P10126 (EF1A1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Elongation factor 1-alpha 1
Short name=EF-1-alpha-1

Alternative name(s):
Elongation factor Tu
Short name=EF-Tu
Eukaryotic elongation factor 1 A-1
Short name=eEF1A-1

Gene names

Name:	Eef1a1
Synonyms:	Eef1a

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	462 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. With PARP1 and TXK, forms a complex that acts as a T helper 1 (Th1) cell-specific transcription factor and binds the promoter of IFN-gamma to directly regulate its transcription, and is thus involved importantly in Th1 cytokine production By similarity.
Subunit structure	Found in a nuclear export complex with XPO5, EEF1A1, Ran and aminoacylated tRNA. Interacts with PARP1, TXK, XPO5 and KARS By similarity. May interact with ERGIC2 By similarity.
Subcellular location	Cytoplasm. Nucleus By similarity.
Post-translational modification	ISGylated. Ref.9 Phosphorylated by TXK. Phosphorylation by PASK increases translation efficiency By similarity.
Sequence similarities	Belongs to the GTP-binding elongation factor family. EF-Tu/EF-1A subfamily.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm Nucleus
Ligand	GTP-binding Nucleotide-binding
Molecular function	Elongation factor
PTM	Acetylation Methylation Phosphoprotein Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular component	cytoplasm Inferred from direct assay. Source: MGI nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct translation elongation factor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TSPY1	Q01534	5	EBI-773865,EBI-1973142	From a different organism.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 462	462	Elongation factor 1-alpha 1		PRO_0000090886
Regions
	Nucleotide binding	14 – 21	8	GTP By similarity
	Nucleotide binding	91 – 95	5	GTP By similarity
	Nucleotide binding	153 – 156	4	GTP By similarity
Amino acid modifications
	Modified residue	29	1	Phosphotyrosine By similarity
	Modified residue	36	1	N6,N6,N6-trimethyllysine By similarity
	Modified residue	41	1	N6-acetyllysine By similarity
	Modified residue	44	1	N6-acetyllysine By similarity
	Modified residue	55	1	N6,N6-dimethyllysine By similarity
	Modified residue	55	1	N6-acetyllysine By similarity
	Modified residue	79	1	N6,N6,N6-trimethyllysine By similarity
	Modified residue	86	1	Phosphotyrosine By similarity
	Modified residue	141	1	Phosphotyrosine By similarity
	Modified residue	146	1	N6-acetyllysine By similarity
	Modified residue	162	1	Phosphotyrosine By similarity
	Modified residue	165	1	N6,N6-dimethyllysine By similarity
	Modified residue	172	1	N6-acetyllysine By similarity
	Modified residue	179	1	N6-acetyllysine By similarity
	Modified residue	255	1	N6-acetyllysine By similarity
	Modified residue	301	1	5-glutamyl glycerylphosphorylethanolamine Ref.8
	Modified residue	318	1	N6,N6,N6-trimethyllysine; alternate By similarity
	Modified residue	318	1	N6-acetyllysine; alternate By similarity
	Modified residue	374	1	5-glutamyl glycerylphosphorylethanolamine Ref.8
	Modified residue	392	1	N6-acetyllysine By similarity
	Modified residue	395	1	N6-acetyllysine By similarity
	Modified residue	432	1	Phosphothreonine; by PASK By similarity
	Modified residue	439	1	N6-acetyllysine By similarity
Experimental info
	Sequence conflict	7	1	H → R in AAA37538. Ref.5
	Sequence conflict	15	1	H → L in AAA37538. Ref.5
	Sequence conflict	23	1	T → S in AAA37538. Ref.5
	Sequence conflict	77 – 78	2	LW → QR in CAA31957. Ref.2
	Sequence conflict	83	1	S → A in CAA27324. Ref.6
	Sequence conflict	91 – 92	2	DA → ES in CAA31957. Ref.2
	Sequence conflict	108	1	Q → R in AAA37538. Ref.5
	Sequence conflict	156	1	D → G in BAC28085. Ref.3
	Sequence conflict	222	1	S → H in AAA50406. Ref.1
	Sequence conflict	224 – 226	3	SGT → VAP in CAA31957. Ref.2
	Sequence conflict	225	1	G → D in AAH04005. Ref.4
	Sequence conflict	239	1	Missing in CAA31957. Ref.2
	Sequence conflict	350	1	P → T in BAC36446. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P10126 [UniParc]. Last modified October 25, 2004. Version 3. Checksum: 71072871DE7405DC	FASTA	462	50,114
	10 20 30 40 50 60 MGKEKTHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAEMG KGSFKYAWVL 70 80 90 100 110 120 DKLKAERERG ITIDISLWKF ETSKYYVTII DAPGHRDFIK NMITGTSQAD CAVLIVAAGV 130 140 150 160 170 180 GEFEAGISKN GQTREHALLA YTLGVKQLIV GVNKMDSTEP PYSQKRYEEI VKEVSTYIKK 190 200 210 220 230 240 IGYNPDTVAF VPISGWNGDN MLEPSANMPW FKGWKVTRKD GSASGTTLLE ALDCILPPTR 250 260 270 280 290 300 PTDKPLRLPL QDVYKIGGIG TVPVGRVETG VLKPGMVVTF APVNVTTEVK SVEMHHEALS 310 320 330 340 350 360 EALPGDNVGF NVKNVSVKDV RRGNVAGDSK NDPPMEAAGF TAQVIILNHP GQISAGYAPV 370 380 390 400 410 420 LDCHTAHIAC KFAELKEKID RRSGKKLEDG PKFLKSGDAA IVDMVPGKPM CVESFSDYPP 430 440 450 460 LGRFAVRDMR QTVAVGVIKA VDKKAAGAGK VTKSAQKAQK AK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and mapping of a gene for protein synthesis initiation factor 4A and its expression during differentiation of murine erythroleukemia cells." Reddy N.S., Roth W.W., Bragg P.W., Wahba A.J. Gene 70:231-243(1988) [PubMed: 3215517] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The complete cDNA sequence of mouse elongation factor 1 alpha (EF 1 alpha) mRNA." Lu X., Werner D. Nucleic Acids Res. 17:442-442(1989) [PubMed: 2911475] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Head, Testis and Thymus.
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Czech II. Tissue: Mammary tumor and Olfactory epithelium.
[5]	"Expression of a gene for mouse eucaryotic elongation factor Tu during murine erythroleukemic cell differentiation." Roth W.W., Bragg P.W., Corrias M.V., Reddy N.S., Dholakia J.N., Wahba A.J. Mol. Cell. Biol. 7:3929-3936(1987) [PubMed: 3481036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-108.
[6]	"Structure of the amino-terminal end of mammalian elongation factor Tu." Rao T.R., Slobin L.I. Nucleic Acids Res. 14:2409-2409(1986) [PubMed: 3960725] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-94.
[7]	Lubec G., Kang S.U., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 6-30; 85-96; 135-146; 155-165; 248-290 AND 431-439, MASS SPECTROMETRY. Strain: C57BL/6 and OF1. Tissue: Brain and Hippocampus.
[8]	"Murine elongation factor 1 alpha (EF-1 alpha) is posttranslationally modified by novel amide-linked ethanolamine-phosphoglycerol moieties. Addition of ethanolamine-phosphoglycerol to specific glutamic acid residues on EF-1 alpha." Whiteheart S.W., Shenbagarmurthi P., Chen L., Cotter R.J., Hart G.W. J. Biol. Chem. 264:14334-14341(1989) [PubMed: 2569467] [Abstract] Cited for: PROTEIN SEQUENCE OF 291-313 AND 372-376, ETHANOLAMINYLATION AT GLU-301 AND GLU-374.
[9]	"Proteomic identification of proteins conjugated to ISG15 in mouse and human cells." Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J., Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E. Biochem. Biophys. Res. Commun. 336:496-506(2005) [PubMed: 16139798] [Abstract] Cited for: ISGYLATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M22432 mRNA. Translation: AAA50406.1. X13661 mRNA. Translation: CAA31957.1. AK032914 mRNA. Translation: BAC28085.1. AK076696 mRNA. Translation: BAC36446.1. AK081725 mRNA. Translation: BAC38311.1. AK083361 mRNA. Translation: BAC38884.1. BC004005 mRNA. Translation: AAH04005.1. BC004067 mRNA. Translation: AAH04067.1. BC005660 mRNA. Translation: AAH05660.1. BC018223 mRNA. Translation: AAH18223.1. BC018485 mRNA. Translation: AAH18485.1. BC083069 mRNA. Translation: AAH83069.1. M17878 Genomic DNA. Translation: AAA37538.1. X03688 mRNA. Translation: CAA27324.1.
IPI	IPI00307837.
PIR	EFMS1. S02114.
RefSeq	NP_034236.2. NM_010106.2.
UniGene	Mm.138471. Mm.335315. Mm.360075. Mm.391071. Mm.485613.
3D structure databases
ProteinModelPortal	P10126.
SMR	P10126. Positions 2-443.
ModBase	Search...
Protein-protein interaction databases
IntAct	P10126. 13 interactions.
STRING	P10126.
PTM databases
PhosphoSite	P10126.
2D gel databases
SWISS-2DPAGE	P10126.
Proteomic databases
PRIDE	P10126.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000042235; ENSMUSP00000042457; ENSMUSG00000037742.
GeneID	13627.
KEGG	mmu:13627.
Organism-specific databases
CTD	1915.
MGI	MGI:1096881. Eef1a1.
Phylogenomic databases
eggNOG	roNOG10172.
HOGENOM	HBG307581.
HOVERGEN	HBG000179.
InParanoid	P10126.
OMA	SIETHHM.
OrthoDB	EOG40K7ZP.
PhylomeDB	P10126.
Gene expression databases
Bgee	P10126.
Genevestigator	P10126.
Family and domain databases
InterPro	IPR000795. ProtSyn_GTP-bd. IPR009001. Transl_elong_EF1A/Init_IF2_C. IPR004539. Transl_elong_EF1A_euk/arc. IPR004161. Transl_elong_EFTu/EF1A_2. IPR004160. Transl_elong_EFTu/EF1A_C. IPR009000. Transl_elong_init/rib_B-barrel. [Graphical view]
KO	K03231.
Pfam	PF00009. GTP_EFTU. 1 hit. PF03144. GTP_EFTU_D2. 1 hit. PF03143. GTP_EFTU_D3. 1 hit. [Graphical view]
PRINTS	PR00315. ELONGATNFCT.
SUPFAM	SSF50465. Elong_init_C. 1 hit. SSF50447. Translat_factor. 1 hit.
TIGRFAMs	TIGR00483. EF-1_alpha. 1 hit.
PROSITE	PS00301. EFACTOR_GTP. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	284304.
SOURCE	Search...

Entry information

Entry name

EF1A1_MOUSE

Accession

Primary (citable) accession number: P10126
Secondary accession number(s): Q61511 , Q6ZWN2, Q8BMB8, Q8BVS8, Q99KU5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	October 25, 2004
Last modified:	January 25, 2012
This is version 135 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program