FOG2_HUMAN
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 03-AUG-2022, entry version 163.
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]: Form of congenital
CC diaphragmatic hernia (CDH). CDH refers to a group of congenital defects
CC in the structural integrity of the diaphragm associated with often
CC lethal pulmonary hypoplasia and pulmonary hypertension.
CC {ECO:0000269|PubMed:16103912}. Note=The disease is caused by variants
CC affecting the gene represented 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}.
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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 RefSeq; NP_036214.2; NM_012082.3. [Q8WW38-1]
DR AlphaFoldDB; Q8WW38; -.
DR BioGRID; 116986; 23.
DR ELM; Q8WW38; -.
DR IntAct; Q8WW38; 14.
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; Q8WW38; -.
DR PeptideAtlas; Q8WW38; -.
DR PRIDE; Q8WW38; -.
DR ProteomicsDB; 74858; -. [Q8WW38-1]
DR ProteomicsDB; 74859; -. [Q8WW38-2]
DR Antibodypedia; 1311; 144 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 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; LKHPMSI; -.
DR OrthoDB; 1030296at2759; -.
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; 11 hits in 1100 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 162 other tissues.
DR ExpressionAtlas; Q8WW38; baseline and differential.
DR Genevisible; Q8WW38; HS.
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: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:0060548; P:negative regulation of cell death; IEA:Ensembl.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; IMP:UniProtKB.
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:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
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 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; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
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
