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O43324 (MCA3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:EEF1E1
Synonyms:AIMP3, P18
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length174 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Positive modulator of ATM response to DNA damage.

Subunit structure

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. Ref.7

Subcellular location

Cytoplasm. Nucleus. Note: Cytoplasmic under growth arrest conditions. Translocated into the nucleus when growth resumes (S phase) and following DNA damage. Ref.7

Tissue specificity

Down-regulated in various cancer tissues. Ref.7

Induction

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

Sequence similarities

Contains 1 GST C-terminal domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

gagP045914EBI-1048486,EBI-6179719From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O43324-1)

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.
Isoform 2 (identifier: O43324-2)

The sequence of this isoform differs from the canonical sequence as follows:
     129-174: VDLTVQEKEKYLNVSRWFCHIQHYPGIRQHLSSVVFIKNRLYTNSH → IRKLRHTEVGN
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 174173Eukaryotic translation elongation factor 1 epsilon-1
PRO_0000221132

Regions

Domain50 – 173124GST C-terminal
Region2 – 5655N-terminal
Region57 – 637Linker
Region64 – 15289C-terminal
Coiled coil153 – 16917 Ref.10

Amino acid modifications

Modified residue21N-acetylalanine Ref.6
Modified residue1381N6-acetyllysine Ref.8

Natural variations

Alternative sequence129 – 17446VDLTV…YTNSH → IRKLRHTEVGN in isoform 2.
VSP_045088

Secondary structure

........................... 174
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 58AAE4BD9E1684E2

FASTA17419,811
        10         20         30         40         50         60 
MAAAAELSLL EKSLGLSKGN KYSAQGERQI PVLQTNNGPS LTGLTTIAAH LVKQANKEYL 

        70         80         90        100        110        120 
LGSTAEEKAI VQQWLEYRVT QVDGHSSKND IHTLLKDLNS YLEDKVYLTG YNFTLADILL 

       130        140        150        160        170 
YYGLHRFIVD LTVQEKEKYL NVSRWFCHIQ HYPGIRQHLS SVVFIKNRLY TNSH 

« Hide

Isoform 2 [UniParc].

Checksum: E11E55B587974D5C
Show »

FASTA13915,548

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Bienvenut W.V., Calvo F., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
Submitted (DEC-2008) to UniProtKB
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS4507.1. [O43324-1]
CCDS47370.1. [O43324-2]
RefSeqNP_001129122.1. NM_001135650.1. [O43324-2]
NP_004271.1. NM_004280.4. [O43324-1]
UniGeneHs.602353.
Hs.745033.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2UZ8X-ray2.00A/B1-174[»]
4BJVX-ray1.99B1-174[»]
4BJWX-ray1.60B1-169[»]
4BL7X-ray1.89B1-174[»]
ProteinModelPortalO43324.
SMRO43324. Positions 1-169.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114898. 30 interactions.
DIPDIP-50581N.
IntActO43324. 3 interactions.
STRING9606.ENSP00000369038.

PTM databases

PhosphoSiteO43324.

Proteomic databases

MaxQBO43324.
PaxDbO43324.
PeptideAtlasO43324.
PRIDEO43324.

Protocols and materials databases

DNASU9521.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000379715; ENSP00000369038; ENSG00000124802. [O43324-1]
ENST00000429723; ENSP00000414363; ENSG00000124802. [O43324-2]
GeneID9521.
KEGGhsa:9521.
UCSCuc003mxz.3. human. [O43324-1]

Organism-specific databases

CTD9521.
GeneCardsGC06M008024.
HGNCHGNC:3212. EEF1E1.
HPAHPA027901.
MIM609206. gene.
neXtProtNX_O43324.
PharmGKBPA27648.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG257622.
HOGENOMHOG000026786.
HOVERGENHBG003019.
InParanoidO43324.
KOK15439.
OMAAVVQQWL.
OrthoDBEOG7GQXX4.
PhylomeDBO43324.
TreeFamTF326005.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.
SignaLinkO43324.

Gene expression databases

ArrayExpressO43324.
BgeeO43324.
CleanExHS_EEF1E1.
GenevestigatorO43324.

Family and domain databases

Gene3D1.20.1050.10. 1 hit.
InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004046. GST_C.
[Graphical view]
PfamPF14497. GST_C_3. 1 hit.
[Graphical view]
SUPFAMSSF47616. SSF47616. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEEF1E1. human.
EvolutionaryTraceO43324.
GeneWikiEEF1E1.
GenomeRNAi9521.
NextBio35684.
PROO43324.
SOURCESearch...

Entry information

Entry nameMCA3_HUMAN
AccessionPrimary (citable) accession number: O43324
Secondary accession number(s): C9JLK5, Q5THS2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: June 1, 1998
Last modified: July 9, 2014
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM