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O43324

- MCA3_HUMAN

UniProt

O43324 - MCA3_HUMAN

Protein

Eukaryotic translation elongation factor 1 epsilon-1

Gene

EEF1E1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 1 (01 Jun 1998)
      Previous versions | rss
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    Functioni

    Positive modulator of ATM response to DNA damage.

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. gene expression Source: Reactome
    2. negative regulation of cell proliferation Source: UniProtKB
    3. positive regulation of apoptotic process Source: UniProtKB
    4. positive regulation of DNA damage response, signal transduction by p53 class mediator Source: UniProtKB
    5. tRNA aminoacylation for protein translation Source: Reactome

    Keywords - Biological processi

    Protein biosynthesis

    Enzyme and pathway databases

    ReactomeiREACT_15306. Cytosolic tRNA aminoacylation.
    SignaLinkiO43324.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Eukaryotic translation elongation factor 1 epsilon-1
    Alternative name(s):
    Aminoacyl tRNA synthetase complex-interacting multifunctional protein 3
    Elongation factor p18
    Multisynthase complex auxiliary component p18
    Gene namesi
    Name:EEF1E1
    Synonyms:AIMP3, P18
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:3212. EEF1E1.

    Subcellular locationi

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

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. extracellular vesicular exosome Source: UniProt
    4. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27648.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 174173Eukaryotic translation elongation factor 1 epsilon-1PRO_0000221132Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei138 – 1381N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiO43324.
    PaxDbiO43324.
    PeptideAtlasiO43324.
    PRIDEiO43324.

    PTM databases

    PhosphoSiteiO43324.

    Expressioni

    Tissue specificityi

    Down-regulated in various cancer tissues.1 Publication

    Inductioni

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

    Gene expression databases

    ArrayExpressiO43324.
    BgeeiO43324.
    CleanExiHS_EEF1E1.
    GenevestigatoriO43324.

    Organism-specific databases

    HPAiHPA027901.

    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.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    gagP045914EBI-1048486,EBI-6179719From a different organism.

    Protein-protein interaction databases

    BioGridi114898. 30 interactions.
    DIPiDIP-50581N.
    IntActiO43324. 3 interactions.
    STRINGi9606.ENSP00000369038.

    Structurei

    Secondary structure

    1
    174
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 1412
    Beta strandi23 – 253
    Turni26 – 294
    Beta strandi30 – 334
    Beta strandi41 – 433
    Helixi44 – 5411
    Helixi58 – 614
    Helixi65 – 8016
    Helixi85 – 10117
    Helixi102 – 1043
    Beta strandi110 – 1123
    Helixi115 – 12814
    Helixi133 – 1386
    Helixi140 – 15011
    Turni153 – 1553

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2UZ8X-ray2.00A/B1-174[»]
    4BJVX-ray1.99B1-174[»]
    4BJWX-ray1.60B1-169[»]
    4BL7X-ray1.89B1-174[»]
    ProteinModelPortaliO43324.
    SMRiO43324. Positions 1-169.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO43324.

    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-terminalAdd
    BLAST
    Regioni57 – 637Linker
    Regioni64 – 15289C-terminalAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili153 – 169171 PublicationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 GST C-terminal domain.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG257622.
    HOGENOMiHOG000026786.
    HOVERGENiHBG003019.
    InParanoidiO43324.
    KOiK15439.
    OMAiAVVQQWL.
    OrthoDBiEOG7GQXX4.
    PhylomeDBiO43324.
    TreeFamiTF326005.

    Family and domain databases

    Gene3Di1.20.1050.10. 1 hit.
    InterProiIPR010987. Glutathione-S-Trfase_C-like.
    IPR004046. GST_C.
    [Graphical view]
    PfamiPF14497. GST_C_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF47616. SSF47616. 1 hit.
    PROSITEiPS50405. GST_CTER. 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. Align

    Isoform 1 (identifier: O43324-1) [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

    MAAAAELSLL EKSLGLSKGN KYSAQGERQI PVLQTNNGPS LTGLTTIAAH    50
    LVKQANKEYL LGSTAEEKAI VQQWLEYRVT QVDGHSSKND IHTLLKDLNS 100
    YLEDKVYLTG YNFTLADILL YYGLHRFIVD LTVQEKEKYL NVSRWFCHIQ 150
    HYPGIRQHLS SVVFIKNRLY TNSH 174
    Length:174
    Mass (Da):19,811
    Last modified:June 1, 1998 - v1
    Checksum:i58AAE4BD9E1684E2
    GO
    Isoform 2 (identifier: O43324-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         129-174: VDLTVQEKEKYLNVSRWFCHIQHYPGIRQHLSSVVFIKNRLYTNSH → IRKLRHTEVGN

    Note: No experimental confirmation available.

    Show »
    Length:139
    Mass (Da):15,548
    Checksum:iE11E55B587974D5C
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei129 – 17446VDLTV…YTNSH → IRKLRHTEVGN in isoform 2. 1 PublicationVSP_045088Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB011079 mRNA. Translation: BAA24926.1.
    AF054186 mRNA. Translation: AAC39916.1.
    BT007306 mRNA. Translation: AAP35970.1.
    AL355499, AL023694, AL451187 Genomic DNA. Translation: CAH72539.1.
    AL023694, AL355499, AL451187 Genomic DNA. Translation: CAI21644.1.
    AL451187, AL023694, AL355499 Genomic DNA. Translation: CAI14747.1.
    BC005291 mRNA. Translation: AAH05291.1.
    CK002875 mRNA. No translation available.
    CCDSiCCDS4507.1. [O43324-1]
    CCDS47370.1. [O43324-2]
    RefSeqiNP_001129122.1. NM_001135650.1. [O43324-2]
    NP_004271.1. NM_004280.4. [O43324-1]
    UniGeneiHs.602353.
    Hs.745033.

    Genome annotation databases

    EnsembliENST00000379715; ENSP00000369038; ENSG00000124802. [O43324-1]
    ENST00000429723; ENSP00000414363; ENSG00000124802. [O43324-2]
    GeneIDi9521.
    KEGGihsa:9521.
    UCSCiuc003mxz.3. human. [O43324-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB011079 mRNA. Translation: BAA24926.1 .
    AF054186 mRNA. Translation: AAC39916.1 .
    BT007306 mRNA. Translation: AAP35970.1 .
    AL355499 , AL023694 , AL451187 Genomic DNA. Translation: CAH72539.1 .
    AL023694 , AL355499 , AL451187 Genomic DNA. Translation: CAI21644.1 .
    AL451187 , AL023694 , AL355499 Genomic DNA. Translation: CAI14747.1 .
    BC005291 mRNA. Translation: AAH05291.1 .
    CK002875 mRNA. No translation available.
    CCDSi CCDS4507.1. [O43324-1 ]
    CCDS47370.1. [O43324-2 ]
    RefSeqi NP_001129122.1. NM_001135650.1. [O43324-2 ]
    NP_004271.1. NM_004280.4. [O43324-1 ]
    UniGenei Hs.602353.
    Hs.745033.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2UZ8 X-ray 2.00 A/B 1-174 [» ]
    4BJV X-ray 1.99 B 1-174 [» ]
    4BJW X-ray 1.60 B 1-169 [» ]
    4BL7 X-ray 1.89 B 1-174 [» ]
    ProteinModelPortali O43324.
    SMRi O43324. Positions 1-169.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114898. 30 interactions.
    DIPi DIP-50581N.
    IntActi O43324. 3 interactions.
    STRINGi 9606.ENSP00000369038.

    PTM databases

    PhosphoSitei O43324.

    Proteomic databases

    MaxQBi O43324.
    PaxDbi O43324.
    PeptideAtlasi O43324.
    PRIDEi O43324.

    Protocols and materials databases

    DNASUi 9521.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000379715 ; ENSP00000369038 ; ENSG00000124802 . [O43324-1 ]
    ENST00000429723 ; ENSP00000414363 ; ENSG00000124802 . [O43324-2 ]
    GeneIDi 9521.
    KEGGi hsa:9521.
    UCSCi uc003mxz.3. human. [O43324-1 ]

    Organism-specific databases

    CTDi 9521.
    GeneCardsi GC06M008024.
    HGNCi HGNC:3212. EEF1E1.
    HPAi HPA027901.
    MIMi 609206. gene.
    neXtProti NX_O43324.
    PharmGKBi PA27648.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG257622.
    HOGENOMi HOG000026786.
    HOVERGENi HBG003019.
    InParanoidi O43324.
    KOi K15439.
    OMAi AVVQQWL.
    OrthoDBi EOG7GQXX4.
    PhylomeDBi O43324.
    TreeFami TF326005.

    Enzyme and pathway databases

    Reactomei REACT_15306. Cytosolic tRNA aminoacylation.
    SignaLinki O43324.

    Miscellaneous databases

    ChiTaRSi EEF1E1. human.
    EvolutionaryTracei O43324.
    GeneWikii EEF1E1.
    GenomeRNAii 9521.
    NextBioi 35684.
    PROi O43324.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O43324.
    Bgeei O43324.
    CleanExi HS_EEF1E1.
    Genevestigatori O43324.

    Family and domain databases

    Gene3Di 1.20.1050.10. 1 hit.
    InterProi IPR010987. Glutathione-S-Trfase_C-like.
    IPR004046. GST_C.
    [Graphical view ]
    Pfami PF14497. GST_C_3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47616. SSF47616. 1 hit.
    PROSITEi PS50405. GST_CTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of cDNA for human p18 from human testis."
      Motegi H., Noda T., Shiba K.
      Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Testis.
    2. "Identification of genes expressed in human CD34(+) hematopoietic stem/progenitor cells by expressed sequence tags and efficient full-length cDNA cloning."
      Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H., He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H., Wang Y.-X., Chen S.-J., Chen Z.
      Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Umbilical cord blood.
    3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORMS 1 AND 2).
      Tissue: Brain cortex and Urinary bladder.
    6. Cited for: PROTEIN SEQUENCE OF 2-12 AND 79-88, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Cervix carcinoma and Ovarian carcinoma.
    7. "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: INTERACTION WITH ATM, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    8. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-138, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Determination of three-dimensional structure and residues of the novel tumor suppressor AIMP3/p18 required for the interaction with ATM."
      Kim K.J., Park M.C., Choi S.J., Oh Y.S., Choi E.C., Cho H.J., Kim M.H., Kim S.H., Kim D.W., Kim S., Kang B.S.
      J. Biol. Chem. 283:14032-14040(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), DOMAIN ARCHITECTURE, COILED-COIL DOMAIN.

    Entry informationi

    Entry nameiMCA3_HUMAN
    AccessioniPrimary (citable) accession number: O43324
    Secondary accession number(s): C9JLK5, Q5THS2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 18, 2001
    Last sequence update: June 1, 1998
    Last modified: October 1, 2014
    This is version 132 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: 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

    Dasty 3