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P39998 (EDC3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Enhancer of mRNA-decapping protein 3
Gene names
Name:EDC3
Synonyms:LSM16
Ordered Locus Names:YEL015W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length551 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Stimulates decapping of both stable and unstable mRNA during mRNA decay. Does not affect nonsense-mediated mRNA decay. Required for normal P-body assembly. Ref.2 Ref.4

Subunit structure

Homodimer. Interacts with DCP2. Ref.2

Subcellular location

CytoplasmP-body. Note: Is concentrated in several cytoplasmic foci called P bodies (or cytoplasmic processing bodies) which represent sites of mRNA decapping and 5' to 3' exonucleotidic decay. Ref.4

Miscellaneous

Present with 2340 molecules/cell in log phase SD medium. Ref.5

Sequence similarities

Belongs to the EDC3 family.

Contains 1 DFDF domain.

Contains 1 YjeF N-terminal domain.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 551551Enhancer of mRNA-decapping protein 3
PRO_0000202613

Regions

Domain93 – 12937DFDF
Domain288 – 527240YjeF N-terminal

Amino acid modifications

Modified residue2571Phosphoserine Ref.6 Ref.7 Ref.8
Modified residue2611Phosphoserine Ref.7 Ref.8

Experimental info

Mutagenesis360 – 3612RH → AA: Abolishes homodimerization. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P39998 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: BF28AE67F9303A73

FASTA55161,340
        10         20         30         40         50         60 
MSQFVGFGVQ VELKDGKLIQ GKIAKATSKG LTLNDVQFGD GGKSQAFKVR ASRLKDLKVL 

        70         80         90        100        110        120 
TVASQSGKRK QQRQQQQQND YNQNRGEHID WQDDDVSKIK QQEDFDFQRN LGMFNKKDVF 

       130        140        150        160        170        180 
AQLKQNDDIL PENRLQGHNR KQTQLQQNNY QNDELVIPDA KKDSWNKISS RNEQSTHQSQ 

       190        200        210        220        230        240 
PQQDAQDDLV LEDDEHEYDV DDIDDPKYLP ITQSLNITHL IHSATNSPSI NDKTKGTVIN 

       250        260        270        280        290        300 
DKDQVLAKLG QMIISQSRSN STSLPAANKQ TTIRSKNTKQ NIPMATPVQL LEMESITSEF 

       310        320        330        340        350        360 
FSINSAGLLE NFAVNASFFL KQKLGGRARL RLQNSNPEPL VVILASDSNR SGAKALALGR 

       370        380        390        400        410        420 
HLCQTGHIRV ITLFTCSQNE LQDSMVKKQT DIYKKCGGKI VNSVSSLESA METLNSPVEI 

       430        440        450        460        470        480 
VIDAMQGYDC TLSDLAGTSE VIESRIKSMI SWCNKQRGST KVWSLDIPNG FDAGSGMPDI 

       490        500        510        520        530        540 
FFSDRIEATG IICSGWPLIA INNLIANLPS LEDAVLIDIG IPQGAYSQRT SLRKFQNCDL 

       550 
FVTDGSLLLD L 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome V."
Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. expand/collapse author list , Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.
Nature 387:78-81(1997) [PubMed: 9169868] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[2]"Crystal structure of human Edc3 and its functional implications."
Ling S.H., Decker C.J., Walsh M.A., She M., Parker R., Song H.
Mol. Cell. Biol. 28:5965-5976(2008) [PubMed: 18678652] [Abstract]
Cited for: FUNCTION, INTERACTION WITH DCP2, MUTAGENESIS OF 360-ARG-HIS-361.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Identification of Edc3p as an enhancer of mRNA decapping in Saccharomyces cerevisiae."
Kshirsagar M., Parker R.
Genetics 166:729-739(2004) [PubMed: 15020463] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[5]"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].
[6]"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-257, MASS SPECTROMETRY.
Strain: ADR376.
[7]"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-257 AND SER-261, MASS SPECTROMETRY.
[8]"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-257 AND SER-261, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U18530 Genomic DNA. Translation: AAB64492.1.
BK006939 Genomic DNA. Translation: DAA07639.1.
PIRS50444.
RefSeqNP_010901.1. NM_001178830.1.

3D structure databases

ProteinModelPortalP39998.
SMRP39998. Positions 2-67.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-842N.
IntActP39998. 23 interactions.
MINTMINT-385078.
STRINGP39998.

Proteomic databases

PeptideAtlasP39998.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYEL015W; YEL015W; YEL015W.
GeneID856700.
KEGGsce:YEL015W.
NMPDRfig|4932.3.peg.1957.

Organism-specific databases

CYGDYEL015w.
SGDS000000741. EDC3.

Phylogenomic databases

eggNOGfuNOG05594.
GeneTreeEFGT00050000003947.
HOGENOMHBG396957.
OMALAMFDKK.
OrthoDBEOG4350GH.

Gene expression databases

ArrayExpressP39998.
GenevestigatorP39998.
GermOnlineYEL015W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR019050. DFDF_motif.
IPR004443. YjeF_N.
[Graphical view]
Gene3DG3DSA:3.40.50.10260. G3DSA:3.40.50.10260. 1 hit.
KOK12615.
PfamPF09532. DFDF. 1 hit.
PF03853. YjeF_N. 1 hit.
[Graphical view]
SUPFAMSSF64153. YjeF_N. 1 hit.
PROSITEPS51512. DFDF. 1 hit.
PS51385. YJEF_N. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio982763.

Entry information

Entry nameEDC3_YEAST
AccessionPrimary (citable) accession number: P39998
Secondary accession number(s): D3DLN5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: December 14, 2011
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome V

Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

SIMILARITY comments

Index of protein domains and families