EDC3/YEL015W Protein Information

Standard Name	Edc3p 1
Systematic Name	Yel015wp
Alias	Dcp3p , Lsm16p
ORF Classification	Verified
Description	Non-essential conserved protein with a role in mRNA decapping; specifically affects the function of the decapping enzyme Dcp1p; localizes to cytoplasmic mRNA processing bodies; forms cytoplasmic foci upon DNA replication stress (2, 3)
Name Description	Enhancer of mRNA DeCapping 1, 2

Experimental Data
Molecules/cell	2340 4

Predicted Sequence	Formatted Sequence or sequence in FASTA format
Length (a.a.)	551
Molecular Weight (Da)	61,340
Isoelectric Point (pI)	6.34

Click on image for expanded interactive view

Post-translational Modifications	PhosphoGRID \| PhosphoPep Database
Domains/motifs	See the graphical view and list of proteins that share domains/motifs in common with Edc3p (InterPro)
Physical Interactions	There are 83 total physical interactions (BioGRID)
Homologs	PDB Homologs \| BLASTP \| BLASTP v. fungi \| Fungal Alignment \| Synteny Viewer
External Sequence Databases	EBI: UPI0000053241 \| P39998 MIPS: YEL015W NCBI: 602382 \| 6320822 \| 731402 \| NP_010901.1 \| NM_001178830.1 GenBank/EMBL/DDBJ: DAA07639.1 \| U18530

Amino Acid Sequence (or in FASTA format)
1 MSQFVGFGVQ VELKDGKLIQ GKIAKATSKG LTLNDVQFGD GGKSQAFKVR 51 ASRLKDLKVL TVASQSGKRK QQRQQQQQND YNQNRGEHID WQDDDVSKIK 101 QQEDFDFQRN LGMFNKKDVF AQLKQNDDIL PENRLQGHNR KQTQLQQNNY 151 QNDELVIPDA KKDSWNKISS RNEQSTHQSQ PQQDAQDDLV LEDDEHEYDV 201 DDIDDPKYLP ITQSLNITHL IHSATNSPSI NDKTKGTVIN DKDQVLAKLG 251 QMIISQSRSN STSLPAANKQ TTIRSKNTKQ NIPMATPVQL LEMESITSEF 301 FSINSAGLLE NFAVNASFFL KQKLGGRARL RLQNSNPEPL VVILASDSNR 351 SGAKALALGR HLCQTGHIRV ITLFTCSQNE LQDSMVKKQT DIYKKCGGKI 401 VNSVSSLESA METLNSPVEI VIDAMQGYDC TLSDLAGTSE VIESRIKSMI 451 SWCNKQRGST KVWSLDIPNG FDAGSGMPDI FFSDRIEATG IICSGWPLIA 501 INNLIANLPS LEDAVLIDIG IPQGAYSQRT SLRKFQNCDL FVTDGSLLLD 551 L*

Amino Acid Sequence (or in FASTA format)

       1  MSQFVGFGVQ VELKDGKLIQ GKIAKATSKG LTLNDVQFGD GGKSQAFKVR
      51  ASRLKDLKVL TVASQSGKRK QQRQQQQQND YNQNRGEHID WQDDDVSKIK
     101  QQEDFDFQRN LGMFNKKDVF AQLKQNDDIL PENRLQGHNR KQTQLQQNNY
     151  QNDELVIPDA KKDSWNKISS RNEQSTHQSQ PQQDAQDDLV LEDDEHEYDV
     201  DDIDDPKYLP ITQSLNITHL IHSATNSPSI NDKTKGTVIN DKDQVLAKLG
     251  QMIISQSRSN STSLPAANKQ TTIRSKNTKQ NIPMATPVQL LEMESITSEF
     301  FSINSAGLLE NFAVNASFFL KQKLGGRARL RLQNSNPEPL VVILASDSNR
     351  SGAKALALGR HLCQTGHIRV ITLFTCSQNE LQDSMVKKQT DIYKKCGGKI
     401  VNSVSSLESA METLNSPVEI VIDAMQGYDC TLSDLAGTSE VIESRIKSMI
     451  SWCNKQRGST KVWSLDIPNG FDAGSGMPDI FFSDRIEATG IICSGWPLIA
     501  INNLIANLPS LEDAVLIDIG IPQGAYSQRT SLRKFQNCDL FVTDGSLLLD
     551  L*

external links for Edc3p

Homologs	Interaction Resources	Protein databases/Other	Localization Resources
BLASTP (NCBI)	BioGRID	SCOP Superfamily	YPL+
Ashbya (AGD)	BOND	GPMdb (Mass Spec.)	YeastGFP
Aspergillus (AspGD)	BioPIXIE	MIPS	YeastRC Public Image Repository
Candida (CGD)	CYC2008 (complexes)	Pfam domains
Candida (CandidaDB)	Complexome	YeastRC Structure Prediction (Seattle)
YGOB	DIP
YOGY	GeneMANIA
	YeastRC Two-Hybrid (Seattle)

References cited on this page View Complete Literature Guide for Edc3p

1)	Samanta MP and Liang S (2003) Predicting protein functions from redundancies in large-scale protein interaction networks. Proc Natl Acad Sci U S A 100(22):12579-83
2)	Kshirsagar M and Parker R (2004) Identification of Edc3p as an enhancer of mRNA decapping in Saccharomyces cerevisiae. Genetics 166(2):729-39
3)	Tkach JM, et al. (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat Cell Biol 14(9):966-76
4)	Ghaemmaghami S, et al. (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41