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Protein

mRNA-capping enzyme subunit beta

Gene

CET1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

First step of mRNA capping. Converts the 5'-triphosphate end of a nascent mRNA chain into a diphosphate end.1 Publication

Catalytic activityi

A 5'-phosphopolynucleotide + H2O = a polynucleotide + phosphate.

Cofactori

a divalent metal cationNote: Divalent metal ions.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei223 – 2231N6-GMP-lysine intermediate
Sitei280 – 2801Essential for dimer formation

GO - Molecular functioni

  • polynucleotide 5'-phosphatase activity Source: SGD

GO - Biological processi

  • 7-methylguanosine mRNA capping Source: SGD
  • polynucleotide dephosphorylation Source: SGD
  • positive regulation of protein localization to nucleus Source: SGD
  • positive regulation of transcription elongation from RNA polymerase II promoter Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

mRNA capping, mRNA processing

Enzyme and pathway databases

BioCyciMetaCyc:G3O-34116-MONOMER.
YEAST:G3O-34116-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
mRNA-capping enzyme subunit beta (EC:3.1.3.33)
Alternative name(s):
Polynucleotide 5'-triphosphatase
mRNA 5'-triphosphatase
Short name:
TPase
Gene namesi
Name:CET1
Ordered Locus Names:YPL228W
ORF Names:P1433
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPL228W.
SGDiS000006149. CET1.

Subcellular locationi

GO - Cellular componenti

  • mRNA cap methyltransferase complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi280 – 2801D → A: Significant growth defects. 1 Publication
Mutagenesisi520 – 5201I → A: No growth. 1 Publication
Mutagenesisi523 – 5231F → A: Temperature sensitive growth phenotype. 1 Publication
Mutagenesisi524 – 5241L → A: Temperature sensitive growth phenotype. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 549548mRNA-capping enzyme subunit betaPRO_0000210119Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Modified residuei15 – 151PhosphoserineCombined sources
Modified residuei124 – 1241PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO13297.
PRIDEiO13297.

PTM databases

iPTMnetiO13297.

Interactioni

Subunit structurei

The mRNA-capping enzyme is composed of two separate chains alpha and beta, respectively a mRNA guanylyltransferase and an RNA 5'-triphosphatase.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CEG1Q011597EBI-4473,EBI-10503

Protein-protein interaction databases

BioGridi35957. 86 interactions.
DIPiDIP-2299N.
IntActiO13297. 5 interactions.
MINTiMINT-647905.

Structurei

Secondary structure

1
549
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi246 – 2483Combined sources
Turni254 – 2585Combined sources
Beta strandi262 – 2643Combined sources
Beta strandi274 – 2763Combined sources
Helixi280 – 29415Combined sources
Turni298 – 3003Combined sources
Helixi301 – 3033Combined sources
Beta strandi304 – 31411Combined sources
Beta strandi319 – 3213Combined sources
Beta strandi330 – 3323Combined sources
Beta strandi338 – 3414Combined sources
Helixi345 – 35915Combined sources
Helixi362 – 3643Combined sources
Turni365 – 3673Combined sources
Beta strandi368 – 38114Combined sources
Beta strandi391 – 40010Combined sources
Beta strandi405 – 41814Combined sources
Beta strandi425 – 43511Combined sources
Beta strandi437 – 4404Combined sources
Helixi441 – 4455Combined sources
Beta strandi446 – 4483Combined sources
Beta strandi453 – 46311Combined sources
Helixi464 – 4663Combined sources
Beta strandi468 – 47710Combined sources
Beta strandi488 – 49710Combined sources
Helixi499 – 5079Combined sources
Turni508 – 5114Combined sources
Helixi514 – 53623Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D8HX-ray2.00A/B/C241-549[»]
1D8IX-ray2.05A/B/C241-549[»]
3KYHX-ray3.00A/B241-549[»]
ProteinModelPortaliO13297.
SMRiO13297. Positions 241-539.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO13297.

Family & Domainsi

Sequence similaritiesi

Belongs to the fungal TPase family.Curated

Phylogenomic databases

GeneTreeiENSGT00530000067072.
HOGENOMiHOG000111552.
InParanoidiO13297.
KOiK01098.
OMAiSSQCVFT.
OrthoDBiEOG7FZ07W.

Family and domain databases

Gene3Di3.20.100.10. 1 hit.
InterProiIPR033469. CYTH-like_dom.
IPR004206. mRNA_triPase_Cet1.
[Graphical view]
PfamiPF02940. mRNA_triPase. 1 hit.
[Graphical view]
SUPFAMiSSF55154. SSF55154. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O13297-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSYTDNPPQT KRALSLDDLV NHDENEKVKL QKLSEAANGS RPFAENLESD
60 70 80 90 100
INQTETGQAA PIDNYKESTG HGSHSQKPKS RKSSNDDEET DTDDEMGASG
110 120 130 140 150
EINFDSEMDF DYDKQHRNLL SNGSPPMNDG SDANAKLEKP SDDSIHQNSK
160 170 180 190 200
SDEEQRIPKQ GNEGNIASNY ITQVPLQKQK QTEKKIAGNA VGSVVKKEEE
210 220 230 240 250
ANAAVDNIFE EKATLQSKKN NIKRDLEVLN EISASSKPSK YRNVPIWAQK
260 270 280 290 300
WKPTIKALQS INVKDLKIDP SFLNIIPDDD LTKSVQDWVY ATIYSIAPEL
310 320 330 340 350
RSFIELEMKF GVIIDAKGPD RVNPPVSSQC VFTELDAHLT PNIDASLFKE
360 370 380 390 400
LSKYIRGISE VTENTGKFSI IESQTRDSVY RVGLSTQRPR FLRMSTDIKT
410 420 430 440 450
GRVGQFIEKR HVAQLLLYSP KDSYDVKISL NLELPVPDND PPEKYKSQSP
460 470 480 490 500
ISERTKDRVS YIHNDSCTRI DITKVENHNQ NSKSRQSETT HEVELEINTP
510 520 530 540
ALLNAFDNIT NDSKEYASLI RTFLNNGTII RRKLSSLSYE IFEGSKKVM
Length:549
Mass (Da):61,850
Last modified:October 5, 2010 - v2
Checksum:i2B946CC53D66F824
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti242 – 2421R → K in BAA23522 (PubMed:9345280).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB008799 Genomic DNA. Translation: BAA23522.1.
Z73584 Genomic DNA. Translation: CAA97944.1.
Z73583 Genomic DNA. Translation: CAA97943.1.
X94561 Genomic DNA. Translation: CAA64259.1.
BK006949 Genomic DNA. Translation: DAA11208.1.
PIRiS61706.
RefSeqiNP_015096.1. NM_001184042.1.

Genome annotation databases

EnsemblFungiiYPL228W; YPL228W; YPL228W.
GeneIDi855873.
KEGGisce:YPL228W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB008799 Genomic DNA. Translation: BAA23522.1.
Z73584 Genomic DNA. Translation: CAA97944.1.
Z73583 Genomic DNA. Translation: CAA97943.1.
X94561 Genomic DNA. Translation: CAA64259.1.
BK006949 Genomic DNA. Translation: DAA11208.1.
PIRiS61706.
RefSeqiNP_015096.1. NM_001184042.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D8HX-ray2.00A/B/C241-549[»]
1D8IX-ray2.05A/B/C241-549[»]
3KYHX-ray3.00A/B241-549[»]
ProteinModelPortaliO13297.
SMRiO13297. Positions 241-539.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35957. 86 interactions.
DIPiDIP-2299N.
IntActiO13297. 5 interactions.
MINTiMINT-647905.

PTM databases

iPTMnetiO13297.

Proteomic databases

MaxQBiO13297.
PRIDEiO13297.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPL228W; YPL228W; YPL228W.
GeneIDi855873.
KEGGisce:YPL228W.

Organism-specific databases

EuPathDBiFungiDB:YPL228W.
SGDiS000006149. CET1.

Phylogenomic databases

GeneTreeiENSGT00530000067072.
HOGENOMiHOG000111552.
InParanoidiO13297.
KOiK01098.
OMAiSSQCVFT.
OrthoDBiEOG7FZ07W.

Enzyme and pathway databases

BioCyciMetaCyc:G3O-34116-MONOMER.
YEAST:G3O-34116-MONOMER.

Miscellaneous databases

EvolutionaryTraceiO13297.
PROiO13297.

Family and domain databases

Gene3Di3.20.100.10. 1 hit.
InterProiIPR033469. CYTH-like_dom.
IPR004206. mRNA_triPase_Cet1.
[Graphical view]
PfamiPF02940. mRNA_triPase. 1 hit.
[Graphical view]
SUPFAMiSSF55154. SSF55154. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of the yeast mRNA capping enzyme beta subunit gene encoding RNA 5'-triphosphatase, which is essential for cell viability."
    Tsukamoto T., Shibagaki Y., Imajoh-Ohmi S., Murakoshi T., Suzuki M., Nakamura A., Gotoh H., Mizumoto K.
    Biochem. Biophys. Res. Commun. 239:116-122(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 26109 / X2180.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
    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.
    Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Messenger RNA guanylyltransferase from Saccharomyces cerevisiae. I. Purification and subunit structure."
    Itoh N., Mizumoto K., Kaziro Y.
    J. Biol. Chem. 259:13923-13929(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  5. "Messenger RNA guanylyltransferase from Saccharomyces cerevisiae. II. Catalytic properties."
    Itoh N., Mizumoto K., Kaziro Y.
    J. Biol. Chem. 259:13930-13936(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  6. "Messenger RNA guanylyltransferase from Saccharomyces cerevisiae. Large scale purification, subunit functions, and subcellular localization."
    Itoh N., Yamada H., Kaziro Y., Mizumoto K.
    J. Biol. Chem. 262:1989-1995(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  7. "Homodimeric quaternary structure is required for the in vivo function and thermal stability of Saccharomyces cerevisiae and Schizosaccharomyces pombe RNA triphosphatases."
    Hausmann S., Pei Y., Shuman S.
    J. Biol. Chem. 278:30487-30496(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, MUTAGENESIS OF ASP-280; ILE-520; PHE-523 AND LEU-524.
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  10. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    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.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-124, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-124, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Structure and mechanism of yeast RNA triphosphatase: an essential component of the mRNA capping apparatus."
    Lima C.D., Wang L.K., Shuman S.
    Cell 99:533-543(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 241-549.

Entry informationi

Entry nameiCET1_YEAST
AccessioniPrimary (citable) accession number: O13297
Secondary accession number(s): D6W3E2, Q12197
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: October 5, 2010
Last modified: July 6, 2016
This is version 158 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 3900 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.