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Q96F86

- EDC3_HUMAN

UniProt

Q96F86 - EDC3_HUMAN

Protein

Enhancer of mRNA-decapping protein 3

Gene

EDC3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    Functioni

    Binds single-stranded RNA. In the process of mRNA degradation, may play a role in mRNA decapping. May play a role in spermiogenesis and oogenesis.3 Publications

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. protein binding Source: UniProtKB
    3. RNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay Source: Reactome
    2. gene expression Source: Reactome
    3. mRNA metabolic process Source: Reactome
    4. nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: Reactome
    5. RNA metabolic process Source: Reactome

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_20518. mRNA decay by 5' to 3' exoribonuclease.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Enhancer of mRNA-decapping protein 3
    Alternative name(s):
    LSM16 homolog
    YjeF N-terminal domain-containing protein 2
    Short name:
    YjeF_N2
    Short name:
    hYjeF_N2
    YjeF domain-containing protein 1
    Gene namesi
    Name:EDC3
    Synonyms:LSM16, YJDC, YJEFN2
    ORF Names:PP844
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:26114. EDC3.

    Subcellular locationi

    CytoplasmP-body 1 Publication
    Note: Processing bodies (PB).

    GO - Cellular componenti

    1. cytoplasmic mRNA processing body Source: UniProtKB-SubCell
    2. cytosol Source: Reactome
    3. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi204 – 2041F → A: Abolishes interaction with DDX6; when associated with A-206. 1 Publication
    Mutagenesisi206 – 2061F → A: Abolishes interaction with DDX6; when associated with A-204. 1 Publication
    Mutagenesisi306 – 3061E → A: Abolishes homodimerization and RNA binding; when associated with A-310. 1 Publication
    Mutagenesisi310 – 3101V → A: Abolishes homodimerization and RNA binding; when associated with A-306. 1 Publication

    Organism-specific databases

    PharmGKBiPA142670551.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 508508Enhancer of mRNA-decapping protein 3PRO_0000119054Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei131 – 1311Phosphoserine2 Publications
    Modified residuei138 – 1381Phosphoserine1 Publication
    Modified residuei140 – 1401Phosphoserine1 Publication
    Modified residuei161 – 1611Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ96F86.
    PaxDbiQ96F86.
    PeptideAtlasiQ96F86.
    PRIDEiQ96F86.

    PTM databases

    PhosphoSiteiQ96F86.

    Expressioni

    Tissue specificityi

    Expressed in theca and granulosa cells in ovary, and in spermatids of the meiotic division part II and apical membrane of Sertoli cells in testis (at protein level). Also expressed in brain and mammary gland.1 Publication

    Gene expression databases

    ArrayExpressiQ96F86.
    BgeeiQ96F86.
    CleanExiHS_EDC3.
    GenevestigatoriQ96F86.

    Organism-specific databases

    HPAiHPA040650.
    HPA044206.

    Interactioni

    Subunit structurei

    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 ZFP36.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-997311,EBI-997311
    DCP1BQ8IZD43EBI-997311,EBI-521595
    DDX6P261962EBI-997311,EBI-351257
    ZFP36P266512EBI-997311,EBI-374248

    Protein-protein interaction databases

    BioGridi123144. 15 interactions.
    DIPiDIP-35516N.
    IntActiQ96F86. 15 interactions.
    MINTiMINT-5005528.
    STRINGi9606.ENSP00000320503.

    Structurei

    Secondary structure

    1
    508
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni4 – 74
    Beta strandi9 – 135
    Turni16 – 183
    Beta strandi20 – 2910
    Turni30 – 334
    Beta strandi34 – 429
    Beta strandi48 – 558
    Helixi56 – 583
    Beta strandi60 – 667
    Helixi206 – 2105
    Helixi215 – 22511
    Beta strandi270 – 2723
    Beta strandi278 – 2803
    Helixi284 – 29613
    Helixi301 – 31919
    Beta strandi336 – 3416
    Helixi345 – 35915
    Beta strandi363 – 3675
    Helixi376 – 38510
    Beta strandi391 – 3944
    Helixi396 – 3983
    Beta strandi405 – 4106
    Helixi419 – 4213
    Helixi423 – 43513
    Beta strandi439 – 4435
    Beta strandi456 – 4638
    Helixi469 – 4713
    Beta strandi473 – 4775
    Helixi483 – 4886
    Turni496 – 4994
    Beta strandi501 – 5066

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2VC8X-ray1.31A1-82[»]
    2WAXX-ray2.30B/D192-228[»]
    2WAYX-ray2.30B/D192-228[»]
    3D3JX-ray2.80A203-508[»]
    3D3KX-ray2.20A/B/C/D250-508[»]
    ProteinModelPortaliQ96F86.
    SMRiQ96F86. Positions 3-74, 197-226, 258-507.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ96F86.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini192 – 22837DFDFPROSITE-ProRule annotationAdd
    BLAST
    Domaini283 – 487205YjeF N-terminalPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 7979Required for P-body targeting and interaction with DCP1ABy similarityAdd
    BLAST
    Regioni191 – 296106Required for interaction with DDX6By similarityAdd
    BLAST

    Domaini

    The DFDF domain is unstructured by itself. It assumes a helical fold upon interaction with DDX6.1 Publication

    Sequence similaritiesi

    Belongs to the EDC3 family.Curated
    Contains 1 DFDF domain.PROSITE-ProRule annotation
    Contains 1 YjeF N-terminal domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG271303.
    HOGENOMiHOG000231481.
    HOVERGENiHBG079428.
    InParanoidiQ96F86.
    KOiK12615.
    OMAiPEVTFRA.
    OrthoDBiEOG7H793B.
    PhylomeDBiQ96F86.
    TreeFamiTF324695.

    Family and domain databases

    Gene3Di3.40.50.10260. 1 hit.
    InterProiIPR025762. DFDF.
    IPR019050. FDF_dom.
    IPR025609. Lsm14_N.
    IPR004443. YjeF_N_dom.
    [Graphical view]
    PfamiPF09532. FDF. 1 hit.
    PF12701. LSM14. 1 hit.
    PF03853. YjeF_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF64153. SSF64153. 1 hit.
    PROSITEiPS51512. DFDF. 1 hit.
    PS51385. YJEF_N. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q96F86-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATDWLGSIV SINCGDSLGV YQGRVSAVDQ VSQTISLTRP FHNGVKCLVP    50
    EVTFRAGDIT ELKILEIPGP GDNQHFGDLH QTELGPSGAG CQVGINQNGT 100
    GKFVKKPASS SSAPQNIPKR TDVKSQDVAV SPQQQQCSKS YVDRHMESLS 150
    QSKSFRRRHN SWSSSSRHPN QATPKKSGLK NGQMKNKDDE CFGDDIEEIP 200
    DTDFDFEGNL ALFDKAAVFE EIDTYERRSG TRSRGIPNER PTRYRHDENI 250
    LESEPIVYRR IIVPHNVSKE FCTDSGLVVP SISYELHKKL LSVAEKHGLT 300
    LERRLEMTGV CASQMALTLL GGPNRLNPKN VHQRPTVALL CGPHVKGAQG 350
    ISCGRHLANH DVQVILFLPN FVKMLESITN ELSLFSKTQG QQVSSLKDLP 400
    TSPVDLVINC LDCPENVFLR DQPWYKAAVA WANQNRAPVL SIDPPVHEVE 450
    QGIDAKWSLA LGLPLPLGEH AGRIYLCDIG IPQQVFQEVG INYHSPFGCK 500
    FVIPLHSA 508
    Length:508
    Mass (Da):56,078
    Last modified:December 1, 2001 - v1
    Checksum:i95346F484FCFC3EA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti74 – 741Q → R in BAB15001. (PubMed:14702039)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF193058 mRNA. Translation: AAG22486.1.
    AK024781 mRNA. Translation: BAB15001.1.
    AK056339 mRNA. Translation: BAG51682.1.
    CH471136 Genomic DNA. Translation: EAW99316.1.
    CH471136 Genomic DNA. Translation: EAW99317.1.
    CH471136 Genomic DNA. Translation: EAW99318.1.
    CH471136 Genomic DNA. Translation: EAW99319.1.
    BC011534 mRNA. Translation: AAH11534.1.
    BC021271 mRNA. Translation: AAH21271.1.
    CCDSiCCDS10267.1.
    RefSeqiNP_001135915.1. NM_001142443.1.
    NP_001135916.1. NM_001142444.1.
    NP_079359.2. NM_025083.3.
    UniGeneiHs.682454.
    Hs.96852.

    Genome annotation databases

    EnsembliENST00000315127; ENSP00000320503; ENSG00000179151.
    ENST00000426797; ENSP00000401343; ENSG00000179151.
    ENST00000568176; ENSP00000455580; ENSG00000179151.
    GeneIDi80153.
    KEGGihsa:80153.
    UCSCiuc002aym.3. human.

    Polymorphism databases

    DMDMi74731669.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF193058 mRNA. Translation: AAG22486.1 .
    AK024781 mRNA. Translation: BAB15001.1 .
    AK056339 mRNA. Translation: BAG51682.1 .
    CH471136 Genomic DNA. Translation: EAW99316.1 .
    CH471136 Genomic DNA. Translation: EAW99317.1 .
    CH471136 Genomic DNA. Translation: EAW99318.1 .
    CH471136 Genomic DNA. Translation: EAW99319.1 .
    BC011534 mRNA. Translation: AAH11534.1 .
    BC021271 mRNA. Translation: AAH21271.1 .
    CCDSi CCDS10267.1.
    RefSeqi NP_001135915.1. NM_001142443.1.
    NP_001135916.1. NM_001142444.1.
    NP_079359.2. NM_025083.3.
    UniGenei Hs.682454.
    Hs.96852.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2VC8 X-ray 1.31 A 1-82 [» ]
    2WAX X-ray 2.30 B/D 192-228 [» ]
    2WAY X-ray 2.30 B/D 192-228 [» ]
    3D3J X-ray 2.80 A 203-508 [» ]
    3D3K X-ray 2.20 A/B/C/D 250-508 [» ]
    ProteinModelPortali Q96F86.
    SMRi Q96F86. Positions 3-74, 197-226, 258-507.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 123144. 15 interactions.
    DIPi DIP-35516N.
    IntActi Q96F86. 15 interactions.
    MINTi MINT-5005528.
    STRINGi 9606.ENSP00000320503.

    PTM databases

    PhosphoSitei Q96F86.

    Polymorphism databases

    DMDMi 74731669.

    Proteomic databases

    MaxQBi Q96F86.
    PaxDbi Q96F86.
    PeptideAtlasi Q96F86.
    PRIDEi Q96F86.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000315127 ; ENSP00000320503 ; ENSG00000179151 .
    ENST00000426797 ; ENSP00000401343 ; ENSG00000179151 .
    ENST00000568176 ; ENSP00000455580 ; ENSG00000179151 .
    GeneIDi 80153.
    KEGGi hsa:80153.
    UCSCi uc002aym.3. human.

    Organism-specific databases

    CTDi 80153.
    GeneCardsi GC15M074922.
    HGNCi HGNC:26114. EDC3.
    HPAi HPA040650.
    HPA044206.
    MIMi 609842. gene.
    neXtProti NX_Q96F86.
    PharmGKBi PA142670551.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG271303.
    HOGENOMi HOG000231481.
    HOVERGENi HBG079428.
    InParanoidi Q96F86.
    KOi K12615.
    OMAi PEVTFRA.
    OrthoDBi EOG7H793B.
    PhylomeDBi Q96F86.
    TreeFami TF324695.

    Enzyme and pathway databases

    Reactomei REACT_20518. mRNA decay by 5' to 3' exoribonuclease.

    Miscellaneous databases

    EvolutionaryTracei Q96F86.
    GeneWikii EDC3.
    GenomeRNAii 80153.
    NextBioi 70444.
    PROi Q96F86.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96F86.
    Bgeei Q96F86.
    CleanExi HS_EDC3.
    Genevestigatori Q96F86.

    Family and domain databases

    Gene3Di 3.40.50.10260. 1 hit.
    InterProi IPR025762. DFDF.
    IPR019050. FDF_dom.
    IPR025609. Lsm14_N.
    IPR004443. YjeF_N_dom.
    [Graphical view ]
    Pfami PF09532. FDF. 1 hit.
    PF12701. LSM14. 1 hit.
    PF03853. YjeF_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF64153. SSF64153. 1 hit.
    PROSITEi PS51512. DFDF. 1 hit.
    PS51385. YJEF_N. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Large-scale cDNA transfection screening for genes related to cancer development and progression."
      Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.
      , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
      Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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].
      Tissue: Eye and Placenta.
    5. "Multiple processing body factors and the ARE binding protein TTP activate mRNA decapping."
      Fenger-Groen M., Fillman C., Norrild B., Lykke-Andersen J.
      Mol. Cell 20:905-915(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH DCP1A; DCP2; DDX6; EDC4 AND ZFP36, SUBCELLULAR LOCATION, FUNCTION.
    6. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "ApoA-I-binding protein (AI-BP) and its homologues hYjeF_N2 and hYjeF_N3 comprise the YjeF_N domain protein family in humans with a role in spermiogenesis and oogenesis."
      Rudolph C., Sigruener A., Hartmann A., Orso E., Bals-Pratsch M., Gronwald W., Seifert B., Kalbitzer H.R., Verdorfer I., Luetjens C.M., Ortmann O., Bornstein S.R., Schmitz G.
      Horm. Metab. Res. 39:322-335(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    11. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138 AND SER-140, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: X-RAY CRYSTALLOGRAPHY (1.31 ANGSTROMS) OF 1-82.
    15. "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] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 250-508, FUNCTION, RNA-BINDING, SUBUNIT, CIRCULAR DICHROISM, MUTAGENESIS OF GLU-306 AND VAL-310.
    16. "Structural basis for the mutually exclusive anchoring of P body components EDC3 and Tral to the DEAD box protein DDX6/Me31B."
      Tritschler F., Braun J.E., Eulalio A., Truffault V., Izaurralde E., Weichenrieder O.
      Mol. Cell 33:661-668(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 192-228 IN COMPLEX WITH DDX6, INTERACTION WITH DDX6, MUTAGENESIS OF PHE-204 AND PHE-206, DOMAIN.

    Entry informationi

    Entry nameiEDC3_HUMAN
    AccessioniPrimary (citable) accession number: Q96F86
    Secondary accession number(s): B3KPH0, D3DW61, Q9H797
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 22, 2005
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 114 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 15
      Human chromosome 15: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

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