ZBTB4_MOUSE
ID ZBTB4_MOUSE Reviewed; 982 AA.
AC Q5F293; Q3UHT8; Q69ZH0;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Zinc finger and BTB domain-containing protein 4;
GN Name=Zbtb4; Synonyms=Kiaa1538;
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].
RC TISSUE=Brain;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
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 [3]
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 [4]
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=27446912; DOI=10.3389/fcell.2016.00058;
RA Alonso-Martin S., Rochat A., Mademtzoglou D., Morais J., de Reynies A.,
RA Aurade F., Chang T.H., Zammit P.S., Relaix F.;
RT "Gene expression profiling of muscle stem cells identifies novel regulators
RT of postnatal myogenesis.";
RL Front. Cell Dev. Biol. 4:58-58(2016).
CC -!- FUNCTION: Transcriptional repressor with bimodal DNA-binding
CC specificity. Represses transcription in a methyl-CpG-dependent manner.
CC Binds with a higher affinity to methylated CpG dinucleotides in the
CC consensus sequence 5'-CGCG-3' but can also bind to the non-methylated
CC consensus sequence 5'-CTGCNA-3' also known as the consensus kaiso
CC binding site (KBS). Can also bind specifically to a single methyl-CpG
CC pair and can bind hemimethylated DNA but with a lower affinity compared
CC to methylated DNA. Plays a role in postnatal myogenesis, may be
CC involved in the regulation of satellite cells self-renewal
CC (PubMed:27446912). {ECO:0000250|UniProtKB:Q9P1Z0,
CC ECO:0000269|PubMed:27446912}.
CC -!- SUBUNIT: Interacts with HIPK2. Interacts with CBFA2T3. Interacts with
CC ZBTB38. {ECO:0000250|UniProtKB:Q9P1Z0}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9P1Z0}.
CC Chromosome {ECO:0000250|UniProtKB:Q9P1Z0}. Note=Localizes to
CC chromocenters. {ECO:0000250|UniProtKB:Q9P1Z0}.
CC -!- TISSUE SPECIFICITY: Expressed in adult and aged myogenic satellite
CC cells. {ECO:0000269|PubMed:27446912}.
CC -!- DEVELOPMENTAL STAGE: Not expressed during development, is induced
CC during establishment of satellite cells and acquisition of quiescence.
CC {ECO:0000269|PubMed:27446912}.
CC -!- PTM: Phosphorylated by HIPK2. This phosphorylation reduces stability
CC and triggers ZBTB4 protein degradation in response to DNA damage.
CC {ECO:0000250|UniProtKB:Q9P1Z0}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE27769.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK147212; BAE27769.1; ALT_INIT; mRNA.
DR EMBL; AK173196; BAD32474.1; -; Transcribed_RNA.
DR EMBL; AL603707; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS36197.2; -.
DR RefSeq; NP_083624.2; NM_029348.2.
DR RefSeq; XP_006534452.1; XM_006534389.3.
DR RefSeq; XP_006534453.1; XM_006534390.3.
DR RefSeq; XP_006534454.1; XM_006534391.3.
DR RefSeq; XP_006534455.1; XM_006534392.3.
DR RefSeq; XP_006534456.1; XM_006534393.3.
DR RefSeq; XP_006534457.1; XM_006534394.3.
DR RefSeq; XP_011247595.1; XM_011249293.2.
DR AlphaFoldDB; Q5F293; -.
DR STRING; 10090.ENSMUSP00000104279; -.
DR iPTMnet; Q5F293; -.
DR PhosphoSitePlus; Q5F293; -.
DR EPD; Q5F293; -.
DR MaxQB; Q5F293; -.
DR PaxDb; Q5F293; -.
DR PRIDE; Q5F293; -.
DR ProteomicsDB; 275267; -.
DR Antibodypedia; 24133; 168 antibodies from 23 providers.
DR Ensembl; ENSMUST00000108639; ENSMUSP00000104279; ENSMUSG00000018750.
DR Ensembl; ENSMUST00000108640; ENSMUSP00000104280; ENSMUSG00000018750.
DR GeneID; 75580; -.
DR KEGG; mmu:75580; -.
DR UCSC; uc007jrm.2; mouse.
DR CTD; 57659; -.
DR MGI; MGI:1922830; Zbtb4.
DR VEuPathDB; HostDB:ENSMUSG00000018750; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000161268; -.
DR HOGENOM; CLU_007011_1_0_1; -.
DR InParanoid; Q5F293; -.
DR OMA; THEVLCK; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q5F293; -.
DR TreeFam; TF333100; -.
DR BioGRID-ORCS; 75580; 4 hits in 73 CRISPR screens.
DR PRO; PR:Q5F293; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5F293; protein.
DR Bgee; ENSMUSG00000018750; Expressed in pineal body and 212 other tissues.
DR ExpressionAtlas; Q5F293; baseline and differential.
DR Genevisible; Q5F293; MM.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008327; F:methyl-CpG binding; ISO:MGI.
DR GO; GO:0010428; F:methyl-CpNpG binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; 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; 1.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 6.
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; 6.
PE 2: Evidence at transcript level;
KW Chromosome; Coiled coil; DNA-binding; Isopeptide bond; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..982
FT /note="Zinc finger and BTB domain-containing protein 4"
FT /id="PRO_0000434408"
FT DOMAIN 30..131
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 210..232
FT /note="C2H2-type 1; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 285..307
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 313..335
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 341..364
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 700..722
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 739..761
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 71..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..324
FT /note="Interaction with CBFA2T3"
FT /evidence="ECO:0000250|UniProtKB:Q9P1Z0"
FT REGION 234..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 591..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 715..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 759..839
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 854..880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..450
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..509
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..575
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..605
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..629
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..823
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P1Z0"
FT MOD_RES 769
FT /note="Phosphothreonine; by HIPK2"
FT /evidence="ECO:0000250|UniProtKB:Q9P1Z0"
FT MOD_RES 771
FT /note="Phosphothreonine; by HIPK2"
FT /evidence="ECO:0000250|UniProtKB:Q9P1Z0"
FT MOD_RES 953
FT /note="Phosphothreonine; by HIPK2"
FT /evidence="ECO:0000250|UniProtKB:Q9P1Z0"
FT CROSSLNK 40
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9P1Z0"
FT CROSSLNK 548
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9P1Z0"
FT CROSSLNK 590
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9P1Z0"
FT CONFLICT 588
FT /note="I -> T (in Ref. 2; BAE27769)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 982 AA; 102663 MW; 58FFCAAB7C1A773F CRC64;
MPPPAEVTDP SHAPAVLHQL NEQRLRGLFC DVTLIAGDTK FPAHRSVLAA SSPFFREALL
ASAPLPLPPV TGGSAPSPAT TTAASSSSSS PPPASPHSSS PPRVLELPGV PAAAFSDVLN
FIYSARLALP GGGGDGAAVA EIGALGRRLG ISRLQGLGEG GDTWVPPAPT SMVTSDPTED
GLGAGPRTDG EWVGDKAEAL TPDSQPRRPF PCPRCGKSFI HPKRLQTHEA QCRRGSNTRG
SAGLGPGVSG SGGPAGVDAS ALPQPVGFRD GPEHVVKVVG GHVLYVCAAC ERSYVTLSSL
KRHSNVHSWR RKYPCRYCEK VFALAEYRTK HEVWHTGERR YQCIFCWDTF VTYYNLKTHQ
RAFHGISPGL LASEKTPNGG YKPRLNTLKL YRLLPMRAAK RPYKTYSQGA PEAPLSPSLH
TPAPAAMPAS PQPLPPPAPE PGPPPSVITF AHPAPSVIVH GSSSSGAAGG GPAGTGGSQA
ASVITYTTPP RPPKKREYPP PPPEPTATPT SPASTAVSPA TAAGPATATE EAKGRNLRAG
RTLTYTAKPV GGLSGSGGSP TGTGRGSSQL QAPPPLCQIT VRIGEEAIVK RRISETDLRP
GELSGEEVEE SEEEEEEEEE EDQEEQEESK AGGEDQLWRP YYSYKPKRKA GATAGGASGV
SGLPRGRRPP RWRQKLERRG WEETPSVEGP GGRGRGERRH RCGDCAQAFA TVRKLRKHQE
AHSGGSHTSR TGRRSSTRFT CPHCAKVCKT AAALNRHGQR HAVERPGGTP TPVIAYSKGS
IGTRPTDVKE EAPQEMQVSS SSGEAGSGSA AAAEASESAS LQDPVISGGE EPPVAGGGSY
VYPPVQEFPL ALIGGSREPS AGKGKPGNEG SLGASEGDRM EGMGTAKVTF YPEPYPLVYG
PQLLAAYPYN FSNLAALPVA LNMVLPDEKG GGALPFLPGV FGYAVNPQAA PPTPPPPLPL
PVSPKGIGGM TGVERTQKGD VG
