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EF1A2_MOUSE
ID   EF1A2_MOUSE             Reviewed;         463 AA.
AC   P62631; P27706;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 160.
DE   RecName: Full=Elongation factor 1-alpha 2;
DE            Short=EF-1-alpha-2;
DE   AltName: Full=Eukaryotic elongation factor 1 A-2;
DE            Short=eEF1A-2;
DE   AltName: Full=Statin-S1;
GN   Name=Eef1a2; Synonyms=Eef1al, Stn;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=7945283; DOI=10.1006/bbrc.1994.2336;
RA   Lee S., Ann D.K., Wang E.;
RT   "Cloning of human and mouse brain cDNAs coding for S1, the second member of
RT   the mammalian elongation factor-1 alpha gene family: analysis of a possible
RT   evolutionary pathway.";
RL   Biochem. Biophys. Res. Commun. 203:1371-1377(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 6-30; 85-96; 135-146; 155-165; 248-266 AND 431-439, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, and Lung;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC       tRNA to the A-site of ribosomes during protein biosynthesis.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Found in a wide range of tissues.
CC   -!- DEVELOPMENTAL STAGE: The statin expression is specific for
CC       nonproliferating cells. Its message is most abundant in G0 phase of 3T3
CC       mouse fibroblasts, but becomes significantly reduced in G1 and S1
CC       phases cells.
CC   -!- PTM: Trimethylated at Lys-165 by EEF1AKMT3. Mono-, di-, and
CC       trimethylated at Lys-36 by EEF1AKMT4; trimethylated form is
CC       predominant. Methylation by EEF1AKMT4 contributes to the fine-tuning of
CC       translation rates for a subset of tRNAs. Trimethylated at the N-
CC       terminus and dimethylated at Lys-55 by METTL13.
CC       {ECO:0000250|UniProtKB:Q05639}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC       subfamily. {ECO:0000305}.
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DR   EMBL; L26479; AAA91870.1; -; mRNA.
DR   EMBL; BC018235; AAH18235.1; -; mRNA.
DR   CCDS; CCDS17201.1; -.
DR   PIR; JC2445; JC2445.
DR   RefSeq; NP_031932.1; NM_007906.2.
DR   AlphaFoldDB; P62631; -.
DR   SMR; P62631; -.
DR   BioGRID; 199386; 30.
DR   IntAct; P62631; 8.
DR   STRING; 10090.ENSMUSP00000054556; -.
DR   iPTMnet; P62631; -.
DR   PhosphoSitePlus; P62631; -.
DR   SwissPalm; P62631; -.
DR   EPD; P62631; -.
DR   jPOST; P62631; -.
DR   MaxQB; P62631; -.
DR   PaxDb; P62631; -.
DR   PeptideAtlas; P62631; -.
DR   PRIDE; P62631; -.
DR   ProteomicsDB; 277686; -.
DR   Antibodypedia; 29757; 258 antibodies from 38 providers.
DR   DNASU; 13628; -.
DR   Ensembl; ENSMUST00000055990; ENSMUSP00000054556; ENSMUSG00000016349.
DR   GeneID; 13628; -.
DR   KEGG; mmu:13628; -.
DR   UCSC; uc008olh.1; mouse.
DR   CTD; 1917; -.
DR   MGI; MGI:1096317; Eef1a2.
DR   VEuPathDB; HostDB:ENSMUSG00000016349; -.
DR   eggNOG; KOG0052; Eukaryota.
DR   GeneTree; ENSGT00950000183029; -.
DR   HOGENOM; CLU_007265_3_5_1; -.
DR   InParanoid; P62631; -.
DR   OMA; VACTFES; -.
DR   OrthoDB; 1150082at2759; -.
DR   PhylomeDB; P62631; -.
DR   TreeFam; TF300304; -.
DR   BioGRID-ORCS; 13628; 2 hits in 74 CRISPR screens.
DR   PRO; PR:P62631; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; P62631; protein.
DR   Bgee; ENSMUSG00000016349; Expressed in perirhinal cortex and 191 other tissues.
DR   Genevisible; P62631; MM.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; IDA:MGI.
DR   GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0045202; C:synapse; IDA:SynGO.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR   GO; GO:0003746; F:translation elongation factor activity; IDA:MGI.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IDA:MGI.
DR   GO; GO:0090218; P:positive regulation of lipid kinase activity; ISO:MGI.
DR   GO; GO:0006412; P:translation; IBA:GO_Central.
DR   GO; GO:0006414; P:translational elongation; IDA:MGI.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00118_A; EF_Tu_A; 1.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR031157; G_TR_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR   InterPro; IPR004539; Transl_elong_EF1A_euk/arc.
DR   InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF03143; GTP_EFTU_D3; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF50465; SSF50465; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00483; EF-1_alpha; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Elongation factor; GTP-binding;
KW   Methylation; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Protein biosynthesis; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..463
FT                   /note="Elongation factor 1-alpha 2"
FT                   /id="PRO_0000090892"
FT   DOMAIN          5..242
FT                   /note="tr-type G"
FT   REGION          14..21
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          70..74
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          91..94
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          153..156
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          194..196
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   REGION          444..463
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         14..21
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         91..95
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         153..156
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N,N,N-trimethylglycine"
FT                   /evidence="ECO:0000250|UniProtKB:P68104"
FT   MOD_RES         36
FT                   /note="N6,N6,N6-trimethyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q05639"
FT   MOD_RES         36
FT                   /note="N6,N6-dimethyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q05639"
FT   MOD_RES         36
FT                   /note="N6-methyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q05639"
FT   MOD_RES         55
FT                   /note="N6,N6,N6-trimethyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q71V39"
FT   MOD_RES         55
FT                   /note="N6,N6-dimethyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q05639"
FT   MOD_RES         79
FT                   /note="N6,N6,N6-trimethyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q05639"
FT   MOD_RES         165
FT                   /note="N6,N6,N6-trimethyllysine; alternate; by EEF1AKMT3"
FT                   /evidence="ECO:0000250|UniProtKB:Q05639"
FT   MOD_RES         165
FT                   /note="N6,N6-dimethyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q05639"
FT   MOD_RES         165
FT                   /note="N6-methyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q05639"
FT   MOD_RES         179
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q05639"
FT   MOD_RES         224
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P62632"
FT   MOD_RES         301
FT                   /note="5-glutamyl glycerylphosphorylethanolamine"
FT                   /evidence="ECO:0000250|UniProtKB:Q71V39"
FT   MOD_RES         374
FT                   /note="5-glutamyl glycerylphosphorylethanolamine"
FT                   /evidence="ECO:0000250|UniProtKB:Q71V39"
FT   MOD_RES         439
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q05639"
SQ   SEQUENCE   463 AA;  50454 MW;  31E4F59BC05D8F8C CRC64;
     MGKEKTHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAEMG KGSFKYAWVL
     DKLKAERERG ITIDISLWKF ETTKYYITII DAPGHRDFIK NMITGTSQAD CAVLIVAAGV
     GEFEAGISKN GQTREHALLA YTLGVKQLIV GVNKMDSTEP AYSEKRYDEI VKEVSAYIKK
     IGYNPATVPF VPISGWHGDN MLEPSPNMPW FKGWKVERKE GNASGVSLLE ALDTILPPTR
     PTDKPLRLPL QDVYKIGGIG TVPVGRVETG ILRPGMVVTF APVNITTEVK SVEMHHEALS
     EALPGDNVGF NVKNVSVKDI RRGNVCGDSK ADPPQEAAQF TSQVIILNHP GQISAGYSPV
     IDCHTAHIAC KFAELKEKID RRSGKKLEDN PKSLKSGDAA IVEMVPGKPM CVESFSQYPP
     LGRFAVRDMR QTVAVGVIKN VEKKSGGAGK VTKSAQKAQK AGK
 
 
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