Q05639 (EF1A2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Elongation factor 1-alpha 2
Short name=EF-1-alpha-2

Alternative name(s):
Eukaryotic elongation factor 1 A-2
Short name=eEF1A-2
Statin-S1

Gene names

Name:	EEF1A2
Synonyms:	EEF1AL, STN

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	463 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.
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	Acetylation Methylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	GTP catabolic process Inferred from electronic annotation. Source: GOC negative regulation of apoptotic process Inferred from electronic annotation. Source: Compara response to inorganic substance Inferred from electronic annotation. Source: Compara
Cellular_component	eukaryotic translation elongation factor 1 complex Inferred from electronic annotation. Source: Compara neuronal cell body Inferred from electronic annotation. Source: Compara 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 translation elongation factor activity Inferred from electronic annotation. Source: UniProtKB-KW translation factor activity, nucleic acid binding Non-traceable author statement PubMed 8812466. Source: ProtInc
Complete GO annotation...

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
Amino acid modifications
	Modified residue	29	1	Phosphotyrosine By similarity
	Modified residue	55	1	N6,N6,N6-trimethyllysine By similarity
	Modified residue	141	1	Phosphotyrosine By similarity
	Modified residue	165	1	N6,N6,N6-trimethyllysine By similarity
	Modified residue	179	1	N6-acetyllysine Ref.8
	Modified residue	301	1	5-glutamyl glycerylphosphorylethanolamine By similarity
	Modified residue	374	1	5-glutamyl glycerylphosphorylethanolamine By similarity
	Modified residue	439	1	N6-acetyllysine Ref.8
Experimental info
	Sequence conflict	427	1	R → P in AAA91835. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	Q05639 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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]. Tissue: Duodenum and Lung.
[7]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 29-463. Tissue: Hippocampus.
[8]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-179 AND LYS-439, MASS SPECTROMETRY.
[9]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]	"The structure of HLA-DR52c: comparison to other HLA-DRB3 alleles." Dai S., Crawford F., Marrack P., Kappler J.W. Proc. Natl. Acad. Sci. U.S.A. 105:11893-11897(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 343-355 IN COMPLEX WITH HLA-DRA/HLA-DRB3 HETERODIMER.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X70940 mRNA. Translation: CAA50280.1.
AF163763 Genomic DNA. Translation: AAF80488.1.
AB451389 mRNA. Translation: BAG70203.1.
AL121829 Genomic DNA. Translation: CAC15522.1.
CH471077 Genomic DNA. Translation: EAW75260.1.
BC000432 mRNA. Translation: AAH00432.1.
BC110409 mRNA. Translation: AAI10410.1.
L10340 mRNA. Translation: AAA91835.1.

IPI

IPI00014424.

PIR

EFHUA2. S35033.

RefSeq

NP_001949.1. NM_001958.3.

UniGene

Hs.433839.

3D structure databases

PDBe
RCSB PDB
PDBj

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

ProteinModelPortal

Q05639.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q05639. 20 interactions.

MINT

MINT-1141378.

STRING

9606.ENSP00000217182.

PTM databases

PhosphoSite

Q05639.

Polymorphism databases

DMDM

544231.

Proteomic databases

PaxDb

Q05639.

PeptideAtlas

Q05639.

PRIDE

Q05639.

Protocols and materials databases

DNASU

1917.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000217182; ENSP00000217182; ENSG00000101210.
ENST00000298049; ENSP00000298049; ENSG00000101210.

GeneID

1917.

KEGG

hsa:1917.

UCSC

uc002yfe.1. human.

Organism-specific databases

CTD

1917.

GeneCards

GC20M062119.

HGNC

HGNC:3192. EEF1A2.

HPA

CAB034019.

MIM

602959. gene.

neXtProt

NX_Q05639.

PharmGKB

PA36219.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5256.

HOGENOM

HOG000229291.

HOVERGEN

HBG000179.

InParanoid

Q05639.

KO

K03231.

OMA

PVFHCHT.

OrthoDB

EOG40K7ZP.

PhylomeDB

Q05639.

Gene expression databases

Bgee

Q05639.

CleanEx

HS_EEF1A2.

Genevestigator

Q05639.

GermOnline

ENSG00000101210. Homo sapiens.

Family and domain databases

InterPro

IPR000795. EF_GTP-bd_dom.
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]

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

BindingDB

Q05639.

ChEMBL

CHEMBL1795122.

EvolutionaryTrace

Q05639.

GenomeRNAi

1917.

NextBio

7803.

SOURCE

Search...

Entry information

Entry name

EF1A2_HUMAN

Accession

Primary (citable) accession number: Q05639
Secondary accession number(s): B5BUF3 , E1P5J1, P54266, Q0VGC7

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	May 1, 2013
This is version 140 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.