MECOM_MOUSE
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 03-AUG-2022, entry version 185.
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; 3.
DR DIP; DIP-46516N; -.
DR IntAct; P14404; 1157.
DR MINT; P14404; -.
DR STRING; 10090.ENSMUSP00000103905; -.
DR iPTMnet; P14404; -.
DR PhosphoSitePlus; P14404; -.
DR PaxDb; P14404; -.
DR PRIDE; P14404; -.
DR ProteomicsDB; 275902; -. [P14404-2]
DR ProteomicsDB; 292286; -.
DR ProteomicsDB; 361307; -.
DR Antibodypedia; 18615; 425 antibodies from 35 providers.
DR DNASU; 14013; -.
DR Ensembl; ENSMUST00000108270; ENSMUSP00000103905; ENSMUSG00000027684. [P14404-1]
DR GeneID; 14013; -.
DR KEGG; mmu:14013; -.
DR UCSC; uc033hsp.1; mouse. [P14404-2]
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; 1318335at2759; -.
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 28 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 233 other tissues.
DR ExpressionAtlas; P14404; baseline and differential.
DR Genevisible; P14404; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000118; C:histone deacetylase complex; ISO:MGI.
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 methyltransferase activity (H3-K9 specific); IDA:UniProtKB.
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:0030154; P:cell differentiation; 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: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:0045892; P:negative regulation of transcription, DNA-templated; IDA: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:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
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; 2.170.270.10; -; 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 Pfam; PF00096; zf-C2H2; 8.
DR SMART; SM00317; SET; 1.
DR SMART; SM00355; ZnF_C2H2; 10.
DR SUPFAM; SSF57667; SSF57667; 5.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 10.
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
