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P10126

- EF1A1_MOUSE

UniProt

P10126 - EF1A1_MOUSE

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
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    • History
      Entry version 158 (01 Oct 2014)
      Sequence version 3 (25 Oct 2004)
      Previous versions | rss
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    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. protein binding Source: UniProtKB
    4. translation elongation factor activity Source: UniProtKB-KW

    GO - Biological processi

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

    Keywords - Molecular functioni

    Elongation factor

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_225256. HSF1 activation.

    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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:1096881. Eef1a1.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus By similarity. Nucleusnucleolus 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. nucleolus Source: UniProtKB
    3. nucleus Source: UniProtKB
    4. plasma membrane Source: MGI

    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.
    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 2-443.
    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

    Phylogenomic databases

    eggNOGiCOG5256.
    HOGENOMiHOG000229291.
    HOVERGENiHBG000179.
    InParanoidiP10126.
    KOiK03231.
    OMAiADKPHMN.
    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

    MGKEKTHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAEMG    50
    KGSFKYAWVL DKLKAERERG ITIDISLWKF ETSKYYVTII DAPGHRDFIK 100
    NMITGTSQAD CAVLIVAAGV GEFEAGISKN GQTREHALLA YTLGVKQLIV 150
    GVNKMDSTEP PYSQKRYEEI VKEVSTYIKK IGYNPDTVAF VPISGWNGDN 200
    MLEPSANMPW FKGWKVTRKD GSASGTTLLE ALDCILPPTR PTDKPLRLPL 250
    QDVYKIGGIG TVPVGRVETG VLKPGMVVTF APVNVTTEVK SVEMHHEALS 300
    EALPGDNVGF NVKNVSVKDV RRGNVAGDSK NDPPMEAAGF TAQVIILNHP 350
    GQISAGYAPV LDCHTAHIAC KFAELKEKID RRSGKKLEDG PKFLKSGDAA 400
    IVDMVPGKPM CVESFSDYPP LGRFAVRDMR QTVAVGVIKA VDKKAAGAGK 450
    VTKSAQKAQK AK 462
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 2-443.
    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 ADKPHMN.
    OrthoDBi EOG7NKKK3.
    PhylomeDBi P10126.
    TreeFami TF300304.

    Enzyme and pathway databases

    Reactomei REACT_225256. HSF1 activation.

    Miscellaneous databases

    NextBioi 284304.
    PROi P10126.
    SOURCEi Search...

    Gene expression databases

    Bgeei P10126.
    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

    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.

    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: October 1, 2014
    This is version 158 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