Q96RS0 (TGS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	TGS1
Synonyms:	HCA137, NCOA6IP, PIMT

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	853 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. Ref.1 Ref.9 Ref.12 Ref.13
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. Ref.1 Ref.9 Ref.10 Ref.11
Subcellular location	Cytoplasm. Nucleus › Cajal 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. Ref.1 Ref.8 Ref.10
Tissue specificity	Ubiquitously expressed. High expression in heart, skeletal muscle, kidney, liver and placenta. Ref.1
Sequence similarities	Belongs to the methyltransferase superfamily. Trimethylguanosine synthase family.
Biophysicochemical properties	Kinetic parameters: KM=30 µM for m7GDP Ref.13 KM=5 µM for S-adenosyl-L-methionine pH dependence: Optimum pH is 8.5-9.5.
Sequence caution	The sequence AAH11999.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAB15516.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
Molecular function	Methyltransferase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	7-methylguanosine RNA capping Inferred from electronic annotation. Source: InterPro cellular lipid metabolic process Traceable author statement. Source: Reactome ncRNA metabolic process Traceable author statement. Source: Reactome regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW ribonucleoprotein complex import into nucleus Inferred by curator Ref.12. Source: BHF-UCL small molecule metabolic process Traceable author statement. Source: Reactome spliceosomal snRNP assembly Traceable author statement. Source: Reactome transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Cajal body Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Traceable author statement. Source: Reactome nucleoplasm Traceable author statement. Source: Reactome small nuclear ribonucleoprotein complex Inferred by curator Ref.12. Source: BHF-UCL
Molecular_function	RNA trimethylguanosine synthase activity Inferred from direct assay Ref.12. Source: BHF-UCL
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 853

853

Trimethylguanosine synthase

PRO_0000204468

Regions

Region

631 – 846

216

Sufficient for catalytic activity

Compositional bias

611 – 624

14

Lys-rich

Sites

Binding site

719

1

S-adenosyl-L-methionine By similarity

Binding site

766

1

7-methylguanosine

Amino acid modifications

Modified residue

55

1

Phosphoserine Ref.14 Ref.15

Modified residue

60

1

Phosphothreonine Ref.14 Ref.15

Modified residue

85

1

Phosphoserine Ref.16

Modified residue

89

1

Phosphoserine Ref.15 Ref.16 Ref.17

Modified residue

154

1

Phosphoserine Ref.14 Ref.15

Modified residue

438

1

Phosphoserine Ref.14 Ref.15

Natural variations

Natural variant

16

1

I → T. Ref.1 Ref.2 Ref.3
Corresponds to variant rs1818 [ dbSNP | Ensembl ].

VAR_024734

Natural variant

160

1

I → V.
Corresponds to variant rs3213971 [ dbSNP | Ensembl ].

VAR_024735

Natural variant

299

1

P → S.
Corresponds to variant rs11986329 [ dbSNP | Ensembl ].

VAR_056241

Natural variant

511

1

I → T.
Corresponds to variant rs10100659 [ dbSNP | Ensembl ].

VAR_024736

Natural variant

576

1

V → I.
Corresponds to variant rs16922259 [ dbSNP | Ensembl ].

VAR_024737

Natural variant

595

1

T → A.
Corresponds to variant rs10109493 [ dbSNP | Ensembl ].

VAR_056242

Natural variant

754

1

F → C.
Corresponds to variant rs7823773 [ dbSNP | Ensembl ].

VAR_024738

Experimental info

Mutagenesis

655

1

F → A: Loss of catalytic activity. Ref.13

Mutagenesis

673

1

T → A: Decreases catalytic activity to 13 percent of wild type. Ref.13

Mutagenesis

696

1

D → A: Loss of catalytic activity. Ref.13

Mutagenesis

704

1

N → A: Decreases catalytic activity to 5 percent of wild type. Ref.13

Mutagenesis

719

1

D → A: Loss of catalytic activity. Ref.13

Mutagenesis

731

1

N → A: Decreases catalytic activity to 4 percent of wild type. Ref.13

Mutagenesis

763

1

S → A: Decreases catalytic activity to 26 percent of wild type. Ref.13 Ref.19

Mutagenesis

766

1

W → A: Loss of catalytic activity. Ref.13 Ref.19

Mutagenesis

807

1

R → A: Decreases catalytic activity to 6 percent of wild type. Ref.13

Mutagenesis

808

1

N → A: Decreases catalytic activity to 11 percent of wild type. Ref.13

Sequence conflict

566

1

Missing in AAK27730. Ref.1

Sequence conflict

624

1

N → T in AAK83025. Ref.3

Sequence conflict

628

1

N → T in AAK83025. Ref.3

Sequence conflict

681

1

I → F in AAK27730. Ref.1

Sequence conflict

771

1

Y → H in AAL99922. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

853

Helix Strand Turn

Details...

Helix

636 – 640

5

Helix

642 – 644

3

Helix

645 – 649

5

Helix

651 – 654

4

Helix

658 – 660

3

Helix

666 – 671

6

Helix

675 – 688

14

Beta strand

692 – 696

5

Helix

703 – 710

8

Beta strand

714 – 720

7

Helix

722 – 734

13

Helix

738 – 740

3

Beta strand

741 – 746

6

Helix

748 – 751

4

Helix

752 – 754

3

Beta strand

758 – 762

5

Helix

769 – 773

5

Beta strand

774 – 777

4

Turn

779 – 781

3

Beta strand

782 – 785

4

Helix

787 – 797

11

Beta strand

801 – 806

6

Helix

811 – 816

6

Beta strand

824 – 831

8

Beta strand

834 – 842

9

Helix

843 – 845

3

Sequences

	Sequence		Length	Mass (Da)
	Q96RS0 [UniParc]. Last modified January 11, 2011. Version 3. Checksum: FF670AFBE0979443	FASTA	853	96,620
	10 20 30 40 50 60 MCCEKWSRVA EMFLFIEERE DCKILCLCSR AFVEDRKLYN LGLKGYYIRD SGNNSGDQAT 70 80 90 100 110 120 EEEEGGYSCG TAESHDSKGI GLDESELDSE AELMRSMGLP LQFGRITAHK DFEVSMNTRN 130 140 150 160 170 180 KVKIKKKKHQ KKYLDEIVQE SWRKEYEEDD ILASDDPSSI EQYENTRTYE LQSKKDTETE 190 200 210 220 230 240 NPPVENTLSP KLEITEKWEK YWNEYGGGLL WQSWQEKHPG QALSSEPWNF PDTKEEWEQH 250 260 270 280 290 300 YSQLYWYYLE QFQYWEAQGW TFDASQSCDT DTYTSKTEAD DKNDEKCMKV DLVSFPSSPI 310 320 330 340 350 360 MVDNDSSGTS DKDHSEILDG ISNIKLNSEE VTQSQLDSCT SHDGHQQLSE VSSKRECPAS 370 380 390 400 410 420 GQSEPRNGGT NEESNSSGNT NTDPPAEDSQ KSSGANTSKD RPHASGTDGD ESEEDPPEHK 430 440 450 460 470 480 PSKLKRSHEL DIDENPASDF DDSGSLLGFK YGSGQKYGGI PNFSHRQVRY LEKNVKLKSK 490 500 510 520 530 540 YLDMRRQIKM KNKHIFFTKE SEKPFFKKSK ILSKVEKFLT WVNKPMDEEA SQESSSHDNV 550 560 570 580 590 600 HDASTSSDSE EQDMSVKKGD DLLETNNPEP EKCQSVSSAG ELETENYERD SLLATVPDEQ 610 620 630 640 650 660 DCVTQEVPDS RQAETEAEVK KKKNKKKNKK VNGLPPEIAA VPELAKYWAQ RYRLFSRFDD 670 680 690 700 710 720 GIKLDREGWF SVTPEKIAEH IAGRVSQSFK CDVVVDAFCG VGGNTIQFAL TGMRVIAIDI 730 740 750 760 770 780 DPVKIALARN NAEVYGIADK IEFICGDFLL LASFLKADVV FLSPPWGGPD YATAETFDIR 790 800 810 820 830 840 TMMSPDGFEI FRLSKKITNN IVYFLPRNAD IDQVASLAGP GGQVEIEQNF LNNKLKTITA 850 YFGDLIRRPA SET

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55; THR-60; SER-154 AND SER-438, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[16]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"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, MASS SPECTROMETRY.
[18]	"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.
[19]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00291376.

RefSeq

NP_079107.6. NM_024831.6.

UniGene

Hs.335068.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3EGI	X-ray	2.21	A/B/C/D	653-853	[»]
3GDH	X-ray	2.00	A/B/C	618-853	[»]

ProteinModelPortal

Q96RS0.

SMR

Q96RS0. Positions 23-53, 634-844.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-49970N.

IntAct

Q96RS0. 4 interactions.

MINT

MINT-2878093.

STRING

9606.ENSP00000260129.

PTM databases

PhosphoSite

Q96RS0.

Polymorphism databases

DMDM

84029363.

Proteomic databases

PaxDb

Q96RS0.

PRIDE

Q96RS0.

Protocols and materials databases

DNASU

96764.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000260129; ENSP00000260129; ENSG00000137574.

GeneID

96764.

KEGG

hsa:96764.

UCSC

uc003xsj.4. human.

Organism-specific databases

CTD

96764.

GeneCards

GC08P056685.

H-InvDB

HIX0007515.

HGNC

HGNC:17843. TGS1.

HPA

HPA025024.

MIM

606461. gene.

neXtProt

NX_Q96RS0.

PharmGKB

PA162405660.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0500.

HOGENOM

HOG000154561.

HOVERGEN

HBG059797.

InParanoid

Q96RS0.

KO

K14292.

OMA

CSRAFVE.

OrthoDB

EOG43TZTV.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.
REACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

Q96RS0.

Bgee

Q96RS0.

CleanEx

HS_TGS1.

Genevestigator

Q96RS0.

GermOnline

ENSG00000137574. Homo sapiens.

Family and domain databases

InterPro

IPR019012. RNA_cap_Gua-N2-MeTrfase.
[Graphical view]

Pfam

PF09445. Methyltransf_15. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q96RS0.

GenomeRNAi

96764.

NextBio

78561.

SOURCE

Search...

Entry information

Entry name

TGS1_HUMAN

Accession

Primary (citable) accession number: Q96RS0
Secondary accession number(s): A6NJQ5 , Q5GH23, Q8TDG9, Q96QU3, Q9H5V3

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	January 11, 2011
Last modified:	May 1, 2013
This is version 98 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.