ID   MTG8R_MOUSE             Reviewed;         594 AA.
AC   O70374; B2RRH8; Q30BK8; Q6P288;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 3.
DT   24-JAN-2024, entry version 166.
DE   RecName: Full=Protein CBFA2T2;
DE   AltName: Full=MTG8-like protein;
DE   AltName: Full=MTG8-related protein 1;
GN   Name=Cbfa2t2; Synonyms=Cbfa2t2h, Mtgr1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RC   STRAIN=C57BL/6 X DBA/2;
RX   PubMed=16227606; DOI=10.1128/mcb.25.21.9576-9585.2005;
RA   Amann J.M., Chyla B.J., Ellis T.C., Martinez A., Moore A.C., Franklin J.L.,
RA   McGhee L., Meyers S., Ohm J.E., Luce K.S., Ouelette A.J., Washington M.K.,
RA   Thompson M.A., King D., Gautam S., Coffey R.J., Whitehead R.H.,
RA   Hiebert S.W.;
RT   "Mtgr1 is a transcriptional corepressor that is required for maintenance of
RT   the secretory cell lineage in the small intestine.";
RL   Mol. Cell. Biol. 25:9576-9585(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 61-140.
RC   STRAIN=129;
RX   PubMed=9790752; DOI=10.1006/geno.1998.5429;
RA   Calabi F., Cilli V.;
RT   "CBFA2T1, a gene rearranged in human leukemia, is a member of a multigene
RT   family.";
RL   Genomics 52:332-341(1998).
RN   [6]
RP   PROTEIN SEQUENCE OF 469-477, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [7]
RP   INTERACTION WITH TCF4.
RX   PubMed=18039847; DOI=10.1128/mcb.01242-07;
RA   Moore A.C., Amann J.M., Williams C.S., Tahinci E., Farmer T.E.,
RA   Martinez J.A., Yang G., Luce K.S., Lee E., Hiebert S.W.;
RT   "Myeloid translocation gene family members associate with T-cell factors
RT   (TCFs) and influence TCF-dependent transcription.";
RL   Mol. Cell. Biol. 28:977-987(2008).
RN   [8]
RP   FUNCTION, AND INTERACTION WITH CBFA2T3 AND TAL1.
RX   PubMed=19799863; DOI=10.1016/j.bbrc.2009.09.111;
RA   Cai Y., Xu Z., Xie J., Ham A.J., Koury M.J., Hiebert S.W., Brandt S.J.;
RT   "Eto2/MTG16 and MTGR1 are heteromeric corepressors of the TAL1/SCL
RT   transcription factor in murine erythroid progenitors.";
RL   Biochem. Biophys. Res. Commun. 390:295-301(2009).
RN   [9]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=19618476; DOI=10.1002/dvdy.22021;
RA   Alishahi A., Koyano-Nakagawa N., Nakagawa Y.;
RT   "Regional expression of MTG genes in the developing mouse central nervous
RT   system.";
RL   Dev. Dyn. 238:2095-2102(2009).
RN   [10]
RP   POSSIBLE INVOLVEMENT IN INTESTINAL TUMORIGENESIS.
RX   PubMed=21303973; DOI=10.1158/0008-5472.can-10-3317;
RA   Barrett C.W., Fingleton B., Williams A., Ning W., Fischer M.A.,
RA   Washington M.K., Chaturvedi R., Wilson K.T., Hiebert S.W., Williams C.S.;
RT   "MTGR1 is required for tumorigenesis in the murine AOM/DSS colitis-
RT   associated carcinoma model.";
RL   Cancer Res. 71:1302-1312(2011).
RN   [11]
RP   FUNCTION, AND INTERACTION WITH RBPJ AND GFI1.
RX   PubMed=25398765; DOI=10.1096/fj.14-254284;
RA   Parang B., Rosenblatt D., Williams A.D., Washington M.K., Revetta F.,
RA   Short S.P., Reddy V.K., Hunt A., Shroyer N.F., Engel M.E., Hiebert S.W.,
RA   Williams C.S.;
RT   "The transcriptional corepressor MTGR1 regulates intestinal secretory
RT   lineage allocation.";
RL   FASEB J. 29:786-795(2015).
RN   [12]
RP   FUNCTION, INTERACTION WITH PRDM14, AND MUTAGENESIS OF LEU-330; LEU-342;
RP   ALA-345; LEU-346; MET-360; LEU-363 AND LEU-374.
RX   PubMed=27281218; DOI=10.1038/nature18004;
RA   Tu S., Narendra V., Yamaji M., Vidal S.E., Rojas L.A., Wang X., Kim S.Y.,
RA   Garcia B.A., Tuschl T., Stadtfeld M., Reinberg D.;
RT   "Co-repressor CBFA2T2 regulates pluripotency and germline development.";
RL   Nature 534:387-390(2016).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 98-206 IN COMPLEX WITH PRDM14,
RP   FUNCTION, MUTAGENESIS OF ARG-105 AND LYS-109, AND TISSUE SPECIFICITY.
RX   PubMed=26523391; DOI=10.7554/elife.10150;
RA   Nady N., Gupta A., Ma Z., Swigut T., Koide A., Koide S., Wysocka J.;
RT   "ETO family protein Mtgr1 mediates Prdm14 functions in stem cell
RT   maintenance and primordial germ cell formation.";
RL   Elife 4:E10150-E10150(2015).
CC   -!- FUNCTION: Transcriptional corepressor which facilitates transcriptional
CC       repression via its association with DNA-binding transcription factors
CC       and recruitment of other corepressors and histone-modifying enzymes.
CC       Via association with PRDM14 is involved in regulation of embryonic stem
CC       cell (ESC) pluripotency. Involved in primordial germ cell (PCG)
CC       formation (PubMed:27281218). Stabilizes PRDM14 and OCT4 on chromatin in
CC       a homooligomerization-dependent mannerCan repress the expression of
CC       MMP7 in a ZBTB33-dependent manner (By similarity). Through
CC       heteromerization with CBFA2T3/MTG16 may be involved in regulation of
CC       the proliferation and the differentiation of erythroid progenitors by
CC       repressing the expression of TAL1 target genes (PubMed:19799863).
CC       Required for the maintenance of the secretory cell lineage in the small
CC       intestine (PubMed:16227606). Can inhibit Notch signaling probably by
CC       association with RBPJ and may be involved in GFI1-mediated Paneth cell
CC       differentiation (PubMed:25398765). {ECO:0000250|UniProtKB:O43439,
CC       ECO:0000269|PubMed:16227606, ECO:0000269|PubMed:25398765,
CC       ECO:0000269|PubMed:27281218}.
CC   -!- SUBUNIT: Homooligomer. Homotetramerization is mediated by the NHR2
CC       domain. Interacts with CBFA2T3/MTG16 (PubMed:19799863). Can interact
CC       with RUNX1T1/CBFA2T1. Heterotetramerization between members of the
CC       CBFA2T family is proposed (By similarity). Interacts with RBP, GFI1,
CC       TCF4, PRDM14 (PubMed:25398765, PubMed:18039847, PubMed:27281218).
CC       Interacts with TAL1 and CBFA2T3/MTG16; the heteromer with CBFA2T3/MTG16
CC       may function in repression of TAL1 (PubMed:19799863).
CC       {ECO:0000250|UniProtKB:O43439, ECO:0000269|PubMed:18039847,
CC       ECO:0000269|PubMed:19799863, ECO:0000269|PubMed:25398765,
CC       ECO:0000269|PubMed:27281218}.
CC   -!- INTERACTION:
CC       O70374; P22091: Tal1; NbExp=8; IntAct=EBI-8006755, EBI-8006437;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00440}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O70374-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O70374-2; Sequence=VSP_030517;
CC   -!- TISSUE SPECIFICITY: Expressed in embryonic stem cells.
CC       {ECO:0000269|PubMed:26523391}.
CC   -!- DEVELOPMENTAL STAGE: First expression detected on embryonic day 11.5.
CC       {ECO:0000269|PubMed:19618476}.
CC   -!- DOMAIN: Nervy homology region 2 (NHR2) mediates homo- and possibly
CC       heterotypic oligomerization by forming a four-helix bundle tetrameric
CC       structure. {ECO:0000250|UniProtKB:Q06455}.
CC   -!- DISEASE: Note=Required for tumorigenesis in a AOM/DSS colitis-
CC       associated carcinoma model. May be involved in intestinal
CC       tumorigenesis. {ECO:0000269|PubMed:21303973}.
CC   -!- MISCELLANEOUS: Loss of Mtgr1 impairs the maturation of secretory cells
CC       in the small intestine.
CC   -!- SIMILARITY: Belongs to the CBFA2T family. {ECO:0000305}.
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DR   EMBL; AK049206; BAC33609.1; -; mRNA.
DR   EMBL; AK040403; BAC30586.1; -; mRNA.
DR   EMBL; AK153602; BAE32114.1; -; mRNA.
DR   EMBL; DQ213025; ABB02690.1; -; mRNA.
DR   EMBL; AL772292; CAM13555.1; -; Genomic_DNA.
DR   EMBL; AL772292; CAM13556.1; -; Genomic_DNA.
DR   EMBL; BC064679; AAH64679.1; -; mRNA.
DR   EMBL; BC138410; AAI38411.1; -; mRNA.
DR   EMBL; BC145679; AAI45680.1; -; mRNA.
DR   EMBL; AF052219; AAC64697.1; -; Genomic_DNA.
DR   CCDS; CCDS16932.1; -. [O70374-1]
DR   RefSeq; NP_033953.1; NM_009823.1.
DR   RefSeq; NP_766448.1; NM_172860.2. [O70374-1]
DR   RefSeq; XP_006498703.1; XM_006498640.2. [O70374-2]
DR   PDB; 5ECJ; X-ray; 3.05 A; A/B=98-206.
DR   PDBsum; 5ECJ; -.
DR   AlphaFoldDB; O70374; -.
DR   SMR; O70374; -.
DR   BioGRID; 198521; 1.
DR   DIP; DIP-62032N; -.
DR   IntAct; O70374; 2.
DR   MINT; O70374; -.
DR   STRING; 10090.ENSMUSP00000043087; -.
DR   iPTMnet; O70374; -.
DR   PhosphoSitePlus; O70374; -.
DR   SwissPalm; O70374; -.
DR   jPOST; O70374; -.
DR   MaxQB; O70374; -.
DR   PaxDb; 10090-ENSMUSP00000043087; -.
DR   PeptideAtlas; O70374; -.
DR   ProteomicsDB; 291450; -. [O70374-1]
DR   ProteomicsDB; 291451; -. [O70374-2]
DR   Antibodypedia; 10684; 311 antibodies from 33 providers.
DR   DNASU; 12396; -.
DR   Ensembl; ENSMUST00000045270.15; ENSMUSP00000043087.9; ENSMUSG00000038533.16. [O70374-1]
DR   GeneID; 12396; -.
DR   KEGG; mmu:12396; -.
DR   UCSC; uc008njf.2; mouse. [O70374-1]
DR   AGR; MGI:1333833; -.
DR   CTD; 9139; -.
DR   MGI; MGI:1333833; Cbfa2t2.
DR   VEuPathDB; HostDB:ENSMUSG00000038533; -.
DR   eggNOG; ENOG502QTD6; Eukaryota.
DR   GeneTree; ENSGT00950000183176; -.
DR   HOGENOM; CLU_022077_2_0_1; -.
DR   InParanoid; O70374; -.
DR   OMA; WKHLDHX; -.
DR   OrthoDB; 5314634at2759; -.
DR   PhylomeDB; O70374; -.
DR   TreeFam; TF106303; -.
DR   BioGRID-ORCS; 12396; 4 hits in 77 CRISPR screens.
DR   ChiTaRS; Cbfa2t2; mouse.
DR   PRO; PR:O70374; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; O70374; Protein.
DR   Bgee; ENSMUSG00000038533; Expressed in substantia nigra and 282 other cell types or tissues.
DR   ExpressionAtlas; O70374; baseline and differential.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003714; F:transcription corepressor activity; IDA:MGI.
DR   GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0030855; P:epithelial cell differentiation; IMP:MGI.
DR   GO; GO:0060575; P:intestinal epithelial cell differentiation; IMP:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:MGI.
DR   GO; GO:0010977; P:negative regulation of neuron projection development; ISS:UniProtKB.
DR   GO; GO:0045746; P:negative regulation of Notch signaling pathway; IMP:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:MGI.
DR   GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR   Gene3D; 6.10.140.2220; -; 1.
DR   Gene3D; 6.10.250.230; -; 1.
DR   Gene3D; 1.20.120.1110; TAFH/NHR1 domain; 1.
DR   InterPro; IPR013289; CBFA2T1/2/3.
DR   InterPro; IPR013291; MTGR1.
DR   InterPro; IPR014896; NHR2.
DR   InterPro; IPR037249; TAFH/NHR1_dom_sf.
DR   InterPro; IPR003894; TAFH_NHR1.
DR   InterPro; IPR002893; Znf_MYND.
DR   PANTHER; PTHR10379; MTG8 ETO EIGHT TWENTY ONE PROTEIN; 1.
DR   PANTHER; PTHR10379:SF13; PROTEIN CBFA2T2; 1.
DR   Pfam; PF08788; NHR2; 1.
DR   Pfam; PF07531; TAFH; 1.
DR   Pfam; PF01753; zf-MYND; 1.
DR   PRINTS; PR01875; ETOFAMILY.
DR   PRINTS; PR01877; MTGR1PROTEIN.
DR   SMART; SM00549; TAFH; 1.
DR   SUPFAM; SSF144232; HIT/MYND zinc finger-like; 1.
DR   SUPFAM; SSF158553; TAFH domain-like; 1.
DR   PROSITE; PS51119; TAFH; 1.
DR   PROSITE; PS01360; ZF_MYND_1; 1.
DR   PROSITE; PS50865; ZF_MYND_2; 1.
DR   Genevisible; O70374; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Coiled coil; Direct protein sequencing;
KW   Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Repressor; Transcription; Transcription regulation;
KW   Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..594
FT                   /note="Protein CBFA2T2"
FT                   /id="PRO_0000218302"
FT   DOMAIN          104..199
FT                   /note="TAFH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00440"
FT   ZN_FING         498..534
FT                   /note="MYND-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   REGION          48..96
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          98..206
FT                   /note="Interaction with PRDM14"
FT                   /evidence="ECO:0000269|PubMed:26523391,
FT                   ECO:0000269|PubMed:27281218"
FT   REGION          220..257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          322..368
FT                   /note="Nervy homology region 2 (NHR2)"
FT                   /evidence="ECO:0000250|UniProtKB:O43439"
FT   REGION          388..416
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          426..475
FT                   /note="Nervy homology region 3 (NHR3)"
FT                   /evidence="ECO:0000250|UniProtKB:O43439"
FT   REGION          538..594
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          442..482
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        55..96
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        224..245
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        394..416
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        567..594
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         498
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   BINDING         501
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   BINDING         509
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   BINDING         512
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   BINDING         518
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   BINDING         522
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   BINDING         530
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   BINDING         534
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   MOD_RES         24
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O43439"
FT   MOD_RES         255
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O43439"
FT   MOD_RES         400
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O43439"
FT   MOD_RES         567
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O43439"
FT   CROSSLNK        29
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:O43439"
FT   CROSSLNK        440
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:O43439"
FT   VAR_SEQ         1..20
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_030517"
FT   MUTAGEN         105
FT                   /note="R->D: Disrupts interaction with PRDM14."
FT                   /evidence="ECO:0000269|PubMed:26523391"
FT   MUTAGEN         109
FT                   /note="K->E: Disrupts interaction with PRDM14."
FT                   /evidence="ECO:0000269|PubMed:26523391"
FT   MUTAGEN         330
FT                   /note="L->E: Reduces PRDM14 and OCT14 occupancy on target
FT                   sites, no effect on interaction with PRDM14, predicted to
FT                   impair homooligomerization; when associated with R-342;
FT                   R-345; E-346; E-360; R-363 and R-374."
FT                   /evidence="ECO:0000269|PubMed:27281218"
FT   MUTAGEN         342
FT                   /note="L->R: Reduces PRDM14 and OCT14 occupancy on target
FT                   sites, no effect on interaction with PRDM14, predicted to
FT                   impair homooligomerization; when associated with R-330;
FT                   R-345; E-346; E-360; R-363 and R-374."
FT                   /evidence="ECO:0000269|PubMed:27281218"
FT   MUTAGEN         345
FT                   /note="A->R: Reduces PRDM14 and OCT14 occupancy on target
FT                   sites, no effect on interaction with PRDM14, predicted to
FT                   impair homooligomerization; when associated with R-330;
FT                   R-342; E-346; E-360; R-363 and R-374."
FT                   /evidence="ECO:0000269|PubMed:27281218"
FT   MUTAGEN         346
FT                   /note="L->E: Reduces PRDM14 and OCT14 occupancy on target
FT                   sites, no effect on interaction with PRDM14, predicted to
FT                   impair homooligomerization; when associated with R-330;
FT                   R-342; R-345; R-363 and R-374."
FT                   /evidence="ECO:0000269|PubMed:27281218"
FT   MUTAGEN         360
FT                   /note="M->E: Reduces PRDM14 and OCT14 occupancy on target
FT                   sites, no effect on interaction with PRDM14, predicted to
FT                   impair homooligomerization; when associated with R-330;
FT                   R-342; R-345; E-346; E-360; R-363 and R-374."
FT                   /evidence="ECO:0000269|PubMed:27281218"
FT   MUTAGEN         363
FT                   /note="L->R: Reduces PRDM14 and OCT14 occupancy on target
FT                   sites, no effect on interaction with PRDM14, predicted to
FT                   impair homooligomerization; when associated with R-330;
FT                   R-342; R-345; E-346; E-360 and R-374."
FT                   /evidence="ECO:0000269|PubMed:27281218"
FT   MUTAGEN         374
FT                   /note="L->R: Reduces PRDM14 and OCT14 occupancy on target
FT                   sites, no effect on interaction with PRDM14, predicted to
FT                   impair homooligomerization; when associated with R-330;
FT                   R-342; R-345; E-346; E-360 and R-363."
FT                   /evidence="ECO:0000269|PubMed:27281218"
FT   CONFLICT        413
FT                   /note="Missing (in Ref. 1; BAC30586, 2; ABB02690 and 3;
FT                   CAM13556)"
FT                   /evidence="ECO:0000305"
FT   HELIX           106..124
FT                   /evidence="ECO:0007829|PDB:5ECJ"
FT   HELIX           126..140
FT                   /evidence="ECO:0007829|PDB:5ECJ"
FT   HELIX           146..157
FT                   /evidence="ECO:0007829|PDB:5ECJ"
FT   HELIX           165..181
FT                   /evidence="ECO:0007829|PDB:5ECJ"
SQ   SEQUENCE   594 AA;  65904 MW;  FCE4A6A0AFD66377 CRC64;
     MVGVPGAAAF QLGCEKRVPA MPGSPVEVKI QSRSSPPIMP PLPPINPGGP RPVSFTPTAL
     SNGINHSPPT LNGAPSPPQR FSNGPASSTS SALTNQQLPA TCGARQLSKL KRFLTTLQQF
     GNDISPEIGE KVRTLVLALV NSTVTIEEFH CKLQEATNFP LRPFVIPFLK ANLPLLQREL
     LHCARAAKQT PSQYLAQHEH LLLNTSIASP ADSSELLMEV HGNGKRPSPE RRDENNFERD
     TVPPEPPAKR VCTISPAPRH SPALTVPLMN PGGQFHPTPP PLQHYTLEDI ATSHLYREPN
     KMLEHREVRE RHHNLSLNGG YQDELVDHRL TEREWADEWK HLDHALNCIM EMVEKTRRSM
     AVLRRCQESD REELNYWKRR FNENTELRKT GTELVSRQHS PGSTDSLSND SQREFTSRPA
     TGYVPVEFWK KTEEAVNKVK IQAMSEVQKA VAEAEQKAFE VIATERARME QTIADVKRQA
     AEDAFLVINE QEESTENCWN CGRKASETCS GCNIARYCGS FCQHKDWERH HRLCGQSLHG
     HSPHSQSRPL LPGGRGSARS ADCSVPSPAL DKTSATTSRS STPASVTAID ANGL
//