MECOM_HUMAN
ID MECOM_HUMAN Reviewed; 1230 AA.
AC Q03112; A1L4F3; A8KA00; B7Z8W7; B7ZLQ3; B7ZLQ4; C9JAK0; D3DNP7; E7EQ57;
AC Q13465; Q13466; Q16122; Q5HYI1; Q6FH90; Q6MZS6; Q8NEI5; Q99917;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 3.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Histone-lysine N-methyltransferase MECOM {ECO:0000305};
DE EC=2.1.1.367 {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}, PRDM3 {ECO:0000303|PubMed:22939622};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 cell
RT 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., Nucifora G.;
RT "Intergenic splicing of MDS1 and EVI1 occurs in normal tissues as well as
RT in myeloid leukemia and produces a new member of the PR domain 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., Yokota J.,
RA Morishita K.;
RT "A novel gene, MEL1, mapped to 1p36.3 is highly homologous to the MDS1/EVI1
RT gene and is transcriptionally activated in t(1;3)(p36;q21)-positive
RT 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA 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., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., 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., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 [LARGE
RP 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 project:
RT 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; DOI=10.1002/j.1460-2075.1994.tb06288.x;
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) causes
RT 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 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 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., Ogawa S.,
RA 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 HISTONE
RP DEACETYLASES, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 743-ASP-LEU-744 AND
RP 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-binding
RT protein (CBP) and p300/CBP-associated factor (P/CAF) results in reversible
RT acetylation of EVI1 and in co-localization in nuclear speckles.";
RL J. Biol. Chem. 276:44936-44943(2001).
RN [15]
RP FUNCTION, ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), HOMOOLIGOMERIZATION,
RP INTERACTION WITH CTBP1 AND SMAD3, AND SUBCELLULAR 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., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT 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 TGFbeta- and
RT 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., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT 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 stem/progenitors and
RT leukemic cells.";
RL Oncogene 28:4364-4374(2009).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1039, AND IDENTIFICATION BY
RP 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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT 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 mammalian
RT heterochromatin integrity.";
RL Cell 150:948-960(2012).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-624; SER-726; SER-1037 AND
RP SER-1039, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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; LYS-721;
RP LYS-735; LYS-752; LYS-787; LYS-1127; LYS-1132 AND LYS-1152, AND
RP 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, AND
RP 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., Irie M.,
RA Sato A., Saito-Nanjo Y., Funayama R., Nagashima T., Inoue S., Nakayama K.,
RA Ozono K., Kure S., Matsubara Y., Imaizumi M., Aoki Y.;
RT "Mutations in MECOM, encoding oncoprotein EVI1, cause radioulnar synostosis
RT 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; LYS-721;
RP LYS-877; LYS-1053; LYS-1132 AND LYS-1152, AND IDENTIFICATION BY MASS
RP 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; LYS-292;
RP LYS-367; LYS-374; LYS-430; LYS-523; LYS-543; LYS-547; LYS-555; LYS-622;
RP LYS-635; LYS-663; LYS-685; LYS-721; LYS-731; LYS-732; LYS-735; LYS-749;
RP LYS-752; LYS-760; LYS-787; LYS-800; LYS-801; LYS-835; LYS-844; LYS-846;
RP LYS-877; LYS-1018; LYS-1053; LYS-1056; LYS-1120; LYS-1127; LYS-1132;
RP LYS-1149; LYS-1152; LYS-1176 AND LYS-1184, SUMOYLATION [LARGE SCALE
RP ANALYSIS] AT LYS-658 (ISOFORM 1), SUMOYLATION [LARGE SCALE ANALYSIS] AT
RP LYS-846 (ISOFORMS 2 AND 8), SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-202
RP AND LYS-723 (ISOFORM 4), SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-138
RP (ISOFORM 6), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
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: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 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:0000250|UniProtKB:P14404}.
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: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 signaling
CC (PubMed:10856240, PubMed:11568182, PubMed:15897867, PubMed:9665135).
CC {ECO:0000250|UniProtKB:P14404, ECO:0000269|PubMed:10856240,
CC ECO:0000269|PubMed:11568182, ECO:0000269|PubMed:15897867,
CC ECO:0000269|PubMed:9665135}.
CC -!- INTERACTION:
CC Q03112; P01100: FOS; NbExp=4; IntAct=EBI-1384862, EBI-852851;
CC Q03112; Q5R372-2: RABGAP1L; NbExp=3; IntAct=EBI-1384862, EBI-10692254;
CC Q03112; Q09028: RBBP4; NbExp=4; IntAct=EBI-1384862, EBI-620823;
CC Q03112; Q96EB6: SIRT1; NbExp=2; IntAct=EBI-1384862, EBI-1802965;
CC Q03112; Q9UBK9: UXT; NbExp=5; IntAct=EBI-1384862, EBI-357355;
CC Q03112; P56546: Ctbp2; Xeno; NbExp=3; IntAct=EBI-1384862, EBI-1384883;
CC Q03112-9; Q92870-2: APBB2; NbExp=3; IntAct=EBI-23820194, EBI-21535880;
CC Q03112-9; O95833: CLIC3; NbExp=3; IntAct=EBI-23820194, EBI-10192241;
CC Q03112-9; P04792: HSPB1; NbExp=3; IntAct=EBI-23820194, EBI-352682;
CC Q03112-9; O60333-2: KIF1B; NbExp=3; IntAct=EBI-23820194, EBI-10975473;
CC Q03112-9; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-23820194, EBI-396669;
CC Q03112-9; O76024: WFS1; NbExp=3; IntAct=EBI-23820194, EBI-720609;
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 Name=2; Synonyms=Evi-1c, Mds1/Evi1;
CC IsoId=Q03112-3; Sequence=VSP_059484;
CC Name=4;
CC IsoId=Q03112-4; Sequence=VSP_059480, VSP_059483, VSP_059484;
CC Name=5;
CC IsoId=Q03112-5; Sequence=VSP_059479;
CC Name=6;
CC IsoId=Q03112-6; Sequence=VSP_059479, VSP_059483;
CC Name=8;
CC IsoId=Q03112-8; Sequence=VSP_059484, VSP_059485, VSP_059486;
CC Name=9; Synonyms=MDS1;
CC IsoId=Q03112-9; Sequence=VSP_059481, VSP_059482;
CC -!- DOMAIN: Both zinc finger regions are required for the transcriptional
CC 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 of
CC chronic myelogenous leukemia (CML). Translocation t(3;21)(q26;q22) with
CC RUNX1/AML1. {ECO:0000269|PubMed:8313895}.
CC -!- DISEASE: Radioulnar synostosis with amegakaryocytic thrombocytopenia 2
CC (RUSAT2) [MIM:616738]: An autosomal dominant disease characterized by
CC proximal fusion of the radius and ulna resulting in extremely limited
CC pronation and supination of the forearm, and congenital
CC thrombocytopenia that progresses to pancytopenia.
CC {ECO:0000269|PubMed:26581901}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Note=A chromosomal aberration involving MDS1 is found in a
CC form of acute myeloid leukemia (AML). Translocation t(3;21) with AML1.
CC {ECO:0000269|PubMed:8643684}.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative promoter usage.
CC Unable to form homooligomers, to interact with CTBP1 and SMAD3 and to
CC repress TGF-beta signaling. {ECO:0000269|PubMed:15897867,
CC ECO:0007744|PubMed:28112733}.
CC -!- MISCELLANEOUS: [Isoform 9]: Produced by alternative promoter usage.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB29907.1; Type=Erroneous initiation; Note=Extended N-terminus.; 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=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/EVI103q26ID19.html";
CC ---------------------------------------------------------------------------
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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 PDB; 6BW3; X-ray; 2.20 A; B/D=1-12.
DR PDBsum; 6BW3; -.
DR AlphaFoldDB; Q03112; -.
DR SMR; Q03112; -.
DR BioGRID; 108423; 247.
DR DIP; DIP-38639N; -.
DR ELM; Q03112; -.
DR IntAct; Q03112; 38.
DR MINT; Q03112; -.
DR STRING; 9606.ENSP00000264674; -.
DR GlyGen; Q03112; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q03112; -.
DR PhosphoSitePlus; Q03112; -.
DR BioMuta; MECOM; -.
DR DMDM; 145559472; -.
DR EPD; Q03112; -.
DR jPOST; Q03112; -.
DR MassIVE; Q03112; -.
DR MaxQB; Q03112; -.
DR PaxDb; Q03112; -.
DR PeptideAtlas; Q03112; -.
DR PRIDE; Q03112; -.
DR ProteomicsDB; 17508; -.
DR ProteomicsDB; 58186; -. [Q03112-1]
DR ProteomicsDB; 58187; -. [Q03112-3]
DR ProteomicsDB; 58188; -. [Q03112-4]
DR ProteomicsDB; 58189; -. [Q03112-5]
DR ProteomicsDB; 58190; -. [Q03112-6]
DR ProteomicsDB; 59462; -.
DR Antibodypedia; 18615; 425 antibodies from 35 providers.
DR DNASU; 2122; -.
DR Ensembl; ENST00000264674.7; ENSP00000264674.3; ENSG00000085276.19. [Q03112-4]
DR Ensembl; ENST00000464456.5; ENSP00000419770.1; ENSG00000085276.19. [Q03112-5]
DR Ensembl; ENST00000468789.5; ENSP00000419995.1; ENSG00000085276.19. [Q03112-1]
DR Ensembl; ENST00000494292.6; ENSP00000417899.1; ENSG00000085276.19. [Q03112-7]
DR Ensembl; ENST00000628990.2; ENSP00000486104.1; ENSG00000085276.19. [Q03112-1]
DR Ensembl; ENST00000651503.2; ENSP00000498411.1; ENSG00000085276.19. [Q03112-3]
DR GeneID; 2122; -.
DR KEGG; hsa:2122; -.
DR MANE-Select; ENST00000651503.2; ENSP00000498411.1; NM_004991.4; NP_004982.2. [Q03112-3]
DR UCSC; uc003ffi.3; human. [Q03112-7]
DR CTD; 2122; -.
DR DisGeNET; 2122; -.
DR GeneCards; MECOM; -.
DR HGNC; HGNC:3498; MECOM.
DR HPA; ENSG00000085276; Tissue enhanced (stomach).
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 inv(3)(q21q26.2) or t(3;3)(q21;q26.2).
DR Orphanet; 71289; Radio-ulnar synostosis-amegakaryocytic thrombocytopenia syndrome.
DR PharmGKB; PA27912; -.
DR VEuPathDB; HostDB:ENSG00000085276; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000157208; -.
DR InParanoid; Q03112; -.
DR OMA; NKHPPVG; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q03112; -.
DR TreeFam; TF315309; -.
DR PathwayCommons; Q03112; -.
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 BioGRID-ORCS; 2122; 41 hits in 1106 CRISPR screens.
DR ChiTaRS; MECOM; human.
DR GeneWiki; MECOM; -.
DR GenomeRNAi; 2122; -.
DR Pharos; Q03112; Tbio.
DR PRO; PR:Q03112; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q03112; protein.
DR Bgee; ENSG00000085276; Expressed in cardia of stomach and 189 other tissues.
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:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0046974; F:histone methyltransferase activity (H3-K9 specific); ISS:UniProtKB.
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:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
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:0070828; P:heterochromatin organization; 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 GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd19214; PR-SET_PRDM3; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR044411; PRDM3_PR-SET.
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; Chromosomal rearrangement; Cytoplasm;
KW Developmental protein; Differentiation; Disease variant; DNA-binding;
KW Isopeptide bond; Metal-binding; Methyltransferase; Nucleus; Phosphoprotein;
KW Proto-oncogene; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Transferase; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1230
FT /note="Histone-lysine N-methyltransferase MECOM"
FT /id="PRO_0000047273"
FT DOMAIN 78..190
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT ZN_FING 209..236
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 263..285
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 291..313
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 319..342
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 348..370
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 376..398
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 405..427
FT /note="C2H2-type 7; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 912..934
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 940..963
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 969..991
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 189..440
FT /note="Interaction with MAPK9, SMAD3 and probably SUV39H1"
FT /evidence="ECO:0000269|PubMed:10856240"
FT REGION 510..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 718..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 990..1009
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1030..1113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 609..622
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 741..745
FT /note="CTBP-binding motif 1"
FT /evidence="ECO:0000250"
FT MOTIF 772..776
FT /note="CTBP-binding motif 2"
FT /evidence="ECO:0000250"
FT COMPBIAS 511..530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..579
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..600
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..618
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..785
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 994..1009
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1030..1045
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1066..1085
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 624
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 726
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 740
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14404"
FT MOD_RES 1037
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1039
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 99
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 190
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 249
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 292
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 367
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 374
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 430
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 523
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 543
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 547
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 555
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 622
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 635
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 663
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 685
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 721
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 731
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 732
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 735
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 749
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 752
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 760
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 787
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 800
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 801
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 835
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 844
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 846
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 877
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 1018
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1053
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 1056
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1120
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1127
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 1132
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 1149
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1152
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 1176
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1184
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..188
FT /note="Missing (in isoform 1, isoform 5 and isoform 6)"
FT /id="VSP_059479"
FT VAR_SEQ 1..125
FT /note="MRSKGRARKLATNNECVYGNYPEIPLEEMPDADGVASTPSLNIQEPCSPATS
FT SEAFTPKEGSPYKAPIYIPDDIPIPAEFELRESNMPGAGLGIWTKRKIEVGEKFGPYVG
FT EQRSNLKDPSYGWE -> M (in isoform 4)"
FT /id="VSP_059480"
FT VAR_SEQ 126..169
FT /note="ILDEFYNVKFCIDASQPDVGSWLKYIRFAGCYDQHNLVACQIND -> VHLP
FT RSRRVSVHSWLYLGKRSSDVGIAFSQADVYMPGLQCAFLS (in isoform 9)"
FT /id="VSP_059481"
FT VAR_SEQ 170..1230
FT /note="Missing (in isoform 9)"
FT /id="VSP_059482"
FT VAR_SEQ 326
FT /note="K -> KQ (in isoform 4 and isoform 6)"
FT /id="VSP_059483"
FT VAR_SEQ 859
FT /note="Q -> QFQLPDQRTW (in isoform 1, isoform 4, isoform 8
FT and isoform 2)"
FT /id="VSP_059484"
FT VAR_SEQ 939..945
FT /note="PYRCKYC -> LKNKDLQ (in isoform 8)"
FT /id="VSP_059485"
FT VAR_SEQ 946..1230
FT /note="Missing (in isoform 8)"
FT /id="VSP_059486"
FT VARIANT 120
FT /note="P -> S (in dbSNP:rs7622799)"
FT /id="VAR_051183"
FT VARIANT 295
FT /note="Q -> R (in dbSNP:rs34896995)"
FT /id="VAR_061928"
FT VARIANT 929
FT /note="R -> W (in RUSAT2; alters transcriptional
FT regulation; dbSNP:rs864309724)"
FT /evidence="ECO:0000269|PubMed:26581901"
FT /id="VAR_076308"
FT VARIANT 930
FT /note="H -> R (in RUSAT2; alters transcriptional
FT regulation; dbSNP:rs864309723)"
FT /evidence="ECO:0000269|PubMed:26581901"
FT /id="VAR_076309"
FT VARIANT 935
FT /note="T -> A (in RUSAT2; alters transcriptional
FT regulation; dbSNP:rs864309722)"
FT /evidence="ECO:0000269|PubMed:26581901"
FT /id="VAR_076310"
FT MUTAGEN 743..744
FT /note="DL->AS: Partial loss of interaction with CTBP1. Loss
FT of interaction with CTBP1; when associated with 586-A-S-
FT 775."
FT /evidence="ECO:0000269|PubMed:11568182"
FT MUTAGEN 774..775
FT /note="DL->AS: Partial loss of interaction with CTBP1. Loss
FT of interaction with CTBP1; when associated with 555-A-S-
FT 744."
FT /evidence="ECO:0000269|PubMed:11568182"
FT CONFLICT 126..127
FT /note="IL -> VR (in Ref. 2; AAB05840)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="Q -> R (in Ref. 6; CAE45952)"
FT /evidence="ECO:0000305"
FT CONFLICT 363
FT /note="L -> P (in Ref. 6; CAE45952)"
FT /evidence="ECO:0000305"
FT CONFLICT 489
FT /note="F -> S (in Ref. 4; BAF85554)"
FT /evidence="ECO:0000305"
FT CONFLICT 491
FT /note="F -> V (in Ref. 1; CAA38735)"
FT /evidence="ECO:0000305"
FT CONFLICT 631
FT /note="S -> P (in Ref. 6; CAI46086)"
FT /evidence="ECO:0000305"
FT CONFLICT 731
FT /note="K -> R (in Ref. 6; CAE45952)"
FT /evidence="ECO:0000305"
FT CONFLICT 909
FT /note="K -> R (in Ref. 4; BAF85554)"
FT /evidence="ECO:0000305"
FT CONFLICT 920
FT /note="I -> V (in Ref. 6; CAI46086)"
FT /evidence="ECO:0000305"
FT CONFLICT 975
FT /note="D -> Y (in Ref. 1; CAA38735)"
FT /evidence="ECO:0000305"
FT CONFLICT 1054
FT /note="D -> E (in Ref. 1; CAA38735)"
FT /evidence="ECO:0000305"
FT CONFLICT 1060
FT /note="T -> P (in Ref. 1; CAA38735)"
FT /evidence="ECO:0000305"
FT CONFLICT 1085
FT /note="N -> Y (in Ref. 1; CAA38735)"
FT /evidence="ECO:0000305"
FT CONFLICT 1171
FT /note="V -> A (in Ref. 4; BAF85554)"
FT /evidence="ECO:0000305"
FT CONFLICT 1187..1191
FT /note="AYAMM -> VQIFP (in Ref. 11; AAB37456)"
FT /evidence="ECO:0000305"
FT CONFLICT 1192
FT /note="L -> P (in Ref. 6; CAE45952)"
FT /evidence="ECO:0000305"
FT CROSSLNK Q03112-1:658
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK Q03112-3:846
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK Q03112-4:202
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK Q03112-4:723
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK Q03112-6:138
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK Q03112-8:846
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
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
