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   24-JAN-2024, entry version 192.
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.
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; 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   GlyCosmos; Q9HC78; 4 sites, 2 glycans.
DR   GlyGen; Q9HC78; 11 sites, 2 O-linked glycans (11 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; 9606-ENSP00000419153; -.
DR   PeptideAtlas; Q9HC78; -.
DR   ProteomicsDB; 81647; -. [Q9HC78-1]
DR   ProteomicsDB; 81648; -. [Q9HC78-2]
DR   Antibodypedia; 16495; 186 antibodies from 25 providers.
DR   DNASU; 26137; -.
DR   Ensembl; ENST00000357258.8; ENSP00000349803.3; ENSG00000181722.18. [Q9HC78-2]
DR   Ensembl; ENST00000462705.5; ENSP00000420324.1; ENSG00000181722.18. [Q9HC78-2]
DR   Ensembl; ENST00000464560.5; ENSP00000417307.1; ENSG00000181722.18. [Q9HC78-2]
DR   Ensembl; ENST00000470311.6; ENSP00000420684.2; ENSG00000181722.18. [Q9HC78-2]
DR   Ensembl; ENST00000471418.5; ENSP00000419902.1; ENSG00000181722.18. [Q9HC78-2]
DR   Ensembl; ENST00000474710.6; ENSP00000419153.1; ENSG00000181722.18. [Q9HC78-1]
DR   Ensembl; ENST00000481632.5; ENSP00000418092.1; ENSG00000181722.18. [Q9HC78-2]
DR   Ensembl; ENST00000675478.1; ENSP00000501561.1; ENSG00000181722.18. [Q9HC78-1]
DR   Ensembl; ENST00000676079.1; ENSP00000502480.1; ENSG00000181722.18. [Q9HC78-1]
DR   Ensembl; ENST00000704358.1; ENSP00000515869.1; ENSG00000181722.18. [Q9HC78-1]
DR   GeneID; 26137; -.
DR   MANE-Select; ENST00000675478.1; ENSP00000501561.1; NM_001348800.3; NP_001335729.1.
DR   UCSC; uc003ebi.5; human. [Q9HC78-1]
DR   AGR; HGNC:13503; -.
DR   DisGeNET; 26137; -.
DR   GeneCards; ZBTB20; -.
DR   GeneReviews; ZBTB20; -.
DR   HGNC; HGNC:13503; ZBTB20.
DR   HPA; ENSG00000181722; Low tissue specificity.
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; SVEQQFM; -.
DR   OrthoDB; 4160080at2759; -.
DR   PhylomeDB; Q9HC78; -.
DR   TreeFam; TF335684; -.
DR   PathwayCommons; Q9HC78; -.
DR   SignaLink; Q9HC78; -.
DR   SIGNOR; Q9HC78; -.
DR   BioGRID-ORCS; 26137; 17 hits in 1212 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 208 other cell types or 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:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
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:0001817; P:regulation of cytokine production; IBA:GO_Central.
DR   GO; GO:0002682; P:regulation of immune system process; IBA:GO_Central.
DR   CDD; cd18208; BTB_POZ_ZBTB20_DPZF; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 4.
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   PANTHER; PTHR46105; AGAP004733-PA; 1.
DR   PANTHER; PTHR46105:SF5; AGAP004733-PA; 1.
DR   Pfam; PF00651; BTB; 1.
DR   Pfam; PF00096; zf-C2H2; 5.
DR   SMART; SM00225; BTB; 1.
DR   SMART; SM00355; ZnF_C2H2; 5.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 2.
DR   SUPFAM; SSF54695; POZ domain; 1.
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
//