EIF3B_MOUSE
ID EIF3B_MOUSE Reviewed; 803 AA.
AC Q8JZQ9; Q922K2;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit B {ECO:0000255|HAMAP-Rule:MF_03001};
DE Short=eIF3b {ECO:0000255|HAMAP-Rule:MF_03001};
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 9 {ECO:0000255|HAMAP-Rule:MF_03001};
DE AltName: Full=eIF-3-eta {ECO:0000255|HAMAP-Rule:MF_03001};
DE AltName: Full=eIF3 p116;
GN Name=Eif3b; Synonyms=Eif3s9;
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], FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Embryonic stem cell;
RX PubMed=12038979; DOI=10.1093/oxfordjournals.jbchem.a003172;
RA Koyanagi-Katsuta R., Akimitsu N., Hamamoto H., Arimitsu N., Hatano T.,
RA Sekimizu K.;
RT "Embryonic lethality of mutant mice deficient in the p116 gene.";
RL J. Biochem. 131:833-837(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Cecum, and Placenta;
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].
RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-31, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [5]
RP INTERACTION WITH EIF3A; EIF3F; EIF3J; EIF4A1; EIF4B; EIF4E; EIF4G1 AND
RP RPS6.
RX PubMed=16541103; DOI=10.1038/sj.emboj.7601047;
RA Harris T.E., Chi A., Shabanowitz J., Hunt D.F., Rhoads R.E.,
RA Lawrence J.C. Jr.;
RT "mTOR-dependent stimulation of the association of eIF4G and eIF3 by
RT insulin.";
RL EMBO J. 25:1659-1668(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [7]
RP FUNCTION, CHARACTERIZATION OF THE EIF-3 COMPLEX, IDENTIFICATION IN THE
RP EIF-3 COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17581632; DOI=10.1038/sj.emboj.7601765;
RA Masutani M., Sonenberg N., Yokoyama S., Imataka H.;
RT "Reconstitution reveals the functional core of mammalian eIF3.";
RL EMBO J. 26:3373-3383(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120 AND SER-123, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Teratocarcinoma;
RX PubMed=17622165; DOI=10.1021/pr070122r;
RA Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT cells.";
RL J. Proteome Res. 6:3174-3186(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68; THR-74; SER-75; SER-79;
RP SER-90; SER-120 AND SER-123, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79; SER-120 AND SER-123, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75 AND SER-79, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-74; SER-75; SER-79; SER-120
RP AND SER-123, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37; SER-40; SER-68; THR-72;
RP SER-75; SER-79; SER-84; SER-88; SER-111; SER-120 AND SER-123, AND
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: RNA-binding component of the eukaryotic translation
CC initiation factor 3 (eIF-3) complex, which is required for several
CC steps in the initiation of protein synthesis. The eIF-3 complex
CC associates with the 40S ribosome and facilitates the recruitment of
CC eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-
CC initiation complex (43S PIC). The eIF-3 complex stimulates mRNA
CC recruitment to the 43S PIC and scanning of the mRNA for AUG
CC recognition. The eIF-3 complex is also required for disassembly and
CC recycling of post-termination ribosomal complexes and subsequently
CC prevents premature joining of the 40S and 60S ribosomal subunits prior
CC to initiation. The eIF-3 complex specifically targets and initiates
CC translation of a subset of mRNAs involved in cell proliferation,
CC including cell cycling, differentiation and apoptosis, and uses
CC different modes of RNA stem-loop binding to exert either translational
CC activation or repression. {ECO:0000255|HAMAP-Rule:MF_03001,
CC ECO:0000269|PubMed:12038979, ECO:0000269|PubMed:17581632}.
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. Also interacts with UPF2 and
CC HNRPD. Interacts with METTL3. Interacts with DDX3X (By similarity).
CC {ECO:0000250|UniProtKB:P55884, ECO:0000255|HAMAP-Rule:MF_03001,
CC ECO:0000269|PubMed:16541103, ECO:0000269|PubMed:17581632}.
CC -!- INTERACTION:
CC Q8JZQ9; Q6NZJ6: Eif4g1; NbExp=2; IntAct=EBI-4286513, EBI-8175606;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03001}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:12038979}.
CC -!- DOMAIN: The RRM domain mediates interaction with EIF3J.
CC {ECO:0000255|HAMAP-Rule:MF_03001}.
CC -!- PTM: Phosphorylated. Phosphorylation is enhanced upon serum
CC stimulation. {ECO:0000255|HAMAP-Rule:MF_03001}.
CC -!- DISRUPTION PHENOTYPE: Embryonic death. {ECO:0000269|PubMed:12038979}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit B family. {ECO:0000255|HAMAP-
CC Rule:MF_03001}.
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DR EMBL; AK033722; BAC28445.1; -; mRNA.
DR EMBL; AK167618; BAE39671.1; -; mRNA.
DR EMBL; AK170938; BAE42128.1; -; mRNA.
DR EMBL; BC007175; AAH07175.1; -; mRNA.
DR EMBL; BC031704; AAH31704.1; -; mRNA.
DR CCDS; CCDS19819.1; -.
DR PIR; JC7862; JC7862.
DR RefSeq; NP_598677.1; NM_133916.2.
DR AlphaFoldDB; Q8JZQ9; -.
DR SMR; Q8JZQ9; -.
DR BioGRID; 205699; 37.
DR IntAct; Q8JZQ9; 11.
DR MINT; Q8JZQ9; -.
DR STRING; 10090.ENSMUSP00000098076; -.
DR iPTMnet; Q8JZQ9; -.
DR PhosphoSitePlus; Q8JZQ9; -.
DR SwissPalm; Q8JZQ9; -.
DR EPD; Q8JZQ9; -.
DR jPOST; Q8JZQ9; -.
DR MaxQB; Q8JZQ9; -.
DR PaxDb; Q8JZQ9; -.
DR PRIDE; Q8JZQ9; -.
DR ProteomicsDB; 275450; -.
DR Antibodypedia; 4313; 142 antibodies from 29 providers.
DR DNASU; 27979; -.
DR Ensembl; ENSMUST00000100507; ENSMUSP00000098076; ENSMUSG00000056076.
DR GeneID; 27979; -.
DR KEGG; mmu:27979; -.
DR UCSC; uc009ahr.1; mouse.
DR CTD; 8662; -.
DR MGI; MGI:106478; Eif3b.
DR VEuPathDB; HostDB:ENSMUSG00000056076; -.
DR eggNOG; KOG2314; Eukaryota.
DR GeneTree; ENSGT00550000074913; -.
DR HOGENOM; CLU_011152_1_0_1; -.
DR InParanoid; Q8JZQ9; -.
DR OMA; NVADCKI; -.
DR OrthoDB; 1194797at2759; -.
DR PhylomeDB; Q8JZQ9; -.
DR TreeFam; TF101521; -.
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; 27979; 25 hits in 78 CRISPR screens.
DR ChiTaRS; Eif3b; mouse.
DR PRO; PR:Q8JZQ9; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8JZQ9; protein.
DR Bgee; ENSMUSG00000056076; Expressed in ectoplacental cone and 256 other tissues.
DR ExpressionAtlas; Q8JZQ9; baseline and differential.
DR Genevisible; Q8JZQ9; 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; IDA:UniProtKB.
DR GO; GO:0071541; C:eukaryotic translation initiation factor 3 complex, eIF3m; IDA:MGI.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0003723; F:RNA binding; ISO:MGI.
DR GO; GO:0003743; F:translation initiation factor activity; ISO:MGI.
DR GO; GO:0031369; F:translation initiation factor binding; IEA:InterPro.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0075522; P:IRES-dependent viral translational initiation; ISO:MGI.
DR GO; GO:0006446; P:regulation of translational initiation; ISO:MGI.
DR GO; GO:0006413; P:translational initiation; IDA:UniProtKB.
DR GO; GO:0075525; P:viral translational termination-reinitiation; ISO:MGI.
DR CDD; cd12278; RRM_eIF3B; 1.
DR Gene3D; 2.130.10.10; -; 2.
DR Gene3D; 3.30.70.330; -; 1.
DR HAMAP; MF_03001; eIF3b; 1.
DR InterPro; IPR011400; EIF3B.
DR InterPro; IPR034363; eIF3B_RRM.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR013979; TIF_beta_prop-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR14068; PTHR14068; 1.
DR Pfam; PF08662; eIF2A; 1.
DR Pfam; PF00076; RRM_1; 1.
DR PIRSF; PIRSF036424; eIF3b; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Initiation factor; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; Repeat; RNA-binding; WD repeat.
FT CHAIN 1..803
FT /note="Eukaryotic translation initiation factor 3 subunit
FT B"
FT /id="PRO_0000223479"
FT DOMAIN 174..257
FT /note="RRM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03001"
FT REPEAT 321..359
FT /note="WD 1"
FT REPEAT 361..406
FT /note="WD 2"
FT REPEAT 410..448
FT /note="WD 3"
FT REPEAT 549..590
FT /note="WD 4"
FT REPEAT 638..683
FT /note="WD 5"
FT REGION 1..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 113..402
FT /note="Sufficient for interaction with EIF3E"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03001"
FT REGION 159..263
FT /note="Sufficient for interaction with EIF3J"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03001"
FT COMPBIAS 68..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P55884, ECO:0000255|HAMAP-
FT Rule:MF_03001"
FT MOD_RES 31
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:15345747"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 72
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 74
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:17622165,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:17622165, ECO:0007744|PubMed:18630941,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55884, ECO:0000255|HAMAP-
FT Rule:MF_03001"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55884, ECO:0000255|HAMAP-
FT Rule:MF_03001"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55884, ECO:0000255|HAMAP-
FT Rule:MF_03001"
FT MOD_RES 198
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P55884"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55884, ECO:0000255|HAMAP-
FT Rule:MF_03001"
FT MOD_RES 277
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P55884"
FT MOD_RES 353
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P55884"
SQ SEQUENCE 803 AA; 91370 MW; D770AC70BFE9832F CRC64;
MQDAENVAVP EAAEERAEPA RQQPASESPP TDEAAGSGGS EVGQTEDAEE DAEAGPEPEV
RAKPAAQSEE ETATSPAASP TPQSAERSPS QEPSAPGKAE AVGEQARGHP SAGAEEEGGS
DGSAAEAEPR ALENGEADEP SFSDPEDFVD DVSEEELLGD VLKDRPQEAD GIDSVIVVDN
VPQVGPDRLE KLKNVIHKIF SKFGKIINDY YPEEDGKTKG YIFLEYASPA HAVDAVKNAD
GYKLDKQHTF RVNLFTDFDK YMTISDEWDI PEKQPFKDLG NLRYWLEEAE CRDQYSVIFE
SGDRTSIFWN DVKDPVSIEE RARWTETYVR WSPKGTYLAT FHQRGIALWG GDKFKQIQRF
SHQGVQLIDF SPCERYLVTF SPLMDTQDDP QAIIIWDILT GHKKRGFHCE SSAHWPIFKW
SHDGKFFARM TLDTLSIYET PSMGLLDKKS LKISGIKDFS WSPGGNIIAF WVPEDKDIPA
RVTLMQLPTR QEIRVRNLFN VVDCKLHWQK NGDYLCVKVD RTPKGTQGVV TNFEIFRMRE
KQVPVDVVEM KETIIAFAWE PNGSKFAVLH GEAPRISVSF YHVKSNGKIE LIKMFDKQQA
NTIFWSPQGQ FVVLAGLRSM NGALAFVDTS DCTVMNIAEH YMASDVEWDP TGRYVVTSVS
WWSHKVDNAY WLWTFQGRLL QKNNKDRFCQ LLWRPRPPTL LSQDQIKQIK KDLKKYSKIF
EQKDRLSQSK ASKELVERRR TMMEDFRQYR KMAQELYMKQ KNERLELRGG VDTDELDSNV
DDWEEETIEF FVTEEVIPLG SQE
