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O43324

- MCA3_HUMAN

UniProt

O43324 - MCA3_HUMAN

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Protein

Eukaryotic translation elongation factor 1 epsilon-1

Gene
EEF1E1, AIMP3, P18
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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

GO - Cellular componenti

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

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.

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

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. VSP_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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 131 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

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