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P85107

- TGS1_RAT

UniProt

P85107 - TGS1_RAT

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Protein
Trimethylguanosine synthase
Gene
Tgs1, Ncoa6ip, Pimt
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 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 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-methionine By similarityBy 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
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_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:Tgs1
Synonyms:Ncoa6ip, Pimt
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.By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 850850Trimethylguanosine synthase
PRO_0000283727Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei61 – 611Phosphothreonine By similarity
Modified residuei152 – 1521Phosphoserine By similarity
Modified residuei431 – 4311Phosphoserine By 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.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi611 – 62414Lys-rich
Add
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

« Hide 'large scale' publications
  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 Norway.
  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: September 3, 2014
This is version 55 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

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