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Protein

Elongation factor 1-gamma

Gene

Eef1g

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Probably plays a role in anchoring the complex to other cellular components.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Elongation factor

Keywords - Biological processi

Protein biosynthesis

Enzyme and pathway databases

ReactomeiR-MMU-156842. Eukaryotic Translation Elongation.

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation factor 1-gamma
Short name:
EF-1-gamma
Alternative name(s):
eEF-1B gamma
Gene namesi
Name:Eef1g
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:1914410. Eef1g.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 437436Elongation factor 1-gammaPRO_0000208814Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei147 – 1471N6-acetyllysineCombined sources
Modified residuei212 – 2121N6-acetyllysineCombined sources
Cross-linki253 – 253Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Modified residuei401 – 4011N6-acetyllysineCombined sources
Modified residuei434 – 4341N6-acetyllysine; alternateCombined sources
Modified residuei434 – 4341N6-malonyllysine; alternateBy similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

EPDiQ9D8N0.
MaxQBiQ9D8N0.
PaxDbiQ9D8N0.
PRIDEiQ9D8N0.

2D gel databases

REPRODUCTION-2DPAGEQ9D8N0.

PTM databases

iPTMnetiQ9D8N0.
PhosphoSiteiQ9D8N0.
SwissPalmiQ9D8N0.

Expressioni

Gene expression databases

BgeeiQ9D8N0.
CleanExiMM_EEF1G.
ExpressionAtlasiQ9D8N0. baseline and differential.
GenevisibleiQ9D8N0. MM.

Interactioni

Subunit structurei

EF-1 is composed of four subunits: alpha, beta, delta, and gamma.By similarity

Protein-protein interaction databases

BioGridi211986. 5 interactions.
DIPiDIP-32124N.
IntActiQ9D8N0. 8 interactions.
MINTiMINT-4094049.
STRINGi10090.ENSMUSP00000093955.

Structurei

3D structure databases

ProteinModelPortaliQ9D8N0.
SMRiQ9D8N0. Positions 1-205, 276-437.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 8786GST N-terminalAdd
BLAST
Domaini88 – 216129GST C-terminalAdd
BLAST
Domaini276 – 437162EF-1-gamma C-terminalPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 EF-1-gamma C-terminal domain.PROSITE-ProRule annotation
Contains 1 GST C-terminal domain.Curated
Contains 1 GST N-terminal domain.Curated

Phylogenomic databases

eggNOGiKOG0867. Eukaryota.
KOG1627. Eukaryota.
COG0625. LUCA.
GeneTreeiENSGT00390000007552.
HOGENOMiHOG000201196.
HOVERGENiHBG051444.
InParanoidiQ9D8N0.
KOiK03233.
OMAiDGWSLWF.
OrthoDBiEOG72G177.
PhylomeDBiQ9D8N0.
TreeFamiTF314343.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.30.70.1010. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
IPR001662. Transl_elong_EF1_G_con.
[Graphical view]
PfamiPF00647. EF1G. 1 hit.
PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
SMARTiSM01183. EF1G. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
SSF89942. SSF89942. 1 hit.
PROSITEiPS50040. EF1G_C. 1 hit.
PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9D8N0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAGTLYTYP ENWRAFKALI AAQYSGAQVR VLSAPPHFHF GQTNRTPEFL
60 70 80 90 100
RKFPAGKVPA FEGDDGFCVF ESNAIAYYVS NEELRGSTPE AAAQVVQWVS
110 120 130 140 150
FADSDIVPPA STWVFPTLGI MHHNKQATEN AKEEVKRILG LLDTHLKTRT
160 170 180 190 200
FLVGERVTLA DITVVCTLLW LYKQVLEPSF RQAFPNTNRW FLTCINQPQF
210 220 230 240 250
RAILGEVKLC EKMAQFDAKK FAESQPKKDT PRKEKGSREE KQKPQAERKE
260 270 280 290 300
EKKAAAPAPE EEMDECEQAL AAEPKAKDPF AHLPKSTFVL DEFKRKYSNE
310 320 330 340 350
DTLSVALPYF WEHFDKDGWS LWYAEYRFPE ELTQTFMSCN LITGMFQRLD
360 370 380 390 400
KLRKNAFASV ILFGTNNSSS ISGVWVFRGQ ELAFPLSPDW QVDYESYTWR
410 420 430
KLDPGSEETQ TLVREYFSWE GTFQHVGKAV NQGKIFK
Length:437
Mass (Da):50,061
Last modified:January 23, 2007 - v3
Checksum:i403A9C0E95E27454
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41G → E in BAB29238 (PubMed:16141072).Curated
Sequence conflicti173 – 1731K → R in AAL23895 (Ref. 1) Curated
Sequence conflicti227 – 2271K → N in BAB27948 (PubMed:16141072).Curated
Sequence conflicti340 – 3401N → T in AAL23895 (Ref. 1) Curated
Sequence conflicti413 – 4131V → G in AAL23895 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF321126 mRNA. Translation: AAL23895.1.
AK007869 mRNA. Translation: BAB25320.1.
AK011951 mRNA. No translation available.
AK011973 mRNA. Translation: BAB27948.1.
AK014277 mRNA. Translation: BAB29238.3.
AK050636 mRNA. Translation: BAC34356.1.
AK081859 mRNA. Translation: BAC38351.1.
BC083071 mRNA. Translation: AAH83071.1.
CCDSiCCDS29563.1.
RefSeqiNP_080283.3. NM_026007.4.
UniGeneiMm.247762.
Mm.379129.

Genome annotation databases

EnsembliENSMUST00000052248; ENSMUSP00000093955; ENSMUSG00000071644.
GeneIDi67160.
KEGGimmu:67160.
UCSCiuc008goi.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF321126 mRNA. Translation: AAL23895.1.
AK007869 mRNA. Translation: BAB25320.1.
AK011951 mRNA. No translation available.
AK011973 mRNA. Translation: BAB27948.1.
AK014277 mRNA. Translation: BAB29238.3.
AK050636 mRNA. Translation: BAC34356.1.
AK081859 mRNA. Translation: BAC38351.1.
BC083071 mRNA. Translation: AAH83071.1.
CCDSiCCDS29563.1.
RefSeqiNP_080283.3. NM_026007.4.
UniGeneiMm.247762.
Mm.379129.

3D structure databases

ProteinModelPortaliQ9D8N0.
SMRiQ9D8N0. Positions 1-205, 276-437.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211986. 5 interactions.
DIPiDIP-32124N.
IntActiQ9D8N0. 8 interactions.
MINTiMINT-4094049.
STRINGi10090.ENSMUSP00000093955.

PTM databases

iPTMnetiQ9D8N0.
PhosphoSiteiQ9D8N0.
SwissPalmiQ9D8N0.

2D gel databases

REPRODUCTION-2DPAGEQ9D8N0.

Proteomic databases

EPDiQ9D8N0.
MaxQBiQ9D8N0.
PaxDbiQ9D8N0.
PRIDEiQ9D8N0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000052248; ENSMUSP00000093955; ENSMUSG00000071644.
GeneIDi67160.
KEGGimmu:67160.
UCSCiuc008goi.1. mouse.

Organism-specific databases

CTDi1937.
MGIiMGI:1914410. Eef1g.

Phylogenomic databases

eggNOGiKOG0867. Eukaryota.
KOG1627. Eukaryota.
COG0625. LUCA.
GeneTreeiENSGT00390000007552.
HOGENOMiHOG000201196.
HOVERGENiHBG051444.
InParanoidiQ9D8N0.
KOiK03233.
OMAiDGWSLWF.
OrthoDBiEOG72G177.
PhylomeDBiQ9D8N0.
TreeFamiTF314343.

Enzyme and pathway databases

ReactomeiR-MMU-156842. Eukaryotic Translation Elongation.

Miscellaneous databases

PROiQ9D8N0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D8N0.
CleanExiMM_EEF1G.
ExpressionAtlasiQ9D8N0. baseline and differential.
GenevisibleiQ9D8N0. MM.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.30.70.1010. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
IPR001662. Transl_elong_EF1_G_con.
[Graphical view]
PfamiPF00647. EF1G. 1 hit.
PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
SMARTiSM01183. EF1G. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
SSF89942. SSF89942. 1 hit.
PROSITEiPS50040. EF1G_C. 1 hit.
PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mouse elongation factor-like protein, mRNA sequence."
    Lee Y., Lu X., He W.
    Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/cJ.
    Tissue: Thymus.
  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].
    Strain: C57BL/6J.
    Tissue: Embryo, Embryonic head, Pancreas and Thymus.
  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].
    Strain: C57BL/6J.
    Tissue: Embryo.
  4. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 234-241, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Brain.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  6. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-147; LYS-212; LYS-401 AND LYS-434, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiEF1G_MOUSE
AccessioniPrimary (citable) accession number: Q9D8N0
Secondary accession number(s): Q920C5
, Q9CRT5, Q9CSU3, Q9D004
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 143 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.