PEG3_HUMAN
ID PEG3_HUMAN Reviewed; 1588 AA.
AC Q9GZU2; A7E2B8; B4DIM4; C9JP50; P78418; Q5H9P9; Q7Z7H7; Q8TF75; Q9GZY2;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Paternally-expressed gene 3 protein;
DE AltName: Full=Zinc finger and SCAN domain-containing protein 24;
GN Name=PEG3; Synonyms=KIAA0287, ZSCAN24;
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] (ISOFORMS 1 AND 2), AND VARIANT LEU-1576.
RC TISSUE=Fetal kidney;
RX PubMed=11677152; DOI=10.1016/s1071-5576(01)00129-0;
RA Van den Veyver I.B., Norman B., Tran C.Q., Bourjac J., Slim R.;
RT "The human homologue (PEG3) of the mouse paternally expressed gene 3 (Peg3)
RT is maternally imprinted but not mutated in women with familial recurrent
RT hydatidiform molar pregnancies.";
RL J. Soc. Gynecol. Invest. 8:305-313(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Hippocampus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 4-1588 (ISOFORM 3), AND VARIANT SER-947.
RC TISSUE=Liver;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 127-456, AND TISSUE SPECIFICITY.
RX PubMed=11331620; DOI=10.1093/hmg/10.10.1093;
RA Hiby S.E., Lough M., Keverne E.B., Surani M.A., Loke Y.W., King A.;
RT "Paternal monoallelic expression of PEG3 in the human placenta.";
RL Hum. Mol. Genet. 10:1093-1100(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 781-1588.
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 302-1588 (ISOFORM 1), FUNCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=11260267; DOI=10.1046/j.1365-2443.2001.00412.x;
RA Kohda T., Asai A., Kuroiwa Y., Kobayashi S., Aisaka K., Nagashima G.,
RA Yoshida M.C., Kondo Y., Kagiyama N., Kirino T., Kaneko-Ishino T.,
RA Ishino F.;
RT "Tumour suppressor activity of human imprinted gene PEG3 in a glioma cell
RT line.";
RL Genes Cells 6:237-247(2001).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 974-1588, AND TISSUE SPECIFICITY.
RX PubMed=9149948; DOI=10.1101/gr.7.5.532;
RA Kim J., Ashworth L., Branscomb E., Stubbs L.;
RT "The human homolog of a mouse-imprinted gene, Peg3, maps to a zinc finger
RT gene-rich region of human chromosome 19q13.4.";
RL Genome Res. 7:532-540(1997).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 974-1588.
RA Lamerdin J.E., McCready P.M., Kim J., Skowronski E., Viswanathan V.,
RA Burkhart-Schultz K., Gordon L., Dias J., Ramirez M., Stilwagen S., Phan H.,
RA Velasco N., Do L., Regala W., Terry A., Garnes J., Danganan L., Erler A.,
RA Christensen M., Georgescu A., Avila J., Liu S., Attix C., Andreise T.,
RA Trankheim M., Amico-Keller G., Coefield J., Duarte S., Lucas S., Bruce R.,
RA Thomas P., Quan G., Kronmiller B., Arellano A., Saunders C., Ow D.,
RA Nolan M., Trong S., Kobayashi A., Olsen A.S., Carrano A.V.;
RT "Sequence analysis of a 2 Mb region containing a zinc finger (ZNF) gene
RT cluster in 19q13.4.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 40-130, SCAN DOMAIN, AND SUBUNIT.
RX PubMed=23936039; DOI=10.1371/journal.pone.0069538;
RA Rimsa V., Eadsforth T.C., Hunter W.N.;
RT "Structure of the SCAN domain of human paternally expressed gene 3
RT protein.";
RL PLoS ONE 8:E69538-E69538(2013).
RN [12]
RP VARIANT [LARGE SCALE ANALYSIS] HIS-594.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Induces apoptosis in cooperation with SIAH1A. Acts as a
CC mediator between p53/TP53 and BAX in a neuronal death pathway that is
CC activated by DNA damage. Acts synergistically with TRAF2 and inhibits
CC TNF induced apoptosis through activation of NF-kappa-B (By similarity).
CC Possesses a tumor suppressing activity in glioma cells. {ECO:0000250,
CC ECO:0000269|PubMed:11260267}.
CC -!- SUBUNIT: Homodimer. Interacts with SIAH1A and SIAH2. Interacts with
CC TRAF2 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}.
CC Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9GZU2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9GZU2-2; Sequence=VSP_020371;
CC Name=3;
CC IsoId=Q9GZU2-3; Sequence=VSP_020372, VSP_020373, VSP_020374;
CC Name=4;
CC IsoId=Q9GZU2-4; Sequence=VSP_020371, VSP_045527, VSP_045528;
CC -!- TISSUE SPECIFICITY: Brain, glial cells, astrocytes, embryo, placenta,
CC testis, ovary and uterus. In the placenta it is found in the layer of
CC villous cytotrophoblast cells while in the ovary it is found in the
CC cells of the ovarian stroma including the thecal layers around the
CC follicles. Expression is highly repressed in glioma cell lines.
CC {ECO:0000269|PubMed:11260267, ECO:0000269|PubMed:11331620,
CC ECO:0000269|PubMed:9149948}.
CC -!- DOMAIN: The SCAN domain enables PEG3 homo- or heterodimerization to
CC control gene expression in a combinatorial fashion.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB85588.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAI45975.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/PEG3ID41690ch19q13.html";
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DR EMBL; AF208980; AAG42324.1; -; Genomic_DNA.
DR EMBL; AF208974; AAG42324.1; JOINED; Genomic_DNA.
DR EMBL; AF208975; AAG42324.1; JOINED; Genomic_DNA.
DR EMBL; AF208976; AAG42324.1; JOINED; Genomic_DNA.
DR EMBL; AF208977; AAG42324.1; JOINED; Genomic_DNA.
DR EMBL; AF208978; AAG42324.1; JOINED; Genomic_DNA.
DR EMBL; AF208979; AAG42324.1; JOINED; Genomic_DNA.
DR EMBL; AF208980; AAG42325.1; -; Genomic_DNA.
DR EMBL; AF208974; AAG42325.1; JOINED; Genomic_DNA.
DR EMBL; AF208975; AAG42325.1; JOINED; Genomic_DNA.
DR EMBL; AF208976; AAG42325.1; JOINED; Genomic_DNA.
DR EMBL; AF208977; AAG42325.1; JOINED; Genomic_DNA.
DR EMBL; AF208978; AAG42325.1; JOINED; Genomic_DNA.
DR EMBL; AF208979; AAG42325.1; JOINED; Genomic_DNA.
DR EMBL; AF208967; AAG35739.1; -; mRNA.
DR EMBL; AF208968; AAG35740.1; -; mRNA.
DR EMBL; AF208969; AAG35741.1; -; mRNA.
DR EMBL; AF208970; AAG35742.1; -; mRNA.
DR EMBL; AK295679; BAG58536.1; -; mRNA.
DR EMBL; CH471135; EAW72474.1; -; Genomic_DNA.
DR EMBL; BC052616; AAH52616.1; -; mRNA.
DR EMBL; BC150272; AAI50273.1; -; mRNA.
DR EMBL; AB003039; BAB85588.1; ALT_FRAME; mRNA.
DR EMBL; CR933682; CAI45975.1; ALT_INIT; mRNA.
DR EMBL; U90336; AAB50011.1; -; mRNA.
DR EMBL; AC006115; AAC83176.1; -; Genomic_DNA.
DR CCDS; CCDS12948.1; -. [Q9GZU2-1]
DR CCDS; CCDS58684.1; -. [Q9GZU2-4]
DR CCDS; CCDS58685.1; -. [Q9GZU2-2]
DR RefSeq; NP_001139656.1; NM_001146184.1. [Q9GZU2-1]
DR RefSeq; NP_001139657.1; NM_001146185.1. [Q9GZU2-2]
DR RefSeq; NP_001139658.1; NM_001146186.1.
DR RefSeq; NP_001139659.1; NM_001146187.1. [Q9GZU2-4]
DR RefSeq; NP_006201.1; NM_006210.2. [Q9GZU2-1]
DR PDB; 4BHX; X-ray; 1.95 A; A/B=40-130.
DR PDBsum; 4BHX; -.
DR AlphaFoldDB; Q9GZU2; -.
DR SMR; Q9GZU2; -.
DR BioGRID; 111204; 10.
DR DIP; DIP-38426N; -.
DR IntAct; Q9GZU2; 6.
DR MINT; Q9GZU2; -.
DR STRING; 9606.ENSP00000326581; -.
DR iPTMnet; Q9GZU2; -.
DR PhosphoSitePlus; Q9GZU2; -.
DR BioMuta; PEG3; -.
DR DMDM; 74762724; -.
DR jPOST; Q9GZU2; -.
DR MassIVE; Q9GZU2; -.
DR MaxQB; Q9GZU2; -.
DR PaxDb; Q9GZU2; -.
DR PeptideAtlas; Q9GZU2; -.
DR PRIDE; Q9GZU2; -.
DR ProteomicsDB; 1789; -.
DR ProteomicsDB; 80145; -. [Q9GZU2-1]
DR ProteomicsDB; 80146; -. [Q9GZU2-2]
DR ProteomicsDB; 80147; -. [Q9GZU2-3]
DR Antibodypedia; 19625; 182 antibodies from 24 providers.
DR DNASU; 5178; -.
DR Ensembl; ENST00000326441.15; ENSP00000326581.7; ENSG00000198300.14. [Q9GZU2-1]
DR Ensembl; ENST00000593695.5; ENSP00000472402.1; ENSG00000198300.14. [Q9GZU2-2]
DR Ensembl; ENST00000598410.5; ENSP00000473190.1; ENSG00000198300.14. [Q9GZU2-4]
DR Ensembl; ENST00000599534.5; ENSP00000472395.1; ENSG00000198300.14. [Q9GZU2-1]
DR Ensembl; ENST00000599577.5; ENSP00000469486.1; ENSG00000198300.14. [Q9GZU2-1]
DR Ensembl; ENST00000648694.1; ENSP00000496914.1; ENSG00000198300.14. [Q9GZU2-4]
DR Ensembl; ENST00000649233.1; ENSP00000498047.1; ENSG00000198300.14. [Q9GZU2-4]
DR Ensembl; ENST00000649428.1; ENSP00000498138.1; ENSG00000198300.14. [Q9GZU2-4]
DR Ensembl; ENST00000649680.1; ENSP00000497512.1; ENSG00000198300.14. [Q9GZU2-4]
DR Ensembl; ENST00000649876.1; ENSP00000496867.1; ENSG00000198300.14. [Q9GZU2-4]
DR Ensembl; ENST00000650102.1; ENSP00000497466.1; ENSG00000198300.14. [Q9GZU2-4]
DR Ensembl; ENST00000650632.1; ENSP00000497971.1; ENSG00000198300.14. [Q9GZU2-4]
DR GeneID; 5178; -.
DR KEGG; hsa:5178; -.
DR MANE-Select; ENST00000326441.15; ENSP00000326581.7; NM_006210.3; NP_006201.1.
DR UCSC; uc002qnv.3; human. [Q9GZU2-1]
DR CTD; 5178; -.
DR DisGeNET; 5178; -.
DR GeneCards; PEG3; -.
DR HGNC; HGNC:8826; PEG3.
DR HPA; ENSG00000198300; Group enriched (adrenal gland, brain, choroid plexus, ovary, placenta).
DR MIM; 601483; gene.
DR neXtProt; NX_Q9GZU2; -.
DR OpenTargets; ENSG00000198300; -.
DR PharmGKB; PA33171; -.
DR VEuPathDB; HostDB:ENSG00000198300; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162525; -.
DR HOGENOM; CLU_005305_0_0_1; -.
DR InParanoid; Q9GZU2; -.
DR OMA; TIYECQD; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9GZU2; -.
DR TreeFam; TF337075; -.
DR PathwayCommons; Q9GZU2; -.
DR SignaLink; Q9GZU2; -.
DR BioGRID-ORCS; 5178; 10 hits in 1041 CRISPR screens.
DR GeneWiki; PEG3; -.
DR GenomeRNAi; 5178; -.
DR Pharos; Q9GZU2; Tbio.
DR PRO; PR:Q9GZU2; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9GZU2; protein.
DR Bgee; ENSG00000198300; Expressed in endothelial cell and 202 other tissues.
DR ExpressionAtlas; Q9GZU2; baseline and differential.
DR Genevisible; Q9GZU2; HS.
DR GO; GO:0005776; C:autophagosome; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd07936; SCAN; 1.
DR Gene3D; 1.10.4020.10; -; 1.
DR InterPro; IPR003309; SCAN_dom.
DR InterPro; IPR038269; SCAN_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF02023; SCAN; 1.
DR Pfam; PF00096; zf-C2H2; 9.
DR SMART; SM00431; SCAN; 1.
DR SMART; SM00355; ZnF_C2H2; 12.
DR SUPFAM; SSF57667; SSF57667; 9.
DR PROSITE; PS50804; SCAN_BOX; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 12.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 12.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoptosis; Cytoplasm; Metal-binding;
KW Nucleus; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..1588
FT /note="Paternally-expressed gene 3 protein"
FT /id="PRO_0000249228"
FT DOMAIN 46..128
FT /note="SCAN box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT REPEAT 1397..1403
FT /note="2-1"
FT REPEAT 1404..1410
FT /note="2-2"
FT REPEAT 1411..1417
FT /note="2-3"
FT REPEAT 1418..1422
FT /note="1-1"
FT REPEAT 1425..1429
FT /note="1-2"
FT REPEAT 1432..1436
FT /note="1-3"
FT REPEAT 1439..1443
FT /note="1-4"
FT ZN_FING 452..474
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 505..527
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 563..585
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 627..649
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 969..991
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1107..1129
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1163..1185
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1225..1247
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1282..1304
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1332..1354
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1505..1527
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1564..1586
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 128..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 839..889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 905..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1056..1104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1396..1495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1397..1417
FT /note="3 X 7 AA repeat of P-E-V-E-A-A-E"
FT REGION 1418..1443
FT /note="4 X 5 AA repeat of P-X-G-E-A"
FT COMPBIAS 139..189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..878
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1056..1083
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1398..1421
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1447..1463
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1472..1495
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..126
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:11677152,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_020371"
FT VAR_SEQ 161
FT /note="S -> SG (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_045527"
FT VAR_SEQ 257
FT /note="L -> LG (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_045528"
FT VAR_SEQ 258..287
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020372"
FT VAR_SEQ 547..550
FT /note="SPTF -> NPCL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020373"
FT VAR_SEQ 551..1588
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020374"
FT VARIANT 235
FT /note="A -> T (in dbSNP:rs2191432)"
FT /id="VAR_027397"
FT VARIANT 594
FT /note="R -> H (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs754473044)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035562"
FT VARIANT 624
FT /note="E -> G (in dbSNP:rs36016896)"
FT /id="VAR_052725"
FT VARIANT 839
FT /note="V -> L (in dbSNP:rs7251798)"
FT /id="VAR_027398"
FT VARIANT 947
FT /note="N -> S (in dbSNP:rs35851866)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_052726"
FT VARIANT 983
FT /note="D -> G (in dbSNP:rs10412932)"
FT /id="VAR_027399"
FT VARIANT 1456
FT /note="A -> V (in dbSNP:rs34831553)"
FT /id="VAR_052727"
FT VARIANT 1576
FT /note="R -> H (in dbSNP:rs34051133)"
FT /id="VAR_052728"
FT VARIANT 1576
FT /note="R -> L (in dbSNP:rs34051133)"
FT /evidence="ECO:0000269|PubMed:11677152"
FT /id="VAR_027400"
FT CONFLICT 310..311
FT /note="SH -> PP (in Ref. 7; BAB85588)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="F -> L (in Ref. 2; BAG58536)"
FT /evidence="ECO:0000305"
FT CONFLICT 677
FT /note="K -> I (in Ref. 7; BAB85588)"
FT /evidence="ECO:0000305"
FT CONFLICT 690
FT /note="G -> A (in Ref. 7; BAB85588)"
FT /evidence="ECO:0000305"
FT CONFLICT 750
FT /note="F -> V (in Ref. 7; BAB85588)"
FT /evidence="ECO:0000305"
FT CONFLICT 755
FT /note="N -> Y (in Ref. 7; BAB85588)"
FT /evidence="ECO:0000305"
FT CONFLICT 1117
FT /note="V -> M (in Ref. 7; BAB85588)"
FT /evidence="ECO:0000305"
FT CONFLICT 1145
FT /note="I -> V (in Ref. 7; BAB85588)"
FT /evidence="ECO:0000305"
FT CONFLICT 1587
FT /note="T -> M (in Ref. 7; BAB85588)"
FT /evidence="ECO:0000305"
FT HELIX 42..51
FT /evidence="ECO:0007829|PDB:4BHX"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:4BHX"
FT HELIX 60..75
FT /evidence="ECO:0007829|PDB:4BHX"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:4BHX"
FT HELIX 82..97
FT /evidence="ECO:0007829|PDB:4BHX"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:4BHX"
FT HELIX 103..109
FT /evidence="ECO:0007829|PDB:4BHX"
FT HELIX 114..121
FT /evidence="ECO:0007829|PDB:4BHX"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:4BHX"
SQ SEQUENCE 1588 AA; 180827 MW; 7E4F34A01F189F3E CRC64;
MLPPKHLSAT KPKKSWAPNL YELDSDLTKE PDVIIGEGPT DSEFFHQRFR NLIYVEFVGP
RKTLIKLRNL CLDWLQPETR TKEEIIELLV LEQYLTIIPE KLKPWVRAKK PENCEKLVTL
LENYKEMYQP EDDNNSDVTS DDDMTRNRRE SSPPHSVHSF SDRDWDRRGR SRDMEPRDRW
SHTRNPRSRM PPRDLSLPVV AKTSFEMDRE DDRDSRAYES RSQDAESYQN VVDLAEDRKP
HNTIQDNMEN YRKLLSLVQL AEDDGHSHMT QGHSSRSKRS AYPSTSRGLK TMPEAKKSTH
RRGICEDESS HGVIMEKFIK DVSRSSKSGR ARESSDRSQR FPRMSDDNWK DISLNKRESV
IQQRVYEGNA FRGGFRFNST LVSRKRVLER KRRYHFDTDG KGSIHDQKGC PRKKPFECGS
EMRKAMSVSS LSSLSSPSFT ESQPIDFGAM PYVCDECGRS FSVISEFVEH QIMHTRENLY
EYGESFIHSV AVSEVQKSQV GGKRFECKDC GETFNKSAAL AEHRKIHARG YLVECKNQEC
EEAFMPSPTF SELQKIYGKD KFYECRVCKE TFLHSSALIE HQKIHFGDDK DNEREHERER
ERERGETFRP SPALNEFQKM YGKEKMYECK VCGETFLHSS SLKEHQKIHT RGNPFENKGK
VCEETFIPGQ SLKRRQKTYN KEKLCDFTDG RDAFMQSSEL SEHQKIHSRK NLFEGRGYEK
SVIHSGPFTE SQKSHTITRP LESDEDEKAF TISSNPYENQ KIPTKENVYE AKSYERSVIH
SLASVEAQKS HSVAGPSKPK VMAESTIQSF DAINHQRVRA GGNTSEGREY SRSVIHSLVA
SKPPRSHNGN ELVESNEKGE SSIYISDLND KRQKIPAREN PCEGGSKNRN YEDSVIQSVF
RAKPQKSVPG EGSGEFKKDG EFSVPSSNVR EYQKARAKKK YIEHRSNETS VIHSLPFGEQ
TFRPRGMLYE CQECGECFAH SSDLTEHQKI HDREKPSGSR NYEWSVIRSL APTDPQTSYA
QEQYAKEQAR NKCKDFRQFF ATSEDLNTNQ KIYDQEKSHG EESQGENTDG EETHSEETHG
QETIEDPVIQ GSDMEDPQKD DPDDKIYECE DCGLGFVDLT DLTDHQKVHS RKCLVDSREY
THSVIHTHSI SEYQRDYTGE QLYECPKCGE SFIHSSFLFE HQRIHEQDQL YSMKGCDDGF
IALLPMKPRR NRAAERNPAL AGSAIRCLLC GQGFIHSSAL NEHMRLHRED DLLEQSQMAE
EAIIPGLALT EFQRSQTEER LFECAVCGES FVNPAELADH VTVHKNEPYE YGSSYTHTSF
LTEPLKGAIP FYECKDCGKS FIHSTVLTKH KELHLEEEEE DEAAAAAAAA AQEVEANVHV
PQVVLRIQGL NVEAAEPEVE AAEPEVEAAE PEVEAAEPNG EAEGPDGEAA EPIGEAGQPN
GEAEQPNGDA DEPDGAGIED PEERAEEPEG KAEEPEGDAD EPDGVGIEDP EEGEDQEIQV
EEPYYDCHEC TETFTSSTAF SEHLKTHASM IIFEPANAFG ECSGYIERAS TSTGGANQAD
EKYFKCDVCG QLFNDRLSLA RHQNTHTG
