ID FOG1_MOUSE Reviewed; 995 AA. AC O35615; DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 27-MAR-2024, entry version 182. DE RecName: Full=Zinc finger protein ZFPM1; DE AltName: Full=Friend of GATA protein 1; DE Short=FOG-1; DE Short=Friend of GATA 1; DE AltName: Full=Zinc finger protein multitype 1; GN Name=Zfpm1; Synonyms=Fog, Fog1; 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], FUNCTION, SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, DEVELOPMENTAL STAGE, AND INTERACTION WITH GATA1; GATA2 AND RP GATA3. RC TISSUE=Erythroleukemia; RX PubMed=9230307; DOI=10.1016/s0092-8674(00)80318-9; RA Tsang A.P., Visvader J.E., Turner C.A., Fujiwara Y., Yu C., Weiss M.J., RA Crossley M., Orkin S.H.; RT "FOG, a multitype zinc finger protein, acts as a cofactor for transcription RT factor GATA-1 in erythroid and megakaryocytic differentiation."; RL Cell 90:109-119(1997). RN [2] RP FUNCTION. RX PubMed=9553047; DOI=10.1101/gad.12.8.1176; RA Tsang A.P., Fujiwara Y., Hom D.B., Orkin S.H.; RT "Failure of megakaryopoiesis and arrested erythropoiesis in mice lacking RT the GATA-1 transcriptional cofactor FOG."; RL Genes Dev. 12:1176-1188(1998). RN [3] RP INTERACTION WITH GATA1, AND MUTAGENESIS OF CYS-698 AND CYS-719. RX PubMed=9837943; DOI=10.1074/jbc.273.50.33595; RA Fox A.H., Kowalski K., King G.F., Mackay J.P., Crossley M.; RT "Key residues characteristic of GATA N-fingers are recognized by FOG."; RL J. Biol. Chem. 273:33595-33603(1998). RN [4] RP FUNCTION, AND MUTAGENESIS OF SER-706. RX PubMed=10078204; DOI=10.1016/s1097-2765(00)80312-3; RA Crispino J.D., Lodish M.B., MacKay J.P., Orkin S.H.; RT "Use of altered specificity mutants to probe a specific protein-protein RT interaction in differentiation: the GATA-1:FOG complex."; RL Mol. Cell 3:219-228(1999). RN [5] RP FUNCTION, INTERACTION WITH GATA1 AND CTBP2, AND MUTAGENESIS OF VAL-254; RP PHE-255; PRO-256; LYS-258; ASP-259; GLY-261; ILE-262; TRP-263; ARG-265; RP SER-266; GLU-267; ARG-268; ASN-269; GLN-271; LEU-274; LEU-275; TYR-276; RP TYR-277; SER-280; ARG-281; 811-PRO--LEU-814; TYR-612; TYR-718 AND TYR-985. RX PubMed=10329627; DOI=10.1093/emboj/18.10.2812; RA Fox A.H., Liew C., Holmes M., Kowalski K., Mackay J., Crossley M.; RT "Transcriptional cofactors of the FOG family interact with GATA proteins by RT means of multiple zinc fingers."; RL EMBO J. 18:2812-2822(1999). RN [6] RP FUNCTION, INTERACTION WITH CTBP2, AND MUTAGENESIS OF 813-ASP-LEU-814. RX PubMed=11940669; DOI=10.1128/mcb.22.9.3121-3128.2002; RA Katz S.G., Cantor A.B., Orkin S.H.; RT "Interaction between FOG-1 and the corepressor C-terminal binding protein RT is dispensable for normal erythropoiesis in vivo."; RL Mol. Cell. Biol. 22:3121-3128(2002). RN [7] RP FUNCTION. RX PubMed=12356738; DOI=10.1093/emboj/cdf527; RA Wang X., Crispino J.D., Letting D.L., Nakazawa M., Poncz M., Blobel G.A.; RT "Control of megakaryocyte-specific gene expression by GATA-1 and FOG-1: RT role of Ets transcription factors."; RL EMBO J. 21:5225-5234(2002). RN [8] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=14614148; DOI=10.1073/pnas.1936250100; RA Katz S.G., Williams A., Yang J., Fujiwara Y., Tsang A.P., Epstein J.A., RA Orkin S.H.; RT "Endothelial lineage-mediated loss of the GATA cofactor Friend of GATA 1 RT impairs cardiac development."; RL Proc. Natl. Acad. Sci. U.S.A. 100:14030-14035(2003). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-925 AND SER-927, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143; SER-286; SER-497; RP SER-500; SER-822; SER-925 AND SER-927, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, RC Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [11] RP STRUCTURE BY NMR OF 328-360, INTERACTION WITH TACC3, AND MUTAGENESIS OF RP VAL-334; LEU-336; LEU-339; SER-340; THR-343; THR-344; LYS-345; ALA-346; RP ASN-347; GLU-349; ARG-350; LEU-352; LYS-353; VAL-354; THR-356 AND ASP-357. RX PubMed=15234987; DOI=10.1074/jbc.m404130200; RA Simpson R.J.Y., Yi Lee S.H., Bartle N., Sum E.Y., Visvader J.E., RA Matthews J.M., Mackay J.P., Crossley M.; RT "A classic zinc finger from Friend of GATA mediates an interaction with the RT coiled-coil of transforming acidic coiled-coil 3."; RL J. Biol. Chem. 279:39789-39797(2004). CC -!- FUNCTION: Transcription regulator that plays an essential role in CC erythroid and megakaryocytic cell differentiation. Essential cofactor CC that acts via the formation of a heterodimer with transcription factors CC of the GATA family GATA1, GATA2 and GATA3. Such heterodimer can both CC activate or repress transcriptional activity, depending on the cell and CC promoter context. The heterodimer formed with GATA proteins is CC essential to activate expression of genes such as NFE2, ITGA2B, CC alpha- and beta-globin, while it represses expression of KLF1. May be CC involved in regulation of some genes in gonads. May also be involved in CC cardiac development, in a non-redundant way with ZFPM2/FOG2. CC {ECO:0000269|PubMed:10078204, ECO:0000269|PubMed:10329627, CC ECO:0000269|PubMed:11940669, ECO:0000269|PubMed:12356738, CC ECO:0000269|PubMed:14614148, ECO:0000269|PubMed:9230307, CC ECO:0000269|PubMed:9553047}. CC -!- SUBUNIT: Interacts with the N-terminal zinc-finger of GATA1, GATA2 and CC GATA3. Interacts with corepressor CTBP2; this interaction is however CC not essential for corepressor activity in erythropoiesis. Interacts CC with TACC3. {ECO:0000269|PubMed:10329627, ECO:0000269|PubMed:11940669, CC ECO:0000269|PubMed:15234987, ECO:0000269|PubMed:9230307, CC ECO:0000269|PubMed:9837943}. CC -!- INTERACTION: CC O35615; P17679: Gata1; NbExp=7; IntAct=EBI-4394596, EBI-3903251; CC O35615; Q6ZQ88: Kdm1a; NbExp=2; IntAct=EBI-4394596, EBI-1216284; CC O35615; Q9JJ11: Tacc3; NbExp=7; IntAct=EBI-4394596, EBI-2553611; CC O35615; P15976: GATA1; Xeno; NbExp=5; IntAct=EBI-4394596, EBI-3909284; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9230307}. CC -!- TISSUE SPECIFICITY: Mainly expressed in hematopoietic tissues. CC Expressed in the spleen, a primary site of hematopoiesis in the adult CC mouse, as well as in the liver and testis, but not in the heart, brain, CC lung, kidney, or skeletal muscle. Among hematopoietic cell lines, it is CC strongly expressed in erythroid and megakaryocytic cell lines. CC Expressed at low level in several lymphoid and early myeloid cell CC lines. Not expressed in mast cell and macrophage lines. Expressed in CC the heart, where it colocalizes with GATA4, GATA5 and GATA6. CC {ECO:0000269|PubMed:14614148, ECO:0000269|PubMed:9230307}. CC -!- DEVELOPMENTAL STAGE: First expressed in two extraembryonic mesodermal CC derivatives, the yolk sac and the allantois in 8.5 dpc embryos. CC Localized to the embryonic red blood cells within the yolk sac blood CC islands. {ECO:0000269|PubMed:9230307}. CC -!- DOMAIN: The CCHC FOG-type zinc fingers 1, 2, 3 and 5 bind directly to CC GATA-type zinc fingers. The Tyr residue adjacent to the last Cys of the CC CCHC FOG-type zinc finger is essential for the interaction with GATA- CC type zinc fingers. CC -!- SIMILARITY: Belongs to the FOG (Friend of GATA) family. CC {ECO:0000255|PROSITE-ProRule:PRU01153}. 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; AF006492; AAC53292.1; -; mRNA. DR CCDS; CCDS22733.1; -. DR RefSeq; NP_033595.1; NM_009569.4. DR RefSeq; XP_006530914.1; XM_006530851.3. DR PDB; 1SRK; NMR; -; A=328-360. DR PDB; 2MPL; NMR; -; A=100-226. DR PDBsum; 1SRK; -. DR PDBsum; 2MPL; -. DR AlphaFoldDB; O35615; -. DR BMRB; O35615; -. DR SMR; O35615; -. DR BioGRID; 204687; 12. DR CORUM; O35615; -. DR DIP; DIP-48414N; -. DR IntAct; O35615; 14. DR MINT; O35615; -. DR STRING; 10090.ENSMUSP00000058037; -. DR iPTMnet; O35615; -. DR PhosphoSitePlus; O35615; -. DR EPD; O35615; -. DR jPOST; O35615; -. DR MaxQB; O35615; -. DR PaxDb; 10090-ENSMUSP00000058037; -. DR PeptideAtlas; O35615; -. DR ProteomicsDB; 271783; -. DR Antibodypedia; 30722; 156 antibodies from 24 providers. DR DNASU; 22761; -. DR Ensembl; ENSMUST00000054052.15; ENSMUSP00000058037.9; ENSMUSG00000049577.16. DR GeneID; 22761; -. DR KEGG; mmu:22761; -. DR UCSC; uc009nsj.1; mouse. DR AGR; MGI:1095400; -. DR CTD; 161882; -. DR MGI; MGI:1095400; Zfpm1. DR VEuPathDB; HostDB:ENSMUSG00000049577; -. DR eggNOG; KOG1721; Eukaryota. DR GeneTree; ENSGT00530000063823; -. DR HOGENOM; CLU_010755_0_0_1; -. DR InParanoid; O35615; -. DR OMA; AHQGVKA; -. DR OrthoDB; 5402989at2759; -. DR PhylomeDB; O35615; -. DR TreeFam; TF331342; -. DR Reactome; R-MMU-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function. DR Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production. DR BioGRID-ORCS; 22761; 5 hits in 81 CRISPR screens. DR ChiTaRS; Apaf1; mouse. DR EvolutionaryTrace; O35615; -. DR PRO; PR:O35615; -. DR Proteomes; UP000000589; Chromosome 8. DR RNAct; O35615; Protein. DR Bgee; ENSMUSG00000049577; Expressed in femorotibial joint and 203 other cell types or tissues. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0005667; C:transcription regulator complex; ISO:MGI. DR GO; GO:0017053; C:transcription repressor complex; ISO:MGI. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IDA:MGI. DR GO; GO:0003714; F:transcription corepressor activity; ISO:MGI. DR GO; GO:0060413; P:atrial septum morphogenesis; IMP:BHF-UCL. DR GO; GO:0003181; P:atrioventricular valve morphogenesis; IMP:BHF-UCL. DR GO; GO:0055008; P:cardiac muscle tissue morphogenesis; IMP:BHF-UCL. DR GO; GO:0060318; P:definitive erythrocyte differentiation; IMP:MGI. DR GO; GO:0035162; P:embryonic hemopoiesis; IMP:BHF-UCL. DR GO; GO:0030218; P:erythrocyte differentiation; IMP:MGI. DR GO; GO:0030851; P:granulocyte differentiation; IMP:MGI. DR GO; GO:0007507; P:heart development; IMP:MGI. DR GO; GO:0048872; P:homeostasis of number of cells; IMP:MGI. DR GO; GO:0035855; P:megakaryocyte development; IMP:MGI. DR GO; GO:0030219; P:megakaryocyte differentiation; IMP:MGI. DR GO; GO:0003192; P:mitral valve formation; IMP:BHF-UCL. DR GO; GO:0032713; P:negative regulation of interleukin-4 production; ISO:MGI. DR GO; GO:0060377; P:negative regulation of mast cell differentiation; IDA:BHF-UCL. DR GO; GO:0032091; P:negative regulation of protein binding; IDA:BHF-UCL. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI. DR GO; GO:0003151; P:outflow tract morphogenesis; IMP:BHF-UCL. DR GO; GO:0030220; P:platelet formation; ISO:MGI. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI. DR GO; GO:0032729; P:positive regulation of type II interferon production; ISO:MGI. DR GO; GO:0060319; P:primitive erythrocyte differentiation; IMP:MGI. DR GO; GO:0032642; P:regulation of chemokine production; IMP:MGI. DR GO; GO:0010724; P:regulation of definitive erythrocyte differentiation; ISO:MGI. DR GO; GO:0003195; P:tricuspid valve formation; IMP:BHF-UCL. DR GO; GO:0060412; P:ventricular septum morphogenesis; IMP:BHF-UCL. DR CDD; cd19215; PR-SET_ZFPM1; 1. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 2. DR IDEAL; IID50059; -. DR InterPro; IPR039746; FOG. DR InterPro; IPR034731; ZF_CCHC_FOG. DR InterPro; IPR049361; ZFPM1/2_PR. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR PANTHER; PTHR12958; FRIEND OF GATA2-RELATED; 1. DR PANTHER; PTHR12958:SF4; ZINC FINGER PROTEIN ZFPM1; 1. DR Pfam; PF21182; FOG1-like_PR; 1. DR Pfam; PF00096; zf-C2H2; 1. DR Pfam; PF12874; zf-met; 1. DR SMART; SM00355; ZnF_C2H2; 9. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 6. DR PROSITE; PS51810; ZF_CCHC_FOG; 5. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2. DR Genevisible; O35615; MM. PE 1: Evidence at protein level; KW 3D-structure; Activator; DNA-binding; Metal-binding; Nucleus; KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription; KW Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1..995 FT /note="Zinc finger protein ZFPM1" FT /id="PRO_0000221042" FT ZN_FING 249..282 FT /note="CCHC FOG-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT ZN_FING 303..327 FT /note="C2H2-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 333..355 FT /note="C2H2-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 361..384 FT /note="C2H2-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 584..617 FT /note="CCHC FOG-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT ZN_FING 690..723 FT /note="CCHC FOG-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT ZN_FING 830..863 FT /note="CCHC FOG-type 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT ZN_FING 868..891 FT /note="C2H2-type 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 957..990 FT /note="CCHC FOG-type 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT REGION 1..103 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 343..354 FT /note="Interaction with TACC3" FT /evidence="ECO:0000269|PubMed:15234987" FT REGION 424..526 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 616..694 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 721..827 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 811..817 FT /note="Interaction with CTBP2" FT REGION 892..960 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 11..40 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 42..67 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 77..96 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 438..462 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 500..519 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 724..744 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 765..786 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 257 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT BINDING 260 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT BINDING 273 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT BINDING 278 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT BINDING 592 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT BINDING 595 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT BINDING 608 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT BINDING 613 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT BINDING 698 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT BINDING 701 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT BINDING 714 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT BINDING 719 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT BINDING 838 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT BINDING 841 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT BINDING 854 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT BINDING 859 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT BINDING 965 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT BINDING 968 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT BINDING 981 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT BINDING 986 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT MOD_RES 99 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8IX07" FT MOD_RES 143 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 286 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 397 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8IX07" FT MOD_RES 497 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 500 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 651 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8IX07" FT MOD_RES 684 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8IX07" FT MOD_RES 803 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8IX07" FT MOD_RES 822 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 925 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:21183079" FT MOD_RES 927 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:21183079" FT MUTAGEN 254 FT /note="V->A: Does not affect the interaction with GATA1." FT /evidence="ECO:0000269|PubMed:10329627" FT MUTAGEN 255 FT /note="F->A: Impairs interaction with GATA1." FT /evidence="ECO:0000269|PubMed:10329627" FT MUTAGEN 256 FT /note="P->A: Does not affect the interaction with GATA1." FT /evidence="ECO:0000269|PubMed:10329627" FT MUTAGEN 258 FT /note="K->A: Does not affect the interaction with GATA1." FT /evidence="ECO:0000269|PubMed:10329627" FT MUTAGEN 259 FT /note="D->A: Does not affect the interaction with GATA1." FT /evidence="ECO:0000269|PubMed:10329627" FT MUTAGEN 261 FT /note="G->A: Slightly affects the interaction with GATA1." FT /evidence="ECO:0000269|PubMed:10329627" FT MUTAGEN 262 FT /note="I->A: Impairs interaction with GATA1." FT /evidence="ECO:0000269|PubMed:10329627" FT MUTAGEN 263 FT /note="W->A: Does not affect the interaction with GATA1." FT /evidence="ECO:0000269|PubMed:10329627" FT MUTAGEN 265 FT /note="R->A: Slightly affects the interaction with GATA1." FT /evidence="ECO:0000269|PubMed:10329627" FT MUTAGEN 266 FT /note="S->A: Does not affect the interaction with GATA1." FT /evidence="ECO:0000269|PubMed:10329627" FT MUTAGEN 267 FT /note="E->A: Slightly affects the interaction with GATA1." FT /evidence="ECO:0000269|PubMed:10329627" FT MUTAGEN 268 FT /note="R->A: Does not affect the interaction with GATA1." FT /evidence="ECO:0000269|PubMed:10329627" FT MUTAGEN 269 FT /note="N->A: Impairs interaction with GATA1." FT /evidence="ECO:0000269|PubMed:10329627" FT MUTAGEN 271 FT /note="Q->A: Does not affect the interaction with GATA1." FT /evidence="ECO:0000269|PubMed:10329627" FT MUTAGEN 274 FT /note="L->A: Slightly affects the interaction with GATA1." FT /evidence="ECO:0000269|PubMed:10329627" FT MUTAGEN 275 FT /note="L->A: Does not affect the interaction with GATA1." FT /evidence="ECO:0000269|PubMed:10329627" FT MUTAGEN 276 FT /note="Y->A: Slightly affects the interaction with GATA1." FT /evidence="ECO:0000269|PubMed:10329627" FT MUTAGEN 277 FT /note="Y->A: Impairs interaction with GATA1. Strongly FT impairs interaction with GATA1; when associated with A-612; FT A-718 and/or A-985." FT /evidence="ECO:0000269|PubMed:10329627" FT MUTAGEN 280 FT /note="S->A: Does not affect the interaction with GATA1." FT /evidence="ECO:0000269|PubMed:10329627" FT MUTAGEN 281 FT /note="R->A: Does not affect the interaction with GATA1." FT /evidence="ECO:0000269|PubMed:10329627" FT MUTAGEN 334 FT /note="V->A: No effect on interaction with TACC3." FT /evidence="ECO:0000269|PubMed:15234987" FT MUTAGEN 336 FT /note="L->A: No effect on interaction with TACC3." FT /evidence="ECO:0000269|PubMed:15234987" FT MUTAGEN 339 FT /note="L->A: No effect on interaction with TACC3." FT /evidence="ECO:0000269|PubMed:15234987" FT MUTAGEN 340 FT /note="S->A: No effect on interaction with TACC3." FT /evidence="ECO:0000269|PubMed:15234987" FT MUTAGEN 343 FT /note="T->A: Impairs interaction with TACC3." FT /evidence="ECO:0000269|PubMed:15234987" FT MUTAGEN 344 FT /note="T->A: Abolishes interaction with TACC3." FT /evidence="ECO:0000269|PubMed:15234987" FT MUTAGEN 345 FT /note="K->A: No effect on interaction with TACC3." FT /evidence="ECO:0000269|PubMed:15234987" FT MUTAGEN 346 FT /note="A->D: No effect on interaction with TACC3." FT /evidence="ECO:0000269|PubMed:15234987" FT MUTAGEN 347 FT /note="N->A: Abolishes interaction with TACC3." FT /evidence="ECO:0000269|PubMed:15234987" FT MUTAGEN 349 FT /note="E->A: No effect on interaction with TACC3." FT /evidence="ECO:0000269|PubMed:15234987" FT MUTAGEN 350 FT /note="R->A: Abolishes interaction with TACC3." FT /evidence="ECO:0000269|PubMed:15234987" FT MUTAGEN 352 FT /note="L->A: No effect on interaction with TACC3." FT /evidence="ECO:0000269|PubMed:15234987" FT MUTAGEN 353 FT /note="K->A: No effect on interaction with TACC3." FT /evidence="ECO:0000269|PubMed:15234987" FT MUTAGEN 354 FT /note="V->A: Abolishes interaction with TACC3." FT /evidence="ECO:0000269|PubMed:15234987" FT MUTAGEN 356 FT /note="T->A: No effect on interaction with TACC3." FT /evidence="ECO:0000269|PubMed:15234987" FT MUTAGEN 357 FT /note="D->A: No effect on interaction with TACC3." FT /evidence="ECO:0000269|PubMed:15234987" FT MUTAGEN 612 FT /note="Y->A: Impairs interaction with GATA1. Strongly FT impairs interaction with GATA1; when associated with A-277; FT A-718 and/or A-985." FT /evidence="ECO:0000269|PubMed:10329627" FT MUTAGEN 698 FT /note="C->A: Abolishes interaction with GATA1." FT /evidence="ECO:0000269|PubMed:9837943" FT MUTAGEN 706 FT /note="S->R: Able to partially restore the interaction with FT the G-205 GATA1 mutant, which is usually unable to interact FT with ZFPM1." FT /evidence="ECO:0000269|PubMed:10078204" FT MUTAGEN 718 FT /note="Y->A: Impairs interaction with GATA1. Strongly FT impairs interaction with GATA1; when associated with A-277; FT A-612 and/or A-985." FT /evidence="ECO:0000269|PubMed:10329627" FT MUTAGEN 719 FT /note="C->A: Abolishes interaction with GATA1." FT /evidence="ECO:0000269|PubMed:9837943" FT MUTAGEN 719 FT /note="C->H: Transforms the C2HC-type zinc finger into a FT C2H2-type, leading to abolition of interaction with GATA1." FT /evidence="ECO:0000269|PubMed:9837943" FT MUTAGEN 811..814 FT /note="PIDL->AIAA: Abolishes interaction with CTBP2." FT /evidence="ECO:0000269|PubMed:10329627" FT MUTAGEN 813..814 FT /note="DL->AS: Abolishes interaction with CTBP2; it however FT does not abolish the corepressor activity in FT erythropoiesis." FT /evidence="ECO:0000269|PubMed:11940669" FT MUTAGEN 985 FT /note="Y->A: Slightly affects the interaction with GATA1. FT Strongly impairs interaction with GATA1; when associated FT with A-277; A-612 and/or A-718." FT /evidence="ECO:0000269|PubMed:10329627" FT STRAND 107..112 FT /evidence="ECO:0007829|PDB:2MPL" FT STRAND 115..122 FT /evidence="ECO:0007829|PDB:2MPL" FT TURN 144..146 FT /evidence="ECO:0007829|PDB:2MPL" FT HELIX 162..164 FT /evidence="ECO:0007829|PDB:2MPL" FT STRAND 168..182 FT /evidence="ECO:0007829|PDB:2MPL" FT STRAND 185..190 FT /evidence="ECO:0007829|PDB:2MPL" FT STRAND 201..204 FT /evidence="ECO:0007829|PDB:2MPL" FT STRAND 336..338 FT /evidence="ECO:0007829|PDB:1SRK" FT STRAND 341..344 FT /evidence="ECO:0007829|PDB:1SRK" FT HELIX 345..352 FT /evidence="ECO:0007829|PDB:1SRK" FT HELIX 353..355 FT /evidence="ECO:0007829|PDB:1SRK" SQ SEQUENCE 995 AA; 105984 MW; 293255B28151ECB8 CRC64; MSRRKQSNPR QIKRSLRDME AGEEAKAMDS SPKEQEAPDP EAPAIEEPPS PPREDVSPPA VPAPPESPED PEDMEGQELE MRPQDEEKEE KEEEAAMASP WSGPEELELA LQDGQRCVRA RLSLTEGLSW GPFYGSIQTR ALSPEREEPG PAVTLMVDES CWLRMLPQVL TEEAANSEIY RKDDALWCRV TKVVPSGGLL YVRLVTEPHG APRHPVQEPV EPGGLAPVHT DIQLLPQQAG MASILATAVI NKDVFPCKDC GIWYRSERNL QAHLLYYCAS RQRAGSPVSA TEEKPKETYP NERVCPFPQC RKSCPSASSL EIHMRSHSGE RPFVCLICLS AFTTKANCER HLKVHTDTLS GVCHNCGFIS TTRDILYSHL VTNHMVCQPG SKGEIYSPGA GHPAAKLPPD SLAGFQQHSL MHSPLVPADK APTPSSGLDS KAEVTNGETR VPPQNGGSSE SPAAPRTIKV EAAEEPEATR ASGPGEPGPQ APSRTPSPHS PNPVRVKTEL SSPTPGSSPG PGELTMAGTL FLPQYVFSPD AGTTTVPTAP QASEILAKMS ELVHNRLQQG AGSSGAAGTP TGLFSGTKGA TCFECEITFN NINNFYVHKR LYCSGRRAPE DPPTVRRPKA ATGPARAPAG AAAEPDPSRS SPGPGPREEE ASGTTTPEAE AAGRGSEGSQ SPGSSVDDAE DDPSRTLCEA CNIRFSRHET YTVHKRYYCA SRHDPPPRRP PAPTTAPGPA APALTAPPVR TRRRRKLYEL PAAGAPPPAA GPAPVPVVPS PTAELPSSPR PGSASAGPAP ALSPSPVPDG PIDLSKRPRR QSPDAPTALP ALADYHECTA CRVSFHSLEA YLAHKKYSCP AAPLRTTALC PYCPPNGRVR GDLVEHLRQA HGLQVAKPAA SPGAEPRTPA ERAPRDSPDG RAPRSPSPAP ENTPSDPADQ GARTPSKGPP APAPAPGGGG GHRYCRLCNI RFSSLSTFIA HKKYYCSSHA AEHVK //