GLIS2_HUMAN
ID GLIS2_HUMAN Reviewed; 524 AA.
AC Q9BZE0; B3KX84;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Zinc finger protein GLIS2;
DE AltName: Full=GLI-similar 2;
DE AltName: Full=Neuronal Krueppel-like protein;
GN Name=GLIS2; Synonyms=NKL;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=11738817; DOI=10.1016/s0378-1119(01)00764-8;
RA Zhang F., Jetten A.M.;
RT "Genomic structure of the gene encoding the human GLI-related, Kruppel-like
RT zinc finger protein GLIS2.";
RL Gene 280:49-57(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION.
RX PubMed=11262234; DOI=10.1242/dev.128.8.1335;
RA Lamar E., Kintner C., Goulding M.;
RT "Identification of NKL, a novel Gli-Kruppel zinc-finger protein that
RT promotes neuronal differentiation.";
RL Development 128:1335-1346(2001).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=17289029; DOI=10.1016/j.febslet.2007.01.058;
RA Kim Y.-S., Kang H.S., Jetten A.M.;
RT "The Kruppel-like zinc finger protein Glis2 functions as a negative
RT modulator of the Wnt/beta-catenin signaling pathway.";
RL FEBS Lett. 581:858-864(2007).
RN [7]
RP INTERACTION WITH CTNND1.
RX PubMed=17344476; DOI=10.1091/mbc.e06-10-0941;
RA Hosking C.R., Ulloa F., Hogan C., Ferber E.C., Figueroa A., Gevaert K.,
RA Birchmeier W., Briscoe J., Fujita Y.;
RT "The transcriptional repressor Glis2 is a novel binding partner for p120
RT catenin.";
RL Mol. Biol. Cell 18:1918-1927(2007).
RN [8]
RP INVOLVEMENT IN NPHP7.
RX PubMed=17618285; DOI=10.1038/ng2072;
RA Attanasio M., Uhlenhaut N.H., Sousa V.H., O'Toole J.F., Otto E., Anlag K.,
RA Klugmann C., Treier A.-C., Helou J., Sayer J.A., Seelow D., Nuernberg G.,
RA Becker C., Chudley A.E., Nuernberg P., Hildebrandt F., Treier M.;
RT "Loss of GLIS2 causes nephronophthisis in humans and mice by increased
RT apoptosis and fibrosis.";
RL Nat. Genet. 39:1018-1024(2007).
CC -!- FUNCTION: Can act either as a transcriptional repressor or as a
CC transcriptional activator, depending on the cell context. Acts as a
CC repressor of the Hedgehog signaling pathway (By similarity). Represses
CC the Hedgehog-dependent expression of Wnt4 (By similarity). Necessary to
CC maintain the differentiated epithelial phenotype in renal cells through
CC the inhibition of SNAI1, which itself induces the epithelial-to-
CC mesenchymal transition (By similarity). Represses transcriptional
CC activation mediated by CTNNB1 in the Wnt signaling pathway. May act by
CC recruiting the corepressors CTBP1 and HDAC3. May be involved in neuron
CC differentiation (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CTBP1 and HDAC3 (By similarity). Interacts with
CC CTNNB1 (By similarity). Interacts with SUFU (By similarity). Interacts
CC with CTNND1. {ECO:0000250, ECO:0000269|PubMed:17344476}.
CC -!- INTERACTION:
CC Q9BZE0; Q08043: ACTN3; NbExp=3; IntAct=EBI-7251368, EBI-2880652;
CC Q9BZE0; Q6PJH3: AKAP9; NbExp=3; IntAct=EBI-7251368, EBI-11745576;
CC Q9BZE0; Q8N2N9-4: ANKRD36B; NbExp=3; IntAct=EBI-7251368, EBI-12170453;
CC Q9BZE0; Q03989: ARID5A; NbExp=3; IntAct=EBI-7251368, EBI-948603;
CC Q9BZE0; P56945: BCAR1; NbExp=3; IntAct=EBI-7251368, EBI-702093;
CC Q9BZE0; Q5BKX5-3: C19orf54; NbExp=5; IntAct=EBI-7251368, EBI-11976299;
CC Q9BZE0; Q03060-25: CREM; NbExp=3; IntAct=EBI-7251368, EBI-12884642;
CC Q9BZE0; O43186: CRX; NbExp=3; IntAct=EBI-7251368, EBI-748171;
CC Q9BZE0; P67870: CSNK2B; NbExp=3; IntAct=EBI-7251368, EBI-348169;
CC Q9BZE0; P56545-3: CTBP2; NbExp=3; IntAct=EBI-7251368, EBI-10171902;
CC Q9BZE0; P35222: CTNNB1; NbExp=6; IntAct=EBI-7251368, EBI-491549;
CC Q9BZE0; A1KXE4-2: FAM168B; NbExp=3; IntAct=EBI-7251368, EBI-12193763;
CC Q9BZE0; P53539: FOSB; NbExp=3; IntAct=EBI-7251368, EBI-2806743;
CC Q9BZE0; O75496: GMNN; NbExp=3; IntAct=EBI-7251368, EBI-371669;
CC Q9BZE0; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-7251368, EBI-5916454;
CC Q9BZE0; Q86YR5-3: GPSM1; NbExp=3; IntAct=EBI-7251368, EBI-10261098;
CC Q9BZE0; Q7Z4W3: KRTAP19-3; NbExp=3; IntAct=EBI-7251368, EBI-12020132;
CC Q9BZE0; Q3LI72: KRTAP19-5; NbExp=5; IntAct=EBI-7251368, EBI-1048945;
CC Q9BZE0; Q3SYF9: KRTAP19-7; NbExp=3; IntAct=EBI-7251368, EBI-10241353;
CC Q9BZE0; Q3LI64: KRTAP6-1; NbExp=3; IntAct=EBI-7251368, EBI-12111050;
CC Q9BZE0; Q3LI66: KRTAP6-2; NbExp=5; IntAct=EBI-7251368, EBI-11962084;
CC Q9BZE0; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-7251368, EBI-10261141;
CC Q9BZE0; Q9Y5B8: NME7; NbExp=3; IntAct=EBI-7251368, EBI-744782;
CC Q9BZE0; O43482: OIP5; NbExp=3; IntAct=EBI-7251368, EBI-536879;
CC Q9BZE0; Q9UF11-2: PLEKHB1; NbExp=3; IntAct=EBI-7251368, EBI-12832742;
CC Q9BZE0; Q96CS7: PLEKHB2; NbExp=5; IntAct=EBI-7251368, EBI-373552;
CC Q9BZE0; P78424: POU6F2; NbExp=3; IntAct=EBI-7251368, EBI-12029004;
CC Q9BZE0; P31321: PRKAR1B; NbExp=3; IntAct=EBI-7251368, EBI-2805516;
CC Q9BZE0; P86480: PRR20D; NbExp=3; IntAct=EBI-7251368, EBI-12754095;
CC Q9BZE0; P57052: RBM11; NbExp=3; IntAct=EBI-7251368, EBI-741332;
CC Q9BZE0; Q93062-3: RBPMS; NbExp=3; IntAct=EBI-7251368, EBI-740343;
CC Q9BZE0; O15266-2: SHOX; NbExp=3; IntAct=EBI-7251368, EBI-12825957;
CC Q9BZE0; Q08117-2: TLE5; NbExp=3; IntAct=EBI-7251368, EBI-11741437;
CC Q9BZE0; Q86WV8: TSC1; NbExp=3; IntAct=EBI-7251368, EBI-12806590;
CC Q9BZE0; Q8WVJ9: TWIST2; NbExp=3; IntAct=EBI-7251368, EBI-1797313;
CC Q9BZE0; Q08AM6: VAC14; NbExp=3; IntAct=EBI-7251368, EBI-2107455;
CC Q9BZE0; P61758: VBP1; NbExp=3; IntAct=EBI-7251368, EBI-357430;
CC Q9BZE0; O95231: VENTX; NbExp=3; IntAct=EBI-7251368, EBI-10191303;
CC Q9BZE0; Q9NZC7-5: WWOX; NbExp=3; IntAct=EBI-7251368, EBI-12040603;
CC Q9BZE0; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-7251368, EBI-527853;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}. Cytoplasm
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in kidney and at low
CC levels in heart, lung and placenta. Expressed in colon.
CC {ECO:0000269|PubMed:11738817, ECO:0000269|PubMed:17289029}.
CC -!- DOMAIN: The C2H2-type zinc finger 1 has a major repressor function and
CC is required for CTNNB1 binding. {ECO:0000250}.
CC -!- PTM: C-terminus cleavage is induced by interaction with CTNND1 and
CC enhanced by Src tyrosine kinase. {ECO:0000250}.
CC -!- DISEASE: Nephronophthisis 7 (NPHP7) [MIM:611498]: An autosomal
CC recessive disorder resulting in end-stage renal disease during
CC childhood or adolescence. It is a progressive tubulo-interstitial
CC kidney disorder histologically characterized by modifications of the
CC tubules with thickening of the basement membrane, interstitial fibrosis
CC and, in the advanced stages, medullary cysts.
CC {ECO:0000269|PubMed:17618285}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the GLI C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; AF325914; AAK00954.1; -; mRNA.
DR EMBL; AK126918; BAG54396.1; -; mRNA.
DR EMBL; AC005356; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC012676; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471112; EAW85317.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85318.1; -; Genomic_DNA.
DR CCDS; CCDS10511.1; -.
DR RefSeq; NP_001305847.1; NM_001318918.1.
DR RefSeq; NP_115964.2; NM_032575.2.
DR RefSeq; XP_005255698.1; XM_005255641.4.
DR AlphaFoldDB; Q9BZE0; -.
DR SMR; Q9BZE0; -.
DR BioGRID; 124182; 121.
DR CORUM; Q9BZE0; -.
DR IntAct; Q9BZE0; 48.
DR MINT; Q9BZE0; -.
DR STRING; 9606.ENSP00000262366; -.
DR iPTMnet; Q9BZE0; -.
DR PhosphoSitePlus; Q9BZE0; -.
DR BioMuta; GLIS2; -.
DR DMDM; 296434515; -.
DR jPOST; Q9BZE0; -.
DR MassIVE; Q9BZE0; -.
DR MaxQB; Q9BZE0; -.
DR PaxDb; Q9BZE0; -.
DR PeptideAtlas; Q9BZE0; -.
DR PRIDE; Q9BZE0; -.
DR ProteomicsDB; 79818; -.
DR Antibodypedia; 11033; 121 antibodies from 23 providers.
DR DNASU; 84662; -.
DR Ensembl; ENST00000262366.7; ENSP00000262366.3; ENSG00000126603.9.
DR Ensembl; ENST00000433375.2; ENSP00000395547.1; ENSG00000126603.9.
DR Ensembl; ENST00000612491.1; ENSP00000484027.1; ENSG00000274636.2.
DR Ensembl; ENST00000633051.1; ENSP00000488242.1; ENSG00000274636.2.
DR GeneID; 84662; -.
DR KEGG; hsa:84662; -.
DR MANE-Select; ENST00000433375.2; ENSP00000395547.1; NM_032575.3; NP_115964.2.
DR UCSC; uc002cwc.2; human.
DR CTD; 84662; -.
DR DisGeNET; 84662; -.
DR GeneCards; GLIS2; -.
DR GeneReviews; GLIS2; -.
DR HGNC; HGNC:29450; GLIS2.
DR HPA; ENSG00000126603; Low tissue specificity.
DR MalaCards; GLIS2; -.
DR MIM; 608539; gene.
DR MIM; 611498; phenotype.
DR neXtProt; NX_Q9BZE0; -.
DR OpenTargets; ENSG00000126603; -.
DR Orphanet; 329469; Acute megakaryoblastic leukemia without Down syndrome.
DR Orphanet; 93592; Juvenile nephronophthisis.
DR PharmGKB; PA134919876; -.
DR VEuPathDB; HostDB:ENSG00000126603; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000158383; -.
DR HOGENOM; CLU_031801_1_0_1; -.
DR InParanoid; Q9BZE0; -.
DR OMA; APKDKCL; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9BZE0; -.
DR TreeFam; TF351425; -.
DR PathwayCommons; Q9BZE0; -.
DR SignaLink; Q9BZE0; -.
DR SIGNOR; Q9BZE0; -.
DR BioGRID-ORCS; 84662; 15 hits in 1097 CRISPR screens.
DR ChiTaRS; GLIS2; human.
DR GenomeRNAi; 84662; -.
DR Pharos; Q9BZE0; Tbio.
DR PRO; PR:Q9BZE0; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9BZE0; protein.
DR Bgee; ENSG00000126603; Expressed in right coronary artery and 94 other tissues.
DR Genevisible; Q9BZE0; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0097730; C:non-motile cilium; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; ISS:BHF-UCL.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISS:BHF-UCL.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:BHF-UCL.
DR GO; GO:0061005; P:cell differentiation involved in kidney development; IEA:Ensembl.
DR GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
DR GO; GO:0061484; P:hematopoietic stem cell homeostasis; IEA:Ensembl.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; ISS:BHF-UCL.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR030432; Glis2.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR19818:SF84; PTHR19818:SF84; 1.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 1: Evidence at protein level;
KW Activator; Ciliopathy; Cytoplasm; Developmental protein; Differentiation;
KW DNA-binding; Metal-binding; Nephronophthisis; Neurogenesis; Nucleus;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..524
FT /note="Zinc finger protein GLIS2"
FT /id="PRO_0000286983"
FT ZN_FING 168..193
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 202..229
FT /note="C2H2-type 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 235..257
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 263..287
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 293..317
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 35..174
FT /note="Interaction with CTNND1"
FT /evidence="ECO:0000250"
FT REGION 39..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..137
FT /note="Transcription activation"
FT /evidence="ECO:0000250"
FT REGION 84..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..171
FT /note="Transcription repression"
FT /evidence="ECO:0000250"
FT REGION 439..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 287..288
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT VARIANT 492
FT /note="T -> A (in dbSNP:rs8057701)"
FT /id="VAR_032256"
FT CONFLICT 49
FT /note="P -> L (in Ref. 1; AAK00954)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 524 AA; 55689 MW; F38BA80C477FDC24 CRC64;
MHSLDEPLDL KLSITKLRAA REKRERTLGV VRPRALHREL GLVDDSPTPG SPGSPPSGFL
LNSKFPEKVE GRFSAAPLVD LSLSPPSGLD SPNGSSSLSP ERQGNGDLPP VPSASDFQPL
RYLDGVPSSF QFFLPLGSGG ALHLPASSFL TPPKDKCLSP DLPLPKQLVC RWAKCNQLFE
LLQDLVDHVN DYHVKPEKDA GYCCHWEGCA RHGRGFNARY KMLIHIRTHT NEKPHRCPTC
SKSFSRLENL KIHNRSHTGE KPYVCPYEGC NKRYSNSSDR FKHTRTHYVD KPYYCKMPGC
HKRYTDPSSL RKHIKAHGHF VSHEQQELLQ LRPPPKPPLP APDGGPYVSG AQIIIPNPAA
LFGGPGLPGL PLPLAPGPLD LSALACGNGG GSGGGGGMGP GLPGPVLPLN LAKNPLLPSP
FGAGGLGLPV VSLLAGAAGG KAEGEKGRGS VPTRALGMEG HKTPLERTES SCSRPSPDGL
PLLPGTVLDL STGVNSAASS PEALAPGWVV IPPGSVLLKP AVVN
