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Protein

Eukaryotic translation elongation factor 1 epsilon-1

Gene

Eef1e1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Positive modulator of ATM response to DNA damage.By similarity

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
Complete GO annotation...

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 Componenti: 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. extracellular vesicular exosome Source: MGI
  4. nucleus Source: UniProtKB
Complete GO annotation...

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

BgeeiQ9D1M4.
ExpressionAtlasiQ9D1M4. baseline and differential.
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 1-168.
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

« Hide

        10         20         30         40         50
MAAAAELRLL EKSLGLKPGN KYSAQGERQI PVLQTNNGPS LMGLSTIATH
60 70 80 90 100
LVKQASKEHL LGSTAEEKAM VQQWLEFRVT RVDGHSSKED TQTLLKDLNS
110 120 130 140 150
YLEDKVYLAG HNITLADILL YYGLHRFIVD LTVQEKEKYL NVSRWFCHIQ
160 170
HYPDIRQHLS SIVFIKNRLY ANSH
Length:174
Mass (Da):19,859
Last modified:May 31, 2001 - v1
Checksum:iAC804776D9C0590E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
AK003335 mRNA. Translation: BAB22723.1.
BC048466 mRNA. Translation: AAH48466.1.
CCDSiCCDS26465.1.
RefSeqiNP_079656.1. NM_025380.2.
UniGeneiMm.490319.

3D structure databases

ProteinModelPortaliQ9D1M4.
SMRiQ9D1M4. Positions 1-168.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9D1M4. 1 interaction.
MINTiMINT-4126622.

PTM databases

PhosphoSiteiQ9D1M4.

Proteomic databases

MaxQBiQ9D1M4.
PaxDbiQ9D1M4.
PRIDEiQ9D1M4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi9521.
MGIiMGI:1913393. Eef1e1.

Phylogenomic databases

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

Miscellaneous databases

NextBioi320758.
PROiQ9D1M4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D1M4.
ExpressionAtlasiQ9D1M4. baseline and differential.
GenevestigatoriQ9D1M4.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(2004) [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(2003) [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(2004) [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 9, 2005
Last sequence update: May 31, 2001
Last modified: March 3, 2015
This is version 104 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.