IF2A_MOUSE
ID IF2A_MOUSE Reviewed; 315 AA.
AC Q6ZWX6; Q3TIQ0;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Eukaryotic translation initiation factor 2 subunit 1;
DE AltName: Full=Eukaryotic translation initiation factor 2 subunit alpha;
DE Short=eIF-2-alpha;
DE Short=eIF-2A;
DE Short=eIF-2alpha;
GN Name=Eif2s1 {ECO:0000312|MGI:MGI:95299}; Synonyms=Eif2a;
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;
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 MRNA].
RC STRAIN=Czech II, and FVB/N; TISSUE=Eye, Kidney, 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 [3]
RP PHOSPHORYLATION AT SER-52.
RC STRAIN=BALB/cJ;
RX PubMed=10504407; DOI=10.1046/j.1432-1327.1999.00780.x;
RA Berlanga J.J., Santoyo J., de Haro C.;
RT "Characterization of a mammalian homolog of the GCN2 eukaryotic initiation
RT factor 2alpha kinase.";
RL Eur. J. Biochem. 265:754-762(1999).
RN [4]
RP PHOSPHORYLATION AT SER-52, AND ACTIVITY REGULATION.
RX PubMed=11106749; DOI=10.1016/s1097-2765(00)00108-8;
RA Harding H.P., Novoa I., Zhang Y., Zeng H., Wek R., Schapira M., Ron D.;
RT "Regulated translation initiation controls stress-induced gene expression
RT in mammalian cells.";
RL Mol. Cell 6:1099-1108(2000).
RN [5]
RP PHOSPHORYLATION, AND ACTIVITY REGULATION.
RX PubMed=12176355; DOI=10.1016/s0960-9822(02)01037-0;
RA Deng J., Harding H.P., Raught B., Gingras A.C., Berlanga J.J., Scheuner D.,
RA Kaufman R.J., Ron D., Sonenberg N.;
RT "Activation of GCN2 in UV-irradiated cells inhibits translation.";
RL Curr. Biol. 12:1279-1286(2002).
RN [6]
RP PHOSPHORYLATION AT SER-52.
RX PubMed=15213227; DOI=10.1074/jbc.m404559200;
RA Anthony T.G., McDaniel B.J., Byerley R.L., McGrath B.C., Cavener D.R.,
RA McNurlan M.A., Wek R.C.;
RT "Preservation of liver protein synthesis during dietary leucine deprivation
RT occurs at the expense of skeletal muscle mass in mice deleted for eIF2
RT kinase GCN2.";
RL J. Biol. Chem. 279:36553-36561(2004).
RN [7]
RP PHOSPHORYLATION, ACTIVITY REGULATION, AND FUNCTION.
RX PubMed=15277680; DOI=10.1073/pnas.0400541101;
RA Vattem K.M., Wek R.C.;
RT "Reinitiation involving upstream ORFs regulates ATF4 mRNA translation in
RT mammalian cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:11269-11274(2004).
RN [8]
RP PHOSPHORYLATION AT SER-52.
RX PubMed=16054071; DOI=10.1016/j.cmet.2005.03.004;
RA Maurin A.C., Jousse C., Averous J., Parry L., Bruhat A., Cherasse Y.,
RA Zeng H., Zhang Y., Harding H.P., Ron D., Fafournoux P.;
RT "The GCN2 kinase biases feeding behavior to maintain amino acid homeostasis
RT in omnivores.";
RL Cell Metab. 1:273-277(2005).
RN [9]
RP IDENTIFICATION IN AN EIF2 COMPLEX WITH CELF1; EIF2S2; CALR; CALR3; HSPA5
RP AND HSP90B1.
RX PubMed=16931514; DOI=10.1074/jbc.m605701200;
RA Timchenko L.T., Salisbury E., Wang G.-L., Nguyen H., Albrecht J.H.,
RA Hershey J.W., Timchenko N.A.;
RT "Age-specific CUGBP1-eIF2 complex increases translation of CCAAT/enhancer-
RT binding protein beta in old liver.";
RL J. Biol. Chem. 281:32806-32819(2006).
RN [10]
RP PHOSPHORYLATION, ACTIVITY REGULATION, AND FUNCTION.
RX PubMed=19131336; DOI=10.1074/jbc.m806735200;
RA Lee Y.Y., Cevallos R.C., Jan E.;
RT "An upstream open reading frame regulates translation of GADD34 during
RT cellular stresses that induce eIF2alpha phosphorylation.";
RL J. Biol. Chem. 284:6661-6673(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-158, AND IDENTIFICATION BY
RP 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).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=19861488; DOI=10.1530/rep-09-0373;
RA Yamaji M., Tanaka T., Shigeta M., Chuma S., Saga Y., Saitou M.;
RT "Functional reconstruction of NANOS3 expression in the germ cell lineage by
RT a novel transgenic reporter reveals distinct subcellular localizations of
RT NANOS3.";
RL Reproduction 139:381-393(2010).
RN [13]
RP PHOSPHORYLATION, ACTIVITY REGULATION, AND FUNCTION.
RX PubMed=21285359; DOI=10.1074/jbc.m110.216093;
RA Palam L.R., Baird T.D., Wek R.C.;
RT "Phosphorylation of eIF2 facilitates ribosomal bypass of an inhibitory
RT upstream ORF to enhance CHOP translation.";
RL J. Biol. Chem. 286:10939-10949(2011).
CC -!- FUNCTION: Functions in the early steps of protein synthesis by forming
CC a ternary complex with GTP and initiator tRNA (PubMed:15277680,
CC PubMed:19131336). This complex binds to a 40S ribosomal subunit,
CC followed by mRNA binding to form a 43S pre-initiation complex
CC (PubMed:15277680, PubMed:19131336). Junction of the 60S ribosomal
CC subunit to form the 80S initiation complex is preceded by hydrolysis of
CC the GTP bound to eIF-2 and release of an eIF-2-GDP binary complex
CC (PubMed:15277680, PubMed:19131336). In order for eIF-2 to recycle and
CC catalyze another round of initiation, the GDP bound to eIF-2 must
CC exchange with GTP by way of a reaction catalyzed by eIF-2B
CC (PubMed:15277680, PubMed:19131336). EIF2S1/eIF-2-alpha is a key
CC component of the integrated stress response (ISR), required for
CC adaptation to various stress: phosphorylation by metabolic-stress
CC sensing protein kinases (EIF2AK1/HRI, EIF2AK2/PKR, EIF2AK3/PERK and
CC EIF2AK4/GCN2) in response to stress converts EIF2S1/eIF-2-alpha in a
CC global protein synthesis inhibitor, leading to a attenuation of cap-
CC dependent translation, while concomitantly initiating the preferential
CC translation of ISR-specific mRNAs, such as the transcriptional
CC activators ATF4 and QRICH1, and hence allowing ATF4- and QRICH1-
CC mediated reprogramming (PubMed:15277680, PubMed:21285359).
CC {ECO:0000269|PubMed:15277680, ECO:0000269|PubMed:19131336,
CC ECO:0000269|PubMed:21285359}.
CC -!- ACTIVITY REGULATION: Activity is regulated by phosphorylation at Ser-49
CC and Ser-52, which stabilizes the eIF-2/GDP/eIF-2B complex and prevents
CC the eIF-2B-mediated exchange of GDP for GTP, thereby preventing the
CC formation of the 43S pre-initiation complex (PIC) (PubMed:11106749,
CC PubMed:12176355, PubMed:15277680, PubMed:19131336, PubMed:21285359).
CC This results in the global attenuation of 5' cap-dependent protein
CC synthesis and concomitant translation of ISR-specific mRNAs that
CC contain a short upstream open reading frame (uORF) in their 5' UTR,
CC such as ATF4, ATF5, DDIT3/CHOP and PPP1R15A/GADD34 (PubMed:15277680,
CC PubMed:19131336, PubMed:21285359). {ECO:0000269|PubMed:11106749,
CC ECO:0000269|PubMed:12176355, ECO:0000269|PubMed:15277680,
CC ECO:0000269|PubMed:19131336, ECO:0000269|PubMed:21285359}.
CC -!- SUBUNIT: Heterotrimer composed of an alpha, a beta and a gamma chain
CC (By similarity). Component of an EIF2 complex at least composed of
CC CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5
CC (PubMed:16931514). Interaction with METAP2 protects EIF2S1 from
CC inhibitory phosphorylation (By similarity). Interacts with ABCF1 (By
CC similarity). Associates with ribosomes (By similarity). Interacts with
CC DDX3X in an RNA-independent manner (By similarity).
CC {ECO:0000250|UniProtKB:P05198, ECO:0000250|UniProtKB:P68101,
CC ECO:0000269|PubMed:16931514}.
CC -!- INTERACTION:
CC Q6ZWX6; Q9Z2R9: Eif2ak1; NbExp=6; IntAct=EBI-1202234, EBI-642878;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, Stress granule
CC {ECO:0000269|PubMed:19861488}. Note=Colocalizes with NANOS3 in the
CC stress granules. {ECO:0000269|PubMed:19861488}.
CC -!- PTM: Phosphorylation at Ser-49 and Ser-52 stabilizes the eIF-2/GDP/eIF-
CC 2B complex and prevents GDP/GTP exchange reaction, thus impairing the
CC recycling of eIF-2 between successive rounds of initiation and leading
CC to global inhibition of translation, while concomitantly initiating the
CC preferential translation of integrated stress response (ISR)-specific
CC mRNAs (PubMed:10504407, PubMed:11106749, PubMed:12176355,
CC PubMed:15213227, PubMed:15277680, PubMed:16054071, PubMed:19131336,
CC PubMed:21285359). Substrate for at least 4 kinases: EIF2AK1/HRI,
CC EIF2AK2/PKR, EIF2AK3/PERK and EIF2AK4/GCN2 (PubMed:10504407,
CC PubMed:11106749, PubMed:12176355, PubMed:15213227, PubMed:15277680,
CC PubMed:16054071). Phosphorylated; phosphorylation on Ser-52 by the
CC EIF2AK4/GCN2 protein kinase occurs in response to amino acid starvation
CC and UV irradiation (PubMed:10504407, PubMed:12176355, PubMed:15213227,
CC PubMed:16054071). {ECO:0000269|PubMed:10504407,
CC ECO:0000269|PubMed:11106749, ECO:0000269|PubMed:12176355,
CC ECO:0000269|PubMed:15213227, ECO:0000269|PubMed:15277680,
CC ECO:0000269|PubMed:16054071, ECO:0000269|PubMed:19131336,
CC ECO:0000269|PubMed:21285359}.
CC -!- SIMILARITY: Belongs to the eIF-2-alpha family. {ECO:0000305}.
CC -!- CAUTION: This gene should not be confused with EIF2A, with which it
CC shares the alias EIF2A. Although both of these proteins function in
CC binding initiator tRNA to the 40S ribosomal subunit, the eIF2 complex
CC requires GTP, whereas the EIF2A protein does so in a codon-dependent
CC manner. {ECO:0000305}.
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DR EMBL; AK010592; BAB27049.1; -; mRNA.
DR EMBL; AK143499; BAE25400.1; -; mRNA.
DR EMBL; AK167763; BAE39796.1; -; mRNA.
DR EMBL; BC005463; AAH05463.1; -; mRNA.
DR EMBL; BC016448; AAH16448.1; -; mRNA.
DR EMBL; BC016497; AAH16497.1; -; mRNA.
DR CCDS; CCDS26003.1; -.
DR RefSeq; NP_080390.1; NM_026114.3.
DR AlphaFoldDB; Q6ZWX6; -.
DR BMRB; Q6ZWX6; -.
DR SMR; Q6ZWX6; -.
DR BioGRID; 199412; 38.
DR IntAct; Q6ZWX6; 13.
DR MINT; Q6ZWX6; -.
DR STRING; 10090.ENSMUSP00000071214; -.
DR ChEMBL; CHEMBL1770036; -.
DR iPTMnet; Q6ZWX6; -.
DR PhosphoSitePlus; Q6ZWX6; -.
DR SwissPalm; Q6ZWX6; -.
DR EPD; Q6ZWX6; -.
DR jPOST; Q6ZWX6; -.
DR MaxQB; Q6ZWX6; -.
DR PaxDb; Q6ZWX6; -.
DR PeptideAtlas; Q6ZWX6; -.
DR PRIDE; Q6ZWX6; -.
DR ProteomicsDB; 267195; -.
DR Antibodypedia; 3181; 924 antibodies from 39 providers.
DR DNASU; 13665; -.
DR Ensembl; ENSMUST00000071230; ENSMUSP00000071214; ENSMUSG00000021116.
DR GeneID; 13665; -.
DR KEGG; mmu:13665; -.
DR UCSC; uc007nzk.1; mouse.
DR CTD; 1965; -.
DR MGI; MGI:95299; Eif2s1.
DR VEuPathDB; HostDB:ENSMUSG00000021116; -.
DR eggNOG; KOG2916; Eukaryota.
DR GeneTree; ENSGT00390000007015; -.
DR HOGENOM; CLU_033458_0_0_1; -.
DR InParanoid; Q6ZWX6; -.
DR OMA; DVNEHQR; -.
DR OrthoDB; 1093186at2759; -.
DR PhylomeDB; Q6ZWX6; -.
DR TreeFam; TF101502; -.
DR Reactome; R-MMU-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-MMU-381042; PERK regulates gene expression.
DR Reactome; R-MMU-382556; ABC-family proteins mediated transport.
DR Reactome; R-MMU-72649; Translation initiation complex formation.
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 Reactome; R-MMU-72731; Recycling of eIF2:GDP.
DR BioGRID-ORCS; 13665; 26 hits in 72 CRISPR screens.
DR ChiTaRS; Eif2s1; mouse.
DR PRO; PR:Q6ZWX6; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q6ZWX6; protein.
DR Bgee; ENSMUSG00000021116; Expressed in ectoplacental cone and 259 other tissues.
DR Genevisible; Q6ZWX6; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IBA:GO_Central.
DR GO; GO:0005850; C:eukaryotic translation initiation factor 2 complex; ISO:MGI.
DR GO; GO:0005851; C:eukaryotic translation initiation factor 2B complex; ISS:UniProtKB.
DR GO; GO:0097451; C:glial limiting end-foot; ISO:MGI.
DR GO; GO:0043614; C:multi-eIF complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0044207; C:translation initiation ternary complex; ISO:MGI.
DR GO; GO:0043022; F:ribosome binding; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003743; F:translation initiation factor activity; ISS:UniProtKB.
DR GO; GO:0007568; P:aging; ISO:MGI.
DR GO; GO:0034198; P:cellular response to amino acid starvation; IDA:UniProtKB.
DR GO; GO:0034605; P:cellular response to heat; ISO:MGI.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:ARUK-UCL.
DR GO; GO:0034644; P:cellular response to UV; IDA:UniProtKB.
DR GO; GO:1905098; P:negative regulation of guanyl-nucleotide exchange factor activity; ISO:MGI.
DR GO; GO:0032057; P:negative regulation of translational initiation in response to stress; IDA:UniProtKB.
DR GO; GO:0036499; P:PERK-mediated unfolded protein response; ISS:UniProtKB.
DR GO; GO:1901216; P:positive regulation of neuron death; ISO:MGI.
DR GO; GO:2000676; P:positive regulation of type B pancreatic cell apoptotic process; ISO:MGI.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:MGI.
DR GO; GO:0043558; P:regulation of translational initiation in response to stress; IDA:MGI.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IDA:UniProtKB.
DR GO; GO:1990737; P:response to manganese-induced endoplasmic reticulum stress; IEA:Ensembl.
DR GO; GO:0034063; P:stress granule assembly; IMP:ARUK-UCL.
DR GO; GO:0006412; P:translation; IDA:MGI.
DR CDD; cd04452; S1_IF2_alpha; 1.
DR Gene3D; 1.10.150.190; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.70.1130; -; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR022967; S1_dom.
DR InterPro; IPR003029; S1_domain.
DR InterPro; IPR044126; S1_IF2_alpha.
DR InterPro; IPR024055; TIF2_asu_C.
DR InterPro; IPR024054; TIF2_asu_middle_sf.
DR InterPro; IPR011488; TIF_2_asu.
DR PANTHER; PTHR10602; PTHR10602; 1.
DR Pfam; PF07541; EIF_2_alpha; 1.
DR Pfam; PF00575; S1; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF110993; SSF110993; 1.
DR SUPFAM; SSF116742; SSF116742; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR PROSITE; PS50126; S1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Initiation factor; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; RNA-binding;
KW Translation regulation.
FT CHAIN 1..315
FT /note="Eukaryotic translation initiation factor 2 subunit
FT 1"
FT /id="PRO_0000137383"
FT DOMAIN 17..88
FT /note="S1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT REGION 292..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..315
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 49
FT /note="Phosphoserine; by HRI"
FT /evidence="ECO:0000250|UniProtKB:P83268"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:10504407,
FT ECO:0000269|PubMed:11106749, ECO:0000269|PubMed:15213227,
FT ECO:0000269|PubMed:16054071"
FT MOD_RES 141
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P05198"
FT MOD_RES 158
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 279
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P05198"
FT MOD_RES 281
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P05198"
SQ SEQUENCE 315 AA; 36108 MW; 018480B89175D118 CRC64;
MPGLSCRFYQ HKFPEVEDVV MVNVRSIAEM GAYVSLLEYN NIEGMILLSE LSRRRIRSIN
KLIRIGRNEC VVVIRVDKEK GYIDLSKRRV SPEEAIKCED KFTKSKTVYS ILRHVAEVLE
YTKDEQLESL FQRTAWVFDD KYKRPGYGAY DAFKHAVSDP SILDSLDLNE DEREVLINNI
NRRLTPQAVK IRADIEVACY GYEGIDAVKE ALRAGLNCST ETMPIKINLI APPRYVMTTT
TLERTEGLSV LNQAMAVIKE KIEEKRGVFN VQMEPKVVTD TDETELARQL ERLERENAEV
DGDDDAEEME AKAED
