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P85107 (TGS1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Tgs1
Synonyms:Ncoa6ip, Pimt
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length850 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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.

Subunit structure

May form homooligomers. Interacts with CREBBP/CBP, EED/WAIT1, EP300/P300, NCOA6/PRIP, PPARBP/PBP and SMN By similarity. UniProtKB Q96RS0

Subcellular location

Cytoplasm By similarity. Nucleus By similarity. Note: A 90 kDa isoform isfound in the nucleus while a 55 kDa isoform isfound in the cytoplasm By similarity. UniProtKB Q96RS0

Tissue specificity

A 55 kDa isoform iswidely expressed while a 90 kDa isoform isdetected exclusively in brain and testis (at protein level). Ref.2

Sequence similarities

Belongs to the methyltransferase superfamily. Trimethylguanosine synthase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 850850Trimethylguanosine synthase
PRO_0000283727

Regions

Compositional bias611 – 62414Lys-rich

Sites

Binding site7131S-adenosyl-L-methionine By similarity UniProtKB Q12052

Amino acid modifications

Modified residue611Phosphothreonine By similarity
Modified residue1521Phosphoserine By similarity
Modified residue4311Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
P85107 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: 1C47E614F90382DD

FASTA85096,045
        10         20         30         40         50         60 
MCCEKWSHVA EMLLFIEDRE EEYKILCLCS RAFVEDRKLY NLGLKGYYVK SSGNNAGDRV 

        70         80         90        100        110        120 
TEEEEDDHSS GTTESHSADE GDLDPEAKLM RSMGLPVRFG RMSTHGSFEV SMNARNKAKV 

       130        140        150        160        170        180 
RQKRRKHRKQ YLDEIVREDW RNDCEEDDLV VSDDPSSVEH CENNSACEIQ SKTDAEAENL 

       190        200        210        220        230        240 
PVENTLAPKL EVTENWEKYW NEYGEGLLWQ SWQEKYPDQT LSSEPWNLPD TKEEWEQHYS 

       250        260        270        280        290        300 
QLYWYYLEQF QYWEAQGWTF VASQNCDKDV CTSHTQVDQN AESSLKADGT TLSSSPNTAE 

       310        320        330        340        350        360 
DESLGSNDND HNEIIAGINK ITLSAEEVEQ SQLDSSEHCD KPLSEVTGKE CPASGGSDSC 

       370        380        390        400        410        420 
HGTPKESDIS ENRSSDQPAQ ELQESSGTNT SKHRPHHNGT DGNESEDDPP DHKPSKMKRS 

       430        440        450        460        470        480 
HELDIDENPD SEVDDNGFHL GFKHGSGQKY GGIPNFSRRQ VRYLEKNVKY KSKYLDMRKR 

       490        500        510        520        530        540 
MTVKNKHIVF SEESGKPFIR KSKVRSKVEK FLKWVNEPVD EEISQEPLSH NKMQDTCTSS 

       550        560        570        580        590        600 
DSEEQDMSME KTDGLMETRD PEPENCQTIS SASELEAEKS EGGSLVAAVP ENCSTEGVAN 

       610        620        630        640        650        660 
SPRAEAEVEI KKKKKKKKKN KNKKINGLPP EIASVPELAK YWAQRYRLFS RFDDGIKLDK 

       670        680        690        700        710        720 
EGWFSVTPEK IAEHIAGRVS QSFNCDIIVD AFCGVGGNTI QFALTGKRVI AIDIDPVKID 

       730        740        750        760        770        780 
LARNNAEVYG VADKIEFICG DFLLLAPCLK ADVVFLSPPW GGPDYATAET FDIRTMMSPD 

       790        800        810        820        830        840 
GFEIFRLSQK ITNNIVYFLP RNADVDQVAS LAGPGGQVEI EQNFLNNKLK TITAYFGDLI 

       850 
RRPALRSAEA 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AABR03040398 Genomic DNA. No translation available.
RefSeqNP_001101374.1. NM_001107904.1.
UniGeneRn.48378.

3D structure databases

ProteinModelPortalP85107.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000010783.

PTM databases

PhosphoSiteP85107.

Proteomic databases

PaxDbP85107.
PRIDEP85107.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000010783; ENSRNOP00000010783; ENSRNOG00000008156.
GeneID312947.
KEGGrno:312947.
UCSCRGD:1309953. rat.

Organism-specific databases

CTD96764.
RGD1309953. Tgs1.

Phylogenomic databases

eggNOGCOG0500.
GeneTreeENSGT00390000018056.
HOGENOMHOG000154561.
HOVERGENHBG059797.
InParanoidP85107.
KOK14292.
OMACSRAFVE.
OrthoDBEOG70CR73.
PhylomeDBP85107.
TreeFamTF313065.

Gene expression databases

GenevestigatorP85107.

Family and domain databases

Gene3D3.40.50.150. 1 hit.
InterProIPR019012. RNA_cap_Gua-N2-MeTrfase.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PfamPF09445. Methyltransf_15. 1 hit.
[Graphical view]
SUPFAMSSF53335. SSF53335. 1 hit.
ProtoNetSearch...

Other

NextBio665415.
PROP85107.

Entry information

Entry nameTGS1_RAT
AccessionPrimary (citable) accession number: P85107
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: April 3, 2007
Last modified: June 11, 2014
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families