Eef1a1

Functionⁱ

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).By similarity

Regions

Feature key	Position(s)	Length	Description
Nucleotide bindingⁱ	14 – 21	8	GTPBy similarity
Nucleotide bindingⁱ	91 – 95	5	GTPBy similarity
Nucleotide bindingⁱ	153 – 156	4	GTPBy similarity

Names & Taxonomyⁱ

Protein namesⁱ	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 namesⁱ	Name:Eef1a1 Synonyms:Eef1a
Organismⁱ	Mus musculus (Mouse)
Taxonomic identifierⁱ	10090 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesⁱ	UP000000589 Componentⁱ: Chromosome 9

Organism-specific databases

MGIⁱ	MGI:1096881. Eef1a1.

Subcellular locationⁱ

Cytoplasm
1 Publication
Manual assertion based on experiment inⁱ
- Ref.11
  "The interaction between interferon-induced protein with tetratricopeptide repeats-1 and eukaryotic elongation factor-1A."
  Li H.T., Su Y.P., Cheng T.M., Xu J.M., Liao J., Chen J.C., Ji C.Y., Ai G.P., Wang J.P.
  Mol. Cell. Biochem. 337:101-110(2010) [PubMed] [Europe PMC] [Abstract]
  Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH IFIT1, SUBCELLULAR LOCATION.
Nucleus By similarity
Nucleus › nucleolus By similarity

Note:

Colocalizes with DLC1 at actin-rich regions in the cell periphery. Translocates together with ZPR1 from the cytoplasm to the nucleus and nucleolus after treatment with mitogens (By similarity).By similarity

GO - Cellular componentⁱ

cortical actin cytoskeleton Source: MGI
cytoplasm
Source: UniProtKB
Inferred from direct assayⁱ
- 19856081
cytosol Source: MGI
extracellular exosome Source: MGI
extracellular space Source: MGI
membrane Source: MGI
myelin sheath
Source: UniProtKB
Inferred from direct assayⁱ
- 17634366
nucleolus Source: UniProtKB
nucleus Source: UniProtKB
plasma membrane
Source: MGI
Inferred from direct assayⁱ
- 21689717
ruffle membrane Source: MGI

Complete GO annotation...

Keywords - Cellular componentⁱ

Cytoplasm, Nucleus

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Chainⁱ	1 – 462	462	Elongation factor 1-alpha 1		PRO_0000090886	Add BLAST

Amino acid modifications

Feature key	Position(s)	Length	Description
Modified residueⁱ	36 – 36	1	N6,N6,N6-trimethyllysineBy similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:P68105 (EF1A1_RABIT)
Modified residueⁱ	55 – 55	1	N6,N6-dimethyllysineBy similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:P68104 (EF1A1_HUMAN)
Modified residueⁱ	79 – 79	1	N6,N6,N6-trimethyllysineBy similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:P68105 (EF1A1_RABIT)
Modified residueⁱ	165 – 165	1	N6,N6-dimethyllysine; alternateBy similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:P68104 (EF1A1_HUMAN)
Modified residueⁱ	165 – 165	1	N6-acetyllysine; alternateCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.12 "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways." Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y. Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-165; LYS-172; LYS-273; LYS-392 AND LYS-439, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-392, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	172 – 172	1	N6-acetyllysineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.12 "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways." Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y. Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-165; LYS-172; LYS-273; LYS-392 AND LYS-439, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-392, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	273 – 273	1	N6-acetyllysineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.12 "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways." Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y. Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-165; LYS-172; LYS-273; LYS-392 AND LYS-439, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-392, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	300 – 300	1	Phosphoserine; by TGFBR1By similarity
Modified residueⁱ	301 – 301	1	5-glutamyl glycerylphosphorylethanolamine1 Publication Manual assertion based on experiment inⁱ Ref.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] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 291-313 AND 372-376, ETHANOLAMINYLATION AT GLU-301 AND GLU-374.
Modified residueⁱ	318 – 318	1	N6,N6,N6-trimethyllysineBy similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:P68105 (EF1A1_RABIT)
Modified residueⁱ	374 – 374	1	5-glutamyl glycerylphosphorylethanolamine1 Publication Manual assertion based on experiment inⁱ Ref.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] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 291-313 AND 372-376, ETHANOLAMINYLATION AT GLU-301 AND GLU-374.
Modified residueⁱ	392 – 392	1	N6-acetyllysine; alternateCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.12 "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways." Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y. Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-165; LYS-172; LYS-273; LYS-392 AND LYS-439, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-392, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	392 – 392	1	N6-succinyllysine; alternateCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.12 "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways." Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y. Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-165; LYS-172; LYS-273; LYS-392 AND LYS-439, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-392, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	432 – 432	1	Phosphothreonine; by PASKBy similarity
Modified residueⁱ	439 – 439	1	N6-acetyllysineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.12 "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways." Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y. Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-165; LYS-172; LYS-273; LYS-392 AND LYS-439, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-392, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Post-translational modificationⁱ

ISGylated.1 Publication

Phosphorylated by TXK. Phosphorylation by PASK increases translation efficiency (By similarity).By similarity

Keywords - PTMⁱ

Acetylation, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDⁱ	P10126.
PaxDbⁱ	P10126.
PeptideAtlasⁱ	P10126.
PRIDEⁱ	P10126.
TopDownProteomicsⁱ	P10126.

2D gel databases

SWISS-2DPAGE	P10126.

SWISS-2DPAGE

P10126.

PTM databases

iPTMnetⁱ	P10126.
PhosphoSiteⁱ	P10126.
SwissPalmⁱ	P10126.

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSMUSG00000037742.
ExpressionAtlasⁱ	P10126. baseline and differential.
Genevisibleⁱ	P10126. MM.

Interactionⁱ

Subunit structureⁱ

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). Interacts with DLC1, facilitating distribution to the membrane periphery and ruffles upon growth factor stimulation (By similarity). Interacts with ZPR1; the interaction occurs in a epidermal growth factor (EGF)-dependent manner (By similarity). Interacts with IFIT1 (via TPR repeats 4-7).By similarity1 Publication

Binary interactionsⁱ

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

With

Entry

#Exp.

IntAct

Notes

TSPY1

Q01534

5

EBI-773865,EBI-1973142

From a different organism.

GO - Molecular functionⁱ

protein kinase binding Source: MGI

Protein-protein interaction databases

BioGridⁱ	199385. 50 interactions.
DIPⁱ	DIP-46609N.
IntActⁱ	P10126. 62 interactions.
MINTⁱ	MINT-1862449.
STRINGⁱ	10090.ENSMUSP00000042457.

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	P10126.
SMRⁱ	P10126. Positions 4-455.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Domainⁱ	5 – 242	238	tr-type G			Add BLAST

Region

Feature key	Position(s)	Length	Description
Regionⁱ	14 – 21	8	G1By similarity
Regionⁱ	70 – 74	5	G2By similarity
Regionⁱ	91 – 94	4	G3By similarity
Regionⁱ	153 – 156	4	G4By similarity
Regionⁱ	194 – 196	3	G5By similarity

Sequence similaritiesⁱ

Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily.Curated

Contains 1 tr-type G (guanine nucleotide-binding) domain.Curated

Phylogenomic databases

eggNOGⁱ	KOG0052. Eukaryota. COG5256. LUCA.
HOGENOMⁱ	HOG000229291.
HOVERGENⁱ	HBG000179.
InParanoidⁱ	P10126.
KOⁱ	K03231.
OMAⁱ	FEQISHE.
OrthoDBⁱ	EOG091G05LW.
PhylomeDBⁱ	P10126.
TreeFamⁱ	TF300304.

Family and domain databases

Gene3Dⁱ	3.40.50.300. 1 hit.
HAMAPⁱ	MF_00118_A. EF_Tu_A. 1 hit.
InterProⁱ	IPR004161. EFTu-like_2. IPR031157. G_TR_CS. IPR027417. P-loop_NTPase. IPR000795. TF_GTP-bd_dom. IPR009000. Transl_B-barrel. IPR009001. Transl_elong_EF1A/Init_IF2_C. IPR004539. Transl_elong_EF1A_euk/arc. IPR004160. Transl_elong_EFTu/EF1A_C. [Graphical view]
Pfamⁱ	PF03144. GTP_EFTU_D2. 1 hit. PF03143. GTP_EFTU_D3. 1 hit. [Graphical view]
PRINTSⁱ	PR00315. ELONGATNFCT.
SUPFAMⁱ	SSF50447. SSF50447. 1 hit. SSF50465. SSF50465. 1 hit. SSF52540. SSF52540. 1 hit.
TIGRFAMsⁱ	TIGR00483. EF-1_alpha. 1 hit.
PROSITEⁱ	PS00301. G_TR_1. 1 hit. PS51722. G_TR_2. 1 hit. [Graphical view]

Sequenceⁱ

Sequence statusⁱ: Complete.

P10126-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MGKEKTHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAEMG 
        60         70         80         90        100
KGSFKYAWVL DKLKAERERG ITIDISLWKF ETSKYYVTII DAPGHRDFIK 
       110        120        130        140        150
NMITGTSQAD CAVLIVAAGV GEFEAGISKN GQTREHALLA YTLGVKQLIV 
       160        170        180        190        200
GVNKMDSTEP PYSQKRYEEI VKEVSTYIKK IGYNPDTVAF VPISGWNGDN 
       210        220        230        240        250
MLEPSANMPW FKGWKVTRKD GSASGTTLLE ALDCILPPTR PTDKPLRLPL 
       260        270        280        290        300
QDVYKIGGIG TVPVGRVETG VLKPGMVVTF APVNVTTEVK SVEMHHEALS 
       310        320        330        340        350
EALPGDNVGF NVKNVSVKDV RRGNVAGDSK NDPPMEAAGF TAQVIILNHP 
       360        370        380        390        400
GQISAGYAPV LDCHTAHIAC KFAELKEKID RRSGKKLEDG PKFLKSGDAA 
       410        420        430        440        450
IVDMVPGKPM CVESFSDYPP LGRFAVRDMR QTVAVGVIKA VDKKAAGAGK 
       460 
VTKSAQKAQK AK

Length:462

Mass (Da):50,114

Last modified:October 25, 2004 - v3

Checksum:ⁱ71072871DE7405DC

GO

Experimental Info

Feature key	Position(s)	Length	Description
Sequence conflictⁱ	7 – 7	1	H → R in AAA37538 (PubMed:3481036).Curated
Sequence conflictⁱ	15 – 15	1	H → L in AAA37538 (PubMed:3481036).Curated
Sequence conflictⁱ	23 – 23	1	T → S in AAA37538 (PubMed:3481036).Curated
Sequence conflictⁱ	77 – 78	2	LW → QR in CAA31957 (PubMed:2911475).Curated
Sequence conflictⁱ	83 – 83	1	S → A in CAA27324 (PubMed:3960725).Curated
Sequence conflictⁱ	91 – 92	2	DA → ES in CAA31957 (PubMed:2911475).Curated
Sequence conflictⁱ	108 – 108	1	Q → R in AAA37538 (PubMed:3481036).Curated
Sequence conflictⁱ	156 – 156	1	D → G in BAC28085 (PubMed:16141072).Curated
Sequence conflictⁱ	222 – 222	1	S → H in AAA50406 (PubMed:3215517).Curated
Sequence conflictⁱ	224 – 226	3	SGT → VAP in CAA31957 (PubMed:2911475).Curated
Sequence conflictⁱ	225 – 225	1	G → D in AAH04005 (PubMed:15489334).Curated
Sequence conflictⁱ	239 – 239	1	Missing in CAA31957 (PubMed:2911475).Curated
Sequence conflictⁱ	350 – 350	1	P → T in BAC36446 (PubMed:16141072).Curated

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	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.
CCDSⁱ	CCDS40703.1.
PIRⁱ	S02114. EFMS1.
RefSeqⁱ	NP_034236.2. NM_010106.2.
UniGeneⁱ	Mm.138471. Mm.335315. Mm.360075. Mm.391071. Mm.485669. Mm.491424.

Genome annotation databases

Ensemblⁱ	ENSMUST00000042235; ENSMUSP00000042457; ENSMUSG00000037742.
GeneIDⁱ	13627.
KEGGⁱ	mmu:13627.
UCSCⁱ	uc009qun.1. mouse.

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	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.
CCDSⁱ	CCDS40703.1.
PIRⁱ	S02114. EFMS1.
RefSeqⁱ	NP_034236.2. NM_010106.2.
UniGeneⁱ	Mm.138471. Mm.335315. Mm.360075. Mm.391071. Mm.485669. Mm.491424.

3D structure databases

ProteinModelPortalⁱ	P10126.
SMRⁱ	P10126. Positions 4-455.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	199385. 50 interactions.
DIPⁱ	DIP-46609N.
IntActⁱ	P10126. 62 interactions.
MINTⁱ	MINT-1862449.
STRINGⁱ	10090.ENSMUSP00000042457.

PTM databases

iPTMnetⁱ	P10126.
PhosphoSiteⁱ	P10126.
SwissPalmⁱ	P10126.

2D gel databases

SWISS-2DPAGE	P10126.

SWISS-2DPAGE

P10126.

Proteomic databases

EPDⁱ	P10126.
PaxDbⁱ	P10126.
PeptideAtlasⁱ	P10126.
PRIDEⁱ	P10126.
TopDownProteomicsⁱ	P10126.

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENSMUST00000042235; ENSMUSP00000042457; ENSMUSG00000037742.
GeneIDⁱ	13627.
KEGGⁱ	mmu:13627.
UCSCⁱ	uc009qun.1. mouse.

Organism-specific databases

CTDⁱ	1915.
MGIⁱ	MGI:1096881. Eef1a1.

Phylogenomic databases

eggNOGⁱ	KOG0052. Eukaryota. COG5256. LUCA.
HOGENOMⁱ	HOG000229291.
HOVERGENⁱ	HBG000179.
InParanoidⁱ	P10126.
KOⁱ	K03231.
OMAⁱ	FEQISHE.
OrthoDBⁱ	EOG091G05LW.
PhylomeDBⁱ	P10126.
TreeFamⁱ	TF300304.

Miscellaneous databases

PROⁱ	P10126.
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSMUSG00000037742.
ExpressionAtlasⁱ	P10126. baseline and differential.
Genevisibleⁱ	P10126. MM.

Family and domain databases

Gene3Dⁱ	3.40.50.300. 1 hit.
HAMAPⁱ	MF_00118_A. EF_Tu_A. 1 hit.
InterProⁱ	IPR004161. EFTu-like_2. IPR031157. G_TR_CS. IPR027417. P-loop_NTPase. IPR000795. TF_GTP-bd_dom. IPR009000. Transl_B-barrel. IPR009001. Transl_elong_EF1A/Init_IF2_C. IPR004539. Transl_elong_EF1A_euk/arc. IPR004160. Transl_elong_EFTu/EF1A_C. [Graphical view]
Pfamⁱ	PF03144. GTP_EFTU_D2. 1 hit. PF03143. GTP_EFTU_D3. 1 hit. [Graphical view]
PRINTSⁱ	PR00315. ELONGATNFCT.
SUPFAMⁱ	SSF50447. SSF50447. 1 hit. SSF50465. SSF50465. 1 hit. SSF52540. SSF52540. 1 hit.
TIGRFAMsⁱ	TIGR00483. EF-1_alpha. 1 hit.
PROSITEⁱ	PS00301. G_TR_1. 1 hit. PS51722. G_TR_2. 1 hit. [Graphical view]
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ

EF1A1_MOUSE

Accessionⁱ

Primary (citable) accession number: P10126
Secondary accession number(s): Q61511

Q99KU5

Entry historyⁱ

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	October 25, 2004
Last modified:	September 7, 2016
This is version 180 of the entry and version 3 of the sequence. [Complete history]

Entry statusⁱ

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

Complete proteome, Direct protein sequencing, Reference proteome

Documents

MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
SIMILARITY comments
Index of protein domains and families

Similar proteinsⁱ

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:

100%	UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%	UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%	UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P10126 (EF1A1_MOUSE)

UniProt

P10126 - EF1A1_MOUSE

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Elongation factor 1-alpha 1

Select a section on the left to see content.

<p>Provides any useful information about the protein, mostly biological knowledge.</p><p><a href='../manual/function_section' target='_top'>More...</a></p>Functioni

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

<p>Provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.</p><p><a href='../manual/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>Provides information on the location and the topology of the mature protein in the cell.</p><p><a href='../manual/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti

<p>Describes post-translational modifications (PTMs) and/or processing events.</p><p><a href='../manual/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Proteomic databases

2D gel databases

PTM databases

<p>Provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.</p><p><a href='../manual/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

<p>Provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.</p><p><a href='../manual/interaction_section' target='_top'>More...</a></p>Interactioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Protein-protein interaction databases

<p>Provides information on the tertiary and secondary structure of a protein.</p><p><a href='../manual/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>Provides information on sequence similarities with other proteins and the domain(s) present in a protein.</p><p><a href='../manual/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

<p>Provides information about the sequence similarity with other proteins.</p><p><a href='../manual/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>Displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.</p><p><a href='../manual/sequences_section' target='_top'>More...</a></p>Sequencei

Experimental Info

Sequence databases

Genome annotation databases

<p>Is used to point to information related to entries and found in data collections other than UniProtKB.</p><p><a href='../manual/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>Provides general information on the entry.</p><p><a href='../manual/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>Contains any relevant information that doesn’t fit in any other defined sections</p><p><a href='../manual/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequenceⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ