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UniProtKB/Swiss-Prot entry O13297


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CET1_YEAST
Primary accession number O13297
Secondary accession number Q12197
Integrated into Swiss-Prot on July 15, 1998
Sequence was last modified on January 1, 1998 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 83)
Name and origin of the protein
Protein name mRNA-capping enzyme subunit beta
Synonyms EC 3.1.3.33
Polynucleotide 5'-triphosphatase
mRNA 5'-triphosphatase
TPase
Gene name
Name: CET1
OrderedLocusNames: YPL228W
ORFNames: P1433
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 26109 / X2180;
DOI=10.1006/bbrc.1997.7439; PubMed=9345280 [NCBI, ExPASy, EBI, Israel, Japan]
Tsukamoto T., Shibagaki Y., Imajoh-Ohmi S., Murakoshi T., Suzuki M., Nakamura A., Gotoh H., Mizumoto K.;
"Isolation and characterization of the yeast mRNA capping enzyme beta subunit gene encoding RNA 5'-triphosphatase, which is essential for cell viability.";
Biochem. Biophys. Res. Commun. 239:116-122(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=9169875 [NCBI, ExPASy, EBI, Israel, Japan]
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
Nature 387:103-105(1997).
[3]
CHARACTERIZATION.
PubMed=6389537 [NCBI, ExPASy, EBI, Israel, Japan]
Itoh N., Mizumoto K., Kaziro Y.;
"Messenger RNA guanylyltransferase from Saccharomyces cerevisiae. I. Purification and subunit structure.";
J. Biol. Chem. 259:13923-13929(1984).
[4]
CHARACTERIZATION.
PubMed=6094533 [NCBI, ExPASy, EBI, Israel, Japan]
Itoh N., Mizumoto K., Kaziro Y.;
"Messenger RNA guanylyltransferase from Saccharomyces cerevisiae. II. Catalytic properties.";
J. Biol. Chem. 259:13930-13936(1984).
[5]
CHARACTERIZATION.
PubMed=3029058 [NCBI, ExPASy, EBI, Israel, Japan]
Itoh N., Yamada H., Kaziro Y., Mizumoto K.;
"Messenger RNA guanylyltransferase from Saccharomyces cerevisiae. Large scale purification, subunit functions, and subcellular localization.";
J. Biol. Chem. 262:1989-1995(1987).
[6]
FUNCTION, SUBUNIT, AND MUTAGENESIS OF ASP-280; ILE-520; PHE-523 AND LEU-524.
DOI=10.1074/jbc.M303060200; PubMed=12788946 [NCBI, ExPASy, EBI, Israel, Japan]
Hausmann S., Pei Y., Shuman S.;
"Homodimeric quaternary structure is required for the in vivo function and thermal stability of Saccharomyces cerevisiae and Schizosaccharomyces pombe RNA triphosphatases.";
J. Biol. Chem. 278:30487-30496(2003).
[7]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND MASS SPECTROMETRY.
DOI=10.1021/pr060559j; PubMed=17330950 [NCBI, ExPASy, EBI, Israel, Japan]
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0607084104; PubMed=17287358 [NCBI, ExPASy, EBI, Israel, Japan]
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0701622104; PubMed=17563356 [NCBI, ExPASy, EBI, Israel, Japan]
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases.";
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-121; SER-124 AND SER-144, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[12]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 241-549.
DOI=10.1016/S0092-8674(00)81541-X; PubMed=10589681 [NCBI, ExPASy, EBI, Israel, Japan]
Lima C.D., Wang L.K., Shuman S.;
"Structure and mechanism of yeast RNA triphosphatase: an essential component of the mRNA capping apparatus.";
Cell 99:533-543(1999).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AB008799; BAA23522.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z73584; CAA97944.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z73583; CAA97943.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X94561; CAA64259.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S61706; S61706.
3D structure databases
PDB
1D8H; X-ray; 2.00 A; A/B/C=241-549.[ExPASy / RCSB / EBI]
1D8I; X-ray; 2.05 A; A/B/C=241-549.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1D8H; -.
1D8I; -.
ModBase O13297.
Protein-protein interaction databases
DIP DIP:2299N; -.
IntAct O13297; 8.
Organism-specific databases
CYGD YPL228w; -.
SGD S000006149; CET1.
Yeast-GFP YPL228W.
Gene expression databases
ArrayExpress O13297; -.
GermOnline YPL228W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0031533; Cellular component: mRNA capping enzyme complex (inferred from genetic interaction from SGD).
GO:0042802; Molecular function: identical protein binding (inferred from physical interaction from IntAct).
GO:0004651; Molecular function: polynucleotide 5'-phosphatase activity (inferred from electronic annotation from InterPro).
GO:0006370; Biological process: mRNA capping (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR004206; mRNA_triPase.
Graphical view of domain structure.
Pfam PF02940; mRNA_triPase; 1.
Pfam graphical view of domain structure.
Proteomic databases
PeptideAtlas O13297; -.
Genome annotation databases
Ensembl YPL228W; Saccharomyces cerevisiae. [Contig view]
GenomeReviews U00094_GR; YPL228W.
Phylogenomic databases
HOGENOM O13297; -.
Other
LinkHub O13297; -.
ProtoNet O13297.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Hydrolase; mRNA capping; mRNA processing; Nucleus; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   549  549     mRNA-capping enzyme subunit beta. PRO_0000210119
ACT_SITE   223   223        N6-GMP-lysine intermediate. 
SITE   280   280  1     Essential for dimer formation. 
MOD_RES   15    15        Phosphoserine. 
MOD_RES   121   121        Phosphoserine. 
MOD_RES   124   124        Phosphoserine. 
MOD_RES   144   144        Phosphoserine. 
MUTAGEN   280   280        D->A: Significant growth defects. 
MUTAGEN   520   520        I->A: No growth. 
MUTAGEN   523   523        F->A: Temperature sensitive growth phenotype. 
MUTAGEN   524   524        L->A: Temperature sensitive growth phenotype. 
CONFLICT   242   242        K -> R (in Ref. 2; CAA97944/CAA64259). 
HELIX   246   248  3      
STRAND   262   264  3      
STRAND   274   276  3      
HELIX   280   294  15      
TURN   298   300  3      
HELIX   301   303  3      
STRAND   304   314  11      
STRAND   319   321  3      
STRAND   330   332  3      
STRAND   338   341  4      
HELIX   345   359  15      
HELIX   362   364  3      
TURN   365   367  3      
STRAND   368   381  14      
STRAND   391   400  10      
STRAND   405   418  14      
STRAND   425   435  11      
HELIX   441   445  5      
STRAND   453   463  11      
HELIX   464   466  3      
STRAND   468   477  10      
STRAND   488   497  10      
HELIX   499   507  9      
TURN   508   511  4      
HELIX   514   536  23      
Sequence information
Length: 549 AA [This is the length of the unprocessed precursor] Molecular weight: 61822 Da [This is the MW of the unprocessed precursor] CRC64: D8A462FFB7E027F9 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSYTDNPPQT KRALSLDDLV NHDENEKVKL QKLSEAANGS RPFAENLESD INQTETGQAA 

        70         80         90        100        110        120 
PIDNYKESTG HGSHSQKPKS RKSSNDDEET DTDDEMGASG EINFDSEMDF DYDKQHRNLL 

       130        140        150        160        170        180 
SNGSPPMNDG SDANAKLEKP SDDSIHQNSK SDEEQRIPKQ GNEGNIASNY ITQVPLQKQK 

       190        200        210        220        230        240 
QTEKKIAGNA VGSVVKKEEE ANAAVDNIFE EKATLQSKKN NIKRDLEVLN EISASSKPSK 

       250        260        270        280        290        300 
YKNVPIWAQK WKPTIKALQS INVKDLKIDP SFLNIIPDDD LTKSVQDWVY ATIYSIAPEL 

       310        320        330        340        350        360 
RSFIELEMKF GVIIDAKGPD RVNPPVSSQC VFTELDAHLT PNIDASLFKE LSKYIRGISE 

       370        380        390        400        410        420 
VTENTGKFSI IESQTRDSVY RVGLSTQRPR FLRMSTDIKT GRVGQFIEKR HVAQLLLYSP 

       430        440        450        460        470        480 
KDSYDVKISL NLELPVPDND PPEKYKSQSP ISERTKDRVS YIHNDSCTRI DITKVENHNQ 

       490        500        510        520        530        540 
NSKSRQSETT HEVELEINTP ALLNAFDNIT NDSKEYASLI RTFLNNGTII RRKLSSLSYE 


IFEGSKKVM 

O13297 in FASTA format

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