Reviewed, UniProtKB/Swiss-Prot O13297 (CET1_YEAST)

Names and origin

Protein names

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 names

Name:	CET1
Ordered Locus Names:	YPL228W
ORF Names:	P1433

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	549 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	First step of mRNA capping. Converts the 5'-triphosphate end of a nascent mRNA chain into a diphosphate end. Ref.6
Catalytic activity	A 5'-phosphopolynucleotide + H2O = a polynucleotide + phosphate.
Cofactor	Divalent ions.
Subunit structure	The mRNA-capping enzyme is composed of two separate chains alpha and beta, respectively a mRNA guanylyltransferase and an RNA 5'-triphosphatase. Ref.6
Subcellular location	Nucleus.
Miscellaneous	Present with 3900 molecules/cell in log phase SD medium. Ref.7
Sequence similarities	Belongs to the fungal TPase family.

Ontologies

Keywords
Biological process	mRNA capping mRNA processing
Cellular component	Nucleus
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	mRNA capping Traceable author statement. Source: SGD
Cellular component	mRNA capping enzyme complex Inferred from genetic interaction. Source: SGD
Molecular function	identical protein binding Inferred from physical interaction. Source: IntAct polynucleotide 5'-phosphatase activity Inferred from direct assay. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-4473,EBI-4473
CEG1	Q01159	1	EBI-4473,EBI-10503

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 549

549

mRNA-capping enzyme subunit beta

PRO_0000210119

Sites

Active site

223

1

N6-GMP-lysine intermediate

Site

280

1

Essential for dimer formation

Amino acid modifications

Modified residue

15

1

Phosphoserine Ref.8 Ref.9 Ref.10 Ref.11

Modified residue

121

1

Phosphoserine Ref.11

Modified residue

124

1

Phosphoserine Ref.11

Modified residue

144

1

Phosphoserine Ref.11

Experimental info

Mutagenesis

280

1

D → A: Significant growth defects. Ref.6

Mutagenesis

520

1

I → A: No growth. Ref.6

Mutagenesis

523

1

F → A: Temperature sensitive growth phenotype. Ref.6

Mutagenesis

524

1

L → A: Temperature sensitive growth phenotype. Ref.6

Sequence conflict

242

1

K → R in CAA97944. Ref.2

Sequence conflict

242

1

K → R in CAA64259. Ref.2

Secondary structure

1

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549

Helix Strand Turn

Details...

Helix

246 – 248

3

Beta strand

262 – 264

3

Beta strand

274 – 276

3

Helix

280 – 294

15

Turn

298 – 300

3

Helix

301 – 303

3

Beta strand

304 – 314

11

Beta strand

319 – 321

3

Beta strand

330 – 332

3

Beta strand

338 – 341

4

Helix

345 – 359

15

Helix

362 – 364

3

Turn

365 – 367

3

Beta strand

368 – 381

14

Beta strand

391 – 400

10

Beta strand

405 – 418

14

Beta strand

425 – 435

11

Helix

441 – 445

5

Beta strand

453 – 463

11

Helix

464 – 466

3

Beta strand

468 – 477

10

Beta strand

488 – 497

10

Helix

499 – 507

9

Turn

508 – 511

4

Helix

514 – 536

23

Sequences

	Sequence		Length	Mass (Da)
	O13297-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: D8A462FFB7E027F9	FASTA	549	61,822
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 9345280] [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: 9169875] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	"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: 6389537] [Abstract] Cited for: CHARACTERIZATION.
[4]	"Messenger RNA guanylyltransferase from Saccharomyces cerevisiae. II. Catalytic properties." Itoh N., Mizumoto K., Kaziro Y. J. Biol. Chem. 259:13930-13936(1984) [PubMed: 6094533] [Abstract] Cited for: CHARACTERIZATION.
[5]	"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: 3029058] [Abstract] Cited for: CHARACTERIZATION.
[6]	"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: 12788946] [Abstract] Cited for: FUNCTION, SUBUNIT, MUTAGENESIS OF ASP-280; ILE-520; PHE-523 AND LEU-524.
[7]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[8]	"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: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, MASS SPECTROMETRY.
[9]	"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: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, MASS SPECTROMETRY.
[10]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, MASS SPECTROMETRY.
[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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-121; SER-124 AND SER-144, MASS SPECTROMETRY.
[12]	"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: 10589681] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 241-549.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AB008799 Genomic DNA. Translation: BAA23522.1.
Z73584 Genomic DNA. Translation: CAA97944.1.
Z73583 Genomic DNA. Translation: CAA97943.1.
X94561 Genomic DNA. Translation: CAA64259.1.

PIR

S61706.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1D8H	X-ray	2.00	A/B/C	243-549	[»]
1D8I	X-ray	2.05	A/B/C	243-549	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:2299N.

IntAct

O13297. 7 interactions.

Proteomic databases

PeptideAtlas

O13297.

PRIDE

O13297.

Genome annotation databases

Ensembl

YPL228W. Saccharomyces cerevisiae. [Contig view]

GenomeReviews

Gene locus YPL228W in contig U00094_GR.

KEGG

sce:YPL228W.

Organism-specific databases

CYGD

YPL228w.

SGD

S000006149. CET1.

Yeast-GFP

Search...

Phylogenomic databases

HOGENOM

O13297.

Enzyme and pathway databases

BRENDA

3.1.3.33. 250.

Gene expression databases

ArrayExpress

O13297.

GermOnline

YPL228W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR004206. mRNA_capping_enz_bsu.
[Graphical view]

Gene3D

G3DSA:3.20.100.10. mRNA_capping_enz_bsu. 1 hit.

Pfam

PF02940. mRNA_triPase. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

CET1_YEAST

Accession

Primary (citable) accession number: O13297
Secondary accession number(s): Q12197

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 1, 1998
Last modified:	June 16, 2009
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)