P68104 (EF1A1_HUMAN) 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
Leukocyte receptor cluster member 7

Gene names

Name:	EEF1A1
Synonyms:	EEF1A, EF1A, LENG7

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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. Ref.8
Subunit structure	Found in a nuclear export complex with XPO5, EEF1A1, Ran and aminoacylated tRNA. Interacts with PARP1, TXK, XPO5 and KARS. May interact with ERGIC2. Ref.8 Ref.12 Ref.13 Ref.20 Ref.21
Subcellular location	Cytoplasm. Nucleus Ref.8.
Tissue specificity	Brain, placenta, lung, liver, kidney, pancreas but barely detectable in heart and skeletal muscle.
Post-translational modification	ISGylated. Ref.14 Phosphorylated by TXK. Phosphorylation by PASK increases translation efficiency. Ref.8 Ref.15 Ref.17 Ref.18 Ref.19
Sequence similarities	Belongs to the GTP-binding elongation factor family. EF-Tu/EF-1A subfamily.
Sequence caution	The sequence AAA52367.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Protein biosynthesis Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Ligand	GTP-binding Nucleotide-binding
Molecular function	Elongation factor
PTM	Acetylation Methylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Traceable author statement. Source: Reactome eukaryotic translation elongation factor 1 complex Traceable author statement Ref.2. Source: UniProtKB nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	GTP binding Traceable author statement Ref.1. Source: UniProtKB GTPase activity Inferred from electronic annotation. Source: InterPro protein kinase binding Inferred from physical interaction Ref.18. Source: UniProtKB translation elongation factor activity Traceable author statement Ref.18. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BBS1	Q8NFJ9	3	EBI-352162,EBI-1805484
MDM2	Q00987	6	EBI-352162,EBI-389668
SPHK1	Q9NYA1	2	EBI-352162,EBI-985303
ZBTB16	Q05516	4	EBI-352162,EBI-711925

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_0000090885

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 Ref.15 Ref.17

Modified residue

36

1

N6,N6,N6-trimethyllysine By similarity

Modified residue

41

1

N6-acetyllysine Ref.22

Modified residue

44

1

N6-acetyllysine Ref.22

Modified residue

55

1

N6,N6-dimethyllysine Ref.7

Modified residue

55

1

N6-acetyllysine Ref.22

Modified residue

79

1

N6,N6,N6-trimethyllysine By similarity

Modified residue

86

1

Phosphotyrosine Ref.17

Modified residue

141

1

Phosphotyrosine Ref.17

Modified residue

146

1

N6-acetyllysine Ref.22

Modified residue

162

1

Phosphotyrosine Ref.19

Modified residue

165

1

N6,N6-dimethyllysine Ref.7

Modified residue

172

1

N6-acetyllysine Ref.22

Modified residue

179

1

N6-acetyllysine Ref.22

Modified residue

255

1

N6-acetyllysine Ref.22

Modified residue

301

1

5-glutamyl glycerylphosphorylethanolamine

Modified residue

318

1

N6,N6,N6-trimethyllysine; alternate By similarity

Modified residue

318

1

N6-acetyllysine; alternate Ref.16 Ref.22

Modified residue

374

1

5-glutamyl glycerylphosphorylethanolamine

Modified residue

392

1

N6-acetyllysine Ref.22

Modified residue

395

1

N6-acetyllysine Ref.22

Modified residue

432

1

Phosphothreonine; by PASK Ref.18

Modified residue

439

1

N6-acetyllysine Ref.22

Experimental info

Mutagenesis

432

1

T → A: Abolishes phosphorylation by PASK. Ref.18

Sequence conflict

83

1

S → A in CAA27325. Ref.6

Sequence conflict

232

1

L → V in CAA34756. Ref.3

Secondary structure

1

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462

Helix Strand Turn

Details...

Beta strand

7 – 14

8

Helix

20 – 31

12

Turn

34 – 36

3

Helix

37 – 46

10

Turn

47 – 49

3

Helix

51 – 53

3

Helix

56 – 60

5

Helix

61 – 63

3

Turn

64 – 66

3

Beta strand

76 – 81

6

Beta strand

86 – 91

6

Helix

96 – 101

6

Helix

103 – 106

4

Beta strand

110 – 116

7

Helix

124 – 127

4

Helix

132 – 134

3

Helix

136 – 143

8

Beta strand

148 – 152

5

Turn

160 – 162

3

Helix

164 – 166

3

Helix

168 – 178

11

Turn

179 – 181

3

Helix

185 – 187

3

Beta strand

188 – 192

5

Turn

195 – 198

4

Beta strand

199 – 203

5

Beta strand

214 – 218

5

Beta strand

221 – 227

7

Helix

228 – 232

5

Beta strand

243 – 245

3

Beta strand

247 – 256

10

Turn

257 – 259

3

Beta strand

260 – 265

6

Beta strand

277 – 283

7

Beta strand

286 – 293

8

Beta strand

300 – 302

3

Beta strand

309 – 314

6

Turn

317 – 319

3

Beta strand

325 – 328

4

Turn

329 – 331

3

Beta strand

337 – 346

10

Beta strand

352 – 354

3

Beta strand

360 – 363

4

Beta strand

366 – 380

15

Turn

381 – 383

3

Beta strand

392 – 395

4

Beta strand

398 – 408

11

Turn

415 – 417

3

Helix

419 – 422

4

Beta strand

423 – 428

6

Beta strand

431 – 442

12

Sequences

	Sequence		Length	Mass (Da)
	P68104 [UniParc]. Last modified August 13, 1987. Version 1. Checksum: D465615545AF686A	FASTA	462	50,141
	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 GNASGTTLLE 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]	"The primary structure of the alpha subunit of human elongation factor 1. Structural aspects of guanine-nucleotide-binding sites." Brands J.H.G.M., Maassen J.A., van Hemert F.J., Amons R., Moeller W. Eur. J. Biochem. 155:167-171(1986) [PubMed: 3512269] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Isolation and characterization of the human chromosomal gene for polypeptide chain elongation factor-1 alpha." Uetsuki T., Naito A., Nagata S., Kaziro Y. J. Biol. Chem. 264:5791-5798(1989) [PubMed: 2564392] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Retropseudogenes constitute the major part of the human elongation factor 1 alpha gene family." Madsen H.O., Poulsen K., Dahl O., Clark B.F.C., Hjorth J.P. Nucleic Acids Res. 18:1513-1516(1990) [PubMed: 2183196] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[4]	"Postnatal expression of a novel mRNA isoform from the human elongation factor-1a gene." Shimazu T., Koike K. Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]	"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]. Tissue: B-cell, Bone marrow, Cervix, Colon, Hippocampus, Lung, Lymph, Mammary gland, Ovary, Pancreas, Placenta, Testis and Uterus.
[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]	Bienvenut W.V., Zebisch A., Kolch W. Submitted (JAN-2010) to UniProtKB Cited for: PROTEIN SEQUENCE OF 6-30; 52-62; 85-96; 101-129; 135-180; 248-313; 396-423 AND 431-439, METHYLATION AT LYS-55 AND LYS-165, MASS SPECTROMETRY. Tissue: Colon carcinoma and Ovarian carcinoma.
[8]	"Txk, a member of the non-receptor tyrosine kinase of the Tec family, forms a complex with poly(ADP-ribose) polymerase 1 and elongation factor 1alpha and regulates interferon-gamma gene transcription in Th1 cells." Maruyama T., Nara K., Yoshikawa H., Suzuki N. Clin. Exp. Immunol. 147:164-175(2007) [PubMed: 17177976] [Abstract] Cited for: PROTEIN SEQUENCE OF 7-16 AND 85-96, INTERACTION WITH PARP1 AND TXK, PHOSPHORYLATION BY TXK, SUBCELLULAR LOCATION, FUNCTION AS A TRANCRIPTION FACTOR.
[9]	Bienvenut W.V. Submitted (JUN-2005) to UniProtKB Cited for: PROTEIN SEQUENCE OF 38-44; 70-79; 85-96; 135-172; 248-290; 386-392 AND 428-439. Tissue: B-cell lymphoma.
[10]	"Retinol-regulated gene expression in human tracheobronchial epithelial cells. Enhanced expression of elongation factor EF-1 alpha." Ann D.K., Wu M.M.J., Huang T., Carlson D.M., Wu R. J. Biol. Chem. 263:3546-3549(1988) [PubMed: 3346208] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 138-462.
[11]	"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: ETHANOLAMINYLATION AT GLU-301 AND GLU-374.
[12]	"Exp5 exports eEF1A via tRNA from nuclei and synergizes with other transport pathways to confine translation to the cytoplasm." Bohnsack M.T., Regener K., Schwappach B., Saffrich R., Paraskeva E., Hartmann E., Goerlich D. EMBO J. 21:6205-6215(2002) [PubMed: 12426392] [Abstract] Cited for: IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH XPO5; RAN AND TRNA, INTERACTION WITH XPO5.
[13]	"Exportin-5-mediated nuclear export of eukaryotic elongation factor 1A and tRNA." Calado A., Treichel N., Mueller E.-C., Otto A., Kutay U. EMBO J. 21:6216-6224(2002) [PubMed: 12426393] [Abstract] Cited for: IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH XPO5; RAN AND TRNA, INTERACTION WITH XPO5.
[14]	"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.
[15]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-29, MASS SPECTROMETRY.
[16]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-318, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-29; TYR-86 AND TYR-141, MASS SPECTROMETRY. Tissue: Lung carcinoma.
[18]	"Male germ cell expression of the PAS domain kinase PASKIN and its novel target eukaryotic translation elongation factor eEF1A1." Eckhardt K., Troger J., Reissmann J., Katschinski D.M., Wagner K.F., Stengel P., Paasch U., Hunziker P., Borter E., Barth S., Schlafli P., Spielmann P., Stiehl D.P., Camenisch G., Wenger R.H. Cell. Physiol. Biochem. 20:227-240(2007) [PubMed: 17595531] [Abstract] Cited for: PHOSPHORYLATION AT THR-432, MUTAGENESIS OF THR-432.
[19]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-162, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[20]	"Lysyl-tRNA synthetase interacts with EF1alpha, aspartyl-tRNA synthetase and p38 in vitro." Guzzo C.M., Yang D.C.H. Biochem. Biophys. Res. Commun. 365:718-723(2008) [PubMed: 18029264] [Abstract] Cited for: INTERACTION WITH KARS.
[21]	"The possible interaction of CDA14 and protein elongation factor 1alpha." Yang Y.F., Chou M.Y., Fan C.Y., Chen S.F., Lyu P.C., Liu C.C., Tseng T.L. Biochim. Biophys. Acta 1784:312-318(2008) [PubMed: 17980171] [Abstract] Cited for: INTERACTION WITH ERGIC2.
[22]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-41; LYS-44; LYS-55; LYS-146; LYS-172; LYS-179; LYS-255; LYS-318; LYS-392; LYS-395 AND LYS-439, MASS SPECTROMETRY.
[23]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X03558 mRNA. Translation: CAA27245.1.
J04617 Genomic DNA. Translation: AAA52343.1.
X16869 mRNA. Translation: CAA34756.1.
AY043301 mRNA. Translation: AAK95378.1.
BC008587 mRNA. Translation: AAH08587.1.
BC009733 mRNA. Translation: AAH09733.1.
BC009875 mRNA. Translation: AAH09875.1.
BC010735 mRNA. Translation: AAH10735.1.
BC012891 mRNA. Translation: AAH12891.1.
BC014224 mRNA. Translation: AAH14224.1.
BC018150 mRNA. Translation: AAH18150.1.
BC018641 mRNA. Translation: AAH18641.1.
BC021686 mRNA. Translation: AAH21686.1.
BC028674 mRNA. Translation: AAH28674.1.
BC038339 mRNA. Translation: AAH38339.1.
BC057391 mRNA. Translation: AAH57391.1.
BC066893 mRNA. Translation: AAH66893.1.
BC072385 mRNA. Translation: AAH72385.1.
BC082268 mRNA. Translation: AAH82268.1.
X03689 mRNA. Translation: CAA27325.1.
M29548 mRNA. Translation: AAA52367.1. Different initiation.

IPI

IPI00396485.

PIR

EFHU1. B24977.

RefSeq

NP_001393.1. NM_001402.5.

UniGene

Hs.520703.
Hs.535192.
Hs.586423.
Hs.695681.
Hs.713109.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1SYW	model	-	A	2-443	[»]

ProteinModelPortal

P68104.

SMR

P68104. Positions 2-443.

ModBase

Search...

Protein-protein interaction databases

IntAct

P68104. 108 interactions.

MINT

MINT-1180846.

STRING

P68104.

PTM databases

PhosphoSite

P68104.

Polymorphism databases

DMDM

55584035.

2D gel databases

SWISS-2DPAGE

P68104.

OGP

P68104.

UCD-2DPAGE

P68104.

Proteomic databases

PRIDE

P68104.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000309268; ENSP00000339053; ENSG00000156508.
ENST00000316292; ENSP00000339063; ENSG00000156508.
ENST00000331523; ENSP00000330054; ENSG00000156508.

GeneID

1915.

KEGG

hsa:1915.

UCSC

uc003phi.1. human.

Organism-specific databases

CTD

1915.

GeneCards

GC06M074225.

H-InvDB

HIX0006010.
HIX0032108.

HGNC

HGNC:3189. EEF1A1.

MIM

130590. gene.

neXtProt

NX_P68104.

PharmGKB

PA27625.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG14262.

HOGENOM

HBG307581.

HOVERGEN

HBG000179.

InParanoid

P68104.

OMA

SIETHHM.

OrthoDB

EOG40K7ZP.

PhylomeDB

P68104.

Enzyme and pathway databases

Reactome

REACT_17015. Metabolism of proteins.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

P68104.

Bgee

P68104.

CleanEx

HS_EEF1A1.

Genevestigator

P68104.

GermOnline

ENSG00000156508. Homo sapiens.

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

7799.

PMAP-CutDB

P68104.

SOURCE

Search...

Entry information

Entry name

EF1A1_HUMAN

Accession

Primary (citable) accession number: P68104
Secondary accession number(s): P04719, P04720

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	August 13, 1987
Last modified:	January 25, 2012
This is version 103 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.