USH_DROME
ID USH_DROME Reviewed; 1191 AA.
AC Q9VPQ6; O18414; Q6AWH0;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Zinc finger protein ush;
DE AltName: Full=Protein U-shaped;
GN Name=ush; ORFNames=CG2762;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Embryo;
RX PubMed=9367989; DOI=10.1101/gad.11.22.3083;
RA Cubadda Y., Heitzler P., Ray R.P., Bourouis M., Ramain P., Gelbart W.,
RA Simpson P., Haenlin M.;
RT "U-shaped encodes a zinc finger protein that regulates the proneural genes
RT achaete and scute during the formation of bristles in Drosophila.";
RL Genes Dev. 11:3083-3095(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND INTERACTION WITH PNR.
RX PubMed=9367990; DOI=10.1101/gad.11.22.3096;
RA Haenlin M., Cubadda Y., Blondeau F., Heitzler P., Lutz Y., Simpson P.,
RA Ramain P.;
RT "Transcriptional activity of pannier is regulated negatively by
RT heterodimerization of the GATA DNA-binding domain with a cofactor encoded
RT by the u-shaped gene of Drosophila.";
RL Genes Dev. 11:3096-3108(1997).
RN [6]
RP DOMAIN.
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 [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=10861002; DOI=10.1073/pnas.97.13.7348;
RA Fossett N., Zhang Q., Gajewski K., Choi C.Y., Kim Y., Schulz R.A.;
RT "The multitype zinc-finger protein U-shaped functions in heart cell
RT specification in the Drosophila embryo.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:7348-7353(2000).
RN [8]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11404479; DOI=10.1073/pnas.131215798;
RA Fossett N., Tevosian S.G., Gajewski K., Zhang Q., Orkin S.H., Schulz R.A.;
RT "The Friend of GATA proteins U-shaped, FOG-1, and FOG-2 function as
RT negative regulators of blood, heart, and eye development in Drosophila.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7342-7347(2001).
RN [9]
RP FUNCTION, AND INTERACTION WITH SRP AND CTBP.
RX PubMed=12374748; DOI=10.1093/emboj/cdf545;
RA Waltzer L., Bataille L., Peyrefitte S., Haenlin M.;
RT "Two isoforms of Serpent containing either one or two GATA zinc fingers
RT have different roles in Drosophila haematopoiesis.";
RL EMBO J. 21:5477-5486(2002).
RN [10]
RP FUNCTION.
RX PubMed=12782269; DOI=10.1016/s0925-4773(03)00042-x;
RA Ghazi A., Paul L., VijayRaghavan K.;
RT "Prepattern genes and signaling molecules regulate stripe expression to
RT specify Drosophila flight muscle attachment sites.";
RL Mech. Dev. 120:519-528(2003).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-118; SER-1013;
RP SER-1015; SER-1017 AND SER-1156, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [12]
RP STRUCTURE BY NMR OF 202-235 AND 1113-1146, ZINC-BINDING, AND MUTAGENESIS OF
RP CYS-231.
RX PubMed=11080638; DOI=10.1016/s0969-2126(00)00527-x;
RA Liew C.K., Kowalski K., Fox A.H., Newton A., Sharpe B.K., Crossley M.,
RA Mackay J.P.;
RT "Solution structures of two CCHC zinc fingers from the FOG family protein
RT U-shaped that mediate protein-protein interactions.";
RL Structure 8:1157-1166(2000).
RN [13]
RP STRUCTURE BY NMR OF 1113-1146 MUTANT CYS-1142.
RX PubMed=12110675; DOI=10.1074/jbc.m204663200;
RA Kowalski K., Liew C.K., Matthews J.M., Gell D.A., Crossley M., Mackay J.P.;
RT "Characterization of the conserved interaction between GATA and FOG family
RT proteins.";
RL J. Biol. Chem. 277:35720-35729(2002).
CC -!- FUNCTION: Transcription regulator that modulates expression mediated by
CC transcription factors of the GATA family such as pnr and srp. Represses
CC transcription of proneural achaete-scute complex (AS-C), which is
CC usually activated by pnr. Involved in cardiogenesis, blood, and eye
CC development. During hematopoiesis, it is required to restrict the
CC number of crystal cells, probably via its interaction with the isoform
CC SrpNC of srp. Negatively regulates expression of sr. Probably acts by
CC interacting with the GATA-type zinc finger of proteins such as pnr and
CC srp, possibly antagonizing the interaction between the GATA-type zinc
CC finger and some cofactor. {ECO:0000269|PubMed:10861002,
CC ECO:0000269|PubMed:11404479, ECO:0000269|PubMed:12374748,
CC ECO:0000269|PubMed:12782269, ECO:0000269|PubMed:9367989,
CC ECO:0000269|PubMed:9367990}.
CC -!- SUBUNIT: Interacts with pnr, although weak this interaction is
CC essential. Interacts with the isoform SrpNC of srp. Interacts with CtBP
CC corepressor. {ECO:0000269|PubMed:12374748, ECO:0000269|PubMed:9367990}.
CC -!- INTERACTION:
CC Q9VPQ6; P17679: Gata1; Xeno; NbExp=2; IntAct=EBI-110692, EBI-3903251;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9367989}.
CC -!- TISSUE SPECIFICITY: First expressed in stage 5 at high levels in the
CC primordium of the amnioserosa. Also expressed in germ band extending
CC embryos in cells of the developing anterior and posterior midgut and in
CC hemocyte precursors present in the cephalic mesoderm. In embryonic
CC stage 8, it is expressed in blood cell precursors. By stage 10, it is
CC expressed in hemocyte precursors that have spread throughout the
CC lateral and ventral head mesoderm. By stage 11, it is expressed in the
CC dorsal ectoderm and in precursor cells of the hemocytes and fat body.
CC As embryogenesis proceeds, it is also expressed in stage 13
CC plasmatocytes migrating throughout the head mesoderm and down the
CC ventral midline. By late embryogenesis, expression strongly decreases
CC but remains in the dorsal ectoderm during dorsal closure, in cells
CC within, or associated with, the central nervous system, and in
CC plasmatocytes circulating throughout the embryonic hemolymph. During
CC larval development, it is expressed in primary and secondary lobes of
CC lymph glands. Expressed in the dorsal part of the thoracic imaginal
CC disk. {ECO:0000269|PubMed:10861002, ECO:0000269|PubMed:11404479,
CC ECO:0000269|PubMed:9367989}.
CC -!- DOMAIN: The CCHC FOG-type zinc fingers 1, 4 and 5 directly bind 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. {ECO:0000269|PubMed:10329627}.
CC -!- SIMILARITY: Belongs to the FOG (Friend of GATA) family.
CC {ECO:0000255|PROSITE-ProRule:PRU01153}.
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DR EMBL; Y12322; CAA72991.1; -; mRNA.
DR EMBL; AE014134; AAF51488.2; -; Genomic_DNA.
DR EMBL; BT015278; AAT94507.1; -; mRNA.
DR PIR; T13850; T13850.
DR RefSeq; NP_476780.1; NM_057432.3.
DR PDB; 1FU9; NMR; -; A=1113-1146.
DR PDB; 1FV5; NMR; -; A=202-235.
DR PDB; 1JN7; NMR; -; A=1113-1146.
DR PDB; 1Y0J; NMR; -; B=202-235.
DR PDB; 2L6Z; NMR; -; B=202-235.
DR PDBsum; 1FU9; -.
DR PDBsum; 1FV5; -.
DR PDBsum; 1JN7; -.
DR PDBsum; 1Y0J; -.
DR PDBsum; 2L6Z; -.
DR AlphaFoldDB; Q9VPQ6; -.
DR BMRB; Q9VPQ6; -.
DR SMR; Q9VPQ6; -.
DR BioGRID; 59481; 14.
DR IntAct; Q9VPQ6; 1.
DR STRING; 7227.FBpp0305228; -.
DR iPTMnet; Q9VPQ6; -.
DR PaxDb; Q9VPQ6; -.
DR PRIDE; Q9VPQ6; -.
DR DNASU; 33225; -.
DR EnsemblMetazoa; FBtr0078063; FBpp0077723; FBgn0003963.
DR GeneID; 33225; -.
DR KEGG; dme:Dmel_CG2762; -.
DR CTD; 33225; -.
DR FlyBase; FBgn0003963; ush.
DR VEuPathDB; VectorBase:FBgn0003963; -.
DR eggNOG; ENOG502QQZP; Eukaryota.
DR GeneTree; ENSGT00530000063823; -.
DR HOGENOM; CLU_002277_0_0_1; -.
DR InParanoid; Q9VPQ6; -.
DR PhylomeDB; Q9VPQ6; -.
DR Reactome; R-DME-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-DME-983231; Factors involved in megakaryocyte development and platelet production.
DR SignaLink; Q9VPQ6; -.
DR BioGRID-ORCS; 33225; 1 hit in 3 CRISPR screens.
DR ChiTaRS; ush; fly.
DR EvolutionaryTrace; Q9VPQ6; -.
DR GenomeRNAi; 33225; -.
DR PRO; PR:Q9VPQ6; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0003963; Expressed in ectoderm and 49 other tissues.
DR ExpressionAtlas; Q9VPQ6; baseline and differential.
DR Genevisible; Q9VPQ6; DM.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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; IPI:FlyBase.
DR GO; GO:0046665; P:amnioserosa maintenance; IMP:FlyBase.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0022416; P:chaeta development; IGI:FlyBase.
DR GO; GO:0048749; P:compound eye development; IMP:FlyBase.
DR GO; GO:0007390; P:germ-band shortening; IMP:FlyBase.
DR GO; GO:0007507; P:heart development; IMP:FlyBase.
DR GO; GO:0035167; P:larval lymph gland hemopoiesis; IMP:FlyBase.
DR GO; GO:0035170; P:lymph gland crystal cell differentiation; IMP:FlyBase.
DR GO; GO:0048542; P:lymph gland development; IMP:FlyBase.
DR GO; GO:0035169; P:lymph gland plasmatocyte differentiation; IMP:FlyBase.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IDA:FlyBase.
DR GO; GO:0045611; P:negative regulation of hemocyte differentiation; IMP:FlyBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:FlyBase.
DR GO; GO:0006963; P:positive regulation of antibacterial peptide biosynthetic process; IMP:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:FlyBase.
DR IDEAL; IID50106; -.
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 SMART; SM00355; ZnF_C2H2; 8.
DR SUPFAM; SSF57667; SSF57667; 6.
DR PROSITE; PS51810; ZF_CCHC_FOG; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1191
FT /note="Zinc finger protein ush"
FT /id="PRO_0000221047"
FT ZN_FING 202..235
FT /note="CCHC FOG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT ZN_FING 279..301
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 335..368
FT /note="CCHC FOG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT ZN_FING 720..753
FT /note="CCHC FOG-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT ZN_FING 791..824
FT /note="CCHC FOG-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT ZN_FING 882..907
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 910..932
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 983..1006
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1113..1146
FT /note="CCHC FOG-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT REGION 1..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1011..1073
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..151
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..536
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1013..1044
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 210
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 231
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 343
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 346
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 359
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 364
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 728
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 731
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 744
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 749
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 799
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 802
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 815
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 820
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 1121
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 1124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 1137
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 1142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1013
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1015
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1017
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1156
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MUTAGEN 231
FT /note="C->A: Abolishes interaction with GATA-type zinc
FT fingers."
FT /evidence="ECO:0000269|PubMed:11080638"
FT MUTAGEN 1142
FT /note="C->H: Transforms the C2HC-type zinc finger into a
FT C2H2-type, leading to abolish interaction with pnr."
FT CONFLICT 524
FT /note="P -> H (in Ref. 1; CAA72991)"
FT /evidence="ECO:0000305"
FT CONFLICT 532
FT /note="A -> S (in Ref. 1; CAA72991)"
FT /evidence="ECO:0000305"
FT CONFLICT 1045
FT /note="P -> A (in Ref. 1; CAA72991)"
FT /evidence="ECO:0000305"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:1FV5"
FT TURN 211..213
FT /evidence="ECO:0007829|PDB:1FV5"
FT HELIX 220..229
FT /evidence="ECO:0007829|PDB:1FV5"
FT STRAND 1113..1115
FT /evidence="ECO:0007829|PDB:1JN7"
FT STRAND 1118..1121
FT /evidence="ECO:0007829|PDB:1JN7"
FT TURN 1122..1124
FT /evidence="ECO:0007829|PDB:1FU9"
FT HELIX 1131..1140
FT /evidence="ECO:0007829|PDB:1FU9"
SQ SEQUENCE 1191 AA; 124533 MW; 77A9D990767FE6ED CRC64;
MLSSNTRGDC SDTAEEMTVD SRDSKDLSAQ DIGEQKQQQM EDQLEDQLND SRDPQNNNNN
IDDDADEDAE FEEPEKANPQ QDQDLGETEM EQEHDLQQED LQQELPANSP STPPRSPSSP
QLIPKLEQPA TPPSEPEASP CPSPSPCPTP KYPKVRLNAL LASDPALKPD AKELTLPDSR
LLAPPPLVKP DTQAQPEVAE PLLKPARFMC LPCGIAFSSP STLEAHQAYY CSHRIKDTDE
AGSDKSGAGG SGATAGDAAG LTGGSTEPPA KMARTGKQYG CTQCSYSADK KVSLNRHMRM
HQTSPAAPTL AGLPSLLQNG IAPPGVTPNP MEDSSSQQTD RYCSHCDIRF NNIKTYRAHK
QHYCSSRRPE GQLTPKPDAS PGAGSGPGSA GGSIGVSAQA ATPGKLSPQA RNKTPTPAMV
AVAAAAAAAA ASLQATPHSH PPFLALPTHP IIIVPCSLIR AASFIPGPLP TPNSGIVNPE
TTCFTVDNGT IKPLATALVG ATLEPERPSA PSSAAEATEA KSSPPEPKRK EAGLTRESAP
LDLSLRRSPI TLNSLSLRQR QLRNALLDVE EVLLAGVGTG KENVETPRGG GSVTPEQIVC
APSLPSSPSM SPSPKRRAIS PRSSGAGSAS SMSPPGLNVA VPHLLDMRSM LPADFGLSES
LLAKTNPELA LKLAAAAAAA AVAGSSGAAA FPPASLPAQT SSGNPGSGGS AGGAQQPQIY
VKKGVSKCME CNIVFCKYEN YLAHKQHYCS ARSQEGASEV DVKSAVSPSI AGAGGLGAGA
AEAASSVETT PVAYQQLICA ACGIKYTSLD NLRAHQNYYC PKGGAVAAPA ATPTDPGQLG
MPKEKCGKCK TLHEIGLPCP PPVANPLAAP TVNPQPATNS LNKCPVCGVV SPTAALAKKH
MEMHGTVKAY RCSICQYKGN TLRGMRTHIR THFDKKTSDV NEELYMTCIF EEDASALSQE
LVTPTGASTT TGHDSMDHPS QMFNCDYCNY VSTYKGNVLR HMKLMHPHVA INSPSISPDT
RDQDVTSNPT TNQHSNSDVS NGEAPSFHIK SEPLDPPPTV NLVHENNNSP IATPHIKAEP
IEVGADAAPG GLVPPMTSPL GNSSSVAAAA AAAAEVMKKY CSTCDISFNY VKTYLAHKQF
YCKNKPIRPE ASDSPSPNHL GGGVAVGLGI GGLVGGHGQQ KNKENLQEAA I
