Reviewed, UniProtKB/Swiss-Prot Q05639 (EF1A2_HUMAN)

Names and origin

Protein names

Recommended name:
    Elongation factor 1-alpha 2
      Short name=EF-1-alpha-2
      Short name=Elongation factor 1 A-2
Alternative name(s):
    eEF1A-2
    Statin S1

Gene names

Name:	EEF1A2
Synonyms:	EEF1AL, STN

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	463 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Subunit structure	Monomer By similarity.
Subcellular location	Nucleus By similarity.
Tissue specificity	Brain, heart, and skeletal muscle.
Sequence similarities	Belongs to the GTP-binding elongation factor family. EF-Tu/EF-1A subfamily.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Nucleus
Ligand	GTP-binding Nucleotide-binding
Molecular function	Elongation factor
PTM	Methylation Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Cellular component	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
EEF1B2	P24534	1	EBI-354943,EBI-354334
EEF1D	P29692	1	EBI-354943,EBI-358607
VARS	P26640	1	EBI-354943,EBI-355765

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 463	463	Elongation factor 1-alpha 2		PRO_0000090891
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
Sites
	Binding site	301	1	Glycerylphosphorylethanolamine (covalent) By similarity
	Binding site	374	1	Glycerylphosphorylethanolamine (covalent) By similarity
Amino acid modifications
	Modified residue	29	1	Phosphotyrosine Ref.7 Ref.8
	Modified residue	55	1	N6,N6,N6-trimethyllysine By similarity
	Modified residue	141	1	Phosphotyrosine Ref.7 Ref.8
	Modified residue	165	1	N6,N6,N6-trimethyllysine By similarity
Experimental info
	Sequence conflict	427	1	R → P in AAA91835. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Q05639-1 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: 31E4E341CEE797EC	FASTA	463	50,470
	10 20 30 40 50 60 MGKEKTHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAEMG KGSFKYAWVL 70 80 90 100 110 120 DKLKAERERG ITIDISLWKF ETTKYYITII DAPGHRDFIK NMITGTSQAD CAVLIVAAGV 130 140 150 160 170 180 GEFEAGISKN GQTREHALLA YTLGVKQLIV GVNKMDSTEP AYSEKRYDEI VKEVSAYIKK 190 200 210 220 230 240 IGYNPATVPF VPISGWHGDN MLEPSPNMPW FKGWKVERKE GNASGVSLLE ALDTILPPTR 250 260 270 280 290 300 PTDKPLRLPL QDVYKIGGIG TVPVGRVETG ILRPGMVVTF APVNITTEVK SVEMHHEALS 310 320 330 340 350 360 EALPGDNVGF NVKNVSVKDI RRGNVCGDSK SDPPQEAAQF TSQVIILNHP GQISAGYSPV 370 380 390 400 410 420 IDCHTAHIAC KFAELKEKID RRSGKKLEDN PKSLKSGDAA IVEMVPGKPM CVESFSQYPP 430 440 450 460 LGRFAVRDMR QTVAVGVIKN VEKKSGGAGK VTKSAQKAQK AGK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Tissue-dependent variation in the expression of elongation factor-1 alpha isoforms: isolation and characterisation of a cDNA encoding a novel variant of human elongation-factor 1 alpha." Knudsen S.M., Frydenberg J., Clark B.F.C., Leffers H. Eur. J. Biochem. 215:549-554(1993) [PubMed: 8354261] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The human elongation factor 1 A-2 gene (EEF1A2): complete sequence and characterization of gene structure and promoter activity." Bischoff C., Kahns S., Lund A., Joergensen H.F., Praestegaard M., Clark B.F.C., Leffers H. Genomics 68:63-70(2000) [PubMed: 10950927] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Human protein factory for converting the transcriptome into an in vitro-expressed proteome." Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B. , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N. Nat. Methods 5:1011-1017(2008) [PubMed: 19054851] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J. Nature 414:865-871(2001) [PubMed: 11780052] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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: Duodenum and Lung.
[6]	"Cloning of human and mouse brain cDNAs coding for S1, the second member of the mammalian elongation factor-1 alpha gene family: analysis of a possible evolutionary pathway." Lee S., Ann D.K., Wang E. Biochem. Biophys. Res. Commun. 203:1371-1377(1994) [PubMed: 7945283] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 29-463. Tissue: Hippocampus.
[7]	"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 AND TYR-141, MASS SPECTROMETRY.
[8]	"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 AND TYR-141, MASS SPECTROMETRY. Tissue: Lung.
[9]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBLGenBankDDBJ

X70940 mRNA. Translation: CAA50280.1.
AF163763 Genomic DNA. Translation: AAF80488.1.
AB451389 mRNA. Translation: BAG70203.1.
AL121829 Genomic DNA. Translation: CAC15522.1.
BC000432 mRNA. Translation: AAH00432.1.
BC110409 mRNA. Translation: AAI10410.1.
L10340 mRNA. Translation: AAA91835.1.

IPI

IPI00014424.

PIR

EFHUA2. S35033.

RefSeq

NP_001949.1.

UniGene

Hs.370895
Hs.433839

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3C5J	X-ray	1.80	C	343-355	[»]

SMR

Q05639. Positions 2-443.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q05639. 20 interactions.

PTM databases

PhosphoSite

Q05639.

Proteomic databases

PeptideAtlas

Q05639.

PRIDE

Q05639.

Genome annotation databases

Ensembl

ENSG00000101210. Homo sapiens. [Contig view]

GeneID

1917.

KEGG

hsa:1917.

NMPDR

fig|9606.3.peg.20674.

Organism-specific databases

GeneCards

GC20M061589.

H-InvDB

HIX0022989.

HGNC

HGNC:3192. EEF1A2.

MIM

602959. gene.

PharmGKB

PA27628.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q05639.

HOVERGEN

Q05639.

OMA

Q05639. EIPQLGR.

Gene expression databases

ArrayExpress

Q05639.

Bgee

Q05639.

CleanEx

HS_EEF1A2.

GermOnline

ENSG00000101210. Homo sapiens.

Family and domain databases

InterPro

IPR000795. ProtSyn_GTP_bd.
IPR004539. Transl_elong_EF1A_euk/arc.
IPR004161. Transl_elong_EFTu/EF1A_2.
IPR004160. Transl_elong_EFTu/EF1A_C.
[Graphical view]

Pfam

PF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
PF03143. GTP_EFTU_D3. 1 hit.
[Graphical view]

PRINTS

PR00315. ELONGATNFCT.

TIGRFAMs

TIGR00483. EF-1_alpha. 1 hit.

PROSITE

PS00301. EFACTOR_GTP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

7803.

SOURCE

Search...

Entry information

Entry name

EF1A2_HUMAN

Accession

Primary (citable) accession number: Q05639
Secondary accession number(s): B5BUF3, P54266, Q0VGC7

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	June 16, 2009
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)