MTG8R_MOUSE
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 03-AUG-2022, entry version 158.
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 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; O70374; -.
DR PeptideAtlas; O70374; -.
DR PRIDE; O70374; -.
DR ProteomicsDB; 291450; -. [O70374-1]
DR ProteomicsDB; 291451; -. [O70374-2]
DR Antibodypedia; 10684; 292 antibodies from 33 providers.
DR DNASU; 12396; -.
DR Ensembl; ENSMUST00000045270; ENSMUSP00000043087; ENSMUSG00000038533. [O70374-1]
DR GeneID; 12396; -.
DR KEGG; mmu:12396; -.
DR UCSC; uc008njf.2; mouse. [O70374-1]
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; ICGQGIH; -.
DR PhylomeDB; O70374; -.
DR TreeFam; TF106303; -.
DR BioGRID-ORCS; 12396; 4 hits in 72 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 278 other tissues.
DR ExpressionAtlas; O70374; baseline and differential.
DR Genevisible; O70374; MM.
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:0030855; P:epithelial cell differentiation; IMP:MGI.
DR GO; GO:0060575; P:intestinal epithelial cell differentiation; IMP:UniProtKB.
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:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 1.20.120.1110; -; 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; PTHR10379; 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; SSF158553; SSF158553; 1.
DR PROSITE; PS51119; TAFH; 1.
DR PROSITE; PS01360; ZF_MYND_1; 1.
DR PROSITE; PS50865; ZF_MYND_2; 1.
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; R-
FT 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; R-
FT 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; R-
FT 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; R-
FT 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; R-
FT 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; R-
FT 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; R-
FT 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
