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Protein

Elongation factor 1-delta

Gene

Eef1d

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

Functioni

Isoform 1: EF-1-beta and EF-1-delta stimulate the exchange of GDP bound to EF-1-alpha to GTP, regenerating EF-1-alpha for another round of transfer of aminoacyl-tRNAs to the ribosome.By similarity
Isoform 3: Regulates induction of heat-shock-responsive genes through association with heat shock transcription factors and direct DNA-binding at heat shock promoter elements (HSE).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Elongation factor

Keywords - Biological processi

Protein biosynthesis, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation factor 1-delta
Short name:
EF-1-delta
Gene namesi
Name:Eef1d
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1913906. Eef1d.

Subcellular locationi

Isoform 3 :
  • Nucleus By similarity

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • eukaryotic translation elongation factor 1 complex Source: InterPro
  • nucleolus Source: MGI
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 281280Elongation factor 1-deltaPRO_0000155047Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei17 – 171N6-acetyllysineBy similarity
Modified residuei60 – 601PhosphoserineBy similarity
Modified residuei106 – 1061PhosphoserineBy similarity
Modified residuei107 – 1071N6-acetyllysineBy similarity
Modified residuei117 – 1171N6-acetyllysine; alternateBy similarity
Modified residuei117 – 1171N6-succinyllysine; alternateCombined sources
Modified residuei129 – 1291PhosphothreonineBy similarity
Modified residuei133 – 1331PhosphoserineCombined sources
Modified residuei147 – 1471PhosphothreonineCombined sources
Modified residuei162 – 1621Phosphoserine; by CK2Combined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP57776.
MaxQBiP57776.
PaxDbiP57776.
PRIDEiP57776.

2D gel databases

REPRODUCTION-2DPAGEP57776.

PTM databases

iPTMnetiP57776.
PhosphoSiteiP57776.
SwissPalmiP57776.

Expressioni

Gene expression databases

BgeeiP57776.

Interactioni

Subunit structurei

EF-1 is composed of 4 subunits: alpha, beta, delta isoform 1, and gamma. Isoform 3 interacts with HSF1 and NFE2L2.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi211625. 2 interactions.
IntActiP57776. 6 interactions.
MINTiMINT-1856784.
STRINGi10090.ENSMUSP00000087110.

Structurei

3D structure databases

ProteinModelPortaliP57776.
SMRiP57776. Positions 153-281.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni80 – 11536Leucine-zipperBy similarityAdd
BLAST
Regioni173 – 281109Catalytic (GEF)By similarityAdd
BLAST

Sequence similaritiesi

Belongs to the EF-1-beta/EF-1-delta family.Curated

Phylogenomic databases

eggNOGiKOG1668. Eukaryota.
COG2092. LUCA.
HOGENOMiHOG000207272.
HOVERGENiHBG000787.
InParanoidiP57776.
KOiK15410.
TreeFamiTF313134.

Family and domain databases

Gene3Di3.30.70.60. 1 hit.
InterProiIPR018940. EF-1_beta_acid_region_euk.
IPR014717. Transl_elong_EF1B/ribosomal_S6.
IPR001326. Transl_elong_EF1B_B/D_CS.
IPR014038. Transl_elong_fac_EF1B_bsu/dsu.
[Graphical view]
PfamiPF10587. EF-1_beta_acid. 1 hit.
PF00736. EF1_GNE. 1 hit.
[Graphical view]
SMARTiSM01182. EF-1_beta_acid. 1 hit.
SM00888. EF1_GNE. 1 hit.
[Graphical view]
SUPFAMiSSF54984. SSF54984. 1 hit.
PROSITEiPS00824. EF1BD_1. 1 hit.
PS00825. EF1BD_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P57776-1) [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

        10         20         30         40         50
MATNFLAHEK IWFDKFKYDD AERRFYEQMN GPVTSGSRQE NGASVILRDI
60 70 80 90 100
ARARENIQKS LAGSSGPGAS SGPGGDHSEL IVRITSLEVE NQNLRGVVQD
110 120 130 140 150
LQQAISKLEA RLSSLEKSSP TPRATAPQTQ HVSPMRQVEP PTKKGATPAE
160 170 180 190 200
DDEDKDIDLF GSDEEEEDKE AARLREERLR QYAEKKAKKP TLVAKSSILL
210 220 230 240 250
DVKPWDDETD MAQLETCVRS IQLDGLVWGA SKLVPVGYGI RKLQIQCVVE
260 270 280
DDKVGTDLLE EEITKFEEHV QSVDIAAFDK I
Length:281
Mass (Da):31,293
Last modified:January 23, 2007 - v3
Checksum:iFD55F872FDA06819
GO
Isoform 2 (identifier: P57776-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     40-63: Missing.

Note: No experimental confirmation available.
Show »
Length:257
Mass (Da):28,729
Checksum:iE0072696BD8CAACF
GO
Isoform 3 (identifier: P57776-3) [UniParc]FASTAAdd to basket

Also known as: eEF1BdeltaLBy similarity

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MRSGKASCAL...MSSLRPNRKM

Show »
Length:660
Mass (Da):72,931
Checksum:i0B4B8EBE385ADDA4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti279 – 2791D → N in BAB26870 (PubMed:16141072).Curated
Sequence conflicti279 – 2791D → N in BAB30841 (PubMed:16141072).Curated
Sequence conflicti279 – 2791D → N in AAH79855 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MRSGKASCALETVWEDRHKY EGAERRFHEQEATQVVAAAA TAAATASASVQQLLDEVPAV NGPSQEDTEDTEEAEAPNTS SRSDPGKSHECKKPIQKKRK RSPKSWLGQADLALVGLSAD HVWLDKPLFDQAESSYRQRL ADVAAQAAQPPALAPRGPCT HGSHVACHHVTWGIWVNKSC FDQAERAFVEWSQSLLLAAE GSHRQGTPDTGQQAVTPDLA LACQPCPPANGQPPLGSLQA LVREVWLEKPRYDAAERGFY EALFDGHPPGKVRLQERASQ AEGTRRGRRDHRSCNNVGNK RAGSKRANGEAPPAFPYWYF LHKDAEAPWLSKPTYDSAEC RHHAVEALRIAWRLEAASLA HRPTPRSGPSMSSLRPNRKM in isoform 3. 1 PublicationVSP_037885
Alternative sequencei40 – 6324Missing in isoform 2. 1 PublicationVSP_001359Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF304351 mRNA. Translation: AAG17466.1.
AK010308 mRNA. No translation available.
AK010347 mRNA. Translation: BAB26870.1.
AK017616 mRNA. Translation: BAB30841.1.
AK017796 mRNA. No translation available.
BC079855 mRNA. Translation: AAH79855.1.
CCDSiCCDS27553.1. [P57776-3]
CCDS27554.1. [P57776-1]
CCDS70638.1. [P57776-2]
RefSeqiNP_001272358.1. NM_001285429.1.
NP_001272359.1. NM_001285430.1.
NP_001272360.1. NM_001285431.1.
NP_001272361.1. NM_001285432.1.
NP_001272362.1. NM_001285433.1.
NP_001272363.1. NM_001285434.1.
NP_075729.2. NM_023240.3.
NP_083939.1. NM_029663.2.
UniGeneiMm.258927.

Genome annotation databases

GeneIDi66656.
KEGGimmu:66656.
UCSCiuc007whj.2. mouse. [P57776-3]
uc007whm.2. mouse. [P57776-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF304351 mRNA. Translation: AAG17466.1.
AK010308 mRNA. No translation available.
AK010347 mRNA. Translation: BAB26870.1.
AK017616 mRNA. Translation: BAB30841.1.
AK017796 mRNA. No translation available.
BC079855 mRNA. Translation: AAH79855.1.
CCDSiCCDS27553.1. [P57776-3]
CCDS27554.1. [P57776-1]
CCDS70638.1. [P57776-2]
RefSeqiNP_001272358.1. NM_001285429.1.
NP_001272359.1. NM_001285430.1.
NP_001272360.1. NM_001285431.1.
NP_001272361.1. NM_001285432.1.
NP_001272362.1. NM_001285433.1.
NP_001272363.1. NM_001285434.1.
NP_075729.2. NM_023240.3.
NP_083939.1. NM_029663.2.
UniGeneiMm.258927.

3D structure databases

ProteinModelPortaliP57776.
SMRiP57776. Positions 153-281.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211625. 2 interactions.
IntActiP57776. 6 interactions.
MINTiMINT-1856784.
STRINGi10090.ENSMUSP00000087110.

PTM databases

iPTMnetiP57776.
PhosphoSiteiP57776.
SwissPalmiP57776.

2D gel databases

REPRODUCTION-2DPAGEP57776.

Proteomic databases

EPDiP57776.
MaxQBiP57776.
PaxDbiP57776.
PRIDEiP57776.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi66656.
KEGGimmu:66656.
UCSCiuc007whj.2. mouse. [P57776-3]
uc007whm.2. mouse. [P57776-2]

Organism-specific databases

CTDi1936.
MGIiMGI:1913906. Eef1d.

Phylogenomic databases

eggNOGiKOG1668. Eukaryota.
COG2092. LUCA.
HOGENOMiHOG000207272.
HOVERGENiHBG000787.
InParanoidiP57776.
KOiK15410.
TreeFamiTF313134.

Miscellaneous databases

ChiTaRSiEef1d. mouse.
NextBioi322289.
PROiP57776.
SOURCEiSearch...

Gene expression databases

BgeeiP57776.

Family and domain databases

Gene3Di3.30.70.60. 1 hit.
InterProiIPR018940. EF-1_beta_acid_region_euk.
IPR014717. Transl_elong_EF1B/ribosomal_S6.
IPR001326. Transl_elong_EF1B_B/D_CS.
IPR014038. Transl_elong_fac_EF1B_bsu/dsu.
[Graphical view]
PfamiPF10587. EF-1_beta_acid. 1 hit.
PF00736. EF1_GNE. 1 hit.
[Graphical view]
SMARTiSM01182. EF-1_beta_acid. 1 hit.
SM00888. EF1_GNE. 1 hit.
[Graphical view]
SUPFAMiSSF54984. SSF54984. 1 hit.
PROSITEiPS00824. EF1BD_1. 1 hit.
PS00825. EF1BD_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mus musculus eukaryotic translation elongation factor 1 delta mRNA."
    Joseph P., Whong W.-Z., Ong T.-M.
    Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: BALB/cJ.
  2. "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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Embryo and Embryonic stem cell.
  3. "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] (ISOFORM 3).
    Strain: C57BL/6J.
    Tissue: Brain.
  4. Bienvenut W.V.
    Submitted (JUL-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-10, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Liver.
  5. "A differential phosphoproteomic analysis of retinoic acid-treated P19 cells."
    Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.
    J. Proteome Res. 6:3174-3186(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-147 AND SER-162, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Teratocarcinoma.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-147 AND SER-162, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
    Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
    J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133 AND SER-162, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133; THR-147 AND SER-162, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  11. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-117, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiEF1D_MOUSE
AccessioniPrimary (citable) accession number: P57776
Secondary accession number(s): Q68FG5
, Q9CWW2, Q9CWY1, Q9CYD4, Q9CYJ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 133 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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

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 one 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.