Q5VTE0 (EF1A3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Putative elongation factor 1-alpha-like 3
Short name=EF-1-alpha-like 3

Alternative name(s):
Eukaryotic elongation factor 1 A-like 3
Short name=eEF1A-like 3
Eukaryotic translation elongation factor 1 alpha-1 pseudogene 5

Gene names

Name:	EEF1A1P5
Synonyms:	EEF1AL3

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	462 AA.
Sequence status	Complete.
Protein existence	Uncertain

General annotation (Comments)

Function	This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the GTP-binding elongation factor family. EF-Tu/EF-1A subfamily.
Caution	Could be the product of a pseudogene.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	GTP-binding Nucleotide-binding
Molecular function	Elongation factor
PTM	Methylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	GTP catabolic process Inferred from electronic annotation. Source: GOC
Cellular_component	cytoplasm 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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 462	462	Putative elongation factor 1-alpha-like 3		PRO_0000340262
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	55	1	N6,N6-dimethyllysine Ref.2 Ref.3
	Modified residue	165	1	N6,N6,N6-trimethyllysine; alternate Ref.2 Ref.3
	Modified residue	165	1	N6,N6-dimethyllysine; alternate Ref.2 Ref.3
	Modified residue	165	1	N6-methyllysine; alternate Ref.2 Ref.3
	Modified residue	301	1	5-glutamyl glycerylphosphorylethanolamine By similarity
	Modified residue	374	1	5-glutamyl glycerylphosphorylethanolamine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5VTE0 [UniParc]. Last modified December 7, 2004. Version 1. Checksum: 7E53152607CE1E68	FASTA	462	50,185
	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 KVKNVSVKDV RRGNVAGDSK NDPPMEAAGF TAQVIILNHP GQISAGYAPV 370 380 390 400 410 420 LDCHMAHIAC KFAELKEKID RRSGKKLEDG PKFLKSGDAA IVDMVPGKPM CVESFSDYPP 430 440 450 460 LGRFAVRDMR QTVAVGVIKA VDKKAAGAGK VTKSAQKAQK AK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 6-30; 52-62; 85-96; 135-166; 173-179; 248-290 AND 431-439, METHYLATION AT LYS-55 AND LYS-165, MASS SPECTROMETRY. Tissue: Colon carcinoma and Ovarian carcinoma.
[3]	Bienvenut W.V., Waridel P., Quadroni M. Submitted (MAR-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 6-30; 52-62; 85-96; 101-129; 135-179; 220-244; 248-290; 396-423 AND 431-439, METHYLATION AT LYS-55 AND LYS-165, MASS SPECTROMETRY. Tissue: Cervix carcinoma and Embryonic kidney.
[4]	"Full-length cDNA libraries and normalization." Li W.B., Gruber C., Jessee J., Polayes D. Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 258-462.
[5]	"Assignment of human elongation factor 1alpha genes: EEF1A maps to chromosome 6q14 and EEF1A2 to 20q13.3." Lund A., Knudsen S.M., Vissing H., Clark B., Tommerup N. Genomics 36:359-361(1996) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL593851 Genomic DNA. No translation available. CR595753 mRNA. No translation available. CR609311 mRNA. No translation available.
IPI	IPI00472724.
3D structure databases
HSSP	HSSP built from PDB template 1F60 based on UniProtKB P02994.
ProteinModelPortal	Q5VTE0.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q5VTE0. 14 interactions.
Polymorphism databases
DMDM	74746925.
Proteomic databases
PRIDE	Q5VTE0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Organism-specific databases
GeneCards	GC09P135910.
HGNC	HGNC:3200. EEF1A1P5.
neXtProt	NX_Q5VTE0.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	HBG000179.
InParanoid	Q5VTE0.
PhylomeDB	Q5VTE0.
Gene expression databases
Genevestigator	Q5VTE0.
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...

Entry information

Entry name

EF1A3_HUMAN

Accession

Primary (citable) accession number: Q5VTE0

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 10, 2008
Last sequence update:	December 7, 2004
Last modified:	May 1, 2013
This is version 63 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.