ZBT46_HUMAN
ID ZBT46_HUMAN Reviewed; 589 AA.
AC Q86UZ6; E1P5K9; Q5JWJ3; Q6GMV4; Q9BQK3; Q9H3Z8; Q9H3Z9;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-FEB-2004, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Zinc finger and BTB domain-containing protein 46;
DE AltName: Full=BTB-ZF protein expressed in effector lymphocytes;
DE Short=BZEL;
DE AltName: Full=BTB/POZ domain-containing protein 4;
DE AltName: Full=Zinc finger protein 340;
GN Name=ZBTB46; Synonyms=BTBD4, ZNF340;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-11.
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [5]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-229, 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 [6]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-229, 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).
CC -!- FUNCTION: Functions as a transcriptional repressor for PRDM1.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- PTM: Sumoylated. Desumoylation by DESI1 reverses transcriptional
CC repression activity (By similarity). {ECO:0000250}.
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DR EMBL; AL121845; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW75205.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75206.1; -; Genomic_DNA.
DR EMBL; BC052269; AAH52269.1; -; mRNA.
DR EMBL; BC073800; AAH73800.1; -; mRNA.
DR CCDS; CCDS13538.1; -.
DR RefSeq; NP_079500.2; NM_025224.3.
DR RefSeq; XP_005260252.1; XM_005260195.4.
DR RefSeq; XP_005260253.1; XM_005260196.3.
DR RefSeq; XP_005260254.1; XM_005260197.4.
DR RefSeq; XP_005260255.1; XM_005260198.4.
DR RefSeq; XP_006723763.1; XM_006723700.3.
DR RefSeq; XP_011526850.1; XM_011528548.2.
DR AlphaFoldDB; Q86UZ6; -.
DR SMR; Q86UZ6; -.
DR BioGRID; 126648; 32.
DR IntAct; Q86UZ6; 16.
DR STRING; 9606.ENSP00000378536; -.
DR iPTMnet; Q86UZ6; -.
DR PhosphoSitePlus; Q86UZ6; -.
DR BioMuta; ZBTB46; -.
DR DMDM; 42558860; -.
DR EPD; Q86UZ6; -.
DR jPOST; Q86UZ6; -.
DR MassIVE; Q86UZ6; -.
DR MaxQB; Q86UZ6; -.
DR PaxDb; Q86UZ6; -.
DR PeptideAtlas; Q86UZ6; -.
DR PRIDE; Q86UZ6; -.
DR ProteomicsDB; 69942; -.
DR Antibodypedia; 2860; 188 antibodies from 24 providers.
DR DNASU; 140685; -.
DR Ensembl; ENST00000245663.9; ENSP00000245663.3; ENSG00000130584.12.
DR Ensembl; ENST00000302995.2; ENSP00000303102.2; ENSG00000130584.12.
DR Ensembl; ENST00000395104.5; ENSP00000378536.1; ENSG00000130584.12.
DR GeneID; 140685; -.
DR KEGG; hsa:140685; -.
DR MANE-Select; ENST00000245663.9; ENSP00000245663.3; NM_001369741.1; NP_001356670.1.
DR UCSC; uc061ypq.1; human.
DR CTD; 140685; -.
DR DisGeNET; 140685; -.
DR GeneCards; ZBTB46; -.
DR HGNC; HGNC:16094; ZBTB46.
DR HPA; ENSG00000130584; Low tissue specificity.
DR MIM; 614639; gene.
DR neXtProt; NX_Q86UZ6; -.
DR OpenTargets; ENSG00000130584; -.
DR PharmGKB; PA25441; -.
DR VEuPathDB; HostDB:ENSG00000130584; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000158060; -.
DR HOGENOM; CLU_022356_2_0_1; -.
DR InParanoid; Q86UZ6; -.
DR OMA; QSERTWD; -.
DR OrthoDB; 755439at2759; -.
DR PhylomeDB; Q86UZ6; -.
DR TreeFam; TF341953; -.
DR PathwayCommons; Q86UZ6; -.
DR SignaLink; Q86UZ6; -.
DR BioGRID-ORCS; 140685; 12 hits in 1132 CRISPR screens.
DR ChiTaRS; ZBTB46; human.
DR GenomeRNAi; 140685; -.
DR Pharos; Q86UZ6; Tbio.
DR PRO; PR:Q86UZ6; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q86UZ6; protein.
DR Bgee; ENSG00000130584; Expressed in oviduct epithelium and 142 other tissues.
DR ExpressionAtlas; Q86UZ6; baseline and differential.
DR Genevisible; Q86UZ6; HS.
DR GO; GO:0000785; C:chromatin; ISS:ARUK-UCL.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISS:ARUK-UCL.
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:0000976; F:transcription cis-regulatory region binding; ISS:ARUK-UCL.
DR GO; GO:0030851; P:granulocyte differentiation; IEA:Ensembl.
DR GO; GO:0030225; P:macrophage differentiation; IEA:Ensembl.
DR GO; GO:2001199; P:negative regulation of dendritic cell differentiation; IEA:Ensembl.
DR GO; GO:0030853; P:negative regulation of granulocyte differentiation; IEA:Ensembl.
DR GO; GO:0002695; P:negative regulation of leukocyte activation; IEA:Ensembl.
DR GO; GO:0045650; P:negative regulation of macrophage differentiation; IEA:Ensembl.
DR GO; GO:0045656; P:negative regulation of monocyte differentiation; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:ARUK-UCL.
DR GO; GO:0002273; P:plasmacytoid dendritic cell differentiation; IEA:Ensembl.
DR GO; GO:2001200; P:positive regulation of dendritic cell differentiation; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ARUK-UCL.
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 SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE 1: Evidence at protein level;
KW Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..589
FT /note="Zinc finger and BTB domain-containing protein 46"
FT /id="PRO_0000047746"
FT DOMAIN 31..99
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 418..436
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 446..468
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 173..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..287
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..565
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 229
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT VARIANT 11
FT /note="T -> A (in dbSNP:rs2281929)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_030629"
SQ SEQUENCE 589 AA; 64083 MW; F03FC7D7BF9B9E09 CRC64;
MNNRKEDMEI TSHYRHLLRE LNEQRQHGVL CDVCVVVEGK VFKAHKNVLL GSSRYFKTLY
CQVQKTSEQA TVTHLDIVTA QGFKAIIDFM YSAHLALTSR NVIEVMSAAS FLQMTDIVQA
CHDFIKAALD ISIKSDASDE LAEFEIGASS SSSTEALISA VMAGRSISPW LARRTSPANS
SGDSAIASCH DGGSSYGKED QEPKADGPDD VSSQPLWPGD VGYGPLRIKE EQVSPSQYGG
SELPSAKDGA VQNSFSEQSA GDAWQPTGRR KNRKNKETVR HITQQVEDDS RASSPVPSFL
PTSGWPFSSR DSNADLSVTE ASSSDSRGER AELYAQVEEG LLGGEASYLG PPLTPEKDDA
LHQATAVANL RAALMSKNSL LSLKADVLGD DGSLLFEYLP RGAHSLSLNE FTVIRKKFKC
PYCSFSAMHQ CILKRHMRSH TGERPYPCEI CGKKFTRREH MKRHTLVHSK DKKYVCKVCS
RVFMSAASVG IRHGSRRHGV CTDCAGRGMA GPLDHGGGGG EGSPEALFPG DGPYLEDPED
PRGEAEELGE DDEGLAPEDA LLADDKDEED SPRPRSPPGG PDKDFAWLS
