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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)DescriptionActionsGraphical viewLength
Active sitei223N6-GMP-lysine intermediate1
Sitei280Essential for dimer formation1

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)DescriptionActionsGraphical viewLength
Mutagenesisi280D → A: Significant growth defects. 1 Publication1
Mutagenesisi520I → A: No growth. 1 Publication1
Mutagenesisi523F → A: Temperature sensitive growth phenotype. 1 Publication1
Mutagenesisi524L → A: Temperature sensitive growth phenotype. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00002101192 – 549mRNA-capping enzyme subunit betaAdd BLAST548

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Modified residuei15PhosphoserineCombined sources1
Modified residuei124PhosphoserineCombined sources1

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 interactors.
DIPiDIP-2299N.
IntActiO13297. 5 interactors.
MINTiMINT-647905.

Structurei

Secondary structure

1549
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi246 – 248Combined sources3
Turni254 – 258Combined sources5
Beta strandi262 – 264Combined sources3
Beta strandi274 – 276Combined sources3
Helixi280 – 294Combined sources15
Turni298 – 300Combined sources3
Helixi301 – 303Combined sources3
Beta strandi304 – 314Combined sources11
Beta strandi319 – 321Combined sources3
Beta strandi330 – 332Combined sources3
Beta strandi338 – 341Combined sources4
Helixi345 – 359Combined sources15
Helixi362 – 364Combined sources3
Turni365 – 367Combined sources3
Beta strandi368 – 381Combined sources14
Beta strandi391 – 400Combined sources10
Beta strandi405 – 418Combined sources14
Beta strandi425 – 435Combined sources11
Beta strandi437 – 440Combined sources4
Helixi441 – 445Combined sources5
Beta strandi446 – 448Combined sources3
Beta strandi453 – 463Combined sources11
Helixi464 – 466Combined sources3
Beta strandi468 – 477Combined sources10
Beta strandi488 – 497Combined sources10
Helixi499 – 507Combined sources9
Turni508 – 511Combined sources4
Helixi514 – 536Combined sources23

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiO13297.

Family & Domainsi

Sequence similaritiesi

Belongs to the fungal TPase family.Curated

Phylogenomic databases

GeneTreeiENSGT00530000067072.
HOGENOMiHOG000111552.
InParanoidiO13297.
KOiK01098.
OMAiSSQCVFT.
OrthoDBiEOG092C2R8I.

Family and domain databases

CDDicd07470. CYTH-like_mRNA_RTPase. 1 hit.
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)DescriptionActionsGraphical viewLength
Sequence conflicti242R → K in BAA23522 (PubMed:9345280).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1D8HX-ray2.00A/B/C241-549[»]
1D8IX-ray2.05A/B/C241-549[»]
3KYHX-ray3.00A/B241-549[»]
ProteinModelPortaliO13297.
SMRiO13297.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35957. 86 interactors.
DIPiDIP-2299N.
IntActiO13297. 5 interactors.
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.
OrthoDBiEOG092C2R8I.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiO13297.
PROiO13297.

Family and domain databases

CDDicd07470. CYTH-like_mRNA_RTPase. 1 hit.
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...

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: November 2, 2016
This is version 161 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.