ID FOG2_HUMAN Reviewed; 1151 AA. AC Q8WW38; Q32MA6; Q9NPL7; Q9NPS4; Q9UNI5; DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot. DT 20-FEB-2007, sequence version 3. DT 24-JAN-2024, entry version 171. DE RecName: Full=Zinc finger protein ZFPM2; DE AltName: Full=Friend of GATA protein 2; DE Short=FOG-2; DE Short=Friend of GATA 2; DE Short=hFOG-2; DE AltName: Full=Zinc finger protein 89B; DE AltName: Full=Zinc finger protein multitype 2; GN Name=ZFPM2; Synonyms=FOG2, ZNF89B; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, RP INTERACTION WITH CTBP2, AND POSSIBLE INTERACTION WITH GATA1. RC TISSUE=Erythroleukemia; RX PubMed=10438528; DOI=10.1074/jbc.274.33.23491; RA Holmes M., Turner J., Fox A.H., Chisholm O., Crossley M., Chong B.; RT "hFOG-2, a novel zinc finger protein, binds the co-repressor mCtBP2 and RT modulates GATA-mediated activation."; RL J. Biol. Chem. 274:23491-23498(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Prostate; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-287 (ISOFORM 2), AND NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 641-1151 (ISOFORM 1). RG The European IMAGE consortium; RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases. RN [4] RP SUMOYLATION AT LYS-324; LYS-471; LYS-915 AND LYS-955, AND SUBCELLULAR RP LOCATION. RX PubMed=23226341; DOI=10.1371/journal.pone.0050637; RA Perdomo J., Jiang X.M., Carter D.R., Khachigian L.M., Chong B.H.; RT "SUMOylation regulates the transcriptional repression activity of FOG-2 and RT its association with GATA-4."; RL PLoS ONE 7:E50637-E50637(2012). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-532; SER-581; SER-904 AND RP SER-1014, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [6] RP INTERACTION WITH GATA4, INVOLVEMENT IN SRXY9, VARIANTS SRXY9 GLN-260; RP ARG-402 AND ILE-544, VARIANTS GLY-403 AND ASP-782, AND CHARACTERIZATION OF RP VARIANTS GLN-260 AND ARG-402. RX PubMed=24549039; DOI=10.1093/hmg/ddu074; RA Bashamboo A., Brauner R., Bignon-Topalovic J., Lortat-Jacob S., RA Karageorgou V., Lourenco D., Guffanti A., McElreavey K.; RT "Mutations in the FOG2/ZFPM2 gene are associated with anomalies of human RT testis determination."; RL Hum. Mol. Genet. 23:3657-3665(2014). RN [7] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-444, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [8] RP VARIANTS TOF GLY-30 AND GLY-657, AND CHARACTERIZATION OF VARIANTS TOF RP GLY-30 AND GLY-657. RX PubMed=14517948; DOI=10.1002/humu.10261; RA Pizzuti A., Sarkozy A., Newton A.L., Conti E., Flex E., Digilio M.C., RA Amati F., Gianni D., Tandoi C., Marino B., Crossley M., Dallapiccola B.; RT "Mutations of ZFPM2/FOG2 gene in sporadic cases of tetralogy of Fallot."; RL Hum. Mutat. 22:372-377(2003). RN [9] RP INVOLVEMENT IN DIH3. RX PubMed=16103912; DOI=10.1371/journal.pgen.0010010; RA Ackerman K.G., Herron B.J., Vargas S.O., Huang H., Tevosian S.G., RA Kochilas L., Rao C., Pober B.R., Babiuk R.P., Epstein J.A., Greer J.J., RA Beier D.R.; RT "Fog2 is required for normal diaphragm and lung development in mice and RT humans."; RL PLoS Genet. 1:58-65(2005). RN [10] RP VARIANT TOF ILE-544, AND VARIANTS CTHM GLY-30 AND VAL-227. RX PubMed=20807224; DOI=10.1111/j.1399-0004.2010.01523.x; RA De Luca A., Sarkozy A., Ferese R., Consoli F., Lepri F., Dentici M.L., RA Vergara P., De Zorzi A., Versacci P., Digilio M.C., Marino B., RA Dallapiccola B.; RT "New mutations in ZFPM2/FOG2 gene in tetralogy of Fallot and double outlet RT right ventricle."; RL Clin. Genet. 80:184-190(2011). CC -!- FUNCTION: Transcription regulator that plays a central role in heart CC morphogenesis and development of coronary vessels from epicardium, by CC regulating genes that are essential during cardiogenesis. Essential CC cofactor that acts via the formation of a heterodimer with CC transcription factors of the GATA family GATA4, GATA5 and GATA6. Such CC heterodimer can both activate or repress transcriptional activity, CC depending on the cell and promoter context. Also required in gonadal CC differentiation, possibly be regulating expression of SRY. Probably CC acts a corepressor of NR2F2 (By similarity). {ECO:0000250, CC ECO:0000269|PubMed:10438528}. CC -!- SUBUNIT: Interacts with the N-terminal zinc-finger of GATA4, GATA5 and CC probably GATA6. Interacts with retinoid nuclear receptor RXRA when CC ligand bound (By similarity). Interacts with corepressor CTBP2; this CC interaction is however not essential for corepressor activity. Able to CC bind GATA1 in vitro. Interacts with NR2F2 and NR2F6 (By similarity). CC Interacts with ATOH8; mediates indirect interaction with GATA4 (By CC similarity). {ECO:0000250|UniProtKB:Q8CCH7, CC ECO:0000269|PubMed:10438528, ECO:0000269|PubMed:24549039}. CC -!- INTERACTION: CC Q8WW38; G5E9A7: DMWD; NbExp=3; IntAct=EBI-947213, EBI-10976677; CC Q8WW38; P14136: GFAP; NbExp=3; IntAct=EBI-947213, EBI-744302; CC Q8WW38; P02545: LMNA; NbExp=3; IntAct=EBI-947213, EBI-351935; CC Q8WW38; O43395: PRPF3; NbExp=3; IntAct=EBI-947213, EBI-744322; CC Q8WW38; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-947213, EBI-5235340; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23226341}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8WW38-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8WW38-2; Sequence=VSP_009701, VSP_009702; CC -!- TISSUE SPECIFICITY: Widely expressed at low level. CC {ECO:0000269|PubMed:10438528}. CC -!- DOMAIN: The CCHC FOG-type zinc fingers 1, 2, 3 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 (By similarity). {ECO:0000250}. CC -!- PTM: Sumoylation reduces transcriptional repression activity. CC {ECO:0000269|PubMed:23226341}. CC -!- DISEASE: Tetralogy of Fallot (TOF) [MIM:187500]: A congenital heart CC anomaly which consists of pulmonary stenosis, ventricular septal CC defect, dextroposition of the aorta (aorta is on the right side instead CC of the left) and hypertrophy of the right ventricle. In this condition, CC blood from both ventricles (oxygen-rich and oxygen-poor) is pumped into CC the body often causing cyanosis. {ECO:0000269|PubMed:14517948, CC ECO:0000269|PubMed:20807224}. Note=The disease may be caused by CC variants affecting the gene represented in this entry. CC -!- DISEASE: Diaphragmatic hernia 3 (DIH3) [MIM:610187]: A form of CC congenital diaphragmatic hernia, a posterolateral defect of the CC diaphragm, generally located on the left side, that permits the CC herniation of abdominal viscera into the thorax. The lungs are CC hypoplastic and have abnormal vessels that cause respiratory CC insufficiency and persistent pulmonary hypertension with high CC mortality. About one third of cases have cardiovascular malformations CC and lesser proportions have skeletal, neural, genitourinary, CC gastrointestinal or other defects. {ECO:0000269|PubMed:16103912}. CC Note=The disease is caused by variants affecting the gene represented CC in this entry. CC -!- DISEASE: 46,XY sex reversal 9 (SRXY9) [MIM:616067]: A disorder of sex CC development. Affected individuals have a 46,XY karyotype but present as CC phenotypically normal females or have ambiguous external genitalia. CC {ECO:0000269|PubMed:24549039}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Conotruncal heart malformations (CTHM) [MIM:217095]: A group CC of congenital heart defects involving the outflow tracts. Examples CC include truncus arteriosus communis, double-outlet right ventricle and CC transposition of great arteries. Truncus arteriosus communis is CC characterized by a single outflow tract instead of a separate aorta and CC pulmonary artery. In transposition of the great arteries, the aorta CC arises from the right ventricle and the pulmonary artery from the left CC ventricle. In double outlet of the right ventricle, both the pulmonary CC artery and aorta arise from the right ventricle. CC {ECO:0000269|PubMed:20807224}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- MISCELLANEOUS: [Isoform 2]: Sequence incomplete. {ECO:0000305}. 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; AF119334; AAD49558.1; -; mRNA. DR EMBL; BC020928; AAH20928.1; -; mRNA. DR EMBL; BC109222; AAI09223.1; -; mRNA. DR EMBL; AL389987; CAB97539.1; -; mRNA. DR EMBL; AL389989; CAB97541.1; -; mRNA. DR CCDS; CCDS47908.1; -. [Q8WW38-1] DR CCDS; CCDS94333.1; -. [Q8WW38-2] DR RefSeq; NP_036214.2; NM_012082.3. [Q8WW38-1] DR AlphaFoldDB; Q8WW38; -. DR BioGRID; 116986; 23. DR ELM; Q8WW38; -. DR IntAct; Q8WW38; 15. DR MINT; Q8WW38; -. DR STRING; 9606.ENSP00000384179; -. DR iPTMnet; Q8WW38; -. DR PhosphoSitePlus; Q8WW38; -. DR BioMuta; ZFPM2; -. DR DMDM; 126302543; -. DR EPD; Q8WW38; -. DR jPOST; Q8WW38; -. DR MassIVE; Q8WW38; -. DR MaxQB; Q8WW38; -. DR PaxDb; 9606-ENSP00000384179; -. DR PeptideAtlas; Q8WW38; -. DR ProteomicsDB; 74858; -. [Q8WW38-1] DR ProteomicsDB; 74859; -. [Q8WW38-2] DR Pumba; Q8WW38; -. DR Antibodypedia; 1311; 162 antibodies from 27 providers. DR DNASU; 23414; -. DR Ensembl; ENST00000407775.7; ENSP00000384179.2; ENSG00000169946.14. [Q8WW38-1] DR GeneID; 23414; -. DR KEGG; hsa:23414; -. DR MANE-Select; ENST00000407775.7; ENSP00000384179.2; NM_012082.4; NP_036214.2. DR UCSC; uc003ymd.4; human. [Q8WW38-1] DR AGR; HGNC:16700; -. DR CTD; 23414; -. DR DisGeNET; 23414; -. DR GeneCards; ZFPM2; -. DR HGNC; HGNC:16700; ZFPM2. DR HPA; ENSG00000169946; Tissue enhanced (brain, ovary). DR MalaCards; ZFPM2; -. DR MIM; 187500; phenotype. DR MIM; 217095; phenotype. DR MIM; 603693; gene. DR MIM; 610187; phenotype. DR MIM; 616067; phenotype. DR neXtProt; NX_Q8WW38; -. DR OpenTargets; ENSG00000169946; -. DR Orphanet; 251510; 46,XY partial gonadal dysgenesis. DR Orphanet; 2140; Congenital diaphragmatic hernia. DR Orphanet; 3303; Tetralogy of Fallot. DR PharmGKB; PA134947303; -. DR VEuPathDB; HostDB:ENSG00000169946; -. DR eggNOG; KOG1721; Eukaryota. DR GeneTree; ENSGT00530000063823; -. DR InParanoid; Q8WW38; -. DR OMA; QISSICP; -. DR OrthoDB; 5402989at2759; -. DR PhylomeDB; Q8WW38; -. DR TreeFam; TF331342; -. DR PathwayCommons; Q8WW38; -. DR Reactome; R-HSA-9690406; Transcriptional regulation of testis differentiation. DR Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production. DR SignaLink; Q8WW38; -. DR SIGNOR; Q8WW38; -. DR BioGRID-ORCS; 23414; 12 hits in 1178 CRISPR screens. DR ChiTaRS; ZFPM2; human. DR GeneWiki; ZFPM2; -. DR GenomeRNAi; 23414; -. DR Pharos; Q8WW38; Tbio. DR PRO; PR:Q8WW38; -. DR Proteomes; UP000005640; Chromosome 8. DR RNAct; Q8WW38; Protein. DR Bgee; ENSG00000169946; Expressed in skeletal muscle tissue of biceps brachii and 163 other cell types or tissues. DR ExpressionAtlas; Q8WW38; baseline and differential. DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB. DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl. DR GO; GO:0001673; C:male germ cell nucleus; IEA:Ensembl. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL. DR GO; GO:0003713; F:transcription coactivator activity; IDA:BHF-UCL. DR GO; GO:0003714; F:transcription corepressor activity; IDA:BHF-UCL. DR GO; GO:0008270; F:zinc ion binding; NAS:BHF-UCL. DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central. DR GO; GO:0048568; P:embryonic organ development; IEA:Ensembl. DR GO; GO:0045444; P:fat cell differentiation; IMP:UniProtKB. DR GO; GO:0007506; P:gonadal mesoderm development; IEA:UniProtKB-KW. DR GO; GO:0007507; P:heart development; IBA:GO_Central. DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl. DR GO; GO:0030324; P:lung development; IEA:Ensembl. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0045599; P:negative regulation of fat cell differentiation; IEA:Ensembl. DR GO; GO:2000195; P:negative regulation of female gonad development; IEA:Ensembl. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL. DR GO; GO:0003148; P:outflow tract septum morphogenesis; IMP:BHF-UCL. DR GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; ISS:BHF-UCL. DR GO; GO:2000020; P:positive regulation of male gonad development; IEA:Ensembl. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL. DR GO; GO:0003221; P:right ventricular cardiac muscle tissue morphogenesis; IMP:BHF-UCL. DR GO; GO:0001570; P:vasculogenesis; IEA:Ensembl. DR GO; GO:0060412; P:ventricular septum morphogenesis; IMP:BHF-UCL. DR CDD; cd19216; PR-SET_ZFPM2; 1. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 2. 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:SF5; ZINC FINGER PROTEIN ZFPM2; 1. DR Pfam; PF21182; FOG1-like_PR; 1. DR Pfam; PF12874; zf-met; 1. DR SMART; SM00355; ZnF_C2H2; 8. 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; Q8WW38; HS. PE 1: Evidence at protein level; KW Activator; Alternative splicing; Cardiomyopathy; Differentiation; KW Disease variant; DNA-binding; Gonadal differentiation; Isopeptide bond; KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat; KW Repressor; Transcription; Transcription regulation; Ubl conjugation; Zinc; KW Zinc-finger. FT CHAIN 1..1151 FT /note="Zinc finger protein ZFPM2" FT /id="PRO_0000221043" FT ZN_FING 244..277 FT /note="CCHC FOG-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT ZN_FING 296..320 FT /note="C2H2-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 335..357 FT /note="C2H2-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 363..385 FT /note="C2H2-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 542..575 FT /note="CCHC FOG-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT ZN_FING 681..714 FT /note="CCHC FOG-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT ZN_FING 848..881 FT /note="CCHC FOG-type 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT ZN_FING 1113..1146 FT /note="CCHC FOG-type 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT REGION 1..102 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 389..487 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 636..683 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 829..835 FT /note="Interaction with CTBP2" FT /evidence="ECO:0000305" FT REGION 1051..1095 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 736..740 FT /note="Nuclear localization signal" FT /evidence="ECO:0000250" FT COMPBIAS 402..431 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 432..446 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 447..487 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1080..1095 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 252 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT BINDING 255 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT BINDING 268 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 550 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT BINDING 553 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT BINDING 566 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT BINDING 571 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT BINDING 689 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT BINDING 692 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT BINDING 705 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT BINDING 710 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT BINDING 856 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 872 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT BINDING 877 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 532 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 581 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 904 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1014 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CROSSLNK 324 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1)" FT /evidence="ECO:0000269|PubMed:23226341" FT CROSSLNK 444 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 471 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1)" FT /evidence="ECO:0000269|PubMed:23226341" FT CROSSLNK 915 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1)" FT /evidence="ECO:0000269|PubMed:23226341" FT CROSSLNK 955 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1)" FT /evidence="ECO:0000269|PubMed:23226341" FT VAR_SEQ 1..132 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|Ref.3" FT /id="VSP_009701" FT VAR_SEQ 247..287 FT /note="KDIFPCKSCGIWYRSERNLQAHLMYYCSGRQREAAPVSEEN -> SKCSVLC FT SPALEVMGIYGRKKCLLTRNQEQTFFLQKKKKKK (in isoform 2)" FT /evidence="ECO:0000303|Ref.3" FT /id="VSP_009702" FT VARIANT 30 FT /note="E -> G (in TOF and CTHM; does not affect its ability FT to interact with GATA4; dbSNP:rs121908601)" FT /evidence="ECO:0000269|PubMed:14517948, FT ECO:0000269|PubMed:20807224" FT /id="VAR_017942" FT VARIANT 227 FT /note="I -> V (in CTHM; dbSNP:rs202204708)" FT /evidence="ECO:0000269|PubMed:20807224" FT /id="VAR_072074" FT VARIANT 260 FT /note="R -> Q (in SRXY9; results in reduced transactivation FT activity on the AMH promoter; does not affect its ability FT to interact with GATA4; dbSNP:rs200834568)" FT /evidence="ECO:0000269|PubMed:24549039" FT /id="VAR_071104" FT VARIANT 402 FT /note="S -> R (in SRXY9; results in reduced transactivation FT activity on the AMH promoter; abolished its ability to FT interact with GATA4; dbSNP:rs606231252)" FT /evidence="ECO:0000269|PubMed:24549039" FT /id="VAR_071105" FT VARIANT 403 FT /note="A -> G (in dbSNP:rs11993776)" FT /evidence="ECO:0000269|PubMed:24549039" FT /id="VAR_024178" FT VARIANT 544 FT /note="M -> I (in SRXY9 and TOF; reduced its ability to FT interact with GATA4; dbSNP:rs187043152)" FT /evidence="ECO:0000269|PubMed:20807224, FT ECO:0000269|PubMed:24549039" FT /id="VAR_072075" FT VARIANT 657 FT /note="S -> G (in TOF; slightly impairs its ability to FT interact with GATA4; dbSNP:rs28374544)" FT /evidence="ECO:0000269|PubMed:14517948" FT /id="VAR_017943" FT VARIANT 782 FT /note="E -> D (in dbSNP:rs2920048)" FT /evidence="ECO:0000269|PubMed:24549039" FT /id="VAR_017944" FT VARIANT 1055 FT /note="A -> V (in dbSNP:rs16873741)" FT /id="VAR_030760" FT CONFLICT 198 FT /note="F -> L (in Ref. 3; CAB97541)" FT /evidence="ECO:0000305" FT CONFLICT 939 FT /note="L -> P (in Ref. 1; AAD49558)" FT /evidence="ECO:0000305" SQ SEQUENCE 1151 AA; 128159 MW; 680E31BA1D044C35 CRC64; MSRRKQSKPR QIKRPLEDAI EDEEEECPSE ETDIISKGDF PLEESFSTEF GPENLSCEEV EYFCNKGDDE GIQETAESDG DTQSEKPGQP GVETDDWDGP GELEVFQKDG ERKIQSRQQL PVGTTWGPFP GKMDLNNNSL KTKAQVPMVL TAGPKWLLDV TWQGVEDNKN NCIVYSKGGQ LWCTTTKAIS EGEELIAFVV DFDSRLQAAS QMTLTEGMYP ARLLDSIQLL PQQAAMASIL PTAIVNKDIF PCKSCGIWYR SERNLQAHLM YYCSGRQREA APVSEENEDS AHQISSLCPF PQCTKSFSNA RALEMHLNSH SGVKMEEFLP PGASLKCTVC SYTADSVINF HQHLFSHLTQ AAFRCNHCHF GFQTQRELLQ HQELHVPSGK LPRESDMEHS PSATEDSLQP ATDLLTRSEL PQSQKAMQTK DASSDTELDK CEKKTQLFLT NQRPEIQPTT NKQSFSYTKI KSEPSSPRLA SSPVQPNIGP SFPVGPFLSQ FSFPQDITMV PQASEILAKM SELVHRRLRH GSSSYPPVIY SPLMPKGATC FECNITFNNL DNYLVHKKHY CSSRWQQMAK SPEFPSVSEK MPEALSPNTG QTSINLLNPA AHSADPENPL LQTSCINSST VLDLIGPNGK GHDKDFSTQT KKLSTSSNND DKINGKPVDV KNPSVPLVDG ESDPNKTTCE ACNITFSRHE TYMVHKQYYC ATRHDPPLKR SASNKVPAMQ RTMRTRKRRK MYEMCLPEQE QRPPLVQQRF LDVANLNNPC TSTQEPTEGL GECYHPRCDI FPGIVSKHLE TSLTINKCVP VSKCDTTHSS VSCLEMDVPI DLSKKCLSQS ERTTTSPKRL LDYHECTVCK ISFNKVENYL AHKQNFCPVT AHQRNDLGQL DGKVFPNPES ERNSPDVSYE RSIIKCEKNG NLKQPSPNGN LFSSHLATLQ GLKVFSEAAQ LIATKEENRH LFLPQCLYPG AIKKAKGADQ LSPYYGIKPS DYISGSLVIH NTDIEQSRNA ENESPKGQAS SNGCAALKKD SLPLLPKNRG MVIVNGGLKQ DERPAANPQQ ENISQNPQHE DDHKSPSWIS ENPLAANENV SPGIPSAEEQ LSSIAKGVNG SSQAPTSGKY CRLCDIQFNN LSNFITHKKF YCSSHAAEHV K //