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I4E1B_MOUSE
ID   I4E1B_MOUSE             Reviewed;         244 AA.
AC   Q3UTA9; Q27ZJ1;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Eukaryotic translation initiation factor 4E type 1B;
DE   AltName: Full=Oocyte-specific eukaryotic translation initiation factor 4E-like;
GN   Name=Eif4e1b; Synonyms=Gm273;
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] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J;
RX   PubMed=17015433; DOI=10.1101/gad.1471006;
RA   Evsikov A.V., Graber J.H., Brockman J.M., Hampl A., Holbrook A.E.,
RA   Singh P., Eppig J.J., Solter D., Knowles B.B.;
RT   "Cracking the egg: molecular dynamics and evolutionary aspects of the
RT   transition from the fully grown oocyte to embryo.";
RL   Genes Dev. 20:2713-2727(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Egg;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [4]
RP   GENE FAMILY.
RX   PubMed=16191198; DOI=10.1186/1471-2148-5-48;
RA   Joshi B., Lee K., Maeder D.L., Jagus R.;
RT   "Phylogenetic analysis of eIF4E-family members.";
RL   BMC Evol. Biol. 5:48-48(2005).
CC   -!- FUNCTION: Recognizes and binds the 7-methylguanosine-containing mRNA
CC       cap during an early step in the initiation of protein synthesis and
CC       facilitates ribosome binding by inducing the unwinding of the mRNAs
CC       secondary structures. {ECO:0000250}.
CC   -!- SUBUNIT: EIF4F is a multi-subunit complex, the composition of which
CC       varies with external and internal environmental conditions. It is
CC       composed of at least EIF4A, EIF4E AND EIF4G (By similarity).
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC         Comment=Additional isoforms seem to exist.;
CC       Name=1;
CC         IsoId=Q3UTA9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3UTA9-2; Sequence=VSP_034476, VSP_034477;
CC   -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4E family.
CC       {ECO:0000305}.
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DR   EMBL; DQ279473; ABB88894.1; -; mRNA.
DR   EMBL; DQ279474; ABB88895.1; -; mRNA.
DR   EMBL; AK139577; BAE24071.1; -; mRNA.
DR   EMBL; BC139143; AAI39144.1; -; mRNA.
DR   EMBL; BC139144; AAI39145.1; -; mRNA.
DR   CCDS; CCDS49269.1; -. [Q3UTA9-1]
DR   CCDS; CCDS49270.1; -. [Q3UTA9-2]
DR   RefSeq; NP_001028441.1; NM_001033269.3. [Q3UTA9-1]
DR   RefSeq; NP_001034772.1; NM_001039683.2. [Q3UTA9-2]
DR   RefSeq; NP_001273107.1; NM_001286178.1.
DR   RefSeq; NP_001273108.1; NM_001286179.1.
DR   RefSeq; NP_001273109.1; NM_001286180.1.
DR   RefSeq; XP_017170974.1; XM_017315485.1. [Q3UTA9-1]
DR   RefSeq; XP_017170975.1; XM_017315486.1. [Q3UTA9-2]
DR   AlphaFoldDB; Q3UTA9; -.
DR   SMR; Q3UTA9; -.
DR   STRING; 10090.ENSMUSP00000123294; -.
DR   PhosphoSitePlus; Q3UTA9; -.
DR   PaxDb; Q3UTA9; -.
DR   PRIDE; Q3UTA9; -.
DR   Antibodypedia; 63751; 30 antibodies from 10 providers.
DR   Ensembl; ENSMUST00000110003; ENSMUSP00000105630; ENSMUSG00000074895. [Q3UTA9-1]
DR   Ensembl; ENSMUST00000132728; ENSMUSP00000123294; ENSMUSG00000074895. [Q3UTA9-1]
DR   Ensembl; ENSMUST00000152204; ENSMUSP00000120619; ENSMUSG00000074895. [Q3UTA9-2]
DR   GeneID; 218268; -.
DR   KEGG; mmu:218268; -.
DR   UCSC; uc007qpg.2; mouse. [Q3UTA9-2]
DR   UCSC; uc007qph.2; mouse. [Q3UTA9-1]
DR   CTD; 253314; -.
DR   MGI; MGI:2685119; Eif4e1b.
DR   VEuPathDB; HostDB:ENSMUSG00000074895; -.
DR   eggNOG; KOG1670; Eukaryota.
DR   GeneTree; ENSGT00940000160838; -.
DR   HOGENOM; CLU_043552_1_1_1; -.
DR   InParanoid; Q3UTA9; -.
DR   OrthoDB; 1394271at2759; -.
DR   PhylomeDB; Q3UTA9; -.
DR   TreeFam; TF101526; -.
DR   BioGRID-ORCS; 218268; 3 hits in 72 CRISPR screens.
DR   ChiTaRS; Eif4e1b; mouse.
DR   PRO; PR:Q3UTA9; -.
DR   Proteomes; UP000000589; Chromosome 13.
DR   RNAct; Q3UTA9; protein.
DR   Bgee; ENSMUSG00000074895; Expressed in secondary oocyte and 15 other tissues.
DR   ExpressionAtlas; Q3UTA9; baseline and differential.
DR   GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; IBA:GO_Central.
DR   GO; GO:0005845; C:mRNA cap binding complex; ISS:UniProtKB.
DR   GO; GO:0000340; F:RNA 7-methylguanosine cap binding; IBA:GO_Central.
DR   GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR   Gene3D; 3.30.760.10; -; 1.
DR   InterPro; IPR023398; TIF_eIF4e-like.
DR   InterPro; IPR001040; TIF_eIF_4E.
DR   InterPro; IPR019770; TIF_eIF_4E_CS.
DR   PANTHER; PTHR11960; PTHR11960; 1.
DR   Pfam; PF01652; IF4E; 1.
DR   SUPFAM; SSF55418; SSF55418; 1.
DR   PROSITE; PS00813; IF4E; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Initiation factor; Protein biosynthesis;
KW   Reference proteome; RNA-binding.
FT   CHAIN           1..244
FT                   /note="Eukaryotic translation initiation factor 4E type 1B"
FT                   /id="PRO_0000342514"
FT   REGION          1..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          65..68
FT                   /note="EIF4EBP1/2/3 binding"
FT                   /evidence="ECO:0000250"
FT   REGION          101..105
FT                   /note="EIF4EBP1/2/3 binding"
FT                   /evidence="ECO:0000250"
FT   REGION          160..167
FT                   /note="EIF4EBP1/2/3 binding"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        1..26
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        43..57
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         84..85
FT                   /ligand="mRNA"
FT                   /ligand_id="ChEBI:CHEBI:33699"
FT                   /ligand_part="N(7)-methylguanosine 5'-triphosphate group"
FT                   /ligand_part_id="ChEBI:CHEBI:74429"
FT                   /ligand_part_note="m7GTP residue in mRNA cap"
FT                   /evidence="ECO:0000250"
FT   BINDING         130..131
FT                   /ligand="mRNA"
FT                   /ligand_id="ChEBI:CHEBI:33699"
FT                   /ligand_part="N(7)-methylguanosine 5'-triphosphate group"
FT                   /ligand_part_id="ChEBI:CHEBI:74429"
FT                   /ligand_part_note="m7GTP residue in mRNA cap"
FT                   /evidence="ECO:0000250"
FT   BINDING         185..190
FT                   /ligand="mRNA"
FT                   /ligand_id="ChEBI:CHEBI:33699"
FT                   /ligand_part="N(7)-methylguanosine 5'-triphosphate group"
FT                   /ligand_part_id="ChEBI:CHEBI:74429"
FT                   /ligand_part_note="m7GTP residue in mRNA cap"
FT                   /evidence="ECO:0000250"
FT   BINDING         233..235
FT                   /ligand="mRNA"
FT                   /ligand_id="ChEBI:CHEBI:33699"
FT                   /ligand_part="N(7)-methylguanosine 5'-triphosphate group"
FT                   /ligand_part_id="ChEBI:CHEBI:74429"
FT                   /ligand_part_note="m7GTP residue in mRNA cap"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         162..183
FT                   /note="LLCLVGNCFEEYSREVCGAVVN -> QGSVRCCREHPHEEGQDCPVDE (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:17015433"
FT                   /id="VSP_034476"
FT   VAR_SEQ         184..244
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:17015433"
FT                   /id="VSP_034477"
SQ   SEQUENCE   244 AA;  27985 MW;  04D3CD02BF38B299 CRC64;
     MNKVEGGGHK EEVVVKEKEV VKEKPSEATA EGVQAGEAKD LPGSLKTQRR KAHREHPPEV
     LSKLHPLQYR WVLWFFKNDR SRAWQDNLQL VTKFNTVEDF WAVYSHIKLA SKLSSGCDYA
     LFKEGILPMW EDNRNKQGGR WLLSIDKQLR HFELDRLWLE TLLCLVGNCF EEYSREVCGA
     VVNIRTKRDK IALWTSEAED KAGVMQIGQI YKERLGISTK TIIGYQAHAD TAAKSNNLAN
     KFVV
 
 
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