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Zinc finger protein ZFPM1 (Friend of GATA protein 1) (FOG-1) (Friend of GATA 1) (Zinc finger protein multitype 1)

 FOG1_MOUSE              Reviewed;         995 AA.
O35615;
15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
25-OCT-2017, entry version 145.
RecName: Full=Zinc finger protein ZFPM1;
AltName: Full=Friend of GATA protein 1;
Short=FOG-1;
Short=Friend of GATA 1;
AltName: Full=Zinc finger protein multitype 1;
Name=Zfpm1; Synonyms=Fog, Fog1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, DEVELOPMENTAL STAGE, AND INTERACTION WITH GATA1; GATA2
AND GATA3.
TISSUE=Erythroleukemia;
PubMed=9230307; DOI=10.1016/S0092-8674(00)80318-9;
Tsang A.P., Visvader J.E., Turner C.A., Fujiwara Y., Yu C.,
Weiss M.J., Crossley M., Orkin S.H.;
"FOG, a multitype zinc finger protein, acts as a cofactor for
transcription factor GATA-1 in erythroid and megakaryocytic
differentiation.";
Cell 90:109-119(1997).
[2]
FUNCTION.
PubMed=9553047; DOI=10.1101/gad.12.8.1176;
Tsang A.P., Fujiwara Y., Hom D.B., Orkin S.H.;
"Failure of megakaryopoiesis and arrested erythropoiesis in mice
lacking the GATA-1 transcriptional cofactor FOG.";
Genes Dev. 12:1176-1188(1998).
[3]
INTERACTION WITH GATA1, AND MUTAGENESIS OF CYS-698 AND CYS-719.
PubMed=9837943; DOI=10.1074/jbc.273.50.33595;
Fox A.H., Kowalski K., King G.F., Mackay J.P., Crossley M.;
"Key residues characteristic of GATA N-fingers are recognized by
FOG.";
J. Biol. Chem. 273:33595-33603(1998).
[4]
FUNCTION, AND MUTAGENESIS OF SER-706.
PubMed=10078204; DOI=10.1016/S1097-2765(00)80312-3;
Crispino J.D., Lodish M.B., MacKay J.P., Orkin S.H.;
"Use of altered specificity mutants to probe a specific protein-
protein interaction in differentiation: the GATA-1:FOG complex.";
Mol. Cell 3:219-228(1999).
[5]
FUNCTION, INTERACTION WITH GATA1 AND CTBP2, AND MUTAGENESIS OF
VAL-254; PHE-255; PRO-256; LYS-258; ASP-259; GLY-261; ILE-262;
TRP-263; ARG-265; SER-266; GLU-267; ARG-268; ASN-269; GLN-271;
LEU-274; LEU-275; TYR-276; TYR-277; SER-280; ARG-281;
811-PRO--LEU-814; TYR-612; TYR-718 AND TYR-985.
PubMed=10329627; DOI=10.1093/emboj/18.10.2812;
Fox A.H., Liew C., Holmes M., Kowalski K., Mackay J., Crossley M.;
"Transcriptional cofactors of the FOG family interact with GATA
proteins by means of multiple zinc fingers.";
EMBO J. 18:2812-2822(1999).
[6]
FUNCTION, INTERACTION WITH CTBP2, AND MUTAGENESIS OF 813-ASP-LEU-814.
PubMed=11940669; DOI=10.1128/MCB.22.9.3121-3128.2002;
Katz S.G., Cantor A.B., Orkin S.H.;
"Interaction between FOG-1 and the corepressor C-terminal binding
protein is dispensable for normal erythropoiesis in vivo.";
Mol. Cell. Biol. 22:3121-3128(2002).
[7]
FUNCTION.
PubMed=12356738; DOI=10.1093/emboj/cdf527;
Wang X., Crispino J.D., Letting D.L., Nakazawa M., Poncz M.,
Blobel G.A.;
"Control of megakaryocyte-specific gene expression by GATA-1 and FOG-
1: role of Ets transcription factors.";
EMBO J. 21:5225-5234(2002).
[8]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=14614148; DOI=10.1073/pnas.1936250100;
Katz S.G., Williams A., Yang J., Fujiwara Y., Tsang A.P.,
Epstein J.A., Orkin S.H.;
"Endothelial lineage-mediated loss of the GATA cofactor Friend of GATA
1 impairs cardiac development.";
Proc. Natl. Acad. Sci. U.S.A. 100:14030-14035(2003).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-925 AND SER-927, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143; SER-286; SER-497;
SER-500; SER-822; SER-925 AND SER-927, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[11]
STRUCTURE BY NMR OF 328-360, INTERACTION WITH TACC3, AND MUTAGENESIS
OF VAL-334; LEU-336; LEU-339; SER-340; THR-343; THR-344; LYS-345;
ALA-346; ASN-347; GLU-349; ARG-350; LEU-352; LYS-353; VAL-354; THR-356
AND ASP-357.
PubMed=15234987; DOI=10.1074/jbc.M404130200;
Simpson R.J.Y., Yi Lee S.H., Bartle N., Sum E.Y., Visvader J.E.,
Matthews J.M., Mackay J.P., Crossley M.;
"A classic zinc finger from Friend of GATA mediates an interaction
with the coiled-coil of transforming acidic coiled-coil 3.";
J. Biol. Chem. 279:39789-39797(2004).
-!- FUNCTION: Transcription regulator that plays an essential role in
erythroid and megakaryocytic cell differentiation. Essential
cofactor that acts via the formation of a heterodimer with
transcription factors of the GATA family GATA1, GATA2 and GATA3.
Such heterodimer can both activate or repress transcriptional
activity, depending on the cell and promoter context. The
heterodimer formed with GATA proteins is essential to activate
expression of genes such as NFE2, ITGA2B, alpha- and beta-globin,
while it represses expression of KLF1. May be involved in
regulation of some genes in gonads. May also be involved in
cardiac development, in a non-redundant way with ZFPM2/FOG2.
{ECO:0000269|PubMed:10078204, ECO:0000269|PubMed:10329627,
ECO:0000269|PubMed:11940669, ECO:0000269|PubMed:12356738,
ECO:0000269|PubMed:14614148, ECO:0000269|PubMed:9230307,
ECO:0000269|PubMed:9553047}.
-!- SUBUNIT: Interacts with the N-terminal zinc-finger of GATA1, GATA2
and GATA3. Interacts with corepressor CTBP2; this interaction is
however not essential for corepressor activity in erythropoiesis.
Interacts with TACC3. {ECO:0000269|PubMed:10329627,
ECO:0000269|PubMed:11940669, ECO:0000269|PubMed:15234987,
ECO:0000269|PubMed:9230307, ECO:0000269|PubMed:9837943}.
-!- INTERACTION:
P17679:Gata1; NbExp=4; IntAct=EBI-4394596, EBI-3903251;
Q9JJ11:Tacc3; NbExp=7; IntAct=EBI-4394596, EBI-2553611;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9230307}.
-!- TISSUE SPECIFICITY: Mainly expressed in hematopoietic tissues.
Expressed in the spleen, a primary site of hematopoiesis in the
adult mouse, as well as in the liver and testis, but not in the
heart, brain, lung, kidney, or skeletal muscle. Among
hematopoietic cell lines, it is strongly expressed in erythroid
and megakaryocytic cell lines. Expressed at low level in several
lymphoid and early myeloid cell lines. Not expressed in mast cell
and macrophage lines. Expressed in the heart, where it colocalizes
with GATA4, GATA5 and GATA6. {ECO:0000269|PubMed:14614148,
ECO:0000269|PubMed:9230307}.
-!- DEVELOPMENTAL STAGE: First expressed in two extraembryonic
mesodermal derivatives, the yolk sac and the allantois in E8.5
embryos. Localized to the embryonic red blood cells within the
yolk sac blood islands. {ECO:0000269|PubMed:9230307}.
-!- DOMAIN: The CCHC FOG-type zinc fingers 1, 2, 3 and 5 bind directly
to GATA-type zinc fingers. The Tyr residue adjacent to the last
Cys of the CCHC FOG-type zinc finger is essential for the
interaction with GATA-type zinc fingers.
-!- SIMILARITY: Belongs to the FOG (Friend of GATA) family.
{ECO:0000255|PROSITE-ProRule:PRU01153}.
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EMBL; AF006492; AAC53292.1; -; mRNA.
CCDS; CCDS22733.1; -.
RefSeq; NP_033595.1; NM_009569.4.
RefSeq; XP_006530914.1; XM_006530851.3.
UniGene; Mm.3105; -.
UniGene; Mm.390068; -.
PDB; 1SRK; NMR; -; A=328-360.
PDB; 2MPL; NMR; -; A=100-226.
PDBsum; 1SRK; -.
PDBsum; 2MPL; -.
ProteinModelPortal; O35615; -.
SMR; O35615; -.
BioGrid; 204687; 11.
CORUM; O35615; -.
DIP; DIP-48414N; -.
IntAct; O35615; 3.
MINT; MINT-6613139; -.
STRING; 10090.ENSMUSP00000058037; -.
iPTMnet; O35615; -.
PhosphoSitePlus; O35615; -.
MaxQB; O35615; -.
PaxDb; O35615; -.
PeptideAtlas; O35615; -.
PRIDE; O35615; -.
Ensembl; ENSMUST00000054052; ENSMUSP00000058037; ENSMUSG00000049577.
GeneID; 22761; -.
KEGG; mmu:22761; -.
UCSC; uc009nsj.1; mouse.
CTD; 161882; -.
MGI; MGI:1095400; Zfpm1.
eggNOG; KOG1721; Eukaryota.
eggNOG; COG5048; LUCA.
GeneTree; ENSGT00530000063823; -.
HOGENOM; HOG000112626; -.
HOVERGEN; HBG101018; -.
InParanoid; O35615; -.
KO; K17441; -.
OMA; PTHPIII; -.
OrthoDB; EOG091G00RC; -.
PhylomeDB; O35615; -.
TreeFam; TF331342; -.
Reactome; R-MMU-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production.
EvolutionaryTrace; O35615; -.
PRO; PR:O35615; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000049577; -.
CleanEx; MM_ZFPM1; -.
Genevisible; O35615; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0005667; C:transcription factor complex; ISO:MGI.
GO; GO:0017053; C:transcriptional repressor complex; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0001102; F:RNA polymerase II activating transcription factor binding; IDA:MGI.
GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IDA:MGI.
GO; GO:0001085; F:RNA polymerase II transcription factor binding; ISO:MGI.
GO; GO:0003714; F:transcription corepressor activity; TAS:MGI.
GO; GO:0008134; F:transcription factor binding; ISO:MGI.
GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding; ISO:MGI.
GO; GO:0060413; P:atrial septum morphogenesis; IMP:BHF-UCL.
GO; GO:0003181; P:atrioventricular valve morphogenesis; IMP:BHF-UCL.
GO; GO:0055008; P:cardiac muscle tissue morphogenesis; IMP:BHF-UCL.
GO; GO:0060318; P:definitive erythrocyte differentiation; IMP:MGI.
GO; GO:0035162; P:embryonic hemopoiesis; IMP:BHF-UCL.
GO; GO:0030218; P:erythrocyte differentiation; IMP:MGI.
GO; GO:0030851; P:granulocyte differentiation; IMP:MGI.
GO; GO:0007507; P:heart development; IMP:MGI.
GO; GO:0048872; P:homeostasis of number of cells; IMP:MGI.
GO; GO:0035855; P:megakaryocyte development; IMP:MGI.
GO; GO:0030219; P:megakaryocyte differentiation; IMP:MGI.
GO; GO:0003192; P:mitral valve formation; IMP:BHF-UCL.
GO; GO:0045599; P:negative regulation of fat cell differentiation; IMP:UniProtKB.
GO; GO:0045403; P:negative regulation of interleukin-4 biosynthetic process; ISO:MGI.
GO; GO:0060377; P:negative regulation of mast cell differentiation; IDA:BHF-UCL.
GO; GO:0032091; P:negative regulation of protein binding; IDA:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0003151; P:outflow tract morphogenesis; IMP:BHF-UCL.
GO; GO:0030220; P:platelet formation; ISO:MGI.
GO; GO:0045078; P:positive regulation of interferon-gamma biosynthetic process; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0060319; P:primitive erythrocyte differentiation; IMP:MGI.
GO; GO:0032642; P:regulation of chemokine production; IMP:MGI.
GO; GO:0010724; P:regulation of definitive erythrocyte differentiation; ISO:MGI.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0071733; P:transcriptional activation by promoter-enhancer looping; IDA:BHF-UCL.
GO; GO:0003195; P:tricuspid valve formation; IMP:BHF-UCL.
GO; GO:0060412; P:ventricular septum morphogenesis; IMP:BHF-UCL.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR034731; ZF_CCHC_FOG.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
SMART; SM00355; ZnF_C2H2; 9.
SUPFAM; SSF57667; SSF57667; 6.
PROSITE; PS51810; ZF_CCHC_FOG; 5.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
1: Evidence at protein level;
3D-structure; Activator; Complete proteome; DNA-binding;
Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.
CHAIN 1 995 Zinc finger protein ZFPM1.
/FTId=PRO_0000221042.
ZN_FING 249 282 CCHC FOG-type 1. {ECO:0000255|PROSITE-
ProRule:PRU01153}.
ZN_FING 303 327 C2H2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 333 355 C2H2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 361 384 C2H2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 584 617 CCHC FOG-type 2. {ECO:0000255|PROSITE-
ProRule:PRU01153}.
ZN_FING 690 723 CCHC FOG-type 3. {ECO:0000255|PROSITE-
ProRule:PRU01153}.
ZN_FING 830 863 CCHC FOG-type 4. {ECO:0000255|PROSITE-
ProRule:PRU01153}.
ZN_FING 868 891 C2H2-type 4. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 957 990 CCHC FOG-type 5. {ECO:0000255|PROSITE-
ProRule:PRU01153}.
REGION 343 354 Interaction with TACC3.
{ECO:0000269|PubMed:15234987}.
REGION 811 817 Interaction with CTBP2.
MOD_RES 99 99 Phosphoserine.
{ECO:0000250|UniProtKB:Q8IX07}.
MOD_RES 143 143 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 286 286 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 397 397 Phosphoserine.
{ECO:0000250|UniProtKB:Q8IX07}.
MOD_RES 497 497 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 500 500 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 651 651 Phosphoserine.
{ECO:0000250|UniProtKB:Q8IX07}.
MOD_RES 684 684 Phosphoserine.
{ECO:0000250|UniProtKB:Q8IX07}.
MOD_RES 803 803 Phosphoserine.
{ECO:0000250|UniProtKB:Q8IX07}.
MOD_RES 822 822 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 925 925 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 927 927 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MUTAGEN 254 254 V->A: Does not affect the interaction
with GATA1.
{ECO:0000269|PubMed:10329627}.
MUTAGEN 255 255 F->A: Impairs interaction with GATA1.
{ECO:0000269|PubMed:10329627}.
MUTAGEN 256 256 P->A: Does not affect the interaction
with GATA1.
{ECO:0000269|PubMed:10329627}.
MUTAGEN 258 258 K->A: Does not affect the interaction
with GATA1.
{ECO:0000269|PubMed:10329627}.
MUTAGEN 259 259 D->A: Does not affect the interaction
with GATA1.
{ECO:0000269|PubMed:10329627}.
MUTAGEN 261 261 G->A: Slightly affects the interaction
with GATA1.
{ECO:0000269|PubMed:10329627}.
MUTAGEN 262 262 I->A: Impairs interaction with GATA1.
{ECO:0000269|PubMed:10329627}.
MUTAGEN 263 263 W->A: Does not affect the interaction
with GATA1.
{ECO:0000269|PubMed:10329627}.
MUTAGEN 265 265 R->A: Slightly affects the interaction
with GATA1.
{ECO:0000269|PubMed:10329627}.
MUTAGEN 266 266 S->A: Does not affect the interaction
with GATA1.
{ECO:0000269|PubMed:10329627}.
MUTAGEN 267 267 E->A: Slightly affects the interaction
with GATA1.
{ECO:0000269|PubMed:10329627}.
MUTAGEN 268 268 R->A: Does not affect the interaction
with GATA1.
{ECO:0000269|PubMed:10329627}.
MUTAGEN 269 269 N->A: Impairs interaction with GATA1.
{ECO:0000269|PubMed:10329627}.
MUTAGEN 271 271 Q->A: Does not affect the interaction
with GATA1.
{ECO:0000269|PubMed:10329627}.
MUTAGEN 274 274 L->A: Slightly affects the interaction
with GATA1.
{ECO:0000269|PubMed:10329627}.
MUTAGEN 275 275 L->A: Does not affect the interaction
with GATA1.
{ECO:0000269|PubMed:10329627}.
MUTAGEN 276 276 Y->A: Slightly affects the interaction
with GATA1.
{ECO:0000269|PubMed:10329627}.
MUTAGEN 277 277 Y->A: Impairs interaction with GATA1.
Strongly impairs interaction with GATA1;
when associated with A-612; A-718 and/or
A-985. {ECO:0000269|PubMed:10329627}.
MUTAGEN 280 280 S->A: Does not affect the interaction
with GATA1.
{ECO:0000269|PubMed:10329627}.
MUTAGEN 281 281 R->A: Does not affect the interaction
with GATA1.
{ECO:0000269|PubMed:10329627}.
MUTAGEN 334 334 V->A: No effect on interaction with
TACC3. {ECO:0000269|PubMed:15234987}.
MUTAGEN 336 336 L->A: No effect on interaction with
TACC3. {ECO:0000269|PubMed:15234987}.
MUTAGEN 339 339 L->A: No effect on interaction with
TACC3. {ECO:0000269|PubMed:15234987}.
MUTAGEN 340 340 S->A: No effect on interaction with
TACC3. {ECO:0000269|PubMed:15234987}.
MUTAGEN 343 343 T->A: Impairs interaction with TACC3.
{ECO:0000269|PubMed:15234987}.
MUTAGEN 344 344 T->A: Abolishes interaction with TACC3.
{ECO:0000269|PubMed:15234987}.
MUTAGEN 345 345 K->A: No effect on interaction with
TACC3. {ECO:0000269|PubMed:15234987}.
MUTAGEN 346 346 A->D: No effect on interaction with
TACC3. {ECO:0000269|PubMed:15234987}.
MUTAGEN 347 347 N->A: Abolishes interaction with TACC3.
{ECO:0000269|PubMed:15234987}.
MUTAGEN 349 349 E->A: No effect on interaction with
TACC3. {ECO:0000269|PubMed:15234987}.
MUTAGEN 350 350 R->A: Abolishes interaction with TACC3.
{ECO:0000269|PubMed:15234987}.
MUTAGEN 352 352 L->A: No effect on interaction with
TACC3. {ECO:0000269|PubMed:15234987}.
MUTAGEN 353 353 K->A: No effect on interaction with
TACC3. {ECO:0000269|PubMed:15234987}.
MUTAGEN 354 354 V->A: Abolishes interaction with TACC3.
{ECO:0000269|PubMed:15234987}.
MUTAGEN 356 356 T->A: No effect on interaction with
TACC3. {ECO:0000269|PubMed:15234987}.
MUTAGEN 357 357 D->A: No effect on interaction with
TACC3. {ECO:0000269|PubMed:15234987}.
MUTAGEN 612 612 Y->A: Impairs interaction with GATA1.
Strongly impairs interaction with GATA1;
when associated with A-277; A-718 and/or
A-985. {ECO:0000269|PubMed:10329627}.
MUTAGEN 698 698 C->A: Abolishes interaction with GATA1.
{ECO:0000269|PubMed:9837943}.
MUTAGEN 706 706 S->R: Able to partially restore the
interaction with the G-205 GATA1 mutant,
which is usually unable to interact with
ZFPM1. {ECO:0000269|PubMed:10078204}.
MUTAGEN 718 718 Y->A: Impairs interaction with GATA1.
Strongly impairs interaction with GATA1;
when associated with A-277; A-612 and/or
A-985. {ECO:0000269|PubMed:10329627}.
MUTAGEN 719 719 C->A: Abolishes interaction with GATA1.
{ECO:0000269|PubMed:9837943}.
MUTAGEN 719 719 C->H: Transforms the C2HC-type zinc
finger into a C2H2-type, leading to
abolition of interaction with GATA1.
{ECO:0000269|PubMed:9837943}.
MUTAGEN 811 814 PIDL->AIAA: Abolishes interaction with
CTBP2. {ECO:0000269|PubMed:10329627}.
MUTAGEN 813 814 DL->AS: Abolishes interaction with CTBP2;
it however does not abolish the
corepressor activity in erythropoiesis.
{ECO:0000269|PubMed:11940669}.
MUTAGEN 985 985 Y->A: Slightly affects the interaction
with GATA1. Strongly impairs interaction
with GATA1; when associated with A-277;
A-612 and/or A-718.
{ECO:0000269|PubMed:10329627}.
STRAND 107 112 {ECO:0000244|PDB:2MPL}.
STRAND 115 122 {ECO:0000244|PDB:2MPL}.
TURN 144 146 {ECO:0000244|PDB:2MPL}.
HELIX 162 164 {ECO:0000244|PDB:2MPL}.
STRAND 168 182 {ECO:0000244|PDB:2MPL}.
STRAND 185 190 {ECO:0000244|PDB:2MPL}.
STRAND 201 204 {ECO:0000244|PDB:2MPL}.
STRAND 336 338 {ECO:0000244|PDB:1SRK}.
STRAND 341 344 {ECO:0000244|PDB:1SRK}.
HELIX 345 352 {ECO:0000244|PDB:1SRK}.
HELIX 353 355 {ECO:0000244|PDB:1SRK}.
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


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