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Q9D1M4 (MCA3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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):
Elongation factor p18
Multisynthase complex auxiliary component p18
Gene names
Name:Eef1e1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

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

General annotation (Comments)

Function

Positive modulator of ATM response to DNA damage By similarity. Ref.3

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 By similarity.

Subcellular location

Cytoplasm. Nucleus. Note: Cytoplasmic under growth arrest conditions. Translocated into the nucleus when growth resumes at S phase and following DNA damage. Ref.3

Induction

By DNA damaging agents, such as UV, adriamycin, actinomycin D and cisplatin. Ref.3

Sequence similarities

Contains 1 GST C-terminal domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 174173Eukaryotic translation elongation factor 1 epsilon-1
PRO_0000221133

Regions

Domain50 – 173124GST C-terminal
Region2 – 5655N-terminal By similarity
Region57 – 637Linker By similarity
Region64 – 15289C-terminal By similarity
Coiled coil153 – 16917 By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue1381N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9D1M4 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: AC804776D9C0590E

FASTA17419,859
        10         20         30         40         50         60 
MAAAAELRLL EKSLGLKPGN KYSAQGERQI PVLQTNNGPS LMGLSTIATH LVKQASKEHL 

        70         80         90        100        110        120 
LGSTAEEKAM VQQWLEFRVT RVDGHSSKED TQTLLKDLNS YLEDKVYLAG HNITLADILL 

       130        140        150        160        170 
YYGLHRFIVD LTVQEKEKYL NVSRWFCHIQ HYPDIRQHLS SIVFIKNRLY ANSH 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK003335 mRNA. Translation: BAB22723.1.
BC048466 mRNA. Translation: AAH48466.1.
CCDSCCDS26465.1.
RefSeqNP_079656.1. NM_025380.2.
UniGeneMm.490319.

3D structure databases

ProteinModelPortalQ9D1M4.
SMRQ9D1M4. Positions 1-169.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9D1M4. 1 interaction.
MINTMINT-4126622.

PTM databases

PhosphoSiteQ9D1M4.

Proteomic databases

MaxQBQ9D1M4.
PaxDbQ9D1M4.
PRIDEQ9D1M4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000001757; ENSMUSP00000001757; ENSMUSG00000001707.
GeneID66143.
KEGGmmu:66143.
UCSCuc007qdw.1. mouse.

Organism-specific databases

CTD9521.
MGIMGI:1913393. Eef1e1.

Phylogenomic databases

eggNOGCOG0073.
GeneTreeENSGT00390000003564.
HOGENOMHOG000026786.
HOVERGENHBG003019.
InParanoidQ9D1M4.
KOK15439.
OMAAVVQQWL.
OrthoDBEOG7GQXX4.
PhylomeDBQ9D1M4.
TreeFamTF326005.

Gene expression databases

ArrayExpressQ9D1M4.
BgeeQ9D1M4.
GenevestigatorQ9D1M4.

Family and domain databases

Gene3D1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF00043. GST_C. 1 hit.
[Graphical view]
SUPFAMSSF47616. SSF47616. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio320758.
PROQ9D1M4.
SOURCESearch...

Entry information

Entry nameMCA3_MOUSE
AccessionPrimary (citable) accession number: Q9D1M4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot