ID MTG8_MOUSE Reviewed; 577 AA. AC Q61909; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 24-JAN-2024, entry version 168. DE RecName: Full=Protein CBFA2T1; DE AltName: Full=Protein MTG8; GN Name=Runx1t1; Synonyms=Cbfa2t1, Cbfa2t1h, Mtg8; 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 [MRNA]. RC STRAIN=ICR; TISSUE=Brain; RX PubMed=8575770; DOI=10.1006/geno.1995.9941; RA Niwa-Kawakita M., Miyoshi H., Gotoh O., Matsushima Y., Nishimura M., RA Shisa H., Ohki M.; RT "Cloning and gene mapping of the mouse homologue of the CBFA2T1 gene RT associated with human acute myeloid leukemia."; RL Genomics 29:755-759(1995). RN [2] RP FUNCTION. RX PubMed=23527555; DOI=10.1111/febs.12256; RA Wang S.S., Huang H.Y., Chen S.Z., Li X., Zhang W.T., Tang Q.Q.; RT "Gdf6 induces commitment of pluripotent mesenchymal C3H10T1/2 cells to the RT adipocyte lineage."; RL FEBS J. 280:2644-2651(2013). 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 Can repress the expression of MMP7 in a ZBTB33-dependent manner. Can CC repress transactivation mediated by TCF12 (By similarity). Acts as a CC negative regulator of adipogenesis (PubMed:23527555). CC {ECO:0000250|UniProtKB:Q06455, ECO:0000269|PubMed:23527555}. CC -!- SUBUNIT: Homotetramer (By similarity). Heterotetramer with CBFA2T2 and CC CBFA2T3 (By similarity). Interacts with TCF12, SIN3A, HDAC1, HDAC2, CC HDAC3, NCOR1 and NCOR2. Interacts with ATN1 (via its N-terminus); the CC interaction enhances the transcriptional repression (By similarity). CC {ECO:0000250|UniProtKB:Q06455}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00440}. CC Note=Colocalizes with ATN1 in discrete nuclear dots. {ECO:0000250}. CC -!- DOMAIN: The TAFH domain mediates interaction with transcription CC regulators. {ECO:0000250|UniProtKB:Q06455}. 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 -!- SIMILARITY: Belongs to the CBFA2T family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D32007; BAA06774.1; -; mRNA. DR CCDS; CCDS17978.1; -. DR RefSeq; NP_033952.1; NM_009822.3. DR AlphaFoldDB; Q61909; -. DR BMRB; Q61909; -. DR SMR; Q61909; -. DR BioGRID; 198520; 7. DR IntAct; Q61909; 9. DR MINT; Q61909; -. DR STRING; 10090.ENSMUSP00000127109; -. DR iPTMnet; Q61909; -. DR PhosphoSitePlus; Q61909; -. DR SwissPalm; Q61909; -. DR MaxQB; Q61909; -. DR PaxDb; 10090-ENSMUSP00000006761; -. DR ProteomicsDB; 286073; -. DR Pumba; Q61909; -. DR Antibodypedia; 25672; 315 antibodies from 34 providers. DR DNASU; 12395; -. DR Ensembl; ENSMUST00000098256.4; ENSMUSP00000095856.4; ENSMUSG00000006586.16. DR GeneID; 12395; -. DR KEGG; mmu:12395; -. DR UCSC; uc008sax.3; mouse. DR AGR; MGI:104793; -. DR CTD; 862; -. DR MGI; MGI:104793; Runx1t1. DR VEuPathDB; HostDB:ENSMUSG00000006586; -. DR eggNOG; ENOG502QTD6; Eukaryota. DR GeneTree; ENSGT00950000183176; -. DR HOGENOM; CLU_022077_2_0_1; -. DR InParanoid; Q61909; -. DR OMA; ESSVMEY; -. DR OrthoDB; 5314634at2759; -. DR BioGRID-ORCS; 12395; 0 hits in 80 CRISPR screens. DR ChiTaRS; Runx1t1; mouse. DR PRO; PR:Q61909; -. DR Proteomes; UP000000589; Chromosome 4. DR RNAct; Q61909; Protein. DR Bgee; ENSMUSG00000006586; Expressed in rostral migratory stream and 240 other cell types or tissues. DR ExpressionAtlas; Q61909; baseline and differential. DR GO; GO:0016363; C:nuclear matrix; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0017053; C:transcription repressor complex; ISS:UniProtKB. DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI. DR GO; GO:0042802; F:identical protein binding; IPI:MGI. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003714; F:transcription corepressor activity; ISO:MGI. DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro. DR GO; GO:0045444; P:fat cell differentiation; IDA:MGI. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISS:UniProtKB. DR GO; GO:0045599; P:negative regulation of fat cell differentiation; IMP:UniProtKB. DR GO; GO:0010977; P:negative regulation of neuron projection development; ISS:UniProtKB. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IDA: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; IPR013290; CBFA2T1. DR InterPro; IPR013289; CBFA2T1/2/3. 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:SF5; PROTEIN CBFA2T1; 1. DR Pfam; PF08788; NHR2; 1. DR Pfam; PF07531; TAFH; 1. DR Pfam; PF01753; zf-MYND; 1. DR PRINTS; PR01875; ETOFAMILY. DR PRINTS; PR01876; MTG8PROTEIN. 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; Q61909; MM. PE 2: Evidence at transcript level; KW DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; KW Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1..577 FT /note="Protein CBFA2T1" FT /id="PRO_0000218300" FT DOMAIN 93..188 FT /note="TAFH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00440" FT ZN_FING 488..524 FT /note="MYND-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134" FT REGION 1..87 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 203..271 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 310..356 FT /note="Important for oligomerization" FT /evidence="ECO:0000250" FT REGION 310..356 FT /note="Nervy homology region 2 (NHR2)" FT /evidence="ECO:0000250|UniProtKB:Q06455" FT REGION 374..396 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 416..465 FT /note="Nervy homology region 3 (NHR3)" FT /evidence="ECO:0000250|UniProtKB:Q06455" FT REGION 529..577 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 38..87 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 208..236 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 243..260 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 488 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134" FT BINDING 491 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134" FT BINDING 499 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134" FT BINDING 502 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134" FT BINDING 508 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134" FT BINDING 512 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134" FT BINDING 520 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134" FT BINDING 524 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134" FT MOD_RES 14 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q06455" FT MOD_RES 390 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q06455" SQ SEQUENCE 577 AA; 64338 MW; 2656F185318C4B11 CRC64; MPDRTEKHST MPDSPVDVKT QSRLTPPAMP PPPTTQGAPR TSSFTPTTLT NGTSHSPTAL NGAPSPPNGF SNGPSSSSSS SLANQQLPPA CGARQLSKLK RFLTTLQQFG NDISPEIGER VRTLVLGLVN STLTIEEFHS KLQEATNFPL RPFVIPFLKA NLPLLQRELL HCARLAKQNP AQYLAQHEQL LLDASTTSPV DSSELLLDVN ENGKRRTPDR TKENGFDREP LHSEHPSKRP CTISPGQRYS PNNGLSYQPN GLPHPTPPPP QHYRLDDMAI AHHYRDSYRH PSHRDLRDRN RPMGLHGTRQ EEMIDHRLTD REWAEEWKHL DHLLNCIMDM VEKTRRSLTV LRRCQEADRE ELNYWIRRYS DAEDLKKGGS SSSSHSRQQS PVNPDPVALD AHREFLHRPA SGYVPEEIWK KAEEAVNEVK RQAMTELQKA VSEAERKAHD MITTERAKME RTVAEAKRQA AEDALAVINQ QEDSSESCWN CGRKASETCS GCNTARYCGS FCQHKDWEKH HHICGQTLQA PQQGDTPAVS SSVTPSSGAG SPMDTPPAAT PRSTTPGTPS TIETTPR //