ID   SET1B_MOUSE             Reviewed;        1985 AA.
AC   Q8CFT2; Q80TK9; Q8CFQ8; Q8CGD1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   27-MAR-2024, entry version 155.
DE   RecName: Full=Histone-lysine N-methyltransferase SETD1B;
DE            EC=2.1.1.364 {ECO:0000250|UniProtKB:Q9UPS6};
DE   AltName: Full=SET domain-containing protein 1B;
GN   Name=Setd1b; Synonyms=Kiaa1076, Set1b;
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 883-1985 (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Eye, 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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1090-1985 (ISOFORM 2).
RX   PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT   The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=17355966; DOI=10.1074/jbc.m609809200;
RA   Lee J.-H., Tate C.M., You J.-S., Skalnik D.G.;
RT   "Identification and characterization of the human Set1B histone H3-Lys4
RT   methyltransferase complex.";
RL   J. Biol. Chem. 282:13419-13428(2007).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1283; SER-1301; SER-1678 AND
RP   SER-1682, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, Liver, Lung, Pancreas, 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   [7]
RP   SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX   PubMed=24550110; DOI=10.1242/dev.098152;
RA   Bledau A.S., Schmidt K., Neumann K., Hill U., Ciotta G., Gupta A.,
RA   Torres D.C., Fu J., Kranz A., Stewart A.F., Anastassiadis K.;
RT   "The H3K4 methyltransferase Setd1a is first required at the epiblast stage,
RT   whereas Setd1b becomes essential after gastrulation.";
RL   Development 141:1022-1035(2014).
RN   [8]
RP   FUNCTION.
RX   PubMed=29916805; DOI=10.7554/elife.27157;
RA   Schmidt K., Zhang Q., Tasdogan A., Petzold A., Dahl A., Arneth B.M.,
RA   Slany R., Fehling H.J., Kranz A., Stewart A.F., Anastassiadis K.;
RT   "The H3K4 methyltransferase Setd1b is essential for hematopoietic stem and
RT   progenitor cell homeostasis in mice.";
RL   Elife 7:0-0(2018).
CC   -!- FUNCTION: Histone methyltransferase that catalyzes methyl group
CC       transfer from S-adenosyl-L-methionine to the epsilon-amino group of
CC       'Lys-4' of histone H3 (H3K4) via a non-processive mechanism. Part of
CC       chromatin remodeling machinery, forms H3K4me1, H3K4me2 and H3K4me3
CC       methylation marks at active chromatin sites where transcription and DNA
CC       repair take place (By similarity). Plays an essential role in
CC       regulating the transcriptional programming of multipotent hematopoietic
CC       progenitor cells and lymphoid lineage specification during
CC       hematopoiesis (PubMed:29916805). {ECO:0000250|UniProtKB:Q9UPS6,
CC       ECO:0000269|PubMed:29916805}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine = H(+) +
CC         N(6)-methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:60264, Rhea:RHEA-COMP:15543, Rhea:RHEA-COMP:15547,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.364;
CC         Evidence={ECO:0000250|UniProtKB:Q9UPS6};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60265;
CC         Evidence={ECO:0000250|UniProtKB:Q9UPS6};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6)-methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine
CC         = H(+) + N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:60268, Rhea:RHEA-COMP:15540, Rhea:RHEA-
CC         COMP:15543, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:61929, ChEBI:CHEBI:61976;
CC         Evidence={ECO:0000250|UniProtKB:Q9UPS6};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60269;
CC         Evidence={ECO:0000250|UniProtKB:Q9UPS6};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-
CC         methionine = H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3]
CC         + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60272, Rhea:RHEA-
CC         COMP:15537, Rhea:RHEA-COMP:15540, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961,
CC         ChEBI:CHEBI:61976; Evidence={ECO:0000250|UniProtKB:Q9UPS6};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60273;
CC         Evidence={ECO:0000250|UniProtKB:Q9UPS6};
CC   -!- SUBUNIT: Component of the SET1B/COMPASS complex composed of the
CC       catalytic subunit SETD1B, WDR5, WDR82, RBBP5, ASH2L/ASH2, CXXC1/CFP1,
CC       HCFC1, DPY30 homotrimer and BOD1. Forms a core complex with the
CC       evolutionary conserved subcomplex WRAD composed of WDR5, RBBP5,
CC       ASH2L/ASH2 and DPY30 subunits; WRAD differentially stimulates the
CC       methyltransferase activity. Interacts with HCFC1 and ASH2L/ASH2.
CC       Interacts (via the RRM domain) with WDR82. Interacts (via the RRM
CC       domain) with hyperphosphorylated C-terminal domain (CTD) of RNA
CC       polymerase II large subunit (POLR2A) only in the presence of WDR82.
CC       Binds specifically to CTD heptad repeats phosphorylated on 'Ser-5' of
CC       each heptad. Interacts with RBM15. Interacts (via WIN motif) with WDR5.
CC       {ECO:0000250|UniProtKB:Q9UPS6}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24550110}. Nucleus
CC       speckle {ECO:0000250|UniProtKB:Q9UPS6}. Chromosome
CC       {ECO:0000250|UniProtKB:Q9UPS6}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q9UPS6}. Note=Localizes to a largely non-
CC       overlapping set of euchromatic nuclear speckles with SETD1A, suggesting
CC       that SETD1A and SETD1B each bind to a unique set of target genes (By
CC       similarity). Predominantly nuclear (By similarity).
CC       {ECO:0000250|UniProtKB:Q9UPS6}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8CFT2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8CFT2-2; Sequence=VSP_030851;
CC   -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:17355966}.
CC   -!- DEVELOPMENTAL STAGE: During preimplantation development expressed
CC       through all stages from oocyte to blastocyst. High expression is
CC       detected in oocyte that declines to a stable level from the 8-cell
CC       stage until 8.5 dpc. Expressed in the blastocyst in both the inner cell
CC       mass and the trophectoderm. {ECO:0000269|PubMed:24550110}.
CC   -!- DISRUPTION PHENOTYPE: Mutant embryos show growth retardation from 7.5
CC       dpc and die before 11.5 dpc. {ECO:0000269|PubMed:24550110}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC       superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
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DR   EMBL; AC158114; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC038367; AAH38367.2; -; mRNA.
DR   EMBL; BC040775; AAH40775.1; -; mRNA.
DR   EMBL; BC041681; AAH41681.1; -; mRNA.
DR   EMBL; AK122435; BAC65717.1; -; mRNA.
DR   CCDS; CCDS59684.1; -. [Q8CFT2-1]
DR   RefSeq; NP_001035488.2; NM_001040398.2. [Q8CFT2-1]
DR   AlphaFoldDB; Q8CFT2; -.
DR   SMR; Q8CFT2; -.
DR   BioGRID; 228940; 4.
DR   IntAct; Q8CFT2; 1.
DR   MINT; Q8CFT2; -.
DR   STRING; 10090.ENSMUSP00000133933; -.
DR   GlyGen; Q8CFT2; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8CFT2; -.
DR   PhosphoSitePlus; Q8CFT2; -.
DR   EPD; Q8CFT2; -.
DR   jPOST; Q8CFT2; -.
DR   MaxQB; Q8CFT2; -.
DR   PaxDb; 10090-ENSMUSP00000133933; -.
DR   PeptideAtlas; Q8CFT2; -.
DR   ProteomicsDB; 261160; -. [Q8CFT2-1]
DR   ProteomicsDB; 261161; -. [Q8CFT2-2]
DR   Pumba; Q8CFT2; -.
DR   Antibodypedia; 9774; 144 antibodies from 26 providers.
DR   Ensembl; ENSMUST00000056053.9; ENSMUSP00000134686.2; ENSMUSG00000038384.17. [Q8CFT2-1]
DR   Ensembl; ENSMUST00000163030.9; ENSMUSP00000133933.2; ENSMUSG00000038384.17. [Q8CFT2-1]
DR   Ensembl; ENSMUST00000174836.8; ENSMUSP00000134461.2; ENSMUSG00000038384.17. [Q8CFT2-2]
DR   GeneID; 208043; -.
DR   KEGG; mmu:208043; -.
DR   UCSC; uc008zng.2; mouse. [Q8CFT2-1]
DR   AGR; MGI:2652820; -.
DR   CTD; 23067; -.
DR   MGI; MGI:2652820; Setd1b.
DR   VEuPathDB; HostDB:ENSMUSG00000038384; -.
DR   eggNOG; KOG1080; Eukaryota.
DR   GeneTree; ENSGT00940000154575; -.
DR   HOGENOM; CLU_001226_0_0_1; -.
DR   InParanoid; Q8CFT2; -.
DR   OMA; PICRPEE; -.
DR   OrthoDB; 950362at2759; -.
DR   PhylomeDB; Q8CFT2; -.
DR   TreeFam; TF106436; -.
DR   Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
DR   Reactome; R-MMU-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR   Reactome; R-MMU-9772755; Formation of WDR5-containing histone-modifying complexes.
DR   BioGRID-ORCS; 208043; 10 hits in 80 CRISPR screens.
DR   ChiTaRS; Setd1b; mouse.
DR   PRO; PR:Q8CFT2; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q8CFT2; Protein.
DR   Bgee; ENSMUSG00000038384; Expressed in humerus cartilage element and 229 other cell types or tissues.
DR   ExpressionAtlas; Q8CFT2; baseline and differential.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0035097; C:histone methyltransferase complex; ISO:MGI.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0048188; C:Set1C/COMPASS complex; ISS:UniProtKB.
DR   GO; GO:0042800; F:histone H3K4 methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0140945; F:histone H3K4 monomethyltransferase activity; IEA:RHEA.
DR   GO; GO:0140999; F:histone H3K4 trimethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd12549; RRM_Set1B; 1.
DR   CDD; cd19169; SET_SETD1; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   Gene3D; 2.170.270.10; SET domain; 1.
DR   InterPro; IPR024657; COMPASS_Set1_N-SET.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR044570; Set1-like.
DR   InterPro; IPR034468; Set1B_RRM.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   InterPro; IPR037841; SET_SETD1A/B.
DR   PANTHER; PTHR45814; HISTONE-LYSINE N-METHYLTRANSFERASE SETD1; 1.
DR   PANTHER; PTHR45814:SF1; HISTONE-LYSINE N-METHYLTRANSFERASE SETD1B; 1.
DR   Pfam; PF11764; N-SET; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM01291; N-SET; 1.
DR   SMART; SM00508; PostSET; 1.
DR   SMART; SM00360; RRM; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS50102; RRM; 1.
DR   PROSITE; PS50280; SET; 1.
DR   Genevisible; Q8CFT2; MM.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; Chromatin regulator; Chromosome;
KW   Cytoplasm; Methyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW   RNA-binding; S-adenosyl-L-methionine; Transcription;
KW   Transcription regulation; Transferase.
FT   CHAIN           1..1985
FT                   /note="Histone-lysine N-methyltransferase SETD1B"
FT                   /id="PRO_0000316994"
FT   DOMAIN          92..180
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          1846..1963
FT                   /note="SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   DOMAIN          1969..1985
FT                   /note="Post-SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          67..97
FT                   /note="Interaction with WDR82"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UPS6"
FT   REGION          234..304
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          353..710
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          955..1480
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1519..1624
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1658..1687
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1786..1819
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1764..1769
FT                   /note="WDR5 interaction motif (WIN)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UPS6"
FT   MOTIF           1817..1822
FT                   /note="RxxxRR motif"
FT                   /evidence="ECO:0000250|UniProtKB:P38827"
FT   COMPBIAS        234..303
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        353..389
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        392..406
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        422..452
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        484..516
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        517..564
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        610..625
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        667..710
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        989..1032
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1033..1054
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1061..1082
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1100..1116
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1146..1175
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1176..1203
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1250..1265
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1328..1381
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1387..1424
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1598..1622
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1658..1674
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1786..1808
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1962
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   MOD_RES         977
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UPS6"
FT   MOD_RES         985
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UPS6"
FT   MOD_RES         1022
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UPS6"
FT   MOD_RES         1283
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1301
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1354
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UPS6"
FT   MOD_RES         1678
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1682
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   VAR_SEQ         1139..1179
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12693553"
FT                   /id="VSP_030851"
FT   CONFLICT        1222
FT                   /note="A -> V (in Ref. 3; BAC65717)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1411
FT                   /note="S -> G (in Ref. 3; BAC65717)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1985 AA;  215352 MW;  760EA261769292EC CRC64;
     MENSHPHHHH QQPPPQPGPS GERRNHHWRS YKLMIDPALK KGHHKLYRYD GQHFSLAMSS
     NRPVEIVEDP RVVGIWTKNK ELELSVPKFK IDEFYVGPVP PKQVTFAKLN DNVRENFLRD
     MCKKYGEVEE VEILYNPKTK KHLGIAKVVF ATVRGAKEAV QHLHSTSVMG NIIHVELDTK
     GETRMRFYEL LVTGRYTPQT LPVGELDAIS PIVSETLQLS DALKRLKDGS LSAGCGSGSS
     SVTPNSGGTP FSQDTAYSSC RLDTPNSYGQ GTPITPRLGT PFSQDSSYSS RQPTPSYLFS
     QDPTATFKAR RHESKFTDAY NRRHEHHYVH NSAVAGATAP FRGSSDLSFG TVGSSGTPFK
     AQSQDATTFA HTPPPAQTAT ASGFKSAFSP YQTPAPPFPP PPEEPTATAA FGSRDSGEFR
     RAPAPPPLPP AEPPAKEKPG TPPGPPPPDS NSMELGGRPT FGWSPEPCDS PGTPTLESSP
     AGPEKPHDSL DSRIEMLLKE QRTKLPFLRE QDSDTEIQME GSPISSSSSQ LSPLSHFGTN
     SQPGFRGPSP PSSRPSSTGL EDISPTPLPD SDEDEDLGLG LGPRPPPEPG PPDPMGLLGQ
     TAEVDLDLAG DRTPTSERMD EGQQSSGEDM EISDDEMPSA PITSADCPKP MVVTPGAGAV
     AAPNVLAPNL PLPPPPGFPP LPPPPPPPPP QPGFPMPPPL PPPPPPPPPA HPAVTVPPPP
     LPAPPGVPPP PILPPLPPFP PGLFPVMQVD MSHVLGGQWG GMPMSFQMQT QMLSRLMTGQ
     GACPYPPFMA AAAAAASAGL QFVNLPPYRS PFSLSNSGPG RGQHWPPLPK FDPSVPPPGY
     IPRQEDPHKA TVDGVLLVVL KELKAIMKRD LNRKMVEVVA FRAFDEWWDK KERMAKASLT
     PVKSGEHKDE DRPKPKDRIA SCLLESWGKG EGLGYEGLGL GIGLRGAIRL PSFKVKRKEP
     PDTASSGDQK RLRPSTSVDE EDEESERERD RDIADAPCEL TKRDPKSVGV RRRPGRPLEL
     DSGGEEDEKE SLSASSSSSA SSSSGSSTTS PSSSASDKEE EDRESTEEEE EEEEEEAEEE
     EEEGPRSRIS SPSSSSSSDK DDEDDNEADS DGQIDSDIDD QGAPLSEASE KDNGDSEEEE
     TESITTSKAP AESSSSSSES SGSSEFESSS ESESSSSSSE DEEEMTVPGV EEEEEEEEEE
     EKETAMAAAT VVAMAEESMP PAGGQDFEQD RAEVPLGPRG PMRESLGTEE EVDIEAEDEV
     PEMQAPELEE PPLPMGARKL EGSPEPPEEP GPNTQGDMLL SPELPARETE EAQLPSPPEH
     GPESDLDMEP EPPPMLSLPL QPPLPPPRLL RPPSPPPEPE TPEPPKPPVP LEPPPEDHPP
     RTPGLCGSLA KSQSTETVPA TPGGEPPLSG SSSGLSLSSP QVPGSPFSYP SPSPGLSSGG
     LPRTPGRDFS FTPTFPEPSG PLLLPVCPLP TGRRDERTGP LASPVLLETG LPLPLPLPLP
     LPLALPVPVL RAQPRPPPQL PPLLPATLAP CPTPIKRKPG RPRRSPPSML SLDGPLVRPP
     PGPALGRDLL LLPGQPPAPI FPSAHDPRAV TLDFRNTGIP APPPPLPPQP PPPPPPPPVE
     STKLPFKELD NQWPSEAIPP GPRRDEVTEE YVDLAKVRGP WRRPPKKRHE DLVAPSASPE
     PSPPQPLFRP RSEFEEMTIL YDIWNGGIDE EDIRFLCVTY ERLLQQDNGM DWLNDTLWVY
     HPSTSLSSAK KKKREDGIRE HVTGCARSEG FYTIDKKDKL RYLNSSRAST DEPPMDTQGM
     SIPAQPHAST RAGSERRSEQ RRLLSSFTGS CDSDLLKFNQ LKFRKKKLKF CKSHIHDWGL
     FAMEPIAADE MVIEYVGQNI RQVIADMREK RYEDEGIGSS YMFRVDHDTI IDATKCGNFA
     RFINHSCNPN CYAKVITVES QKKIVIYSKQ HINVNEEITY DYKFPIEDVK IPCLCGSENC
     RGTLN
//