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Protein

Enhancer of mRNA-decapping protein 4

Gene

Edc4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

In the process of mRNA degradation, seems to play a role in mRNA decapping. Component of a complex containing DCP2 and DCP1A which functions in decapping of ARE-containing mRNAs. Promotes complex formation between DCP1A and DCP2. Enhances the catalytic activity of DCP2 (in vitro) (By similarity).By similarity

Names & Taxonomyi

Protein namesi
Recommended name:
Enhancer of mRNA-decapping protein 4
Gene namesi
Name:Edc4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:2446249. Edc4.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 14061405Enhancer of mRNA-decapping protein 4PRO_0000278963Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei3 – 31PhosphoserineBy similarity
Modified residuei6 – 61PhosphoserineBy similarity
Modified residuei125 – 1251N6-acetyllysineBy similarity
Modified residuei560 – 5601PhosphoserineBy similarity
Modified residuei565 – 5651PhosphoserineBy similarity
Modified residuei583 – 5831PhosphoserineBy similarity
Modified residuei585 – 5851PhosphoserineBy similarity
Modified residuei680 – 6801PhosphoserineCombined sources
Modified residuei712 – 7121PhosphoserineBy similarity
Modified residuei727 – 7271PhosphoserineBy similarity
Modified residuei729 – 7291PhosphoserineBy similarity
Modified residuei731 – 7311PhosphothreonineCombined sources
Modified residuei733 – 7331PhosphoserineBy similarity
Modified residuei745 – 7451PhosphoserineCombined sources
Modified residuei826 – 8261PhosphothreonineBy similarity
Modified residuei849 – 8491PhosphoserineBy similarity
Modified residuei876 – 8761PhosphoserineBy similarity
Modified residuei879 – 8791PhosphothreonineCombined sources
Modified residuei880 – 8801PhosphoserineBy similarity
Modified residuei884 – 8841PhosphoserineCombined sources
Modified residuei892 – 8921PhosphoserineCombined sources
Modified residuei895 – 8951PhosphoserineCombined sources
Modified residuei897 – 8971PhosphoserineBy similarity
Modified residuei906 – 9061PhosphothreonineCombined sources
Modified residuei1385 – 13851PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ3UJB9.
MaxQBiQ3UJB9.
PaxDbiQ3UJB9.
PeptideAtlasiQ3UJB9.
PRIDEiQ3UJB9.

PTM databases

iPTMnetiQ3UJB9.
PhosphoSiteiQ3UJB9.

Expressioni

Gene expression databases

BgeeiQ3UJB9.
CleanExiMM_EDC4.

Interactioni

Subunit structurei

Part of a decapping complex consisting of DCP1A, DCP2, EDC3, EDC4 and probably DDX6. Part of a complex consisting of DCP1A, EDC3, EDC4 and DDX6. Part of a complex consisting of DCP1B, EDC3, EDC4 and DDX6. Interacts with DCP2 (By similarity). Interacts with RC3H1.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Rc3h1Q4VGL63EBI-2553526,EBI-2366263

Protein-protein interaction databases

BioGridi231562. 21 interactions.
IntActiQ3UJB9. 25 interactions.
MINTiMINT-4382632.
STRINGi10090.ENSMUSP00000113854.

Structurei

3D structure databases

ProteinModelPortaliQ3UJB9.
SMRiQ3UJB9. Positions 1273-1402.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati174 – 21441WD 1Add
BLAST
Repeati230 – 27748WD 2Add
BLAST
Repeati295 – 33440WD 3Add
BLAST
Repeati342 – 39352WD 4Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili971 – 103060Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi609 – 68375Ser-richAdd
BLAST

Sequence similaritiesi

Belongs to the WD repeat EDC4 family.Curated
Contains 4 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat, WD repeat

Phylogenomic databases

eggNOGiKOG1916. Eukaryota.
ENOG410XP6V. LUCA.
HOGENOMiHOG000013082.
HOVERGENiHBG053855.
InParanoidiQ3UJB9.
KOiK12616.
PhylomeDBiQ3UJB9.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR032401. EDC4_WD40.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF16529. Ge1_WD40. 1 hit.
[Graphical view]
SMARTiSM00320. WD40. 3 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS50082. WD_REPEATS_2. 1 hit.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q3UJB9-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MASCASIDIE DATQHLRDIL KLDRPAGGSN AESQRPSSAY NGDLNGLLVP
60 70 80 90 100
DPLSSGDGNS TNKPGIRTMP PINLQEKQVI CLSGDDSSTC IGILAKEVEI
110 120 130 140 150
VASSDSSISS KARGSNKVKI QPVAKYDWEQ KYYYGNLIAV SNSFLAYAIR
160 170 180 190 200
AANNGSAMVR VISVSTSERT LLKGFTGSVA DLAFAHLNSP QLACLDEAGN
210 220 230 240 250
LFVWRLALVK GKIQEEILVH IRQPEGTALN HFRRIIWCPF IPEESEDCCE
260 270 280 290 300
ESSPTVALLH EDRAEVWDLD MLRSSHNTWP VDVSQIKQGF IVVKGHSTCL
310 320 330 340 350
SEGALSPDGT VLATASHDGF VKFWQIYIEG QDEPRCLHEW KPHDGRPLSC
360 370 380 390 400
LLFCDNHKKQ DPEVPFWRFL ITGADQNREL KMWCTVSWTC LQTIRFSPDI
410 420 430 440 450
FSSVSVPPSL KVCLDLSAEY LILSDVQRKV LYVMELLQNQ DEGRACFSSI
460 470 480 490 500
SEFLLTHPVL SFGIQVVSRC RLRHTEVLPA EEENDSLGTE SSHGAGALES
510 520 530 540 550
AAGVLIKLFC VHTKALQDVQ IRFQPQLNPD VVAPLSTHTA HEDFTFGESR
560 570 580 590 600
PELGSEGLAS AAHGSQPDLR RIVELPAPAD FLSLSSETKP ELMTPDAFMT
610 620 630 640 650
PTASLQQISA SPSSSSSSSS SSSSSSSSSS SSLTAVSAVS SSSAMDPSLP
660 670 680 690 700
RPPEELTLSP KLQLDGSLTL NSSSSSLQAS PRSLLPGLLP GPADKLISKG
710 720 730 740 750
PGQVSTAASA LSLDLQEVEP LGLPQASPSR TRSPDVISSA STALSQDIPE
760 770 780 790 800
IASEALSRGF GSSVPEGLIE PNSMASAASA LHLLSPRPRQ GPELGSQLGL
810 820 830 840 850
DGGPGDGDRH STPSLLEAAL TQEVATPDSQ VWPTAPDITR ETCSTLTESP
860 870 880 890 900
RNGLQEKHKS LAFHRPPYHL LQQRDSQDTS AEQSDHDDEV ASLASASGGF
910 920 930 940 950
GSKIPTPRLP SKDWKTKGSP RTSPKLKRKS KKDDGDSAVG SRLTEHQVAE
960 970 980 990 1000
PPEDWPALIW QQQRELAELW HNQEELLQRL CAQLEGLQST VTDHVERALE
1010 1020 1030 1040 1050
TRHEQEQRRL ERALAEGQQR GGQLQEQLTQ QLSQALSSAV AGRLERSVRD
1060 1070 1080 1090 1100
EIKKTVPPCV SRSLEPVAGQ LSNSVATKLT AVEGSMKENI SKLLKSKNLT
1110 1120 1130 1140 1150
DAIARAAADT LQGPMQAAYR EAFQSVVLPA FEKSCQAMFQ QINDSFRLGT
1160 1170 1180 1190 1200
QEYLQQLESH MKSRKAREQE AREPVLAQLR GLVSTLQSAT EQMAATVSSS
1210 1220 1230 1240 1250
VRAEVQHQLH VAVGSLQESI LAQVQRIVKG EVSVALKEQQ ATVTSSIMQA
1260 1270 1280 1290 1300
MRSAAGTPVP SAHLDCQAQQ AHILQLLQQG HLNQAFQQAL TAADLNLVLY
1310 1320 1330 1340 1350
VCETVDPAQV FGQPPCPLSQ PVLLSLIQQL ASDLGTRSDL KLSYLEEAVM
1360 1370 1380 1390 1400
HLDHSDPITR DHMGSVMAQV RQKLFQFLQA DPHNSLSKAA RRLSLMLHGL

VTPSLP
Length:1,406
Mass (Da):152,484
Last modified:March 6, 2007 - v2
Checksum:iF89969FDD9EF0725
GO
Isoform 2 (identifier: Q3UJB9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     849-864: Missing.

Show »
Length:1,390
Mass (Da):150,653
Checksum:iBA388F90A9B6DB6B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti591 – 5911E → K in AAH53081 (PubMed:15489334).Curated
Sequence conflicti772 – 7721N → D in AAH53081 (PubMed:15489334).Curated
Sequence conflicti1152 – 11521E → G in BAE27236 (PubMed:16141072).Curated
Sequence conflicti1152 – 11521E → G in BAE31626 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei849 – 86416Missing in isoform 2. 1 PublicationVSP_023413Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK146527 mRNA. Translation: BAE27236.1.
AK152963 mRNA. Translation: BAE31626.1.
BC022641 mRNA. Translation: AAH22641.1.
BC053081 mRNA. Translation: AAH53081.1.
CCDSiCCDS52662.1. [Q3UJB9-2]
CCDS80923.1. [Q3UJB9-1]
RefSeqiNP_001288029.1. NM_001301100.1.
NP_853625.1. NM_181594.3.
UniGeneiMm.28979.

Genome annotation databases

GeneIDi234699.
KEGGimmu:234699.
UCSCiuc009nek.2. mouse. [Q3UJB9-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK146527 mRNA. Translation: BAE27236.1.
AK152963 mRNA. Translation: BAE31626.1.
BC022641 mRNA. Translation: AAH22641.1.
BC053081 mRNA. Translation: AAH53081.1.
CCDSiCCDS52662.1. [Q3UJB9-2]
CCDS80923.1. [Q3UJB9-1]
RefSeqiNP_001288029.1. NM_001301100.1.
NP_853625.1. NM_181594.3.
UniGeneiMm.28979.

3D structure databases

ProteinModelPortaliQ3UJB9.
SMRiQ3UJB9. Positions 1273-1402.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi231562. 21 interactions.
IntActiQ3UJB9. 25 interactions.
MINTiMINT-4382632.
STRINGi10090.ENSMUSP00000113854.

PTM databases

iPTMnetiQ3UJB9.
PhosphoSiteiQ3UJB9.

Proteomic databases

EPDiQ3UJB9.
MaxQBiQ3UJB9.
PaxDbiQ3UJB9.
PeptideAtlasiQ3UJB9.
PRIDEiQ3UJB9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi234699.
KEGGimmu:234699.
UCSCiuc009nek.2. mouse. [Q3UJB9-2]

Organism-specific databases

CTDi23644.
MGIiMGI:2446249. Edc4.

Phylogenomic databases

eggNOGiKOG1916. Eukaryota.
ENOG410XP6V. LUCA.
HOGENOMiHOG000013082.
HOVERGENiHBG053855.
InParanoidiQ3UJB9.
KOiK12616.
PhylomeDBiQ3UJB9.

Miscellaneous databases

ChiTaRSiEdc4. mouse.
PROiQ3UJB9.
SOURCEiSearch...

Gene expression databases

BgeeiQ3UJB9.
CleanExiMM_EDC4.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR032401. EDC4_WD40.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF16529. Ge1_WD40. 1 hit.
[Graphical view]
SMARTiSM00320. WD40. 3 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS50082. WD_REPEATS_2. 1 hit.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Bone marrow and Kidney.
  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] (ISOFORM 2).
    Strain: C57BL/6J and FVB/N.
    Tissue: Brain and Colon.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-892, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  4. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-680; THR-731; SER-745; THR-879; SER-884; SER-892; SER-895 AND THR-906, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  7. "Roquin binds inducible costimulator mRNA and effectors of mRNA decay to induce microRNA-independent post-transcriptional repression."
    Glasmacher E., Hoefig K.P., Vogel K.U., Rath N., Du L., Wolf C., Kremmer E., Wang X., Heissmeyer V.
    Nat. Immunol. 11:725-733(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RC3H1.
  8. "Roquin paralogs 1 and 2 redundantly repress the Icos and Ox40 costimulator mRNAs and control follicular helper T cell differentiation."
    Vogel K.U., Edelmann S.L., Jeltsch K.M., Bertossi A., Heger K., Heinz G.A., Zoller J., Warth S.C., Hoefig K.P., Lohs C., Neff F., Kremmer E., Schick J., Repsilber D., Geerlof A., Blum H., Wurst W., Heikenwalder M., Schmidt-Supprian M., Heissmeyer V.
    Immunity 38:655-668(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RC3H1.

Entry informationi

Entry nameiEDC4_MOUSE
AccessioniPrimary (citable) accession number: Q3UJB9
Secondary accession number(s): Q3U6U8, Q7TS78, Q8R223
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: March 6, 2007
Last modified: July 6, 2016
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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.