA. Translation: AAK83025.1.
    AC100817 Genomic DNA. No translation available.
    AY534911 mRNA. Translation: AAT02709.1.
    BC011999 mRNA. Translation: AAH11999.1. Different initiation.
    AK026648 mRNA. Translation: BAB15516.1. Different initiation.
    CCDSiCCDS34894.1.
    RefSeqiNP_079107.6. NM_024831.6.
    UniGeneiHs.335068.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3EGIX-ray2.21A/B/C/D653-853[»]
    3GDHX-ray2.00A/B/C618-853[»]
    ProteinModelPortaliQ96RS0.
    SMRiQ96RS0. Positions 634-844.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi125179. 12 interactions.
    DIPiDIP-49970N.
    IntActiQ96RS0. 7 interactions.
    MINTiMINT-2878093.
    STRINGi9606.ENSP00000260129.

    PTM databases

    PhosphoSiteiQ96RS0.

    Polymorphism and mutation databases

    BioMutaiTGS1.
    DMDMi317373500.

    Proteomic databases

    MaxQBiQ96RS0.
    PaxDbiQ96RS0.
    PRIDEiQ96RS0.

    Protocols and materials databases

    DNASUi96764.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000260129; ENSP00000260129; ENSG00000137574.
    GeneIDi96764.
    KEGGihsa:96764.
    UCSCiuc003xsj.4. human.

    Organism-specific databases

    CTDi96764.
    GeneCardsiGC08P056685.
    H-InvDBHIX0007515.
    HGNCiHGNC:17843. TGS1.
    HPAiHPA025024.
    HPA029824.
    MIMi606461. gene.
    neXtProtiNX_Q96RS0.
    PharmGKBiPA162405660.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG0500.
    GeneTreeiENSGT00390000018056.
    HOGENOMiHOG000154561.
    HOVERGENiHBG059797.
    InParanoidiQ96RS0.
    KOiK14292.
    OMAiMNTRNKV.
    OrthoDBiEOG70CR73.
    PhylomeDBiQ96RS0.
    TreeFamiTF313065.

    Enzyme and pathway databases

    ReactomeiREACT_11066. snRNP Assembly.
    REACT_111118. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
    REACT_116145. PPARA activates gene expression.
    REACT_118659. RORA activates gene expression.
    REACT_118713. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
    REACT_147904. Activation of gene expression by SREBF (SREBP).
    REACT_19241. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
    REACT_24941. Circadian Clock.
    REACT_264212. Transcriptional activation of mitochondrial biogenesis.
    REACT_27161. Transcriptional regulation of white adipocyte differentiation.

    Miscellaneous databases

    ChiTaRSiTGS1. human.
    EvolutionaryTraceiQ96RS0.
    GeneWikiiTGS1.
    GenomeRNAii96764.
    NextBioi78561.
    PROiQ96RS0.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ96RS0.
    CleanExiHS_TGS1.
    ExpressionAtlasiQ96RS0. baseline and differential.
    GenevisibleiQ96RS0. HS.

    Family and domain databases

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

    Publicationsi

    « Hide 'large scale' publications
    1. "Cloning and characterization of PIMT, a protein with a methyltransferase domain, which interacts with and enhances nuclear receptor coactivator PRIP function."
      Zhu Y.-J., Qi C., Cao W.-Q., Yeldandi A.V., Rao M.S., Reddy J.K.
      Proc. Natl. Acad. Sci. U.S.A. 98:10380-10385(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH NCOA6, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANT THR-16.
      Tissue: Liver.
    2. "Identification of tumor-associated antigens in chronic lymphocytic leukemia by SEREX."
      Krackhardt A.M., Witzens M., Harig S., Hodi F.S., Zauls A.J., Chessia M., Barrett P., Gribben J.G.
      Blood 100:2123-2131(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT THR-16.
    3. "Large scale identification of human hepatocellular carcinoma-associated antigens by autoantibodies."
      Wang Y., Han K.-J., Pang X.-W., Vaughan H.A., Qu W., Dong X.-Y., Peng J.-R., Zhao H.-T., Rui J.-A., Leng X.-S., Cebon J., Burgess A.W., Chen W.-F.
      J. Immunol. 169:1102-1109(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT THR-16.
    4. "DNA sequence and analysis of human chromosome 8."
      Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
      , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
      Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "SEREX-defined rhabdomyosarcoma antigens."
      Behrends U., Gotz C., Mautner J.
      Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 276-853.
      Tissue: Rhabdomyosarcoma.
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 574-853.
      Tissue: Urinary bladder.
    7. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 629-853.
    8. "Mammalian and yeast U3 snoRNPs are matured in specific and related nuclear compartments."
      Verheggen C., Lafontaine D.L.J., Samarsky D., Mouaikel J., Blanchard J.-M., Bordonne R., Bertrand E.
      EMBO J. 21:2736-2745(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    9. "Interaction of PIMT with transcriptional coactivators CBP, p300, and PBP differential role in transcriptional regulation."
      Misra P., Qi C., Yu S., Shah S.H., Cao W.Q., Rao M.S., Thimmapaya B., Zhu Y., Reddy J.K.
      J. Biol. Chem. 277:20011-20019(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CREBBP; EP300 AND PPARBP.
    10. "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: INTERACTION WITH EED, SUBCELLULAR LOCATION.
    11. "Interaction between the small-nuclear-RNA cap hypermethylase and the spinal muscular atrophy protein, survival of motor neuron."
      Mouaikel J., Narayanan U., Verheggen C., Matera A.G., Bertrand E., Tazi J., Bordonne R.
      EMBO Rep. 4:616-622(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SMN.
    12. "Ongoing U snRNP biogenesis is required for the integrity of Cajal bodies."
      Lemm I., Girard C., Kuhn A.N., Watkins N.J., Schneider M., Bordonne R., Luehrmann R.
      Mol. Biol. Cell 17:3221-3231(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "Genetic and biochemical analysis of yeast and human cap trimethylguanosine synthase: functional overlap of 2,2,7-trimethylguanosine caps, small nuclear ribonucleoprotein components, pre-mRNA splicing factors, and RNA decay pathways."
      Hausmann S., Zheng S., Costanzo M., Brost R.L., Garcin D., Boone C., Shuman S., Schwer B.
      J. Biol. Chem. 283:31706-31718(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF PHE-655; THR-673; ASP-696; ASN-704; ASP-719; ASN-731; SER-763; TRP-766; ARG-807 AND ASN-808.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55; THR-60; SER-154 AND SER-438, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55; THR-60; SER-89; SER-154 AND SER-438, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    17. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85 AND SER-89, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Structure analysis of the conserved methyltransferase domain of human trimethylguanosine synthase TGS1."
      Monecke T., Dickmanns A., Strasser A., Ficner R.
      Acta Crystallogr. D 65:332-338(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 653-853.
    20. "Structural basis for m7G-cap hypermethylation of small nuclear, small nucleolar and telomerase RNA by the dimethyltransferase TGS1."
      Monecke T., Dickmanns A., Ficner R.
      Nucleic Acids Res. 37:3865-3877(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 618-853 IN COMPLEX WITH 7-METHYLGUANOSINE AND S-ADENOSYL-L-HOMOCYSTEINE, MUTAGENESIS OF SER-763 AND TRP-766.

    Entry informationi

    Entry nameiTGS1_HUMAN
    AccessioniPrimary (citable) accession number: Q96RS0
    Secondary accession number(s): A6NJQ5
    , Q5GH23, Q8TDG9, Q96QU3, Q9H5V3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 20, 2005
    Last sequence update: January 11, 2011
    Last modified: July 22, 2015
    This is version 120 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 8
      Human chromosome 8: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.