ZBT20_HUMAN
ID ZBT20_HUMAN Reviewed; 741 AA.
AC Q9HC78; Q63HP6; Q8N6R5; Q9Y410;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 3.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Zinc finger and BTB domain-containing protein 20;
DE AltName: Full=Dendritic-derived BTB/POZ zinc finger protein;
DE AltName: Full=Zinc finger protein 288;
GN Name=ZBTB20; Synonyms=DPZF, ZNF288;
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, AND TISSUE SPECIFICITY.
RX PubMed=11352661; DOI=10.1006/bbrc.2001.4689;
RA Zhang W., Mi J., Li N., Sui L., Wan T., Zhang J., Chen T., Cao X.;
RT "Identification and characterization of DPZF, a novel human BTB/POZ zinc
RT finger protein sharing homology to BCL-6.";
RL Biochem. Biophys. Res. Commun. 282:1067-1073(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Kidney;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Endometrium;
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 [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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Colon;
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-211 AND SER-353, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [9]
RP INVOLVEMENT IN PRIMS, VARIANTS PRIMS GLN-590; ARG-596; ALA-602 AND PHE-621,
RP AND CHARACTERIZATION OF VARIANTS PRIMS GLN-590; ARG-596; ALA-602 AND
RP PHE-621.
RX PubMed=25017102; DOI=10.1038/ng.3035;
RA Cordeddu V., Redeker B., Stellacci E., Jongejan A., Fragale A.,
RA Bradley T.E., Anselmi M., Ciolfi A., Cecchetti S., Muto V., Bernardini L.,
RA Azage M., Carvalho D.R., Espay A.J., Male A., Molin A.M., Posmyk R.,
RA Battisti C., Casertano A., Melis D., van Kampen A., Baas F., Mannens M.M.,
RA Bocchinfuso G., Stella L., Tartaglia M., Hennekam R.C.;
RT "Mutations in ZBTB20 cause Primrose syndrome.";
RL Nat. Genet. 46:815-817(2014).
RN [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-330, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-330, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-330, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-330, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-330; LYS-371 AND LYS-723, AND
RP IDENTIFICATION BY MASS 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).
CC -!- FUNCTION: May be a transcription factor that may be involved in
CC hematopoiesis, oncogenesis, and immune responses (PubMed:11352661).
CC Plays a role in postnatal myogenesis, may be involved in the regulation
CC of satellite cells self-renewal (By similarity).
CC {ECO:0000250|UniProtKB:Q8K0L9, ECO:0000269|PubMed:11352661}.
CC -!- SUBUNIT: Can homodimerize. Binds to DNA.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8K0L9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9HC78-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9HC78-2; Sequence=VSP_032503;
CC -!- TISSUE SPECIFICITY: Expressed in spleen, lymph node, thymus, peripheral
CC blood leukocytes, and fetal liver. {ECO:0000269|PubMed:11352661}.
CC -!- PTM: Sumoylated with SUMO1. {ECO:0000250}.
CC -!- DISEASE: Primrose syndrome (PRIMS) [MIM:259050]: A disease
CC characterized by macrocephaly, intellectual disability, disturbed
CC behavior, dysmorphic facial features, ectopic calcifications, large
CC calcified ear auricles, and progressive muscle wasting.
CC {ECO:0000269|PubMed:25017102}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
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DR EMBL; AF139460; AAG28340.2; -; mRNA.
DR EMBL; AL050276; CAB43377.1; -; mRNA.
DR EMBL; BX647778; CAH56190.1; -; mRNA.
DR EMBL; CH471052; EAW79598.1; -; Genomic_DNA.
DR EMBL; BC029041; AAH29041.1; -; mRNA.
DR CCDS; CCDS2981.1; -. [Q9HC78-2]
DR CCDS; CCDS54626.1; -. [Q9HC78-1]
DR PIR; T08725; T08725.
DR RefSeq; NP_001157814.1; NM_001164342.2. [Q9HC78-1]
DR RefSeq; NP_001157815.1; NM_001164343.2. [Q9HC78-2]
DR RefSeq; NP_001157816.1; NM_001164344.2. [Q9HC78-2]
DR RefSeq; NP_001157817.1; NM_001164345.2. [Q9HC78-2]
DR RefSeq; NP_001157818.1; NM_001164346.2. [Q9HC78-2]
DR RefSeq; NP_001157819.1; NM_001164347.2. [Q9HC78-2]
DR RefSeq; NP_001335729.1; NM_001348800.1. [Q9HC78-1]
DR RefSeq; NP_001335731.1; NM_001348802.1. [Q9HC78-2]
DR RefSeq; NP_001335732.1; NM_001348803.1. [Q9HC78-1]
DR RefSeq; NP_001335733.1; NM_001348804.1. [Q9HC78-2]
DR RefSeq; NP_001335734.1; NM_001348805.1. [Q9HC78-2]
DR RefSeq; NP_056457.3; NM_015642.5. [Q9HC78-2]
DR AlphaFoldDB; Q9HC78; -.
DR SMR; Q9HC78; -.
DR BioGRID; 117573; 51.
DR IntAct; Q9HC78; 15.
DR STRING; 9606.ENSP00000419153; -.
DR GlyGen; Q9HC78; 4 sites, 2 O-linked glycans (4 sites).
DR iPTMnet; Q9HC78; -.
DR PhosphoSitePlus; Q9HC78; -.
DR BioMuta; ZBTB20; -.
DR DMDM; 172045933; -.
DR EPD; Q9HC78; -.
DR jPOST; Q9HC78; -.
DR MassIVE; Q9HC78; -.
DR MaxQB; Q9HC78; -.
DR PaxDb; Q9HC78; -.
DR PeptideAtlas; Q9HC78; -.
DR PRIDE; Q9HC78; -.
DR ProteomicsDB; 81647; -. [Q9HC78-1]
DR ProteomicsDB; 81648; -. [Q9HC78-2]
DR Antibodypedia; 16495; 161 antibodies from 25 providers.
DR DNASU; 26137; -.
DR Ensembl; ENST00000357258.8; ENSP00000349803.3; ENSG00000181722.17. [Q9HC78-2]
DR Ensembl; ENST00000393785.6; ENSP00000377375.2; ENSG00000181722.17. [Q9HC78-2]
DR Ensembl; ENST00000462705.5; ENSP00000420324.1; ENSG00000181722.17. [Q9HC78-2]
DR Ensembl; ENST00000464560.5; ENSP00000417307.1; ENSG00000181722.17. [Q9HC78-2]
DR Ensembl; ENST00000471418.5; ENSP00000419902.1; ENSG00000181722.17. [Q9HC78-2]
DR Ensembl; ENST00000474710.5; ENSP00000419153.1; ENSG00000181722.17. [Q9HC78-1]
DR Ensembl; ENST00000481632.5; ENSP00000418092.1; ENSG00000181722.17. [Q9HC78-2]
DR Ensembl; ENST00000675478.1; ENSP00000501561.1; ENSG00000181722.17. [Q9HC78-1]
DR Ensembl; ENST00000676079.1; ENSP00000502480.1; ENSG00000181722.17. [Q9HC78-1]
DR GeneID; 26137; -.
DR KEGG; hsa:26137; -.
DR MANE-Select; ENST00000675478.1; ENSP00000501561.1; NM_001348800.3; NP_001335729.1.
DR UCSC; uc003ebi.5; human. [Q9HC78-1]
DR CTD; 26137; -.
DR DisGeNET; 26137; -.
DR GeneCards; ZBTB20; -.
DR GeneReviews; ZBTB20; -.
DR HGNC; HGNC:13503; ZBTB20.
DR HPA; ENSG00000181722; Tissue enriched (brain).
DR MalaCards; ZBTB20; -.
DR MIM; 259050; phenotype.
DR MIM; 606025; gene.
DR neXtProt; NX_Q9HC78; -.
DR OpenTargets; ENSG00000181722; -.
DR Orphanet; 3042; Intellectual disability-cataracts-calcified pinnae-myopathy syndrome.
DR PharmGKB; PA37789; -.
DR VEuPathDB; HostDB:ENSG00000181722; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000158617; -.
DR HOGENOM; CLU_019055_0_0_1; -.
DR InParanoid; Q9HC78; -.
DR OMA; EQQFMAG; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9HC78; -.
DR TreeFam; TF335684; -.
DR PathwayCommons; Q9HC78; -.
DR SignaLink; Q9HC78; -.
DR SIGNOR; Q9HC78; -.
DR BioGRID-ORCS; 26137; 17 hits in 1134 CRISPR screens.
DR ChiTaRS; ZBTB20; human.
DR GeneWiki; ZBTB20; -.
DR GenomeRNAi; 26137; -.
DR Pharos; Q9HC78; Tbio.
DR PRO; PR:Q9HC78; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9HC78; protein.
DR Bgee; ENSG00000181722; Expressed in corpus epididymis and 206 other tissues.
DR ExpressionAtlas; Q9HC78; baseline and differential.
DR Genevisible; Q9HC78; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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: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:UniProtKB.
DR GO; GO:0071333; P:cellular response to glucose stimulus; ISS:UniProtKB.
DR GO; GO:0055088; P:lipid homeostasis; ISS:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:0045821; P:positive regulation of glycolytic process; ISS:UniProtKB.
DR GO; GO:0032728; P:positive regulation of interferon-beta production; IEA:Ensembl.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IEA:Ensembl.
DR GO; GO:0046889; P:positive regulation of lipid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF00096; zf-C2H2; 5.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE 1: Evidence at protein level;
KW Alternative splicing; Disease variant; DNA-binding;
KW Intellectual disability; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..741
FT /note="Zinc finger and BTB domain-containing protein 20"
FT /id="PRO_0000047733"
FT DOMAIN 104..167
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 578..600
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 606..628
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 634..656
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 662..684
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 715..737
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 211
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 357
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8K0L9"
FT MOD_RES 690
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8K0L9"
FT MOD_RES 695
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8K0L9"
FT CROSSLNK 330
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 330
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 371
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 723
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..73
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11230166,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005"
FT /id="VSP_032503"
FT VARIANT 590
FT /note="K -> Q (in PRIMS; does not affect subcellular
FT location; strongly reduced DNA binding; reduced ability to
FT repress transcription; dominant-negative effect of the
FT mutant on the wild-type allele; dbSNP:rs483353064)"
FT /evidence="ECO:0000269|PubMed:25017102"
FT /id="VAR_072583"
FT VARIANT 596
FT /note="H -> R (in PRIMS; strongly reduced DNA binding;
FT strongly reduced ability to repress transcription;
FT dominant-negative effect of the mutant on the wild-type
FT allele; dbSNP:rs483353066)"
FT /evidence="ECO:0000269|PubMed:25017102"
FT /id="VAR_072584"
FT VARIANT 602
FT /note="G -> A (in PRIMS; strongly reduced DNA binding;
FT strongly reduced ability to repress transcription;
FT dominant-negative effect of the mutant on the wild-type
FT allele; dbSNP:rs483353068)"
FT /evidence="ECO:0000269|PubMed:25017102"
FT /id="VAR_072585"
FT VARIANT 621
FT /note="L -> F (in PRIMS; strongly reduced DNA binding;
FT reduced ability to repress transcription; dominant-negative
FT effect of the mutant on the wild-type allele;
FT dbSNP:rs483353070)"
FT /evidence="ECO:0000269|PubMed:25017102"
FT /id="VAR_072586"
FT CONFLICT 224
FT /note="S -> G (in Ref. 1; AAG28340)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="V -> M (in Ref. 1; AAG28340)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="E -> G (in Ref. 3; CAH56190)"
FT /evidence="ECO:0000305"
FT CONFLICT 337
FT /note="Y -> F (in Ref. 1; AAG28340)"
FT /evidence="ECO:0000305"
FT CONFLICT 465
FT /note="S -> F (in Ref. 1; AAG28340)"
FT /evidence="ECO:0000305"
FT CONFLICT 517
FT /note="A -> V (in Ref. 1; AAG28340)"
FT /evidence="ECO:0000305"
FT CONFLICT 543
FT /note="S -> F (in Ref. 5; AAH29041)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 741 AA; 81083 MW; 913DDA9E6771C1EF CRC64;
MLERKKPKTA ENQKASEENE ITQPGGSSAK PGLPCLNFEA VLSPDPALIH STHSLTNSHA
HTGSSDCDIS CKGMTERIHS INLHNFSNSV LETLNEQRNR GHFCDVTVRI HGSMLRAHRC
VLAAGSPFFQ DKLLLGYSDI EIPSVVSVQS VQKLIDFMYS GVLRVSQSEA LQILTAASIL
QIKTVIDECT RIVSQNVGDV FPGIQDSGQD TPRGTPESGT SGQSSDTESG YLQSHPQHSV
DRIYSALYAC SMQNGSGERS FYSGAVVSHH ETALGLPRDH HMEDPSWITR IHERSQQMER
YLSTTPETTH CRKQPRPVRI QTLVGNIHIK QEMEDDYDYY GQQRVQILER NESEECTEDT
DQAEGTESEP KGESFDSGVS SSIGTEPDSV EQQFGPGAAR DSQAEPTQPE QAAEAPAEGG
PQTNQLETGA SSPERSNEVE MDSTVITVSN SSDKSVLQQP SVNTSIGQPL PSTQLYLRQT
ETLTSNLRMP LTLTSNTQVI GTAGNTYLPA LFTTQPAGSG PKPFLFSLPQ PLAGQQTQFV
TVSQPGLSTF TAQLPAPQPL ASSAGHSTAS GQGEKKPYEC TLCNKTFTAK QNYVKHMFVH
TGEKPHQCSI CWRSFSLKDY LIKHMVTHTG VRAYQCSICN KRFTQKSSLN VHMRLHRGEK
SYECYICKKK FSHKTLLERH VALHSASNGT PPAGTPPGAR AGPPGVVACT EGTTYVCSVC
PAKFDQIEQF NDHMRMHVSD G
