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Database: UniProt
Entry: P14404
LinkDB: P14404
Original site: P14404 
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   10-APR-2019, entry version 167.
DE   RecName: Full=Histone-lysine N-methyltransferase MECOM {ECO:0000305};
DE            EC=2.1.1.43 {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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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
RT   factors EVI1 and MDS1-EVI1 in murine tissues and during in vitro
RT   hematopoietic 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
RT   in 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.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the 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;
RA   Matsugi T., Morishita K., Ihle J.N.;
RT   "Identification, nuclear localization, and DNA-binding activity of the
RT   zinc 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.,
RA   Potter S.S., Ihle J.N., Mucenski M.L.;
RT   "The Evi1 proto-oncogene is required at midgestation for neural,
RT   heart, and 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
RT   stem/progenitors and leukemic cells.";
RL   Oncogene 28:4364-4374(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-626; SER-742 AND
RP   SER-1041, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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
RT   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
RT   mammalian heterochromatin integrity.";
RL   Cell 150:948-960(2012).
CC   -!- FUNCTION: Isoform 1: Functions as a transcriptional regulator
CC       binding to DNA sequences in the promoter region of target genes
CC       and regulating positively or negatively their expression. Oncogene
CC       which plays a role in development, cell proliferation and
CC       differentiation. May also play a role in apoptosis through
CC       regulation of the JNK and TGF-beta signaling. Involved in
CC       hematopoiesis. {ECO:0000269|PubMed:15889140,
CC       ECO:0000269|PubMed:18619962, ECO:0000269|PubMed:19767769}.
CC   -!- FUNCTION: Isoform 3: Displays histone methyltransferase activity
CC       and monomethylates 'Lys-9' of histone H3 (H3K9me1) in vitro.
CC       Probably catalyzes the monomethylation of free histone H3 in the
CC       cytoplasm which is then transported to the nucleus and
CC       incorporated into nucleosomes where SUV39H methyltransferases use
CC       it as a substrate to catalyze histone H3 'Lys-9' trimethylation.
CC       Likely to be one of the primary histone methyltransferases along
CC       with PRDM16 that direct cytoplasmic H3K9me1 methylation.
CC       {ECO:0000269|PubMed:22939622}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) +
CC         N(6)-methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.43;
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
CC       with SMAD4; through interaction with SMAD3. Interacts with CREBBP,
CC       KAT2B and histone deacetylases. Interacts with MAPK8 and MAPK9;
CC       inhibits JNK signaling (By similarity). Interacts with SUV39H1
CC       (via SET domain); enhances MECOM transcriptional repression
CC       activity. {ECO:0000250|UniProtKB:Q03112,
CC       ECO:0000269|PubMed:18619962}.
CC   -!- INTERACTION:
CC       P01101:Fos; NbExp=2; IntAct=EBI-1994523, EBI-4288185;
CC       Q9Z2D8:Mbd3; NbExp=4; IntAct=EBI-1994523, EBI-1994548;
CC       Q9Z2D8-1:Mbd3; NbExp=5; IntAct=EBI-1994523, EBI-1994598;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:2106070}.
CC       Nucleus 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         Note=Produced by alternative promoter usage. May be due to
CC         intron retention.;
CC   -!- DEVELOPMENTAL STAGE: Expressed at 8.5 dpc in the anterior section
CC       of the primary head folds. Ubiquitously expressed at 9.5 dpc with
CC       higher expression in forebrain, mesenchyme of the branchial
CC       arches, nasal pits, limb buds and mesonephric ducts. Also detected
CC       at 10.5 dpc in hindbrain and lateral region of the neural tube.
CC       {ECO:0000269|PubMed:9256345}.
CC   -!- DOMAIN: Both zinc finger regions are required for the
CC       transcriptional 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
CC       11.5 dpc. At 10.5 dpc embryos display multiple malformations
CC       associated with hypocellularity and reduced body size. Required
CC       for neural, heart and paraxial mesenchyme.
CC       {ECO:0000269|PubMed:9256345}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA40581.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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   UniGene; Mm.426829; -.
DR   UniGene; Mm.56965; -.
DR   ProteinModelPortal; P14404; -.
DR   SMR; P14404; -.
DR   BioGrid; 199542; 2.
DR   DIP; DIP-46516N; -.
DR   IntAct; P14404; 6.
DR   MINT; P14404; -.
DR   STRING; 10090.ENSMUSP00000103905; -.
DR   iPTMnet; P14404; -.
DR   PhosphoSitePlus; P14404; -.
DR   PaxDb; P14404; -.
DR   PRIDE; P14404; -.
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   eggNOG; KOG1721; Eukaryota.
DR   eggNOG; COG5048; LUCA.
DR   GeneTree; ENSGT00940000157208; -.
DR   HOGENOM; HOG000231144; -.
DR   HOVERGEN; HBG031707; -.
DR   InParanoid; P14404; -.
DR   KO; K04462; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; P14404; -.
DR   TreeFam; TF315309; -.
DR   Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
DR   Reactome; R-MMU-8943724; Regulation of PTEN gene transcription.
DR   ChiTaRS; Mecom; mouse.
DR   Proteomes; UP000000589; Chromosome 3.
DR   Bgee; ENSMUSG00000027684; Expressed in 279 organ(s), highest expression level in pes.
DR   ExpressionAtlas; P14404; baseline and differential.
DR   Genevisible; P14404; MM.
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; IC:NTNU_SB.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; 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:0000977; F:RNA polymerase II 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: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:0042127; P:regulation of cell population proliferation; IMP:MGI.
DR   GO; GO:0072001; P:renal system development; IGI:MGI.
DR   GO; GO:0009617; P:response to bacterium; IMP:MGI.
DR   InterPro; IPR036970; MECOM.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR24393:SF11; PTHR24393:SF11; 1.
DR   Pfam; PF00096; zf-C2H2; 8.
DR   SMART; SM00317; SET; 1.
DR   SMART; SM00355; ZnF_C2H2; 10.
DR   SUPFAM; SSF57667; SSF57667; 5.
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   Acetylation; Alternative promoter usage; Alternative splicing;
KW   Apoptosis; Complete proteome; Cytoplasm; Developmental protein;
KW   Differentiation; DNA-binding; Isopeptide bond; Metal-binding;
KW   Methyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW   Repeat; Transcription; Transcription regulation; Transferase;
KW   Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN         1   1232       Histone-lysine N-methyltransferase MECOM.
FT                                /FTId=PRO_0000047274.
FT   DOMAIN       80    192       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   ZN_FING     211    238       C2H2-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     265    287       C2H2-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     293    315       C2H2-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     321    344       C2H2-type 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     350    372       C2H2-type 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     378    400       C2H2-type 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     407    429       C2H2-type 7; atypical.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00042}.
FT   ZN_FING     914    936       C2H2-type 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     942    965       C2H2-type 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     971    993       C2H2-type 10. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   REGION      191    442       Interaction with SUV39H1 and probably
FT                                MAPK9 and SMAD3.
FT                                {ECO:0000269|PubMed:18619962}.
FT   MOTIF       611    624       Nuclear localization signal.
FT                                {ECO:0000255}.
FT   MOTIF       743    747       CTBP-binding motif 1. {ECO:0000250}.
FT   MOTIF       774    778       CTBP-binding motif 2. {ECO:0000250}.
FT   COMPBIAS   1067   1118       Asp/Glu-rich (acidic).
FT   MOD_RES     626    626       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     728    728       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q03112}.
FT   MOD_RES     742    742       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    1039   1039       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q03112}.
FT   MOD_RES    1041   1041       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   CROSSLNK    101    101       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q03112}.
FT   CROSSLNK    192    192       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q03112}.
FT   CROSSLNK    294    294       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q03112}.
FT   CROSSLNK    369    369       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q03112}.
FT   CROSSLNK    376    376       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q03112}.
FT   CROSSLNK    432    432       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q03112}.
FT   CROSSLNK    525    525       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q03112}.
FT   CROSSLNK    545    545       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q03112}.
FT   CROSSLNK    549    549       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q03112}.
FT   CROSSLNK    557    557       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q03112}.
FT   CROSSLNK    624    624       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q03112}.
FT   CROSSLNK    637    637       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q03112}.
FT   CROSSLNK    665    665       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q03112}.
FT   CROSSLNK    687    687       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q03112}.
FT   CROSSLNK    723    723       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q03112}.
FT   CROSSLNK    733    733       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q03112}.
FT   CROSSLNK    734    734       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q03112}.
FT   CROSSLNK    737    737       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q03112}.
FT   CROSSLNK    751    751       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q03112}.
FT   CROSSLNK    754    754       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q03112}.
FT   CROSSLNK    762    762       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q03112}.
FT   CROSSLNK    789    789       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q03112}.
FT   CROSSLNK    802    802       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q03112}.
FT   CROSSLNK    803    803       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q03112}.
FT   CROSSLNK    837    837       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q03112}.
FT   CROSSLNK    846    846       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q03112}.
FT   CROSSLNK    848    848       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q03112}.
FT   CROSSLNK    879    879       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q03112}.
FT   CROSSLNK   1020   1020       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q03112}.
FT   CROSSLNK   1055   1055       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q03112}.
FT   CROSSLNK   1058   1058       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q03112}.
FT   CROSSLNK   1122   1122       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q03112}.
FT   CROSSLNK   1129   1129       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q03112}.
FT   CROSSLNK   1134   1134       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q03112}.
FT   CROSSLNK   1151   1151       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q03112}.
FT   CROSSLNK   1178   1178       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q03112}.
FT   CROSSLNK   1186   1186       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q03112}.
FT   VAR_SEQ       1    190       Missing (in isoform 1).
FT                                /FTId=VSP_059487.
FT   VAR_SEQ     128    129       IL -> NR (in isoform 4).
FT                                /FTId=VSP_059488.
FT   VAR_SEQ     130   1232       Missing (in isoform 4).
FT                                /FTId=VSP_059489.
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
//
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