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Q9D1M4

- MCA3_MOUSE

UniProt

Q9D1M4 - MCA3_MOUSE

Protein

Eukaryotic translation elongation factor 1 epsilon-1

Gene

Eef1e1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    Positive modulator of ATM response to DNA damage.By similarity

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. DNA repair Source: UniProtKB
    2. embryo development Source: UniProtKB
    3. negative regulation of cell proliferation Source: UniProtKB
    4. positive regulation of apoptotic process Source: UniProtKB
    5. positive regulation of apoptotic signaling pathway Source: MGI
    6. positive regulation of DNA damage response, signal transduction by p53 class mediator Source: UniProtKB
    7. translation Source: UniProtKB-KW

    Keywords - Biological processi

    Protein biosynthesis

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Eukaryotic translation elongation factor 1 epsilon-1
    Alternative name(s):
    Elongation factor p18
    Multisynthase complex auxiliary component p18
    Gene namesi
    Name:Eef1e1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 13

    Organism-specific databases

    MGIiMGI:1913393. Eef1e1.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication
    Note: Cytoplasmic under growth arrest conditions. Translocated into the nucleus when growth resumes at S phase and following DNA damage.

    GO - Cellular componenti

    1. aminoacyl-tRNA synthetase multienzyme complex Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 174173Eukaryotic translation elongation factor 1 epsilon-1PRO_0000221133Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei138 – 1381N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9D1M4.
    PaxDbiQ9D1M4.
    PRIDEiQ9D1M4.

    PTM databases

    PhosphoSiteiQ9D1M4.

    Expressioni

    Inductioni

    By DNA damaging agents, such as UV, adriamycin, actinomycin D and cisplatin.1 Publication

    Gene expression databases

    ArrayExpressiQ9D1M4.
    BgeeiQ9D1M4.
    GenevestigatoriQ9D1M4.

    Interactioni

    Subunit structurei

    Component of the multisynthase complex which is comprised of a bifunctional glutamyl-prolyl-tRNA synthase, the monospecific isoleucyl, leucyl, glutaminyl, methionyl, lysyl, arginyl and aspartyl-tRNA synthases, and three auxiliary proteins, EEF1E1/p18, AIMP2/p38 and AIMP1/p43. Interacts with ATM and ATR. The interaction with ATM, which takes place independently of TP53, is induced by DNA damage that may occur during genotoxic stress or cell growth. The interaction with ATR is enhanced by UV irradiation By similarity.By similarity

    Protein-protein interaction databases

    IntActiQ9D1M4. 1 interaction.
    MINTiMINT-4126622.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9D1M4.
    SMRiQ9D1M4. Positions 1-169.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini50 – 173124GST C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 5655N-terminalBy similarityAdd
    BLAST
    Regioni57 – 637LinkerBy similarity
    Regioni64 – 15289C-terminalBy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili153 – 16917By similarityAdd
    BLAST

    Sequence similaritiesi

    Contains 1 GST C-terminal domain.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG0073.
    GeneTreeiENSGT00390000003564.
    HOGENOMiHOG000026786.
    HOVERGENiHBG003019.
    InParanoidiQ9D1M4.
    KOiK15439.
    OMAiAVVQQWL.
    OrthoDBiEOG7GQXX4.
    PhylomeDBiQ9D1M4.
    TreeFamiTF326005.

    Family and domain databases

    Gene3Di1.20.1050.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProiIPR010987. Glutathione-S-Trfase_C-like.
    IPR004046. GST_C.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF00043. GST_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF47616. SSF47616. 1 hit.
    PROSITEiPS50405. GST_CTER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9D1M4-1 [UniParc]FASTAAdd to Basket

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    MAAAAELRLL EKSLGLKPGN KYSAQGERQI PVLQTNNGPS LMGLSTIATH    50
    LVKQASKEHL LGSTAEEKAM VQQWLEFRVT RVDGHSSKED TQTLLKDLNS 100
    YLEDKVYLAG HNITLADILL YYGLHRFIVD LTVQEKEKYL NVSRWFCHIQ 150
    HYPDIRQHLS SIVFIKNRLY ANSH 174
    Length:174
    Mass (Da):19,859
    Last modified:June 1, 2001 - v1
    Checksum:iAC804776D9C0590E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK003335 mRNA. Translation: BAB22723.1.
    BC048466 mRNA. Translation: AAH48466.1.
    CCDSiCCDS26465.1.
    RefSeqiNP_079656.1. NM_025380.2.
    UniGeneiMm.490319.

    Genome annotation databases

    EnsembliENSMUST00000001757; ENSMUSP00000001757; ENSMUSG00000001707.
    GeneIDi66143.
    KEGGimmu:66143.
    UCSCiuc007qdw.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK003335 mRNA. Translation: BAB22723.1 .
    BC048466 mRNA. Translation: AAH48466.1 .
    CCDSi CCDS26465.1.
    RefSeqi NP_079656.1. NM_025380.2.
    UniGenei Mm.490319.

    3D structure databases

    ProteinModelPortali Q9D1M4.
    SMRi Q9D1M4. Positions 1-169.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9D1M4. 1 interaction.
    MINTi MINT-4126622.

    PTM databases

    PhosphoSitei Q9D1M4.

    Proteomic databases

    MaxQBi Q9D1M4.
    PaxDbi Q9D1M4.
    PRIDEi Q9D1M4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000001757 ; ENSMUSP00000001757 ; ENSMUSG00000001707 .
    GeneIDi 66143.
    KEGGi mmu:66143.
    UCSCi uc007qdw.1. mouse.

    Organism-specific databases

    CTDi 9521.
    MGIi MGI:1913393. Eef1e1.

    Phylogenomic databases

    eggNOGi COG0073.
    GeneTreei ENSGT00390000003564.
    HOGENOMi HOG000026786.
    HOVERGENi HBG003019.
    InParanoidi Q9D1M4.
    KOi K15439.
    OMAi AVVQQWL.
    OrthoDBi EOG7GQXX4.
    PhylomeDBi Q9D1M4.
    TreeFami TF326005.

    Miscellaneous databases

    NextBioi 320758.
    PROi Q9D1M4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9D1M4.
    Bgeei Q9D1M4.
    Genevestigatori Q9D1M4.

    Family and domain databases

    Gene3Di 1.20.1050.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProi IPR010987. Glutathione-S-Trfase_C-like.
    IPR004046. GST_C.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    Pfami PF00043. GST_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47616. SSF47616. 1 hit.
    PROSITEi PS50405. GST_CTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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].
      Strain: C57BL/6J.
      Tissue: Embryo.
    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].
      Tissue: Brain.
    3. "The haploinsufficient tumor suppressor p18 upregulates p53 via interactions with ATM/ATR."
      Park B.-J., Kang J.W., Lee S.W., Choi S.-J., Shin Y.K., Ahn Y.H., Choi Y.H., Choi D., Lee K.S., Kim S.
      Cell 120:209-221(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INDUCTION.

    Entry informationi

    Entry nameiMCA3_MOUSE
    AccessioniPrimary (citable) accession number: Q9D1M4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 10, 2005
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 99 of the entry and version 1 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

    External Data

    Dasty 3