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P10126

- EF1A1_MOUSE

UniProt

P10126 - EF1A1_MOUSE

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Protein

Elongation factor 1-alpha 1

Gene

Eef1a1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Display
All None

  • Function
  • Names & Taxonomy
  • Subcellular locationSubcell. location
  • Pathology & BiotechPathol./Biotech
  • PTM / Processing
  • Expression
  • Interaction
  • Structure
  • Family & Domains
  • Sequence
  • Cross-references
  • Publications
  • Entry information
  • Miscellaneous
  • Similar proteins
Top

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi14 – 218GTPBy similarity
Nucleotide bindingi91 – 955GTPBy similarity
Nucleotide bindingi153 – 1564GTPBy similarity

GO - Molecular functioni

  1. GTPase activity Source: InterPro
  2. GTP binding Source: UniProtKB-KW
  3. poly(A) RNA binding Source: Ensembl
  4. translation elongation factor activity Source: UniProtKB-KW

GO - Biological processi

  1. cellular response to epidermal growth factor stimulus Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Elongation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_225256. HSF1 activation.
REACT_232254. Eukaryotic Translation Elongation.
REACT_253640. Peptide chain elongation.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus
ProteomesiUP000000589: Chromosome 9

Organism-specific databases

MGIiMGI:1096881. Eef1a1.

Subcellular locationi

Cytoplasm 1 Publication. 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

  1. cytoplasm Source: UniProtKB
  2. extracellular space Source: Ensembl
  3. extracellular vesicular exosome Source: Ensembl
  4. nucleolus Source: UniProtKB
  5. nucleus Source: UniProtKB
  6. plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 462462Elongation factor 1-alpha 1PRO_0000090886Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei36 – 361N6,N6,N6-trimethyllysineBy similarity
Modified residuei55 – 551N6,N6-dimethyllysineBy similarity
Modified residuei79 – 791N6,N6,N6-trimethyllysineBy similarity
Modified residuei165 – 1651N6,N6-dimethyllysine; alternateBy similarity
Modified residuei165 – 1651N6-acetyllysine; alternate1 Publication
Modified residuei172 – 1721N6-acetyllysine1 Publication
Modified residuei273 – 2731N6-acetyllysine1 Publication
Modified residuei300 – 3001Phosphoserine; by TGFBR1By similarity
Modified residuei301 – 30115-glutamyl glycerylphosphorylethanolamine1 Publication
Modified residuei318 – 3181N6,N6,N6-trimethyllysineBy similarity
Modified residuei374 – 37415-glutamyl glycerylphosphorylethanolamine1 Publication
Modified residuei392 – 3921N6-acetyllysine; alternate1 Publication
Modified residuei392 – 3921N6-succinyllysine; alternate1 Publication
Modified residuei432 – 4321Phosphothreonine; by PASKBy similarity
Modified residuei439 – 4391N6-acetyllysine1 Publication

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

MaxQBiP10126.
PaxDbiP10126.
PRIDEiP10126.

2D gel databases

SWISS-2DPAGEP10126.

PTM databases

PhosphoSiteiP10126.

Expressioni

Gene expression databases

BgeeiP10126.
ExpressionAtlasiP10126. baseline.
GenevestigatoriP10126.

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

WithEntry#Exp.IntActNotes
TSPY1Q015345EBI-773865,EBI-1973142From a different organism.

Protein-protein interaction databases

BioGridi199385. 13 interactions.
DIPiDIP-46609N.
IntActiP10126. 25 interactions.
MINTiMINT-1862449.

Structurei

3D structure databases

ProteinModelPortaliP10126.
SMRiP10126. Positions 4-455.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 242238tr-type GAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni14 – 218G1By similarity
Regioni70 – 745G2By similarity
Regioni91 – 944G3By similarity
Regioni153 – 1564G4By similarity
Regioni194 – 1963G5By 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

eggNOGiCOG5256.
HOGENOMiHOG000229291.
HOVERGENiHBG000179.
InParanoidiP10126.
KOiK03231.
OMAiAIRDMGM.
OrthoDBiEOG7NKKK3.
PhylomeDBiP10126.
TreeFamiTF300304.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00118_A. EF_Tu_A.
InterProiIPR000795. EF_GTP-bd_dom.
IPR027417. P-loop_NTPase.
IPR009000. Transl_B-barrel.
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.
[Graphical view]
PfamiPF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
PF03143. GTP_EFTU_D3. 1 hit.
[Graphical view]
PRINTSiPR00315. ELONGATNFCT.
SUPFAMiSSF50447. SSF50447. 1 hit.
SSF50465. SSF50465. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00483. EF-1_alpha. 1 hit.
PROSITEiPS00301. G_TR_1. 1 hit.
PS51722. G_TR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P10126-1 [UniParc]FASTAAdd 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71H → R in AAA37538. (PubMed:3481036)Curated
Sequence conflicti15 – 151H → L in AAA37538. (PubMed:3481036)Curated
Sequence conflicti23 – 231T → S in AAA37538. (PubMed:3481036)Curated
Sequence conflicti77 – 782LW → QR in CAA31957. (PubMed:2911475)Curated
Sequence conflicti83 – 831S → A in CAA27324. (PubMed:3960725)Curated
Sequence conflicti91 – 922DA → ES in CAA31957. (PubMed:2911475)Curated
Sequence conflicti108 – 1081Q → R in AAA37538. (PubMed:3481036)Curated
Sequence conflicti156 – 1561D → G in BAC28085. (PubMed:16141072)Curated
Sequence conflicti222 – 2221S → H in AAA50406. (PubMed:3215517)Curated
Sequence conflicti224 – 2263SGT → VAP in CAA31957. (PubMed:2911475)Curated
Sequence conflicti225 – 2251G → D in AAH04005. (PubMed:15489334)Curated
Sequence conflicti239 – 2391Missing in CAA31957. (PubMed:2911475)Curated
Sequence conflicti350 – 3501P → 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.
CCDSiCCDS40703.1.
PIRiS02114. EFMS1.
RefSeqiNP_034236.2. NM_010106.2.
UniGeneiMm.138471.
Mm.335315.
Mm.360075.
Mm.391071.
Mm.485669.
Mm.491424.

Genome annotation databases

EnsembliENSMUST00000042235; ENSMUSP00000042457; ENSMUSG00000037742.
GeneIDi13627.
KEGGimmu:13627.
UCSCiuc009qun.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. 13 interactions.
DIPi DIP-46609N.
IntActi P10126. 25 interactions.
MINTi MINT-1862449.

PTM databases

PhosphoSitei P10126.

2D gel databases

SWISS-2DPAGE P10126.

Proteomic databases

MaxQBi P10126.
PaxDbi P10126.
PRIDEi P10126.

Protocols and materials databases

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 COG5256.
HOGENOMi HOG000229291.
HOVERGENi HBG000179.
InParanoidi P10126.
KOi K03231.
OMAi AIRDMGM.
OrthoDBi EOG7NKKK3.
PhylomeDBi P10126.
TreeFami TF300304.

Enzyme and pathway databases

Reactomei REACT_225256. HSF1 activation.
REACT_232254. Eukaryotic Translation Elongation.
REACT_253640. Peptide chain elongation.

Miscellaneous databases

NextBioi 284304.
PROi P10126.
SOURCEi Search...

Gene expression databases

Bgeei P10126.
ExpressionAtlasi P10126. baseline.
Genevestigatori P10126.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
HAMAPi MF_00118_A. EF_Tu_A.
InterProi IPR000795. EF_GTP-bd_dom.
IPR027417. P-loop_NTPase.
IPR009000. Transl_B-barrel.
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.
[Graphical view ]
Pfami PF00009. GTP_EFTU. 1 hit.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and mapping of a gene for protein synthesis initiation factor 4A and its expression during differentiation of murine erythroleukemia cells."
    Reddy N.S., Roth W.W., Bragg P.W., Wahba A.J.
    Gene 70:231-243(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The complete cDNA sequence of mouse elongation factor 1 alpha (EF 1 alpha) mRNA."
    Lu X., Werner D.
    Nucleic Acids Res. 17:442-442(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Head, Testis and Thymus.
  4. "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].
    Strain: Czech II.
    Tissue: Mammary tumor and Olfactory epithelium.
  5. "Expression of a gene for mouse eucaryotic elongation factor Tu during murine erythroleukemic cell differentiation."
    Roth W.W., Bragg P.W., Corrias M.V., Reddy N.S., Dholakia J.N., Wahba A.J.
    Mol. Cell. Biol. 7:3929-3936(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-108.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-94.
  7. Lubec G., Kang S.U., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 6-30; 85-96; 135-146; 155-165; 248-290 AND 431-439, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6 and OF1.
    Tissue: Brain and Hippocampus.
  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.
  9. Cited for: ISGYLATION.
  10. "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.
  11. "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].
    Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Entry informationi

Entry nameiEF1A1_MOUSE
AccessioniPrimary (citable) accession number: P10126
Secondary accession number(s): Q61511
, Q6ZWN2, Q8BMB8, Q8BVS8, Q99KU5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: October 25, 2004
Last modified: January 7, 2015
This is version 161 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

External Data

Dasty 3

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 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.
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