SET_MOUSE
ID SET_MOUSE Reviewed; 289 AA.
AC Q9EQU5; A2BE95; Q9CY82; Q9D0A9; Q9Z181;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Protein SET;
DE AltName: Full=Phosphatase 2A inhibitor I2PP2A;
DE Short=I-2PP2A;
DE AltName: Full=Template-activating factor I;
DE Short=TAF-I;
GN Name=Set;
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] (ISOFORM 1).
RC STRAIN=C57BL/6 X DBA/2; TISSUE=Blastocyst;
RX PubMed=11078917; DOI=10.1016/s0304-3835(00)00598-x;
RA Fukukawa C., Shima H., Tamura N., Ogawa K., Kikuchi K.;
RT "Up-regulation of I-2PP2A/SET gene expression in rat primary hepatomas and
RT regenerating livers.";
RL Cancer Lett. 161:89-95(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Czech II; 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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-222 (ISOFORM 2).
RC TISSUE=Embryo;
RX PubMed=11231286; DOI=10.1046/j.1432-1327.2001.02000.x;
RA Minakuchi M., Kakazu N., Gorrin-Rivas M.J., Abe T., Copeland T.D., Ueda K.,
RA Adachi Y.;
RT "Identification and characterization of SEB, a novel protein that binds to
RT the acute undifferentiated leukemia-associated protein SET.";
RL Eur. J. Biochem. 268:1340-1351(2001).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-145, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [7]
RP GLYCYLATION.
RX PubMed=19524510; DOI=10.1016/j.cell.2009.05.020;
RA Rogowski K., Juge F., van Dijk J., Wloga D., Strub J.-M., Levilliers N.,
RA Thomas D., Bre M.-H., Van Dorsselaer A., Gaertig J., Janke C.;
RT "Evolutionary divergence of enzymatic mechanisms for posttranslational
RT polyglycylation.";
RL Cell 137:1076-1087(2009).
RN [8]
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).
RN [9]
RP CLEAVAGE OF INITIATOR METHIONINE, METHYLATION AT ALA-2, AND MUTAGENESIS OF
RP LYS-4.
RX PubMed=20668449; DOI=10.1038/nature09343;
RA Tooley C.E., Petkowski J.J., Muratore-Schroeder T.L., Balsbaugh J.L.,
RA Shabanowitz J., Sabat M., Minor W., Hunt D.F., Macara I.G.;
RT "NRMT is an alpha-N-methyltransferase that methylates RCC1 and
RT retinoblastoma protein.";
RL Nature 466:1125-1128(2010).
RN [10]
RP INTERACTION WITH CHTOP.
RX PubMed=22872859; DOI=10.1074/mcp.m112.017194;
RA Fanis P., Gillemans N., Aghajanirefah A., Pourfarzad F., Demmers J.,
RA Esteghamat F., Vadlamudi R.K., Grosveld F., Philipsen S., van Dijk T.B.;
RT "Five friends of methylated chromatin target of protein-arginine-
RT methyltransferase[prmt]-1 (chtop), a complex linking arginine methylation
RT to desumoylation.";
RL Mol. Cell. Proteomics 11:1263-1273(2012).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-23 AND LYS-67, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Multitasking protein, involved in apoptosis, transcription,
CC nucleosome assembly and histone chaperoning. Isoform 2 anti-apoptotic
CC activity is mediated by inhibition of the GZMA-activated DNase, NME1.
CC In the course of cytotoxic T-lymphocyte (CTL)-induced apoptosis, GZMA
CC cleaves SET, disrupting its binding to NME1 and releasing NME1
CC inhibition. Isoform 1 and isoform 2 are potent inhibitors of protein
CC phosphatase 2A. Isoform 1 and isoform 2 inhibit EP300/CREBBP and PCAF-
CC mediated acetylation of histones (HAT) and nucleosomes, most probably
CC by masking the accessibility of lysines of histones to the acetylases.
CC The predominant target for inhibition is histone H4. HAT inhibition
CC leads to silencing of HAT-dependent transcription and prevents active
CC demethylation of DNA. Both isoforms stimulate DNA replication of the
CC adenovirus genome complexed with viral core proteins; however, isoform
CC 2 specific activity is higher (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Headphone-shaped homodimer. Isoform 1 and isoform 2 interact
CC directly with each other and with ANP32A within the tripartite INHAT
CC (inhibitor of acetyltransferases) complex. Isoform 1 and isoform 2
CC interact also with histones. Isoform 2 is a omponent of the SET
CC complex, composed of at least ANP32A, APEX1, HMGB2, NME1, SET and
CC TREX1, but not NME2 or TREX2. Within this complex, directly interacts
CC with ANP32A, NME1, HMGB2 and TREX1; the interaction with ANP32A is
CC enhanced after cleavage. Interacts with APBB1, CHTOP, SETBP1, SGO1.
CC {ECO:0000269|PubMed:22872859}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Endoplasmic
CC reticulum {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Note=In
CC the cytoplasm, found both in the cytosol and associated with the
CC endoplasmic reticulum. The SET complex is associated with the
CC endoplasmic reticulum. Following CTL attack and cleavage by GZMA, moves
CC rapidly to the nucleus, where it is found in the nucleoplasm, avoiding
CC the nucleolus. Similar translocation to the nucleus is also observed
CC for lymphocyte-activated killer cells after the addition of calcium (By
CC similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=TAF-I alpha;
CC IsoId=Q9EQU5-1; Sequence=Displayed;
CC Name=2; Synonyms=TAF-I beta;
CC IsoId=Q9EQU5-2; Sequence=VSP_009869;
CC Name=3;
CC IsoId=Q9EQU5-3; Sequence=VSP_009870, VSP_009871;
CC -!- DOMAIN: A long alpha helix in the N-terminus mediates dimerization,
CC while the earmuff domain is responsible for core histone and dsDNA
CC binding. The C-terminal acidic domain mediates the inhibition of
CC histone acetyltransferases and is required for the DNA replication
CC stimulatory activity (By similarity). {ECO:0000250}.
CC -!- PTM: Some glutamate residues are glycylated by TTLL8. This modification
CC occurs exclusively on glutamate residues and results in a glycine chain
CC on the gamma-carboxyl group.
CC -!- PTM: N-terminus of isoform 1 is methylated by METTL11A/NTM1. Mainly
CC trimethylated. {ECO:0000269|PubMed:20668449}.
CC -!- PTM: [Isoform 2]: Cleaved after Lys-176 by GZMA. The cleavage inhibits
CC its nucleosome assembly activity and disrupts the inhibition on NME1
CC (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the nucleosome assembly protein (NAP) family.
CC {ECO:0000305}.
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DR EMBL; AB044937; BAB20793.1; -; mRNA.
DR EMBL; AK011630; BAB27745.1; -; mRNA.
DR EMBL; AK019960; BAB31936.1; -; mRNA.
DR EMBL; BX005298; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC018255; AAH18255.1; -; mRNA.
DR EMBL; AB015613; BAA34736.1; -; mRNA.
DR CCDS; CCDS15866.1; -. [Q9EQU5-1]
DR CCDS; CCDS57162.1; -. [Q9EQU5-2]
DR RefSeq; NP_001191804.1; NM_001204875.1. [Q9EQU5-2]
DR RefSeq; NP_076360.1; NM_023871.4. [Q9EQU5-1]
DR AlphaFoldDB; Q9EQU5; -.
DR SMR; Q9EQU5; -.
DR BioGRID; 207808; 112.
DR IntAct; Q9EQU5; 71.
DR STRING; 10090.ENSMUSP00000099930; -.
DR iPTMnet; Q9EQU5; -.
DR PhosphoSitePlus; Q9EQU5; -.
DR CPTAC; non-CPTAC-3874; -.
DR EPD; Q9EQU5; -.
DR jPOST; Q9EQU5; -.
DR MaxQB; Q9EQU5; -.
DR PaxDb; Q9EQU5; -.
DR PeptideAtlas; Q9EQU5; -.
DR PRIDE; Q9EQU5; -.
DR ProteomicsDB; 261172; -. [Q9EQU5-1]
DR ProteomicsDB; 261173; -. [Q9EQU5-2]
DR ProteomicsDB; 261174; -. [Q9EQU5-3]
DR DNASU; 56086; -.
DR Ensembl; ENSMUST00000067996; ENSMUSP00000070002; ENSMUSG00000054766. [Q9EQU5-2]
DR Ensembl; ENSMUST00000102866; ENSMUSP00000099930; ENSMUSG00000054766. [Q9EQU5-1]
DR GeneID; 56086; -.
DR KEGG; mmu:56086; -.
DR UCSC; uc008jaw.2; mouse. [Q9EQU5-1]
DR UCSC; uc008jax.2; mouse. [Q9EQU5-3]
DR UCSC; uc008jay.2; mouse. [Q9EQU5-2]
DR CTD; 6418; -.
DR MGI; MGI:1860267; Set.
DR VEuPathDB; HostDB:ENSMUSG00000054766; -.
DR eggNOG; KOG1508; Eukaryota.
DR GeneTree; ENSGT00940000154891; -.
DR HOGENOM; CLU_051687_4_0_1; -.
DR InParanoid; Q9EQU5; -.
DR OMA; WPVALMN; -.
DR PhylomeDB; Q9EQU5; -.
DR TreeFam; TF313386; -.
DR Reactome; R-MMU-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-MMU-450520; HuR (ELAVL1) binds and stabilizes mRNA.
DR BioGRID-ORCS; 56086; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Set; mouse.
DR PRO; PR:Q9EQU5; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9EQU5; protein.
DR Bgee; ENSMUSG00000054766; Expressed in rhombomere 4 and 271 other tissues.
DR ExpressionAtlas; Q9EQU5; baseline and differential.
DR Genevisible; Q9EQU5; MM.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005811; C:lipid droplet; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR InterPro; IPR037231; NAP-like_sf.
DR InterPro; IPR002164; NAP_family.
DR PANTHER; PTHR11875; PTHR11875; 1.
DR Pfam; PF00956; NAP; 1.
DR SUPFAM; SSF143113; SSF143113; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chaperone; Cytoplasm; DNA-binding;
KW Endoplasmic reticulum; Isopeptide bond; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:20668449"
FT CHAIN 2..289
FT /note="Protein SET"
FT /id="PRO_0000185663"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 31..77
FT /note="Dimerization"
FT /evidence="ECO:0000250"
FT REGION 78..224
FT /note="Earmuff domain"
FT /evidence="ECO:0000250"
FT REGION 157..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..289
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N,N,N-trimethylalanine; by NTM1"
FT /evidence="ECO:0000269|PubMed:20668449"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01105"
FT MOD_RES 23
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01105"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01105"
FT MOD_RES 67
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 145
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT MOD_RES 149
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q01105"
FT MOD_RES 171
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q01105"
FT CROSSLNK 153
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q01105"
FT VAR_SEQ 1..36
FT /note="MAPKRQSAILPQPKKPRPAAAPKLEDKSASPGLPKG -> MSAPTAKASKKE
FT LNSNHDGADETS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11231286,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_009869"
FT VAR_SEQ 83..146
FT /note="RSELIAKIPNFWVTTFVNHPQVSALLGEEDEEALHYLTRVEVTEFEDIKSGY
FT RIDFYFDENPYF -> STTWFPTWMMKKERQKMMMTTTKRRRGWKILMKKEMRMKVKKM
FT TMRMKGRKERRTKARMISTED (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_009870"
FT VAR_SEQ 147..289
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_009871"
FT MUTAGEN 4
FT /note="K->Q: Almost abolishes N-terminal methylation at A-
FT 2."
FT /evidence="ECO:0000269|PubMed:20668449"
FT CONFLICT 91
FT /note="P -> L (in Ref. 5; BAA34736)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="Q -> L (in Ref. 5; BAA34736)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="D -> A (in Ref. 5; BAA34736)"
FT /evidence="ECO:0000305"
FT MOD_RES Q9EQU5-2:11
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000305"
FT MOD_RES Q9EQU5-2:15
FT /note="Phosphoserine"
FT /evidence="ECO:0000305"
FT MOD_RES Q9EQU5-2:23
FT /note="Phosphothreonine"
FT /evidence="ECO:0000305"
SQ SEQUENCE 289 AA; 33378 MW; B8FDD71A78107019 CRC64;
MAPKRQSAIL PQPKKPRPAA APKLEDKSAS PGLPKGEKEQ QEAIEHIDEV QNEIDRLNEQ
ASEEILKVEQ KYNKLRQPFF QKRSELIAKI PNFWVTTFVN HPQVSALLGE EDEEALHYLT
RVEVTEFEDI KSGYRIDFYF DENPYFENKV LSKEFHLNES GDPSSKSTEI KWKSGKDLTK
RSSQTQNKAS RKRQHEEPES FFTWFTDHSD AGADELGEVI KDDIWPNPLQ YYLVPDMDDE
EGEAEDDDDD DEEEEGLEDI DEEGDEDEGE EDDDEDEGEE GEEDEGEDD
