IF2P_MOUSE
ID IF2P_MOUSE Reviewed; 1216 AA.
AC Q05D44; Q3SYI4; Q3TQJ8; Q3UL37; Q3UM39; Q6PAI0; Q8CFF4; Q8CGD6;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Eukaryotic translation initiation factor 5B;
DE Short=eIF-5B;
DE EC=3.6.5.3;
DE AltName: Full=Translation initiation factor IF-2;
GN Name=Eif5b; Synonyms=If2;
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 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-771.
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and Mammary gland;
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] OF 1-402.
RC STRAIN=FVB/N; TISSUE=Limb, and 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 SUBCELLULAR LOCATION.
RX PubMed=12426392; DOI=10.1093/emboj/cdf613;
RA Bohnsack M.T., Regener K., Schwappach B., Saffrich R., Paraskeva E.,
RA Hartmann E., Goerlich D.;
RT "Exp5 exports eEF1A via tRNA from nuclei and synergizes with other
RT transport pathways to confine translation to the cytoplasm.";
RL EMBO J. 21:6205-6215(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215, 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187 AND SER-191, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114; SER-137; SER-139;
RP SER-187; SER-191 AND SER-215, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137 AND SER-139, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165 AND SER-215, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114; SER-137; SER-139 AND
RP SER-215, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-107; SER-108; SER-114;
RP SER-137; SER-139; SER-145; SER-183; SER-184; SER-187; SER-191; SER-209;
RP SER-215 AND SER-223, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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: Plays a role in translation initiation. Translational GTPase
CC that catalyzes the joining of the 40S and 60S subunits to form the 80S
CC initiation complex with the initiator methionine-tRNA in the P-site
CC base paired to the start codon. GTP binding and hydrolysis induces
CC conformational changes in the enzyme that renders it active for
CC productive interactions with the ribosome. The release of the enzyme
CC after formation of the initiation complex is a prerequisite to form
CC elongation-competent ribosomes. {ECO:0000250|UniProtKB:P39730}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.3;
CC Evidence={ECO:0000250|UniProtKB:P39730};
CC -!- COFACTOR:
CC Name=a monovalent cation; Xref=ChEBI:CHEBI:60242;
CC Evidence={ECO:0000250|UniProtKB:G0S8G9};
CC Note=Binds 1 monovalent cation per monomer in the active site.
CC Structural cofactor that stabilizes the GTP-bound 'on' state. May also
CC act as a transition state stabilizer of the hydrolysis reaction.
CC {ECO:0000250|UniProtKB:G0S8G9};
CC -!- SUBUNIT: Interacts with ANXA5 in a calcium and phospholipid-dependent
CC manner. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12426392}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH18347.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH37150.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH40746.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH60288.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AC114583; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK145146; BAE26259.1; -; mRNA.
DR EMBL; AK145732; BAE26614.1; -; mRNA.
DR EMBL; AK163527; BAE37384.1; -; mRNA.
DR EMBL; BC018347; AAH18347.1; ALT_SEQ; mRNA.
DR EMBL; BC037150; AAH37150.1; ALT_SEQ; mRNA.
DR EMBL; BC040746; AAH40746.1; ALT_SEQ; mRNA.
DR EMBL; BC060288; AAH60288.1; ALT_SEQ; mRNA.
DR CCDS; CCDS35544.1; -.
DR RefSeq; NP_938045.2; NM_198303.2.
DR AlphaFoldDB; Q05D44; -.
DR SMR; Q05D44; -.
DR BioGRID; 230580; 22.
DR IntAct; Q05D44; 2.
DR MINT; Q05D44; -.
DR STRING; 10090.ENSMUSP00000027252; -.
DR iPTMnet; Q05D44; -.
DR PhosphoSitePlus; Q05D44; -.
DR SwissPalm; Q05D44; -.
DR EPD; Q05D44; -.
DR jPOST; Q05D44; -.
DR MaxQB; Q05D44; -.
DR PaxDb; Q05D44; -.
DR PeptideAtlas; Q05D44; -.
DR PRIDE; Q05D44; -.
DR ProteomicsDB; 267211; -.
DR Antibodypedia; 32818; 180 antibodies from 27 providers.
DR DNASU; 226982; -.
DR Ensembl; ENSMUST00000027252; ENSMUSP00000027252; ENSMUSG00000026083.
DR GeneID; 226982; -.
DR KEGG; mmu:226982; -.
DR UCSC; uc007aso.1; mouse.
DR CTD; 9669; -.
DR MGI; MGI:2441772; Eif5b.
DR VEuPathDB; HostDB:ENSMUSG00000026083; -.
DR eggNOG; KOG1144; Eukaryota.
DR GeneTree; ENSGT00940000162583; -.
DR HOGENOM; CLU_002656_0_1_1; -.
DR InParanoid; Q05D44; -.
DR OMA; RDVMMAG; -.
DR OrthoDB; 1124591at2759; -.
DR PhylomeDB; Q05D44; -.
DR TreeFam; TF101535; -.
DR Reactome; R-MMU-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR BioGRID-ORCS; 226982; 20 hits in 74 CRISPR screens.
DR ChiTaRS; Eif5b; mouse.
DR PRO; PR:Q05D44; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q05D44; protein.
DR Bgee; ENSMUSG00000026083; Expressed in embryonic post-anal tail and 253 other tissues.
DR Genevisible; Q05D44; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003743; F:translation initiation factor activity; ISO:MGI.
DR GO; GO:0006446; P:regulation of translational initiation; ISO:MGI.
DR GO; GO:0006413; P:translational initiation; IBA:GO_Central.
DR Gene3D; 3.40.50.10050; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR015760; TIF_IF2.
DR InterPro; IPR023115; TIF_IF2_dom3.
DR InterPro; IPR036925; TIF_IF2_dom3_sf.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR PANTHER; PTHR43381; PTHR43381; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF11987; IF-2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52156; SSF52156; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; GTP-binding; Hydrolase; Initiation factor; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..1216
FT /note="Eukaryotic translation initiation factor 5B"
FT /id="PRO_0000354071"
FT DOMAIN 625..842
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 1..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 634..641
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 659..663
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 698..701
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 752..755
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 820..822
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..338
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..420
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..458
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..506
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..525
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..564
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..604
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 634..641
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
FT MOD_RES 107
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:17622165, ECO:0007744|PubMed:21183079"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:17622165, ECO:0007744|PubMed:21183079"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 300
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
FT MOD_RES 437
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
FT MOD_RES 497
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
FT MOD_RES 544
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B2GUV7"
FT MOD_RES 553
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B2GUV7"
FT MOD_RES 556
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
FT MOD_RES 584
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
FT MOD_RES 585
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
FT MOD_RES 587
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
FT MOD_RES 591
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
FT MOD_RES 1164
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
FT CONFLICT 121
FT /note="D -> N (in Ref. 2; BAE26259)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="G -> C (in Ref. 2; BAE26259)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="M -> L (in Ref. 2; BAE26259)"
FT /evidence="ECO:0000305"
FT CONFLICT 302
FT /note="A -> V (in Ref. 2; BAE26259)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1216 AA; 137616 MW; 38D1C21648E4EAEC CRC64;
MGKKQKNKSE DSTKDDTDLG ALAAEIEGAG AAKEQEPQKS KGKKKKEKKK QDFDENDILR
ELEELSLEAQ GIRADRDAAA VKPTENNEEE SASKQDKKKK GQKGKKTSFD ENDSEELEDK
DSKSKKTARP NSEAPLSGSE DADDSNKLSK KGKKAQKSTK KRDGSEEDED NSKRSKERSR
VNSSGESGGE SDEFLQSRKG QKKNQKNKSV PTVDSGNEDD DSSFKIKTVA QKKAEKKERE
KKKRDEEKAK LRKMKEKEEL EKGKKEQSKQ REPQKRPEEE VLTLRGTPDT GAASEEKGDT
AAALEDDNEG DKKKKDKKKK KTEKDEKEKE KKKGPSKSTV KAIQEALAKL KEEEERQKRE
EEERIKRLEE LEAKRKEEER LEQEKRERKK QKEKERKERL KKEGKLLTKS QREARARAEV
TLRHLQAQGV EVPSKDSLPK KRPVYEDKKK KKTPQQLESK EVSETLEISA PVEAVDQGGP
EKEETPPSVE PEEEEDTEDA GLDDWEAMAS DEEREKEGNM IHIEVEENPE EEEEEEEEEE
EEESEDEEEE GDSEGSDGDE EDCKLSDEKD SGKAGDTKPS KDASSDSEYD SDDDRTKEER
AYDKAKRRIE KRRLEHGKNV NTEKLRAPII CVLGHVDTGK TKILDKLRHT HVQDGEAGGI
TQQIGATNVP LEAINEQTKM IKNFDRENVR IPGMLIIDTP GHESFSNLRN RGSSLCDIAI
LVVDIMHGLE PQTIESINIL KSKKCPFIVA LNKIDRLYDW KKSPDSDVAV TLKKQKKNTK
DEFEERAKAI IVEFAQQGLN AALFYENKDP RTFVSLVPTS AHTGDGMGSL IYLLVELTQT
MLSKRLAHCE ELRAQVMEVK ALPGMGTTID VILINGRLKE GDTIIVPGVE GPIVTQIRGL
LLPPPMKELR VKNQYEKHKE VEAAQGVKIL GKDLEKTLAG LPLLVAYKDD EIPVLKDELI
HELKQTLNAI KLEEKGVYVQ ASTLGSLEAL LEFLKTSEVP YAGINIGPVH KKDVMKASVM
LEHDPQYAVI LAFDVRIERD AQEMADSLGV RIFSAEIIYH LFDAFTKYRQ DYKKQKQEEF
KHIAVFPCKM KILPQYIFNS RDPIVIGVTV EAGQVKQGTP MCVPSKNFVD IGIVTSIEIN
HKQVDVAKKG QEVCVKIEPI PGESPKMFGR HFEATDILVS KISRQSIDAL KDWFRDEMQK
SDWQLIVELK KVFEII
