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Q8K2D3 (EDC3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Enhancer of mRNA-decapping protein 3
Alternative name(s):
YjeF domain-containing protein 1
Gene names
Name:Edc3
Synonyms:Yjdc
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length508 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds single-stranded RNA. In the process of mRNA degradation, may play a role in mRNA decapping By similarity.

Subunit structure

Homodimer (via YjeF N-terminal domain). Forms a complex with DCP1A, DCP2, DDX6 and EDC4/HEDLS, within this complex directly interacts with DCP1A and DDX6. Interacts with ZFP36 By similarity.

Subcellular location

CytoplasmP-body By similarity. Note: Processing bodies (PB) By similarity.

Domain

The DFDF domain is unstructured by itself. It assumes a helical fold upon interaction with DDX6 By similarity.

Sequence similarities

Belongs to the EDC3 family.

Contains 1 DFDF domain.

Contains 1 YjeF N-terminal domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandRNA-binding
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentcytoplasmic mRNA processing body

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 508508Enhancer of mRNA-decapping protein 3
PRO_0000119056

Regions

Domain192 – 22837DFDF
Domain283 – 487205YjeF N-terminal
Region1 – 7979Required for P-body targeting and interaction with DCP1A By similarity
Region191 – 296106Required for interaction with DDX6 By similarity

Amino acid modifications

Modified residue1311Phosphoserine Ref.3
Modified residue1381Phosphoserine By similarity
Modified residue1401Phosphoserine By similarity
Modified residue1611Phosphoserine By similarity

Experimental info

Sequence conflict2371P → T in BAE40089. Ref.1
Sequence conflict3331Q → R in BAE40089. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8K2D3 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: DD1F449BEF1341C8

FASTA50855,957
        10         20         30         40         50         60 
MAMDWLGSIV SINCGDSLGV YQGRVSAVDQ VSQTISLTRP FHNGVKCLVP EVTFRAGDIT 

        70         80         90        100        110        120 
ELKILEIPGP GDNQQVGDLH QTELGPSGVG YQMSISQNGT GKVVKKPASS SSAPQSIPKR 

       130        140        150        160        170        180 
TDVKSQDVAI SPQQQQCSKS YVDRHMESLS QSKSFRRRHN SWSSSSRHPN QATPKKSGLK 

       190        200        210        220        230        240 
NGQMKNKDDE CFGDDIEELP DTDFDFEGNL ALFDKAAVFE EIDTYERRSG SRSRGVPNER 

       250        260        270        280        290        300 
PARYRHDENI LESEPIVYRR ITVPHSVSKE FCTDSGLVVP SVSYELHKKL LSVAEKHGLT 

       310        320        330        340        350        360 
LERRLEMTGV CASQMALTLL GGPNRLNPKN VHQRPTVALL CGPHVKGAQG ISCGRHLANH 

       370        380        390        400        410        420 
DVQVILFLPN FVKMLESITN ELSLFSKTQG QQVSSLRDLP ASPVDLVINC LDCPENAFLR 

       430        440        450        460        470        480 
DQPWYKAAVA WANQNRAPVL SIDPPVHEVE QGIDAKWSLA LGLPLPLGEH AGRVYLCDIG 

       490        500 
IPQQVFQEVG INYHSPFGCK FVIPLHSA 

« Hide

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and DBA/2.
Tissue: Mammary gland and Stomach.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Czech II and FVB/N.
Tissue: Mammary tumor.
[3]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK146804 mRNA. Translation: BAE27445.1.
AK166286 mRNA. Translation: BAE38683.1.
AK168118 mRNA. Translation: BAE40089.1.
BC031725 mRNA. Translation: AAH31725.1.
BC033484 mRNA. Translation: AAH33484.1.
CCDSCCDS23231.1.
RefSeqNP_722494.1. NM_153799.3.
UniGeneMm.268104.

3D structure databases

ProteinModelPortalQ8K2D3.
SMRQ8K2D3. Positions 4-74, 197-226, 258-507.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid237268. 1 interaction.

PTM databases

PhosphoSiteQ8K2D3.

Proteomic databases

MaxQBQ8K2D3.
PaxDbQ8K2D3.
PRIDEQ8K2D3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000043990; ENSMUSP00000049146; ENSMUSG00000038957.
GeneID353190.
KEGGmmu:353190.
UCSCuc009pvp.1. mouse.

Organism-specific databases

CTD80153.
MGIMGI:2142951. Edc3.

Phylogenomic databases

eggNOGNOG271303.
GeneTreeENSGT00390000016435.
HOGENOMHOG000231481.
HOVERGENHBG079428.
InParanoidQ8K2D3.
KOK12615.
OMAPEVTFRA.
OrthoDBEOG7H793B.
PhylomeDBQ8K2D3.
TreeFamTF324695.

Gene expression databases

ArrayExpressQ8K2D3.
BgeeQ8K2D3.
GenevestigatorQ8K2D3.

Family and domain databases

Gene3D3.40.50.10260. 1 hit.
InterProIPR025762. DFDF.
IPR019050. FDF_dom.
IPR025609. Lsm14_N.
IPR004443. YjeF_N_dom.
[Graphical view]
PfamPF09532. FDF. 1 hit.
PF12701. LSM14. 1 hit.
PF03853. YjeF_N. 1 hit.
[Graphical view]
SUPFAMSSF64153. SSF64153. 1 hit.
PROSITEPS51512. DFDF. 1 hit.
PS51385. YJEF_N. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEDC3. mouse.
NextBio400339.
PROQ8K2D3.
SOURCESearch...

Entry information

Entry nameEDC3_MOUSE
AccessionPrimary (citable) accession number: Q8K2D3
Secondary accession number(s): Q3THV7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: October 1, 2002
Last modified: July 9, 2014
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot