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EIF3M_MOUSE
ID   EIF3M_MOUSE             Reviewed;         374 AA.
AC   Q99JX4; Q3TI04; Q5EBI5;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 153.
DE   RecName: Full=Eukaryotic translation initiation factor 3 subunit M {ECO:0000255|HAMAP-Rule:MF_03012};
DE            Short=eIF3m {ECO:0000255|HAMAP-Rule:MF_03012};
DE   AltName: Full=PCI domain-containing protein 1;
GN   Name=Eif3m; Synonyms=Pcid1;
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 [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and DBA/2J; TISSUE=Embryo, and Heart;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Brain, Jaw, Limb, Mammary tumor, and Molar;
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC   Spleen, and Testis;
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: Component of the eukaryotic translation initiation factor 3
CC       (eIF-3) complex, which is required for several steps in the initiation
CC       of protein synthesis. The eIF-3 complex associates with the 40S
CC       ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-
CC       2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex
CC       (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC
CC       and scanning of the mRNA for AUG recognition. The eIF-3 complex is also
CC       required for disassembly and recycling of post-termination ribosomal
CC       complexes and subsequently prevents premature joining of the 40S and
CC       60S ribosomal subunits prior to initiation. The eIF-3 complex
CC       specifically targets and initiates translation of a subset of mRNAs
CC       involved in cell proliferation, including cell cycling, differentiation
CC       and apoptosis, and uses different modes of RNA stem-loop binding to
CC       exert either translational activation or repression.
CC       {ECO:0000255|HAMAP-Rule:MF_03012}.
CC   -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC       (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B, EIF3C,
CC       EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L and
CC       EIF3M. The eIF-3 complex appears to include 3 stable modules: module A
CC       is composed of EIF3A, EIF3B, EIF3G and EIF3I; module B is composed of
CC       EIF3F, EIF3H, and EIF3M; and module C is composed of EIF3C, EIF3D,
CC       EIF3E, EIF3K and EIF3L. EIF3C of module C binds EIF3B of module A and
CC       EIF3H of module B, thereby linking the three modules. EIF3J is a labile
CC       subunit that binds to the eIF-3 complex via EIF3B. The eIF-3 complex
CC       interacts with RPS6KB1 under conditions of nutrient depletion.
CC       Mitogenic stimulation leads to binding and activation of a complex
CC       composed of MTOR and RPTOR, leading to phosphorylation and release of
CC       RPS6KB1 and binding of EIF4B to eIF-3. {ECO:0000255|HAMAP-
CC       Rule:MF_03012}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03012}.
CC   -!- SIMILARITY: Belongs to the eIF-3 subunit M family. {ECO:0000255|HAMAP-
CC       Rule:MF_03012}.
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DR   EMBL; AK077480; BAC36821.1; -; mRNA.
DR   EMBL; AK084738; BAC39270.1; -; mRNA.
DR   EMBL; AK146222; BAE26990.1; -; mRNA.
DR   EMBL; AK168066; BAE40042.1; -; mRNA.
DR   EMBL; AL606494; CAM17236.1; -; Genomic_DNA.
DR   EMBL; BC005598; AAH05598.1; -; mRNA.
DR   EMBL; BC089568; AAH89568.1; -; mRNA.
DR   EMBL; BC103795; AAI03796.1; -; mRNA.
DR   EMBL; BC116787; AAI16788.1; -; mRNA.
DR   EMBL; BC116789; AAI16790.1; -; mRNA.
DR   CCDS; CCDS16495.1; -.
DR   RefSeq; NP_663355.1; NM_145380.2.
DR   AlphaFoldDB; Q99JX4; -.
DR   SMR; Q99JX4; -.
DR   BioGRID; 221017; 19.
DR   DIP; DIP-59784N; -.
DR   IntAct; Q99JX4; 3.
DR   STRING; 10090.ENSMUSP00000028592; -.
DR   iPTMnet; Q99JX4; -.
DR   PhosphoSitePlus; Q99JX4; -.
DR   SwissPalm; Q99JX4; -.
DR   EPD; Q99JX4; -.
DR   jPOST; Q99JX4; -.
DR   MaxQB; Q99JX4; -.
DR   PaxDb; Q99JX4; -.
DR   PeptideAtlas; Q99JX4; -.
DR   PRIDE; Q99JX4; -.
DR   ProteomicsDB; 275656; -.
DR   Antibodypedia; 25628; 265 antibodies from 35 providers.
DR   DNASU; 98221; -.
DR   Ensembl; ENSMUST00000028592; ENSMUSP00000028592; ENSMUSG00000027170.
DR   GeneID; 98221; -.
DR   KEGG; mmu:98221; -.
DR   UCSC; uc008lkl.1; mouse.
DR   CTD; 10480; -.
DR   MGI; MGI:1351744; Eif3m.
DR   VEuPathDB; HostDB:ENSMUSG00000027170; -.
DR   eggNOG; KOG2753; Eukaryota.
DR   GeneTree; ENSGT00390000004456; -.
DR   HOGENOM; CLU_035254_1_0_1; -.
DR   InParanoid; Q99JX4; -.
DR   OMA; REDAQRC; -.
DR   OrthoDB; 679771at2759; -.
DR   PhylomeDB; Q99JX4; -.
DR   TreeFam; TF106148; -.
DR   Reactome; R-MMU-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR   Reactome; R-MMU-72649; Translation initiation complex formation.
DR   Reactome; R-MMU-72689; Formation of a pool of free 40S subunits.
DR   Reactome; R-MMU-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR   Reactome; R-MMU-72702; Ribosomal scanning and start codon recognition.
DR   Reactome; R-MMU-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR   BioGRID-ORCS; 98221; 25 hits in 76 CRISPR screens.
DR   ChiTaRS; Eif3m; mouse.
DR   PRO; PR:Q99JX4; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q99JX4; protein.
DR   Bgee; ENSMUSG00000027170; Expressed in epiblast (generic) and 75 other tissues.
DR   ExpressionAtlas; Q99JX4; baseline and differential.
DR   Genevisible; Q99JX4; MM.
DR   GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; ISO:MGI.
DR   GO; GO:0071541; C:eukaryotic translation initiation factor 3 complex, eIF3m; IDA:MGI.
DR   GO; GO:0003743; F:translation initiation factor activity; ISO:MGI.
DR   GO; GO:0031369; F:translation initiation factor binding; IDA:MGI.
DR   GO; GO:0002183; P:cytoplasmic translational initiation; IBA:GO_Central.
DR   GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0006412; P:translation; IMP:MGI.
DR   HAMAP; MF_03012; eIF3m; 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR045237; COPS7/eIF3m.
DR   InterPro; IPR027528; eIF3m.
DR   InterPro; IPR040750; eIF3m_C_helix.
DR   InterPro; IPR000717; PCI_dom.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR15350; PTHR15350; 1.
DR   Pfam; PF18005; eIF3m_C_helix; 1.
DR   Pfam; PF01399; PCI; 1.
DR   SMART; SM00088; PINT; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   PROSITE; PS50250; PCI; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Initiation factor; Phosphoprotein;
KW   Protein biosynthesis; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03012"
FT   CHAIN           2..374
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   M"
FT                   /id="PRO_0000308196"
FT   DOMAIN          180..339
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7L2H7, ECO:0000255|HAMAP-
FT                   Rule:MF_03012"
FT   MOD_RES         2
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7L2H7"
FT   MOD_RES         152
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7L2H7"
FT   MOD_RES         254
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7L2H7"
FT   MOD_RES         367
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7L2H7"
FT   CONFLICT        29
FT                   /note="L -> I (in Ref. 3; AAH89568)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        141
FT                   /note="P -> Q (in Ref. 1; BAE40042)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        155
FT                   /note="K -> N (in Ref. 3; AAH89568)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   374 AA;  42517 MW;  09845D87E792B783 CRC64;
     MSVPAFIDIS EEDQAAELRA YLKSKGAELS EENSEGGLHV DLAQIIEACD VCLKEDDKDV
     ESVMNSVVSL LLILEPDKQE ALIESLCEKL VKFREGERPS LRLQLLSNLF HGMDKNTPVR
     YTVYCSLIKV AASCGAIQYI PTELDQVRKW ISDWKLTTEK KHTLLRLLYE ALVDCKKSDA
     ASKVMVELLG SYTEDNASQA RVDAHRCIVR ALKDPNAFLF DHLLTLKPVK FLEGELIHDL
     LTIFVSAKLA SYVKFYQNNK DFIDSLGLLH EQNMAKMRLL TFMGMAVENK EISFDTMQQE
     LQIGADDVEA FVIDAVRTKM VYCKIDQTQR KVVVSHSTHR TFGKQQWQQL YDTLNAWKQN
     LNKVKNSLLS LSDT
 
 
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