FOG1_MOUSE
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 03-AUG-2022, entry version 173.
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, Spleen,
RC 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}.
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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; O35615; -.
DR PeptideAtlas; O35615; -.
DR PRIDE; O35615; -.
DR ProteomicsDB; 271783; -.
DR Antibodypedia; 30722; 122 antibodies from 24 providers.
DR DNASU; 22761; -.
DR Ensembl; ENSMUST00000054052; ENSMUSP00000058037; ENSMUSG00000049577.
DR GeneID; 22761; -.
DR KEGG; mmu:22761; -.
DR UCSC; uc009nsj.1; mouse.
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; PPCGIRF; -.
DR OrthoDB; 76702at2759; -.
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 76 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 200 other tissues.
DR Genevisible; O35615; MM.
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:0030154; P:cell differentiation; IBA:GO_Central.
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:0045599; P:negative regulation of fat cell differentiation; IMP:UniProtKB.
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:0032729; P:positive regulation of interferon-gamma production; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA: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 IDEAL; IID50059; -.
DR InterPro; IPR039746; FOG.
DR InterPro; IPR034731; ZF_CCHC_FOG.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR12958; PTHR12958; 1.
DR Pfam; PF00096; zf-C2H2; 1.
DR SMART; SM00355; ZnF_C2H2; 9.
DR SUPFAM; SSF57667; SSF57667; 6.
DR PROSITE; PS51810; ZF_CCHC_FOG; 5.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
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
