Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q96RS0 (TGS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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):
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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length853 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. 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. NucleusCajal body. Note: A 90 kDa isoform isfound in the nucleus while a 55 kDa isoform isfound 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 processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_process7-methylguanosine RNA capping

Inferred from electronic annotation. Source: InterPro

7-methylguanosine cap hypermethylation

Inferred from direct assay Ref.12. Source: BHF-UCL

RNA metabolic process

Traceable author statement. Source: Reactome

cellular lipid metabolic process

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

ncRNA metabolic process

Traceable author statement. Source: Reactome

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

ribonucleoprotein complex biogenesis

Inferred by curator Ref.12. Source: BHF-UCL

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-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentCajal body

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 22664934. Source: UniProt

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

small nuclear ribonucleoprotein complex

Inferred by curator Ref.12. Source: BHF-UCL

   Molecular_functionRNA trimethylguanosine synthase activity

Inferred from direct assay Ref.12. Source: BHF-UCL

protein binding

Inferred from physical interaction PubMed 21522132. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NOP58Q9Y2X32EBI-949244,EBI-395469

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 853853Trimethylguanosine synthase
PRO_0000204468

Regions

Region631 – 846216Sufficient for catalytic activity
Compositional bias611 – 62414Lys-rich

Sites

Binding site7191S-adenosyl-L-methionine By similarity
Binding site76617-methylguanosine

Amino acid modifications

Modified residue551Phosphoserine Ref.14 Ref.16
Modified residue601Phosphothreonine Ref.14 Ref.16
Modified residue851Phosphoserine Ref.17
Modified residue891Phosphoserine Ref.16 Ref.17 Ref.18
Modified residue1541Phosphoserine Ref.14 Ref.16
Modified residue4381Phosphoserine Ref.14 Ref.16

Natural variations

Natural variant161I → T. Ref.1 Ref.2 Ref.3
Corresponds to variant rs1818 [ dbSNP | Ensembl ].
VAR_024734
Natural variant1601I → V.
Corresponds to variant rs3213971 [ dbSNP | Ensembl ].
VAR_024735
Natural variant2991P → S.
Corresponds to variant rs11986329 [ dbSNP | Ensembl ].
VAR_056241
Natural variant5111I → T.
Corresponds to variant rs10100659 [ dbSNP | Ensembl ].
VAR_024736
Natural variant5761V → I.
Corresponds to variant rs16922259 [ dbSNP | Ensembl ].
VAR_024737
Natural variant5951T → A.
Corresponds to variant rs10109493 [ dbSNP | Ensembl ].
VAR_056242
Natural variant7541F → C.
Corresponds to variant rs7823773 [ dbSNP | Ensembl ].
VAR_024738

Experimental info

Mutagenesis6551F → A: Loss of catalytic activity. Ref.13
Mutagenesis6731T → A: Decreases catalytic activity to 13 percent of wild type. Ref.13
Mutagenesis6961D → A: Loss of catalytic activity. Ref.13
Mutagenesis7041N → A: Decreases catalytic activity to 5 percent of wild type. Ref.13
Mutagenesis7191D → A: Loss of catalytic activity. Ref.13
Mutagenesis7311N → A: Decreases catalytic activity to 4 percent of wild type. Ref.13
Mutagenesis7631S → A: Decreases catalytic activity to 26 percent of wild type. Ref.13 Ref.20
Mutagenesis7661W → A: Loss of catalytic activity. Ref.13 Ref.20
Mutagenesis8071R → A: Decreases catalytic activity to 6 percent of wild type. Ref.13
Mutagenesis8081N → A: Decreases catalytic activity to 11 percent of wild type. Ref.13
Sequence conflict5661Missing in AAK27730. Ref.1
Sequence conflict6241N → T in AAK83025. Ref.3
Sequence conflict6281N → T in AAK83025. Ref.3
Sequence conflict6811I → F in AAK27730. Ref.1
Sequence conflict7711Y → H in AAL99922. Ref.2

Secondary structure

............................................... 853
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q96RS0 [UniParc].

Last modified January 11, 2011. Version 3.
Checksum: FF670AFBE0979443

FASTA85396,620
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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, 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.
+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.
CCDSCCDS34894.1.
RefSeqNP_079107.6. NM_024831.6.
UniGeneHs.335068.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3EGIX-ray2.21A/B/C/D653-853[»]
3GDHX-ray2.00A/B/C618-853[»]
ProteinModelPortalQ96RS0.
SMRQ96RS0. Positions 634-844.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid125179. 9 interactions.
DIPDIP-49970N.
IntActQ96RS0. 7 interactions.
MINTMINT-2878093.
STRING9606.ENSP00000260129.

PTM databases

PhosphoSiteQ96RS0.

Polymorphism databases

DMDM317373500.

Proteomic databases

MaxQBQ96RS0.
PaxDbQ96RS0.
PRIDEQ96RS0.

Protocols and materials databases

DNASU96764.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000260129; ENSP00000260129; ENSG00000137574.
GeneID96764.
KEGGhsa:96764.
UCSCuc003xsj.4. human.

Organism-specific databases

CTD96764.
GeneCardsGC08P056685.
H-InvDBHIX0007515.
HGNCHGNC:17843. TGS1.
HPAHPA025024.
HPA029824.
MIM606461. gene.
neXtProtNX_Q96RS0.
PharmGKBPA162405660.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0500.
HOGENOMHOG000154561.
HOVERGENHBG059797.
InParanoidQ96RS0.
KOK14292.
OMACSRAFVE.
OrthoDBEOG70CR73.
PhylomeDBQ96RS0.
TreeFamTF313065.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ96RS0.
BgeeQ96RS0.
CleanExHS_TGS1.
GenevestigatorQ96RS0.

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

EvolutionaryTraceQ96RS0.
GeneWikiTGS1.
GenomeRNAi96764.
NextBio78561.
PROQ96RS0.
SOURCESearch...

Entry information

Entry nameTGS1_HUMAN
AccessionPrimary (citable) accession number: Q96RS0
Secondary accession number(s): A6NJQ5 expand/collapse secondary AC list , Q5GH23, Q8TDG9, Q96QU3, Q9H5V3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: January 11, 2011
Last modified: July 9, 2014
This is version 108 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM