ID   MECOM_MOUSE             Reviewed;        1232 AA.
AC   P14404; G3UWT0; Q9Z1L8;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   28-MAR-2018, sequence version 2.
DT   27-MAR-2024, entry version 194.
DE   RecName: Full=Histone-lysine N-methyltransferase MECOM {ECO:0000305};
DE            EC=2.1.1.367 {ECO:0000269|PubMed:22939622};
DE   AltName: Full=Ecotropic virus integration site 1 protein;
DE            Short=EVI-1;
DE   AltName: Full=MDS1 and EVI1 complex locus protein {ECO:0000305};
DE   AltName: Full=Myelodysplasia syndrome 1 protein homolog;
GN   Name=Mecom {ECO:0000312|MGI:MGI:95457};
GN   Synonyms=Evi1, Mds1, Prdm3 {ECO:0000303|PubMed:22939622};
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 4).
RX   PubMed=9837768; DOI=10.1006/bbrc.1998.9588;
RA   Wimmer K., Vinatzer U., Zwirn P., Fonatsch C., Wieser R.;
RT   "Comparative expression analysis of the antagonistic transcription factors
RT   EVI1 and MDS1-EVI1 in murine tissues and during in vitro hematopoietic
RT   differentiation.";
RL   Biochem. Biophys. Res. Commun. 252:691-696(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX   PubMed=2842066; DOI=10.1016/s0092-8674(88)91175-0;
RA   Morishita K., Parker D.S., Mucenski M.L., Jenkins N.A., Copeland N.G.,
RA   Ihle J.N.;
RT   "Retroviral activation of a novel gene encoding a zinc finger protein in
RT   IL-3-dependent myeloid leukemia cell lines.";
RL   Cell 54:831-840(1988).
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   SUBCELLULAR LOCATION, DNA-BINDING, AND PHOSPHORYLATION.
RX   PubMed=2106070; DOI=10.1128/mcb.10.3.1259-1264.1990;
RA   Matsugi T., Morishita K., Ihle J.N.;
RT   "Identification, nuclear localization, and DNA-binding activity of the zinc
RT   finger protein encoded by the Evi-1 myeloid transforming gene.";
RL   Mol. Cell. Biol. 10:1259-1264(1990).
RN   [5]
RP   DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX   PubMed=9256345; DOI=10.1016/s0925-4773(97)00057-9;
RA   Hoyt P.R., Bartholomew C., Davis A.J., Yutzey K., Gamer L.W., Potter S.S.,
RA   Ihle J.N., Mucenski M.L.;
RT   "The Evi1 proto-oncogene is required at midgestation for neural, heart, and
RT   paraxial mesenchyme development.";
RL   Mech. Dev. 65:55-70(1997).
RN   [6]
RP   FUNCTION IN CELL PROLIFERATION, AND DNA-BINDING.
RX   PubMed=15889140; DOI=10.1038/sj.emboj.7600679;
RA   Yuasa H., Oike Y., Iwama A., Nishikata I., Sugiyama D., Perkins A.,
RA   Mucenski M.L., Suda T., Morishita K.;
RT   "Oncogenic transcription factor Evi1 regulates hematopoietic stem cell
RT   proliferation through GATA-2 expression.";
RL   EMBO J. 24:1976-1987(2005).
RN   [7]
RP   INTERACTION WITH SUV39H1, AND FUNCTION.
RX   PubMed=18619962; DOI=10.1016/j.febslet.2008.06.056;
RA   Spensberger D., Delwel R.;
RT   "A novel interaction between the proto-oncogene Evi1 and histone
RT   methyltransferases, SUV39H1 and G9a.";
RL   FEBS Lett. 582:2761-2767(2008).
RN   [8]
RP   FUNCTION.
RX   PubMed=19767769; DOI=10.1038/onc.2009.288;
RA   Shimabe M., Goyama S., Watanabe-Okochi N., Yoshimi A., Ichikawa M.,
RA   Imai Y., Kurokawa M.;
RT   "Pbx1 is a downstream target of Evi-1 in hematopoietic stem/progenitors and
RT   leukemic cells.";
RL   Oncogene 28:4364-4374(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-626; SER-742 AND SER-1041,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Kidney, and Lung;
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   [10]
RP   FUNCTION (ISOFORM 3), AND CATALYTIC ACTIVITY.
RX   PubMed=22939622; DOI=10.1016/j.cell.2012.06.048;
RA   Pinheiro I., Margueron R., Shukeir N., Eisold M., Fritzsch C.,
RA   Richter F.M., Mittler G., Genoud C., Goyama S., Kurokawa M., Son J.,
RA   Reinberg D., Lachner M., Jenuwein T.;
RT   "Prdm3 and Prdm16 are H3K9me1 methyltransferases required for mammalian
RT   heterochromatin integrity.";
RL   Cell 150:948-960(2012).
CC   -!- FUNCTION: [Isoform 1]: Functions as a transcriptional regulator binding
CC       to DNA sequences in the promoter region of target genes and regulating
CC       positively or negatively their expression. Oncogene which plays a role
CC       in development, cell proliferation and differentiation. May also play a
CC       role in apoptosis through regulation of the JNK and TGF-beta signaling.
CC       Involved in hematopoiesis. {ECO:0000269|PubMed:15889140,
CC       ECO:0000269|PubMed:18619962, ECO:0000269|PubMed:19767769}.
CC   -!- FUNCTION: [Isoform 3]: Displays histone methyltransferase activity and
CC       monomethylates 'Lys-9' of histone H3 (H3K9me1) in vitro. Probably
CC       catalyzes the monomethylation of free histone H3 in the cytoplasm which
CC       is then transported to the nucleus and incorporated into nucleosomes
CC       where SUV39H methyltransferases use it as a substrate to catalyze
CC       histone H3 'Lys-9' trimethylation. Likely to be one of the primary
CC       histone methyltransferases along with PRDM16 that direct cytoplasmic
CC       H3K9me1 methylation. {ECO:0000269|PubMed:22939622}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl(9)-[histone H3] + S-adenosyl-L-methionine = H(+) +
CC         N(6)-methyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:60280, Rhea:RHEA-COMP:15542, Rhea:RHEA-COMP:15546,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.367;
CC         Evidence={ECO:0000269|PubMed:22939622};
CC   -!- SUBUNIT: [Isoform 1]: Homooligomer. Interacts with CTBP1. Interacts
CC       with SMAD3 (via MH2 domain); the interaction is direct. Interacts with
CC       SMAD4; through interaction with SMAD3. Interacts with CREBBP, KAT2B and
CC       histone deacetylases. Interacts with MAPK8 and MAPK9; inhibits JNK
CC       signaling (By similarity). Interacts with SUV39H1 (via SET domain);
CC       enhances MECOM transcriptional repression activity.
CC       {ECO:0000250|UniProtKB:Q03112, ECO:0000269|PubMed:18619962}.
CC   -!- INTERACTION:
CC       P14404; P01101: Fos; NbExp=2; IntAct=EBI-1994523, EBI-4288185;
CC       P14404; Q9Z2D8: Mbd3; NbExp=4; IntAct=EBI-1994523, EBI-1994548;
CC       P14404; Q9Z2D8-1: Mbd3; NbExp=5; IntAct=EBI-1994523, EBI-1994598;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:2106070}. Nucleus
CC       speckle {ECO:0000250|UniProtKB:Q03112}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q03112}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative promoter usage, Alternative splicing; Named isoforms=3;
CC       Name=3 {ECO:0000305};
CC         IsoId=P14404-2; Sequence=Displayed;
CC       Name=1 {ECO:0000305};
CC         IsoId=P14404-1; Sequence=VSP_059487;
CC       Name=4 {ECO:0000305}; Synonyms=Mds1;
CC         IsoId=P14404-3; Sequence=VSP_059488, VSP_059489;
CC   -!- DEVELOPMENTAL STAGE: Expressed at 8.5 dpc in the anterior section of
CC       the primary head folds. Ubiquitously expressed at 9.5 dpc with higher
CC       expression in forebrain, mesenchyme of the branchial arches, nasal
CC       pits, limb buds and mesonephric ducts. Also detected at 10.5 dpc in
CC       hindbrain and lateral region of the neural tube.
CC       {ECO:0000269|PubMed:9256345}.
CC   -!- DOMAIN: Both zinc finger regions are required for the transcriptional
CC       activation of PBX1. {ECO:0000250}.
CC   -!- PTM: May be acetylated by CREBBP and KAT2B.
CC       {ECO:0000250|UniProtKB:Q03112}.
CC   -!- DISRUPTION PHENOTYPE: Mice develop until 9.5 dpc but die before 11.5
CC       dpc. At 10.5 dpc embryos display multiple malformations associated with
CC       hypocellularity and reduced body size. Required for neural, heart and
CC       paraxial mesenchyme. {ECO:0000269|PubMed:9256345}.
CC   -!- MISCELLANEOUS: [Isoform 4]: Produced by alternative promoter usage. May
CC       be due to intron retention. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA40581.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AJ010015; CAA08971.1; -; mRNA.
DR   EMBL; M21829; AAA40581.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AC119995; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL683891; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL691419; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL772145; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL929377; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; A31591; A31591.
DR   RefSeq; NP_067417.1; NM_021442.2. [P14404-3]
DR   PDB; 6XAU; X-ray; 1.89 A; A=74-193.
DR   PDBsum; 6XAU; -.
DR   AlphaFoldDB; P14404; -.
DR   SMR; P14404; -.
DR   BioGRID; 199542; 4.
DR   DIP; DIP-46516N; -.
DR   IntAct; P14404; 1157.
DR   MINT; P14404; -.
DR   iPTMnet; P14404; -.
DR   PhosphoSitePlus; P14404; -.
DR   PaxDb; 10090-ENSMUSP00000103905; -.
DR   ProteomicsDB; 275902; -. [P14404-2]
DR   ProteomicsDB; 292286; -.
DR   ProteomicsDB; 361307; -.
DR   Pumba; P14404; -.
DR   Antibodypedia; 18615; 459 antibodies from 35 providers.
DR   DNASU; 14013; -.
DR   Ensembl; ENSMUST00000108270.10; ENSMUSP00000103905.4; ENSMUSG00000027684.17. [P14404-1]
DR   GeneID; 14013; -.
DR   KEGG; mmu:14013; -.
DR   UCSC; uc033hsp.1; mouse. [P14404-2]
DR   AGR; MGI:95457; -.
DR   CTD; 2122; -.
DR   MGI; MGI:95457; Mecom.
DR   VEuPathDB; HostDB:ENSMUSG00000027684; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000157208; -.
DR   HOGENOM; CLU_006627_0_0_1; -.
DR   InParanoid; P14404; -.
DR   OrthoDB; 3039682at2759; -.
DR   PhylomeDB; P14404; -.
DR   TreeFam; TF315309; -.
DR   BRENDA; 2.1.1.367; 3474.
DR   Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
DR   Reactome; R-MMU-8943724; Regulation of PTEN gene transcription.
DR   BioGRID-ORCS; 14013; 3 hits in 31 CRISPR screens.
DR   ChiTaRS; Mecom; mouse.
DR   PRO; PR:P14404; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; P14404; Protein.
DR   Bgee; ENSMUSG00000027684; Expressed in urinary bladder urothelium and 236 other cell types or tissues.
DR   ExpressionAtlas; P14404; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IMP:NTNU_SB.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR   GO; GO:0046974; F:histone H3K9 methyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0140948; F:histone H3K9 monomethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0140947; F:histone H3K9me2 methyltransferase activity; IEA:RHEA.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IMP:NTNU_SB.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0035115; P:embryonic forelimb morphogenesis; IMP:MGI.
DR   GO; GO:0035116; P:embryonic hindlimb morphogenesis; IMP:MGI.
DR   GO; GO:0030900; P:forebrain development; IMP:MGI.
DR   GO; GO:0071425; P:hematopoietic stem cell proliferation; IMP:UniProtKB.
DR   GO; GO:0070828; P:heterochromatin organization; IMP:UniProtKB.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0006954; P:inflammatory response; IMP:MGI.
DR   GO; GO:0098727; P:maintenance of cell number; IGI:MGI.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB.
DR   GO; GO:0046329; P:negative regulation of JNK cascade; ISS:UniProtKB.
DR   GO; GO:0043069; P:negative regulation of programmed cell death; ISS:UniProtKB.
DR   GO; GO:0001780; P:neutrophil homeostasis; IMP:MGI.
DR   GO; GO:0060039; P:pericardium development; IMP:MGI.
DR   GO; GO:0090336; P:positive regulation of brown fat cell differentiation; IMP:MGI.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR   GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR   GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR   GO; GO:1902033; P:regulation of hematopoietic stem cell proliferation; IMP:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0009617; P:response to bacterium; IMP:MGI.
DR   GO; GO:0072197; P:ureter morphogenesis; IGI:MGI.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 8.
DR   Gene3D; 2.170.270.10; SET domain; 1.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR24393:SF15; IP01201P-RELATED; 1.
DR   PANTHER; PTHR24393; ZINC FINGER PROTEIN; 1.
DR   Pfam; PF21549; PRDM2_PR; 1.
DR   Pfam; PF00096; zf-C2H2; 8.
DR   Pfam; PF13912; zf-C2H2_6; 1.
DR   SMART; SM00317; SET; 1.
DR   SMART; SM00355; ZnF_C2H2; 10.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 5.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 10.
DR   Genevisible; P14404; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative promoter usage;
KW   Alternative splicing; Apoptosis; Cytoplasm; Developmental protein;
KW   Differentiation; DNA-binding; Isopeptide bond; Metal-binding;
KW   Methyltransferase; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW   Transcription; Transcription regulation; Transferase; Ubl conjugation;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..1232
FT                   /note="Histone-lysine N-methyltransferase MECOM"
FT                   /id="PRO_0000047274"
FT   DOMAIN          80..192
FT                   /note="SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   ZN_FING         211..238
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         265..287
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         293..315
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         321..344
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         350..372
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         378..400
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         407..429
FT                   /note="C2H2-type 7; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         914..936
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         942..965
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         971..993
FT                   /note="C2H2-type 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          22..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          191..442
FT                   /note="Interaction with SUV39H1 and probably MAPK9 and
FT                   SMAD3"
FT                   /evidence="ECO:0000269|PubMed:18619962"
FT   REGION          548..622
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          720..823
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1032..1107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           611..624
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   MOTIF           743..747
FT                   /note="CTBP-binding motif 1"
FT                   /evidence="ECO:0000250"
FT   MOTIF           774..778
FT                   /note="CTBP-binding motif 2"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        43..61
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        561..581
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        582..602
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        604..622
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        759..777
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        788..808
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1032..1047
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1068..1086
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1087..1104
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         626
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         728
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q03112"
FT   MOD_RES         742
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1039
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q03112"
FT   MOD_RES         1041
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CROSSLNK        101
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q03112"
FT   CROSSLNK        192
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q03112"
FT   CROSSLNK        294
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q03112"
FT   CROSSLNK        369
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q03112"
FT   CROSSLNK        376
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q03112"
FT   CROSSLNK        432
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q03112"
FT   CROSSLNK        525
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q03112"
FT   CROSSLNK        545
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q03112"
FT   CROSSLNK        549
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q03112"
FT   CROSSLNK        557
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q03112"
FT   CROSSLNK        624
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q03112"
FT   CROSSLNK        637
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q03112"
FT   CROSSLNK        665
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q03112"
FT   CROSSLNK        687
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q03112"
FT   CROSSLNK        723
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q03112"
FT   CROSSLNK        733
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q03112"
FT   CROSSLNK        734
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q03112"
FT   CROSSLNK        737
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q03112"
FT   CROSSLNK        751
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q03112"
FT   CROSSLNK        754
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q03112"
FT   CROSSLNK        762
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q03112"
FT   CROSSLNK        789
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q03112"
FT   CROSSLNK        802
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q03112"
FT   CROSSLNK        803
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q03112"
FT   CROSSLNK        837
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q03112"
FT   CROSSLNK        846
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q03112"
FT   CROSSLNK        848
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q03112"
FT   CROSSLNK        879
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q03112"
FT   CROSSLNK        1020
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q03112"
FT   CROSSLNK        1055
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q03112"
FT   CROSSLNK        1058
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q03112"
FT   CROSSLNK        1122
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q03112"
FT   CROSSLNK        1129
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q03112"
FT   CROSSLNK        1134
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q03112"
FT   CROSSLNK        1151
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q03112"
FT   CROSSLNK        1178
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q03112"
FT   CROSSLNK        1186
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q03112"
FT   VAR_SEQ         1..190
FT                   /note="Missing (in isoform 1)"
FT                   /id="VSP_059487"
FT   VAR_SEQ         128..129
FT                   /note="IL -> NR (in isoform 4)"
FT                   /id="VSP_059488"
FT   VAR_SEQ         130..1232
FT                   /note="Missing (in isoform 4)"
FT                   /id="VSP_059489"
FT   STRAND          82..86
FT                   /evidence="ECO:0007829|PDB:6XAU"
FT   STRAND          94..100
FT                   /evidence="ECO:0007829|PDB:6XAU"
FT   STRAND          114..117
FT                   /evidence="ECO:0007829|PDB:6XAU"
FT   STRAND          123..129
FT                   /evidence="ECO:0007829|PDB:6XAU"
FT   STRAND          135..140
FT                   /evidence="ECO:0007829|PDB:6XAU"
FT   HELIX           149..152
FT                   /evidence="ECO:0007829|PDB:6XAU"
FT   STRAND          164..169
FT                   /evidence="ECO:0007829|PDB:6XAU"
FT   STRAND          172..177
FT                   /evidence="ECO:0007829|PDB:6XAU"
SQ   SEQUENCE   1232 AA;  138100 MW;  044BB6F19DBD1403 CRC64;
     MRSKGRARKL ATSNECAYGN YPEIPLEEMP DADADGITSV PSLHIQEPCS PATSSESFTP
     KEGSPYKAPI YIPDDIPIPD EFELRESTMP GAGLGIWTKR KIEIGEKFGP YMGEQRSDLK
     DSSYGWEILD EFCNVKFCID ASQPDVGSWL KYIRFAGCYD QHNLVACQIN DQIFYRVVAD
     IAPGEELLLF MKSEEDPHEP MAPDIHEERQ HRCEDCDQLF ESKAELADHQ KFPCSTPHSA
     FSMVEEDLQQ NLESESDLRE IHGNQDCKEC DRVFPDLQSL EKHMLSHTEE REYKCDQCPK
     AFNWKSNLIR HQMSHDSGKH YECENCAKVF TDPSNLQRHI RSQHVGARAH ACPECGKTFA
     TSSGLKQHKH IHSSVKPFIC EVCHKSYTQF SNLCRHKRMH ADCRTQIKCK DCGQMFSTTS
     SLNKHRRFCE GKNHFAAGGF FGQGISLPGT PAMDKTSMVN MSHANPGLAD YFGTNRHPAG
     LTFPTAPGFS FSFPGLFPSG LYHRPPLIPA SPPVKGLSST EQSNKCQSPL LTHPQILPAT
     QDILKALSKH PPVGDNKPVE LLPERSSEER PLEKISDQSE SSDLDDVSTP SGSDLETTSG
     SDLESDLESD KEKCKENGKM FKDKVSPLQN LASITNKKEH NNHSVFSASV EEQSAVSGAV
     NDSIKAIASI AEKYFGSTGL VGLQDKKVGA LPYPSMFPLP FFPAFSQSMY PFPDRDLRSL
     PLKMEPQSPS EVKKLQKGSS ESPFDLTTKR KDEKPLTSGP SKPSGTPATS QDQPLDLSMG
     SRGRASGTKL TEPRKNHVFG EKKGSNMDTR PSSDGSLQHA RPTPFFMDPI YRVEKRKLTD
     PLEALKEKYL RPSPGFLFHP QMSAIENMAE KLESFSALKP EASELLQSVP SMFSFRAPPN
     TLPENLLRKG KERYTCRYCG KIFPRSANLT RHLRTHTGEQ PYRCKYCDRS FSISSNLQRH
     VRNIHNKEKP FKCHLCDRCF GQQTNLDRHL KKHENGNMSG TATSSPHSEL ESAGAILDDK
     EDAYFTEIRN FIGNSNHGSQ SPRNMEERMN GSHFKDKKAL ATSQNSDLLD DEEVEDEVLL
     DEEDEDNDIP GKPRKELGVT RLDEEIPEDD YEEAGALEMS CKASPVRYKE EDYKSGLSAL
     DHIRHFTDSL KMREMEENQY TDAELSSISS SHVPEELKQT LHRKSKSQAY AMMLSLSDKD
     SLHPTSHSSS NVWHSMARAA AESSAIQSIS HV
//