P85107 (TGS1_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	Tgs1
Synonyms:	Ncoa6ip, Pimt

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	850 AA.
Sequence status	Complete.
Protein existence	Evidence 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 is found in the nucleus while a 55 kDa isoform is found in the cytoplasm By similarity. UniProtKB Q96RS0
Tissue specificity	A 55 kDa isoform is widely expressed while a 90 kDa isoform is detected exclusively in brain and testis (at protein level). Ref.2
Sequence similarities	Belongs to the methyltransferase superfamily. Trimethylguanosine synthase family.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Molecular function	Methyltransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	7-methylguanosine RNA capping Inferred from electronic annotation. Source: InterPro regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	RNA trimethylguanosine synthase activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 850	850	Trimethylguanosine synthase		PRO_0000283727
Regions
	Compositional bias	611 – 624	14	Lys-rich
Sites
	Binding site	713	1	S-adenosyl-L-methionine By similarity UniProtKB Q12052
Amino acid modifications
	Modified residue	61	1	Phosphothreonine By similarity
	Modified residue	152	1	Phosphoserine By similarity
	Modified residue	431	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P85107 [UniParc]. Last modified April 3, 2007. Version 1. Checksum: 1C47E614F90382DD	FASTA	850	96,045
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
IPI	IPI00870235.
RefSeq	NP_001101374.1. NM_001107904.1.
UniGene	Rn.48378.
3D structure databases
ProteinModelPortal	P85107.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000010783.
PTM databases
PhosphoSite	P85107.
Proteomic databases
PaxDb	P85107.
PRIDE	P85107.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000010783; ENSRNOP00000010783; ENSRNOG00000008156.
GeneID	312947.
KEGG	rno:312947.
UCSC	RGD:1309953. rat.
Organism-specific databases
CTD	96764.
RGD	1309953. Tgs1.
Phylogenomic databases
eggNOG	COG0500.
GeneTree	ENSGT00390000018056.
HOGENOM	HOG000154561.
HOVERGEN	HBG059797.
InParanoid	P85107.
KO	K14292.
OrthoDB	EOG43TZTV.
Gene expression databases
Genevestigator	P85107.
Family and domain databases
InterPro	IPR019012. RNA_cap_Gua-N2-MeTrfase. [Graphical view]
Pfam	PF09445. Methyltransf_15. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	665415.

Entry information

Entry name

TGS1_RAT

Accession

Primary (citable) accession number: P85107

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 3, 2007
Last sequence update:	April 3, 2007
Last modified:	April 3, 2013
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program