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Database: UniProt
Entry: Q03112
LinkDB: Q03112
Original site: Q03112 
ID   MECOM_HUMAN             Reviewed;        1230 AA.
AC   Q03112; A1L4F3; A8KA00; B7Z8W7; B7ZLQ3; B7ZLQ4; C9JAK0; D3DNP7;
AC   E7EQ57; Q13465; Q13466; Q16122; Q5HYI1; Q6FH90; Q6MZS6; Q8NEI5;
AC   Q99917;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   28-MAR-2018, sequence version 3.
DT   10-APR-2019, entry version 187.
DE   RecName: Full=Histone-lysine N-methyltransferase MECOM {ECO:0000305};
DE            EC=2.1.1.43 {ECO:0000250|UniProtKB:P14404};
DE   AltName: Full=Ecotropic virus integration site 1 protein homolog;
DE            Short=EVI-1;
DE   AltName: Full=MDS1 and EVI1 complex locus protein {ECO:0000305};
DE   AltName: Full=Myelodysplasia syndrome 1 protein;
DE   AltName: Full=Myelodysplasia syndrome-associated protein 1;
GN   Name=MECOM {ECO:0000312|HGNC:HGNC:3498};
GN   Synonyms=EVI1 {ECO:0000303|PubMed:8643684},
GN   MDS1 {ECO:0000303|PubMed:8643684},
GN   PRDM3 {ECO:0000303|PubMed:22939622};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND ALTERNATIVE SPLICING.
RX   PubMed=2115646;
RA   Morishita K., Parganas E., Douglass E.C., Ihle J.N.;
RT   "Unique expression of the human Evi-1 gene in an endometrial carcinoma
RT   cell line: sequence of cDNAs and structure of alternatively spliced
RT   transcripts.";
RL   Oncogene 5:963-971(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 9), NUCLEOTIDE SEQUENCE [MRNA] OF
RP   14-127 (ISOFORMS 2/7/8), AND CHROMOSOMAL TRANSLOCATION WITH AML1.
RC   TISSUE=Kidney, and Pancreas;
RX   PubMed=8643684; DOI=10.1073/pnas.93.4.1642;
RA   Fears S., Mathieu C., Zeleznik-Le N., Huang S., Rowley J.D.,
RA   Nucifora G.;
RT   "Intergenic splicing of MDS1 and EVI1 occurs in normal tissues as well
RT   as in myeloid leukemia and produces a new member of the PR domain
RT   family.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:1642-1647(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX   PubMed=11050005;
RA   Mochizuki N., Shimizu S., Nagasawa T., Tanaka H., Taniwaki M.,
RA   Yokota J., Morishita K.;
RT   "A novel gene, MEL1, mapped to 1p36.3 is highly homologous to the
RT   MDS1/EVI1 gene and is transcriptionally activated in t(1;3)(p36;q21)-
RT   positive leukemia cells.";
RL   Blood 96:3209-3214(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 8).
RC   TISSUE=Trachea;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 9).
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC   TISSUE=Adipose tissue, and Fetal kidney;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16641997; DOI=10.1038/nature04728;
RA   Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
RA   Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA   Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA   Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA   Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA   Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA   Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA   Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA   Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA   Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA   Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA   Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA   Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA   Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA   Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA   Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA   Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA   Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
RA   Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA   Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA   Gibbs R.A.;
RT   "The DNA sequence, annotation and analysis of human chromosome 3.";
RL   Nature 440:1194-1198(2006).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 6), NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] (ISOFORM 9), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 704-1230 (ISOFORM 7).
RC   TISSUE=Lung;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 13-1230 (ISOFORM 7), AND CHROMOSOMAL
RP   TRANSLOCATION WITH RUNX1 IN CHRONIC MYELOCYTIC LEUKEMIA.
RX   PubMed=8313895;
RA   Mitani K., Ogawa S., Tanaka T., Miyoshi H., Kurokawa M., Mano H.,
RA   Yazaki Y., Ohki M., Hirai H.;
RT   "Generation of the AML1-EVI-1 fusion gene in the t(3;21)(q26;q22)
RT   causes blastic crisis in chronic myelocytic leukemia.";
RL   EMBO J. 13:504-510(1994).
RN   [11]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1149-1191.
RX   PubMed=8700545;
RA   Ogawa S., Kurokawa M., Tanaka T., Mitani K., Inazawa J., Hangaishi A.,
RA   Tanaka K., Matsuo Y., Minowada J., Tsubota T., Yazaki Y., Hirai H.;
RT   "Structurally altered Evi-1 protein generated in the 3q21q26
RT   syndrome.";
RL   Oncogene 13:183-191(1996).
RN   [12]
RP   FUNCTION IN TGF-BETA SIGNALING, INTERACTION WITH SMAD3 AND SMAD4, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=9665135; DOI=10.1038/27945;
RA   Kurokawa M., Mitani K., Irie K., Matsuyama T., Takahashi T., Chiba S.,
RA   Yazaki Y., Matsumoto K., Hirai H.;
RT   "The oncoprotein Evi-1 represses TGF-beta signalling by inhibiting
RT   Smad3.";
RL   Nature 394:92-96(1998).
RN   [13]
RP   FUNCTION, AND INTERACTION WITH MAPK8 AND MAPK9.
RX   PubMed=10856240; DOI=10.1093/emboj/19.12.2958;
RA   Kurokawa M., Mitani K., Yamagata T., Takahashi T., Izutsu K.,
RA   Ogawa S., Moriguchi T., Nishida E., Yazaki Y., Hirai H.;
RT   "The evi-1 oncoprotein inhibits c-Jun N-terminal kinase and prevents
RT   stress-induced cell death.";
RL   EMBO J. 19:2958-2968(2000).
RN   [14]
RP   FUNCTION, ACETYLATION, INTERACTION WITH CREBBP; CTBP1; KAT2B AND
RP   HISTONE DEACETYLASES, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP   743-ASP-LEU-744 AND 774-ASP-LEU-775.
RX   PubMed=11568182; DOI=10.1074/jbc.M106733200;
RA   Chakraborty S., Senyuk V., Sitailo S., Chi Y., Nucifora G.;
RT   "Interaction of EVI1 with cAMP-responsive element-binding protein-
RT   binding protein (CBP) and p300/CBP-associated factor (P/CAF) results
RT   in reversible acetylation of EVI1 and in co-localization in nuclear
RT   speckles.";
RL   J. Biol. Chem. 276:44936-44943(2001).
RN   [15]
RP   FUNCTION, ALTERNATIVE SPLICING (ISOFORMS 1 AND 2),
RP   HOMOOLIGOMERIZATION, INTERACTION WITH CTBP1 AND SMAD3, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=15897867; DOI=10.1038/sj.onc.1208754;
RA   Nitta E., Izutsu K., Yamaguchi Y., Imai Y., Ogawa S., Chiba S.,
RA   Kurokawa M., Hirai H.;
RT   "Oligomerization of Evi-1 regulated by the PR domain contributes to
RT   recruitment of corepressor CtBP.";
RL   Oncogene 24:6165-6173(2005).
RN   [16]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [17]
RP   FUNCTION IN APOPTOSIS.
RX   PubMed=16462766; DOI=10.1038/sj.onc.1209403;
RA   Liu Y., Chen L., Ko T.C., Fields A.P., Thompson E.A.;
RT   "Evi1 is a survival factor which conveys resistance to both
RT   TGFbeta- and taxol-mediated cell death via PI3K/AKT.";
RL   Oncogene 25:3565-3575(2006).
RN   [18]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18220336; DOI=10.1021/pr0705441;
RA   Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA   Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT   efficient phosphoproteomic analysis.";
RL   J. Proteome Res. 7:1346-1351(2008).
RN   [19]
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   [20]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1039, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [21]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
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).
RN   [22]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-624; SER-726; SER-1037
RP   AND SER-1039, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [23]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-190; LYS-555; LYS-685;
RP   LYS-721; LYS-735; LYS-752; LYS-787; LYS-1127; LYS-1132 AND LYS-1152,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25218447; DOI=10.1038/nsmb.2890;
RA   Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA   Vertegaal A.C.;
RT   "Uncovering global SUMOylation signaling networks in a site-specific
RT   manner.";
RL   Nat. Struct. Mol. Biol. 21:927-936(2014).
RN   [24]
RP   INVOLVEMENT IN RUSAT2, VARIANTS RUSAT2 TRP-929; ARG-930 AND ALA-935,
RP   AND CHARACTERIZATION OF VARIANTS RUSAT2 TRP-929; ARG-930 AND ALA-935.
RX   PubMed=26581901; DOI=10.1016/j.ajhg.2015.10.010;
RA   Niihori T., Ouchi-Uchiyama M., Sasahara Y., Kaneko T., Hashii Y.,
RA   Irie M., Sato A., Saito-Nanjo Y., Funayama R., Nagashima T., Inoue S.,
RA   Nakayama K., Ozono K., Kure S., Matsubara Y., Imaizumi M., Aoki Y.;
RT   "Mutations in MECOM, encoding oncoprotein EVI1, cause radioulnar
RT   synostosis with amegakaryocytic thrombocytopenia.";
RL   Am. J. Hum. Genet. 97:848-854(2015).
RN   [25]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-190; LYS-555; LYS-685;
RP   LYS-721; LYS-877; LYS-1053; LYS-1132 AND LYS-1152, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA   Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA   Vertegaal A.C.;
RT   "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL   Cell Rep. 10:1778-1791(2015).
RN   [26]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-99; LYS-190; LYS-249;
RP   LYS-292; LYS-367; LYS-374; LYS-430; LYS-523; LYS-543; LYS-547;
RP   LYS-555; LYS-622; LYS-635; LYS-663; LYS-685; LYS-721; LYS-731;
RP   LYS-732; LYS-735; LYS-749; LYS-752; LYS-760; LYS-787; LYS-800;
RP   LYS-801; LYS-835; LYS-844; LYS-846; LYS-877; LYS-1018; LYS-1053;
RP   LYS-1056; LYS-1120; LYS-1127; LYS-1132; LYS-1149; LYS-1152; LYS-1176
RP   AND LYS-1184, SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-658 (ISOFORM
RP   1), SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-846 (ISOFORMS 2 AND 8),
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-202 AND LYS-723 (ISOFORM 4),
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-138 (ISOFORM 6), AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-
RT   modification with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
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:10856240,
CC       ECO:0000269|PubMed:11568182, ECO:0000269|PubMed:15897867,
CC       ECO:0000269|PubMed:16462766, ECO:0000269|PubMed:19767769,
CC       ECO:0000269|PubMed:9665135}.
CC   -!- FUNCTION: Isoform 7: 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:0000250|UniProtKB:P14404}.
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:0000250|UniProtKB:P14404};
CC   -!- SUBUNIT: Isoform 1: Homooligomer. Interacts with SUV39H1 (via SET
CC       domain); enhances MECOM transcriptional repression activity (By
CC       similarity). Interacts with CTBP1. Interacts with SMAD3 (via MH2
CC       domain); the interaction is direct. Interacts with SMAD4; through
CC       interaction with SMAD3. Interacts with CREBBP, KAT2B and histone
CC       deacetylases. Interacts with MAPK8 and MAPK9; inhibits JNK
CC       signaling (PubMed:10856240, PubMed:11568182, PubMed:15897867,
CC       PubMed:9665135). {ECO:0000250|UniProtKB:P14404,
CC       ECO:0000269|PubMed:10856240, ECO:0000269|PubMed:11568182,
CC       ECO:0000269|PubMed:15897867, ECO:0000269|PubMed:9665135}.
CC   -!- INTERACTION:
CC       P56546:Ctbp2 (xeno); NbExp=3; IntAct=EBI-1384862, EBI-1384883;
CC       P01100:FOS; NbExp=4; IntAct=EBI-1384862, EBI-852851;
CC       Q5R372-2:RABGAP1L; NbExp=3; IntAct=EBI-1384862, EBI-10692254;
CC       Q96EB6:SIRT1; NbExp=2; IntAct=EBI-1384862, EBI-1802965;
CC       Q9UBK9:UXT; NbExp=5; IntAct=EBI-1384862, EBI-357355;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11568182,
CC       ECO:0000269|PubMed:15897867, ECO:0000269|PubMed:9665135}. Nucleus
CC       speckle {ECO:0000269|PubMed:11568182}. Cytoplasm
CC       {ECO:0000269|PubMed:22939622}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative promoter usage, Alternative splicing; Named isoforms=8;
CC       Name=7;
CC         IsoId=Q03112-7; Sequence=Displayed;
CC       Name=1; Synonyms=Long, Evi-1a;
CC         IsoId=Q03112-1; Sequence=VSP_059479, VSP_059484;
CC         Note=Contains a glycyl lysine isopeptide (Lys-Gly) (interchain
CC         with G-Cter in SUMO2) at position 658.
CC         {ECO:0000244|PubMed:28112733};
CC       Name=2; Synonyms=Evi-1c, Mds1/Evi1;
CC         IsoId=Q03112-3; Sequence=VSP_059484;
CC         Note=Produced by alternative promoter usage. Unable to form
CC         homooligomers, to interact with CTBP1 and SMAD3 and to repress
CC         TGF-beta signaling. Contains a glycyl lysine isopeptide
CC         (Lys-Gly) (interchain with G-Cter in SUMO2) at position 846.
CC         {ECO:0000244|PubMed:28112733, ECO:0000269|PubMed:15897867};
CC       Name=4;
CC         IsoId=Q03112-4; Sequence=VSP_059480, VSP_059483, VSP_059484;
CC         Note=Contains a glycyl lysine isopeptide (Lys-Gly) (interchain
CC         with G-Cter in SUMO2) at position 202. Contains a glycyl lysine
CC         isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) at
CC         position 723. {ECO:0000244|PubMed:28112733};
CC       Name=5;
CC         IsoId=Q03112-5; Sequence=VSP_059479;
CC       Name=6;
CC         IsoId=Q03112-6; Sequence=VSP_059479, VSP_059483;
CC         Note=Contains a glycyl lysine isopeptide (Lys-Gly) (interchain
CC         with G-Cter in SUMO2) at position 138.
CC         {ECO:0000244|PubMed:28112733};
CC       Name=8;
CC         IsoId=Q03112-8; Sequence=VSP_059484, VSP_059485, VSP_059486;
CC         Note=Contains a glycyl lysine isopeptide (Lys-Gly) (interchain
CC         with G-Cter in SUMO2) at position 846.
CC         {ECO:0000244|PubMed:28112733};
CC       Name=9; Synonyms=MDS1;
CC         IsoId=Q03112-9; Sequence=VSP_059481, VSP_059482;
CC         Note=Produced by alternative promoter usage.;
CC   -!- DOMAIN: Both zinc finger regions are required for the
CC       transcriptional activation of PBX1.
CC   -!- PTM: Phosphorylated. {ECO:0000250}.
CC   -!- PTM: May be acetylated by CREBBP and KAT2B.
CC       {ECO:0000269|PubMed:11568182}.
CC   -!- DISEASE: Note=A chromosomal aberration involving EVI1 is a cause
CC       of chronic myelogenous leukemia (CML). Translocation
CC       t(3;21)(q26;q22) with RUNX1/AML1. {ECO:0000269|PubMed:8313895}.
CC   -!- DISEASE: Radioulnar synostosis with amegakaryocytic
CC       thrombocytopenia 2 (RUSAT2) [MIM:616738]: An autosomal dominant
CC       disease characterized by proximal fusion of the radius and ulna
CC       resulting in extremely limited pronation and supination of the
CC       forearm, and congenital thrombocytopenia that progresses to
CC       pancytopenia. {ECO:0000269|PubMed:26581901}. Note=The disease is
CC       caused by mutations affecting the gene represented in this entry.
CC   -!- DISEASE: Note=A chromosomal aberration involving MDS1 is found in
CC       a form of acute myeloid leukemia (AML). Translocation t(3;21) with
CC       AML1. {ECO:0000269|PubMed:8643684}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB29907.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
CC       Sequence=AAB29907.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA that is the result of a chromosomal aberration involving EVI1 and RUNX1.; Evidence={ECO:0000305};
CC       Sequence=AAI30521.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/EVI103q26ID19.html";
DR   EMBL; X54989; CAA38735.1; -; mRNA.
DR   EMBL; U43292; AAB05839.1; -; mRNA.
DR   EMBL; U43293; AAB05840.1; -; mRNA.
DR   EMBL; AK292865; BAF85554.1; -; mRNA.
DR   EMBL; AK304098; BAH14103.1; -; mRNA.
DR   EMBL; CR541866; CAG46664.1; -; mRNA.
DR   EMBL; CR541886; CAG46684.1; -; mRNA.
DR   EMBL; BX640908; CAE45952.1; -; mRNA.
DR   EMBL; BX647613; CAI46086.1; -; mRNA.
DR   EMBL; AC007849; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC024099; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC069220; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC074033; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC078985; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KF457717; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471052; EAW78549.1; -; Genomic_DNA.
DR   EMBL; CH471052; EAW78553.1; -; Genomic_DNA.
DR   EMBL; CH471052; EAW78556.1; -; Genomic_DNA.
DR   EMBL; CH471052; EAW78557.1; -; Genomic_DNA.
DR   EMBL; BC031019; AAH31019.1; -; mRNA.
DR   EMBL; BC069498; AAH69498.1; -; mRNA.
DR   EMBL; BC130520; AAI30521.1; ALT_INIT; mRNA.
DR   EMBL; BC143951; AAI43952.1; -; mRNA.
DR   EMBL; BC143952; AAI43953.1; -; mRNA.
DR   EMBL; S69002; AAB29907.1; ALT_SEQ; mRNA.
DR   EMBL; S82592; AAB37456.1; -; mRNA.
DR   CCDS; CCDS3205.1; -. [Q03112-1]
DR   CCDS; CCDS54669.1; -. [Q03112-5]
DR   CCDS; CCDS54670.1; -. [Q03112-4]
DR   PIR; A60191; A60191.
DR   PIR; S41705; S41705.
DR   RefSeq; NP_001098547.3; NM_001105077.3. [Q03112-4]
DR   RefSeq; NP_001098548.2; NM_001105078.3. [Q03112-1]
DR   RefSeq; NP_001157471.1; NM_001163999.1. [Q03112-6]
DR   RefSeq; NP_001157472.1; NM_001164000.1. [Q03112-5]
DR   RefSeq; NP_001192123.1; NM_001205194.1. [Q03112-1]
DR   RefSeq; NP_004982.2; NM_004991.3. [Q03112-3]
DR   RefSeq; NP_005232.2; NM_005241.3. [Q03112-1]
DR   RefSeq; XP_005247272.1; XM_005247215.3.
DR   RefSeq; XP_005247276.1; XM_005247219.2.
DR   RefSeq; XP_005247277.1; XM_005247220.2.
DR   RefSeq; XP_005247278.1; XM_005247221.2.
DR   RefSeq; XP_005247280.1; XM_005247223.2.
DR   RefSeq; XP_016861363.1; XM_017005874.1. [Q03112-4]
DR   RefSeq; XP_016861364.1; XM_017005875.1.
DR   RefSeq; XP_016861365.1; XM_017005876.1.
DR   UniGene; Hs.656395; -.
DR   UniGene; Hs.744090; -.
DR   PDB; 6BW3; X-ray; 2.20 A; B/D=1-12.
DR   PDBsum; 6BW3; -.
DR   ProteinModelPortal; Q03112; -.
DR   SMR; Q03112; -.
DR   BioGrid; 108423; 54.
DR   DIP; DIP-38639N; -.
DR   ELM; Q03112; -.
DR   IntAct; Q03112; 13.
DR   MINT; Q03112; -.
DR   STRING; 9606.ENSP00000264674; -.
DR   iPTMnet; Q03112; -.
DR   PhosphoSitePlus; Q03112; -.
DR   BioMuta; MECOM; -.
DR   DMDM; 145559472; -.
DR   jPOST; Q03112; -.
DR   MaxQB; Q03112; -.
DR   PaxDb; Q03112; -.
DR   PeptideAtlas; Q03112; -.
DR   PRIDE; Q03112; -.
DR   ProteomicsDB; 58186; -.
DR   ProteomicsDB; 58187; -. [Q03112-3]
DR   ProteomicsDB; 58188; -. [Q03112-4]
DR   ProteomicsDB; 58189; -. [Q03112-5]
DR   ProteomicsDB; 58190; -. [Q03112-6]
DR   ProteomicsDB; 59462; -.
DR   DNASU; 2122; -.
DR   Ensembl; ENST00000264674; ENSP00000264674; ENSG00000085276. [Q03112-4]
DR   Ensembl; ENST00000464456; ENSP00000419770; ENSG00000085276. [Q03112-5]
DR   Ensembl; ENST00000468789; ENSP00000419995; ENSG00000085276. [Q03112-1]
DR   Ensembl; ENST00000494292; ENSP00000417899; ENSG00000085276. [Q03112-7]
DR   Ensembl; ENST00000628990; ENSP00000486104; ENSG00000085276. [Q03112-1]
DR   GeneID; 2122; -.
DR   KEGG; hsa:2122; -.
DR   UCSC; uc003ffi.3; human. [Q03112-7]
DR   CTD; 2122; -.
DR   DisGeNET; 2122; -.
DR   EuPathDB; HostDB:ENSG00000085276.17; -.
DR   GeneCards; MECOM; -.
DR   H-InvDB; HIX0003836; -.
DR   HGNC; HGNC:3498; MECOM.
DR   HPA; HPA046537; -.
DR   MalaCards; MECOM; -.
DR   MIM; 165215; gene.
DR   MIM; 600049; gene.
DR   MIM; 616738; phenotype.
DR   neXtProt; NX_Q03112; -.
DR   OpenTargets; ENSG00000085276; -.
DR   Orphanet; 402020; Acute myeloid leukemia with inv3(q21;q26.2) or t(3;3)(q21;q26.2).
DR   Orphanet; 52688; Myelodysplastic syndrome.
DR   Orphanet; 71289; Radio-ulnar synostosis-amegakaryocytic thrombocytopenia syndrome.
DR   PharmGKB; PA27912; -.
DR   PharmGKB; PA30722; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   eggNOG; COG5048; LUCA.
DR   GeneTree; ENSGT00940000157208; -.
DR   HOVERGEN; HBG005619; -.
DR   InParanoid; Q03112; -.
DR   KO; K04462; -.
DR   OMA; SMVNMNH; -.
DR   OrthoDB; 406002at2759; -.
DR   PhylomeDB; Q03112; -.
DR   TreeFam; TF315309; -.
DR   Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
DR   Reactome; R-HSA-8943724; Regulation of PTEN gene transcription.
DR   SignaLink; Q03112; -.
DR   SIGNOR; Q03112; -.
DR   ChiTaRS; MECOM; human.
DR   GeneWiki; MECOM; -.
DR   GenomeRNAi; 2122; -.
DR   PRO; PR:Q03112; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   Bgee; ENSG00000085276; Expressed in 221 organ(s), highest expression level in endometrium.
DR   ExpressionAtlas; Q03112; baseline and differential.
DR   Genevisible; Q03112; HS.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; TAS:Reactome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0071425; P:hematopoietic stem cell proliferation; ISS:UniProtKB.
DR   GO; GO:0046329; P:negative regulation of JNK cascade; IMP:UniProtKB.
DR   GO; GO:0043069; P:negative regulation of programmed cell death; IMP:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0051726; P:regulation of cell cycle; IDA:UniProtKB.
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   3D-structure; Acetylation; Alternative promoter usage;
KW   Alternative splicing; Apoptosis; Chromosomal rearrangement;
KW   Complete proteome; Cytoplasm; Developmental protein; Differentiation;
KW   Disease mutation; DNA-binding; Isopeptide bond; Metal-binding;
KW   Methyltransferase; Nucleus; Phosphoprotein; Polymorphism;
KW   Proto-oncogene; Reference proteome; Repeat; Transcription;
KW   Transcription regulation; Transferase; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN         1   1230       Histone-lysine N-methyltransferase MECOM.
FT                                /FTId=PRO_0000047273.
FT   DOMAIN       78    190       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   ZN_FING     209    236       C2H2-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     263    285       C2H2-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     291    313       C2H2-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     319    342       C2H2-type 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     348    370       C2H2-type 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     376    398       C2H2-type 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     405    427       C2H2-type 7; atypical.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00042}.
FT   ZN_FING     912    934       C2H2-type 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     940    963       C2H2-type 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     969    991       C2H2-type 10. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   REGION      189    440       Interaction with MAPK9, SMAD3 and
FT                                probably SUV39H1.
FT                                {ECO:0000269|PubMed:10856240}.
FT   MOTIF       609    622       Nuclear localization signal.
FT                                {ECO:0000255}.
FT   MOTIF       741    745       CTBP-binding motif 1. {ECO:0000250}.
FT   MOTIF       772    776       CTBP-binding motif 2. {ECO:0000250}.
FT   COMPBIAS   1065   1116       Asp/Glu-rich (acidic).
FT   MOD_RES     624    624       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     726    726       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     740    740       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P14404}.
FT   MOD_RES    1037   1037       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES    1039   1039       Phosphoserine.
FT                                {ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:23186163}.
FT   CROSSLNK     99     99       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    190    190       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447,
FT                                ECO:0000244|PubMed:25772364,
FT                                ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    249    249       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    292    292       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    367    367       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    374    374       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    430    430       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    523    523       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    543    543       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    547    547       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    555    555       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447,
FT                                ECO:0000244|PubMed:25772364,
FT                                ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    622    622       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    635    635       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    663    663       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    685    685       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447,
FT                                ECO:0000244|PubMed:25772364,
FT                                ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    721    721       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447,
FT                                ECO:0000244|PubMed:25772364,
FT                                ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    731    731       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    732    732       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    735    735       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447,
FT                                ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    749    749       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    752    752       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447,
FT                                ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    760    760       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    787    787       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447,
FT                                ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    800    800       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    801    801       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    835    835       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    844    844       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    846    846       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    877    877       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25772364,
FT                                ECO:0000244|PubMed:28112733}.
FT   CROSSLNK   1018   1018       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK   1053   1053       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25772364,
FT                                ECO:0000244|PubMed:28112733}.
FT   CROSSLNK   1056   1056       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK   1120   1120       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK   1127   1127       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447,
FT                                ECO:0000244|PubMed:28112733}.
FT   CROSSLNK   1132   1132       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447,
FT                                ECO:0000244|PubMed:25772364,
FT                                ECO:0000244|PubMed:28112733}.
FT   CROSSLNK   1149   1149       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK   1152   1152       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447,
FT                                ECO:0000244|PubMed:25772364,
FT                                ECO:0000244|PubMed:28112733}.
FT   CROSSLNK   1176   1176       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK   1184   1184       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   VAR_SEQ       1    188       Missing (in isoform 1, isoform 5 and
FT                                isoform 6).
FT                                /FTId=VSP_059479.
FT   VAR_SEQ       1    125       MRSKGRARKLATNNECVYGNYPEIPLEEMPDADGVASTPSL
FT                                NIQEPCSPATSSEAFTPKEGSPYKAPIYIPDDIPIPAEFEL
FT                                RESNMPGAGLGIWTKRKIEVGEKFGPYVGEQRSNLKDPSYG
FT                                WE -> M (in isoform 4).
FT                                /FTId=VSP_059480.
FT   VAR_SEQ     126    169       ILDEFYNVKFCIDASQPDVGSWLKYIRFAGCYDQHNLVACQ
FT                                IND -> VHLPRSRRVSVHSWLYLGKRSSDVGIAFSQADVY
FT                                MPGLQCAFLS (in isoform 9).
FT                                /FTId=VSP_059481.
FT   VAR_SEQ     170   1230       Missing (in isoform 9).
FT                                /FTId=VSP_059482.
FT   VAR_SEQ     326    326       K -> KQ (in isoform 4 and isoform 6).
FT                                /FTId=VSP_059483.
FT   VAR_SEQ     859    859       Q -> QFQLPDQRTW (in isoform 1, isoform 4,
FT                                isoform 8 and isoform 2).
FT                                /FTId=VSP_059484.
FT   VAR_SEQ     939    945       PYRCKYC -> LKNKDLQ (in isoform 8).
FT                                /FTId=VSP_059485.
FT   VAR_SEQ     946   1230       Missing (in isoform 8).
FT                                /FTId=VSP_059486.
FT   VARIANT     120    120       P -> S (in dbSNP:rs7622799).
FT                                /FTId=VAR_051183.
FT   VARIANT     295    295       Q -> R (in dbSNP:rs34896995).
FT                                /FTId=VAR_061928.
FT   VARIANT     929    929       R -> W (in RUSAT2; alters transcriptional
FT                                regulation; dbSNP:rs864309724).
FT                                {ECO:0000269|PubMed:26581901}.
FT                                /FTId=VAR_076308.
FT   VARIANT     930    930       H -> R (in RUSAT2; alters transcriptional
FT                                regulation; dbSNP:rs864309723).
FT                                {ECO:0000269|PubMed:26581901}.
FT                                /FTId=VAR_076309.
FT   VARIANT     935    935       T -> A (in RUSAT2; alters transcriptional
FT                                regulation; dbSNP:rs864309722).
FT                                {ECO:0000269|PubMed:26581901}.
FT                                /FTId=VAR_076310.
FT   MUTAGEN     743    744       DL->AS: Partial loss of interaction with
FT                                CTBP1. Loss of interaction with CTBP1;
FT                                when associated with 586-A-S-775.
FT                                {ECO:0000269|PubMed:11568182}.
FT   MUTAGEN     774    775       DL->AS: Partial loss of interaction with
FT                                CTBP1. Loss of interaction with CTBP1;
FT                                when associated with 555-A-S-744.
FT                                {ECO:0000269|PubMed:11568182}.
FT   CONFLICT    126    127       IL -> VR (in Ref. 2; AAB05840).
FT                                {ECO:0000305}.
FT   CONFLICT    208    208       Q -> R (in Ref. 6; CAE45952).
FT                                {ECO:0000305}.
FT   CONFLICT    363    363       L -> P (in Ref. 6; CAE45952).
FT                                {ECO:0000305}.
FT   CONFLICT    489    489       F -> S (in Ref. 4; BAF85554).
FT                                {ECO:0000305}.
FT   CONFLICT    491    491       F -> V (in Ref. 1; CAA38735).
FT                                {ECO:0000305}.
FT   CONFLICT    631    631       S -> P (in Ref. 6; CAI46086).
FT                                {ECO:0000305}.
FT   CONFLICT    731    731       K -> R (in Ref. 6; CAE45952).
FT                                {ECO:0000305}.
FT   CONFLICT    909    909       K -> R (in Ref. 4; BAF85554).
FT                                {ECO:0000305}.
FT   CONFLICT    920    920       I -> V (in Ref. 6; CAI46086).
FT                                {ECO:0000305}.
FT   CONFLICT    975    975       D -> Y (in Ref. 1; CAA38735).
FT                                {ECO:0000305}.
FT   CONFLICT   1054   1054       D -> E (in Ref. 1; CAA38735).
FT                                {ECO:0000305}.
FT   CONFLICT   1060   1060       T -> P (in Ref. 1; CAA38735).
FT                                {ECO:0000305}.
FT   CONFLICT   1085   1085       N -> Y (in Ref. 1; CAA38735).
FT                                {ECO:0000305}.
FT   CONFLICT   1171   1171       V -> A (in Ref. 4; BAF85554).
FT                                {ECO:0000305}.
FT   CONFLICT   1187   1191       AYAMM -> VQIFP (in Ref. 11; AAB37456).
FT                                {ECO:0000305}.
FT   CONFLICT   1192   1192       L -> P (in Ref. 6; CAE45952).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1230 AA;  138136 MW;  49E9B7CBCD422042 CRC64;
     MRSKGRARKL ATNNECVYGN YPEIPLEEMP DADGVASTPS LNIQEPCSPA TSSEAFTPKE
     GSPYKAPIYI PDDIPIPAEF ELRESNMPGA GLGIWTKRKI EVGEKFGPYV GEQRSNLKDP
     SYGWEILDEF YNVKFCIDAS QPDVGSWLKY IRFAGCYDQH NLVACQINDQ IFYRVVADIA
     PGEELLLFMK SEDYPHETMA PDIHEERQYR CEDCDQLFES KAELADHQKF PCSTPHSAFS
     MVEEDFQQKL ESENDLQEIH TIQECKECDQ VFPDLQSLEK HMLSHTEERE YKCDQCPKAF
     NWKSNLIRHQ MSHDSGKHYE CENCAKVFTD PSNLQRHIRS QHVGARAHAC PECGKTFATS
     SGLKQHKHIH SSVKPFICEV CHKSYTQFSN LCRHKRMHAD CRTQIKCKDC GQMFSTTSSL
     NKHRRFCEGK NHFAAGGFFG QGISLPGTPA MDKTSMVNMS HANPGLADYF GANRHPAGLT
     FPTAPGFSFS FPGLFPSGLY HRPPLIPASS PVKGLSSTEQ TNKSQSPLMT HPQILPATQD
     ILKALSKHPS VGDNKPVELQ PERSSEERPF EKISDQSESS DLDDVSTPSG SDLETTSGSD
     LESDIESDKE KFKENGKMFK DKVSPLQNLA SINNKKEYSN HSIFSPSLEE QTAVSGAVND
     SIKAIASIAE KYFGSTGLVG LQDKKVGALP YPSMFPLPFF PAFSQSMYPF PDRDLRSLPL
     KMEPQSPGEV KKLQKGSSES PFDLTTKRKD EKPLTPVPSK PPVTPATSQD QPLDLSMGSR
     SRASGTKLTE PRKNHVFGGK KGSNVESRPA SDGSLQHARP TPFFMDPIYR VEKRKLTDPL
     EALKEKYLRP SPGFLFHPQM SAIENMAEKL ESFSALKPEA SELLQSVPSM FNFRAPPNAL
     PENLLRKGKE RYTCRYCGKI FPRSANLTRH LRTHTGEQPY RCKYCDRSFS ISSNLQRHVR
     NIHNKEKPFK CHLCDRCFGQ QTNLDRHLKK HENGNMSGTA TSSPHSELES TGAILDDKED
     AYFTEIRNFI GNSNHGSQSP RNVEERMNGS HFKDEKALVT SQNSDLLDDE EVEDEVLLDE
     EDEDNDITGK TGKEPVTSNL HEGNPEDDYE ETSALEMSCK TSPVRYKEEE YKSGLSALDH
     IRHFTDSLKM RKMEDNQYSE AELSSFSTSH VPEELKQPLH RKSKSQAYAM MLSLSDKESL
     HSTSHSSSNV WHSMARAAAE SSAIQSISHV
//
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