ZBT46_MOUSE
ID ZBT46_MOUSE Reviewed; 600 AA.
AC Q8BID6; A2AUD2; Q3U2R2; Q9D0G6; Q9D492;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-FEB-2004, sequence version 2.
DT 03-AUG-2022, entry version 155.
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;
GN Name=Zbtb46; Synonyms=Btbd4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Dendritic cell, Embryo, Hypothalamus, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=NMRI; TISSUE=Mammary gland;
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 FUNCTION, AND DESUMOYLATION BY DESI1.
RX PubMed=22370726; DOI=10.1038/embor.2012.3;
RA Shin E.J., Shin H.M., Nam E., Kim W.S., Kim J.H., Oh B.H., Yun Y.;
RT "DeSUMOylating isopeptidase: a second class of SUMO protease.";
RL EMBO Rep. 13:339-346(2012).
CC -!- FUNCTION: Functions as a transcriptional repressor for PRDM1.
CC {ECO:0000269|PubMed:22370726}.
CC -!- INTERACTION:
CC Q8BID6; Q9CQT7: Desi1; NbExp=2; IntAct=EBI-7768990, EBI-7768710;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BID6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BID6-2; Sequence=VSP_009387, VSP_009388;
CC -!- PTM: Sumoylated. Desumoylation by DESI1 reverses transcriptional
CC repression activity. {ECO:0000269|PubMed:22370726}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB30386.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC30190.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK011461; BAB27633.1; -; mRNA.
DR EMBL; AK016700; BAB30386.1; ALT_INIT; mRNA.
DR EMBL; AK038975; BAC30190.1; ALT_INIT; mRNA.
DR EMBL; AK155148; BAE33078.1; -; mRNA.
DR EMBL; AL929094; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC058179; AAH58179.1; -; mRNA.
DR CCDS; CCDS17212.1; -. [Q8BID6-2]
DR CCDS; CCDS50854.1; -. [Q8BID6-1]
DR RefSeq; NP_081932.1; NM_027656.2. [Q8BID6-1]
DR RefSeq; NP_082401.1; NM_028125.3. [Q8BID6-2]
DR RefSeq; XP_006500775.1; XM_006500712.3. [Q8BID6-1]
DR RefSeq; XP_006500776.1; XM_006500713.2. [Q8BID6-1]
DR AlphaFoldDB; Q8BID6; -.
DR SMR; Q8BID6; -.
DR IntAct; Q8BID6; 2.
DR MINT; Q8BID6; -.
DR STRING; 10090.ENSMUSP00000084672; -.
DR iPTMnet; Q8BID6; -.
DR PhosphoSitePlus; Q8BID6; -.
DR MaxQB; Q8BID6; -.
DR PaxDb; Q8BID6; -.
DR PRIDE; Q8BID6; -.
DR ProteomicsDB; 298498; -. [Q8BID6-1]
DR ProteomicsDB; 298499; -. [Q8BID6-2]
DR Antibodypedia; 2860; 188 antibodies from 24 providers.
DR DNASU; 72147; -.
DR Ensembl; ENSMUST00000029106; ENSMUSP00000029106; ENSMUSG00000027583. [Q8BID6-1]
DR Ensembl; ENSMUST00000087409; ENSMUSP00000084672; ENSMUSG00000027583. [Q8BID6-2]
DR Ensembl; ENSMUST00000180222; ENSMUSP00000137014; ENSMUSG00000027583. [Q8BID6-1]
DR GeneID; 72147; -.
DR KEGG; mmu:72147; -.
DR UCSC; uc008omh.2; mouse. [Q8BID6-2]
DR UCSC; uc008omi.1; mouse. [Q8BID6-1]
DR CTD; 140685; -.
DR MGI; MGI:1919397; Zbtb46.
DR VEuPathDB; HostDB:ENSMUSG00000027583; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000158060; -.
DR HOGENOM; CLU_022356_2_0_1; -.
DR InParanoid; Q8BID6; -.
DR OMA; QSERTWD; -.
DR OrthoDB; 755439at2759; -.
DR PhylomeDB; Q8BID6; -.
DR TreeFam; TF341953; -.
DR BioGRID-ORCS; 72147; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Zbtb46; mouse.
DR PRO; PR:Q8BID6; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8BID6; protein.
DR Bgee; ENSMUSG00000027583; Expressed in animal zygote and 213 other tissues.
DR ExpressionAtlas; Q8BID6; baseline and differential.
DR Genevisible; Q8BID6; MM.
DR GO; GO:0000785; C:chromatin; IDA:ARUK-UCL.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA: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; IDA:ARUK-UCL.
DR GO; GO:0097028; P:dendritic cell differentiation; IMP:MGI.
DR GO; GO:0030851; P:granulocyte differentiation; IMP:MGI.
DR GO; GO:0030225; P:macrophage differentiation; IMP:MGI.
DR GO; GO:2001199; P:negative regulation of dendritic cell differentiation; IMP:MGI.
DR GO; GO:0030853; P:negative regulation of granulocyte differentiation; IMP:MGI.
DR GO; GO:0002695; P:negative regulation of leukocyte activation; IMP:MGI.
DR GO; GO:0045650; P:negative regulation of macrophage differentiation; IMP:MGI.
DR GO; GO:0045656; P:negative regulation of monocyte differentiation; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:ARUK-UCL.
DR GO; GO:0002273; P:plasmacytoid dendritic cell differentiation; IMP:MGI.
DR GO; GO:2001200; P:positive regulation of dendritic cell differentiation; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
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; 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 Alternative splicing; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..600
FT /note="Zinc finger and BTB domain-containing protein 46"
FT /id="PRO_0000047747"
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..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..600
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 238..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..557
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..584
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UZ6"
FT CROSSLNK 229
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q86UZ6"
FT VAR_SEQ 408..434
FT /note="LNEFTVIRKKFKCPYCSFSAMHQCILK -> RKCKFWCVTVSSFGLSTSVQP
FT FRPWSH (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_009387"
FT VAR_SEQ 435..600
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_009388"
FT CONFLICT 363
FT /note="Q -> K (in Ref. 1; BAC30190)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 600 AA; 65499 MW; C89E77D5B7C1C0B3 CRC64;
MNNRKEDMEI TSHYRHLLRE LNEQRQHGVL CDACVVVEGK VFKAHKNVLL GSSRYFKTLY
CQVQKTSDQA TVTHLDIVTA QGFKAIIDFM YSAHLALTSR NVIEVMSAAS FLQMTDIVQA
CHDFIKAALD ISIKSDASDE LSEFEIGTPA SNSTEALISA VMAGRSISPW LARRTSPANS
SGDSAIASCH EGGSSYGKED QEPKADGPDD VSSQSLWPGD VGYGSLRIKE EQISPSHYGG
SELPSSKDTA IQNSLSEQGS GDGWQPTGRR KNRKNKETVR HITQQVEEDS QAGSPVPSFL
PTSGWPFSSR DSNVDLTVTE ASSLDSRGER AELYAHIDEG LLGGETSYLG PPLTPEKEEA
LHQATAVANL RAALMSKNSL LSLKADVLGD DGSLLFEYLP KGAHSLSLNE FTVIRKKFKC
PYCSFSAMHQ CILKRHMRSH TGERPYPCEI CGKKFTRREH MKRHTLVHSK DKKYVCKVCS
RVFMSAASVG IKHGSRRHGV CADCAGRGVG TPLDHGGGGE GSPEALFAGE GPYLEDPDDP
RGEAEEELVE DEDEDVAKWK DDVGLAHEDA LLGDDKDDED SPQGPHSPSG EPDKDFAWIS
