ZBT17_MOUSE
ID ZBT17_MOUSE Reviewed; 794 AA.
AC Q60821; A2ADB9; Q60699;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Zinc finger and BTB domain-containing protein 17;
DE AltName: Full=LP-1;
DE AltName: Full=Polyomavirus late initiator promoter-binding protein;
DE AltName: Full=Zinc finger protein 100;
DE Short=Zfp-100;
DE AltName: Full=Zinc finger protein 151;
DE AltName: Full=Zinc finger protein Z13;
GN Name=Zbtb17; Synonyms=Zfp100, Znf151;
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 [MRNA].
RA Rapp L., Carmichael G.G.;
RT "cDNA for polyomavirus late initiator promoter binding protein, LP-1.";
RL Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=CBA/J; TISSUE=Kidney;
RX PubMed=7575457; DOI=10.1042/bj3110219;
RA Schulz T.C., Hopwood B., Rathjen P.D., Wells J.R.E.;
RT "An unusual arrangement of 13 zinc fingers in the vertebrate gene Z13.";
RL Biochem. J. 311:219-224(1995).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=14560010; DOI=10.1128/mcb.23.21.7648-7657.2003;
RA Adhikary S., Peukert K., Karsunky H., Beuger V., Lutz W., Elsaesser H.-P.,
RA Moeroey T., Eilers M.;
RT "Miz1 is required for early embryonic development during gastrulation.";
RL Mol. Cell. Biol. 23:7648-7657(2003).
RN [6]
RP INTERACTION WITH GFI1, AND FUNCTION.
RX PubMed=20190815; DOI=10.1038/onc.2010.48;
RA Liu Q., Basu S., Qiu Y., Tang F., Dong F.;
RT "A role of Miz-1 in Gfi-1-mediated transcriptional repression of CDKN1A.";
RL Oncogene 29:2843-2852(2010).
RN [7]
RP FUNCTION IN LYMPHOCYTE DEVELOPMENT.
RX PubMed=21258009; DOI=10.1182/blood-2010-09-310680;
RA Saba I., Kosan C., Vassen L., Moroy T.;
RT "IL-7R-dependent survival and differentiation of early T-lineage
RT progenitors is regulated by the BTB/POZ domain transcription factor Miz-
RT 1.";
RL Blood 117:3370-3381(2011).
RN [8]
RP UBIQUITINATION AT LYS-388 AND LYS-472, AND INTERACTION WITH TRAF2.
RX PubMed=22184250; DOI=10.1073/pnas.1105176108;
RA Liu J., Yan J., Jiang S., Wen J., Chen L., Zhao Y., Lin A.;
RT "Site-specific ubiquitination is required for relieving the transcription
RT factor Miz1-mediated suppression on TNF-alpha-induced JNK activation and
RT inflammation.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:191-196(2012).
CC -!- FUNCTION: Transcription factor that can function as an activator or
CC repressor depending on its binding partners, and by targeting negative
CC regulators of cell cycle progression. Has been shown to bind to the
CC promoters of adenovirus major late protein and cyclin D1 and activate
CC transcription. Required for early embryonic development during
CC gastrulation. Plays a critical role in early lymphocyte development,
CC where it is essential to prevent apoptosis in lymphoid precursors,
CC allowing them to survive in response to IL7 and undergo proper lineage
CC commitment. Represses RB1 transcription; this repression can be blocked
CC by interaction with ZBTB49 (By similarity).
CC {ECO:0000250|UniProtKB:Q13105, ECO:0000269|PubMed:14560010,
CC ECO:0000269|PubMed:20190815, ECO:0000269|PubMed:21258009}.
CC -!- SUBUNIT: Homooligomerizes (via the BTB/POZ domain), multimerization is
CC required for DNA binding. Binds to the C-terminal helix-loop-helix
CC motif of MYC which inhibits ZBTB17 transactivation and growth arrest
CC activities and renders it insoluble in the nucleus. Also interacts with
CC HCFC1, MAGEA4 and TMPRSS11A. Interacts (via the C-terminal zinc
CC fingers) with GFI1; the interaction results in the recruitment of MYC
CC to the CDKN1A/p21 and CDKN1B promoters and repression of transcription.
CC Interacts with TRAF2, interfering with the binding of UBC13 to TRAF2,
CC and inhibiting TRAF2 E3 ligase activity. Interacts with BCL6; the
CC interaction inhibits ZBTB17 transactivation activity on target genes
CC involved in cell cycle arrest. Interacts with ZBTB49; this interaction
CC blocks ZBTB17-mediated repression of RB1 (By similarity).
CC {ECO:0000250|UniProtKB:Q13105, ECO:0000269|PubMed:20190815,
CC ECO:0000269|PubMed:22184250}.
CC -!- INTERACTION:
CC Q60821; Q07120: Gfi1; Xeno; NbExp=3; IntAct=EBI-11598394, EBI-4289236;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Found in all the embryonic and adult tissues
CC examined.
CC -!- DEVELOPMENTAL STAGE: Expressed ubiquitously from early embryogenesis
CC (6.5 dpc) to organogenesis, predominantly in neural and epithelial
CC tissues. {ECO:0000269|PubMed:14560010}.
CC -!- PTM: Undergoes 'Lys-48'-linked polyubiquitination at Lys-388 and Lys-
CC 472 and subsequent proteasomal degradation in a TRAF2-dependent manner
CC and upon TNFA stimulation. {ECO:0000269|PubMed:22184250}.
CC -!- DISRUPTION PHENOTYPE: Mice produce inviable embryos which are severely
CC retarded in early development and do not undergo normal gastrulation
CC due to massive apoptosis of ectodermal cells around day 7.5.
CC {ECO:0000269|PubMed:14560010}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; U22396; AAA64848.1; -; mRNA.
DR EMBL; U14556; AAA85493.1; -; mRNA.
DR EMBL; AL670285; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466615; EDL13378.1; -; Genomic_DNA.
DR CCDS; CCDS18875.1; -.
DR PIR; S59069; S59069.
DR RefSeq; NP_033567.2; NM_009541.2.
DR AlphaFoldDB; Q60821; -.
DR SMR; Q60821; -.
DR BioGRID; 204631; 29.
DR DIP; DIP-48690N; -.
DR IntAct; Q60821; 1.
DR STRING; 10090.ENSMUSP00000006377; -.
DR iPTMnet; Q60821; -.
DR PhosphoSitePlus; Q60821; -.
DR EPD; Q60821; -.
DR MaxQB; Q60821; -.
DR PaxDb; Q60821; -.
DR PRIDE; Q60821; -.
DR ProteomicsDB; 302038; -.
DR Antibodypedia; 904; 151 antibodies from 25 providers.
DR DNASU; 22642; -.
DR Ensembl; ENSMUST00000006377; ENSMUSP00000006377; ENSMUSG00000006215.
DR GeneID; 22642; -.
DR KEGG; mmu:22642; -.
DR UCSC; uc008vol.2; mouse.
DR CTD; 7709; -.
DR MGI; MGI:107410; Zbtb17.
DR VEuPathDB; HostDB:ENSMUSG00000006215; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000159957; -.
DR HOGENOM; CLU_002678_30_1_1; -.
DR InParanoid; Q60821; -.
DR OMA; DKGHKCP; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q60821; -.
DR TreeFam; TF332047; -.
DR BioGRID-ORCS; 22642; 12 hits in 74 CRISPR screens.
DR ChiTaRS; Zbtb17; mouse.
DR PRO; PR:Q60821; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q60821; protein.
DR Bgee; ENSMUSG00000006215; Expressed in saccule of membranous labyrinth and 265 other tissues.
DR Genevisible; Q60821; MM.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0032993; C:protein-DNA complex; ISO:MGI.
DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0001223; F:transcription coactivator binding; ISO:MGI.
DR GO; GO:0007398; P:ectoderm development; IMP:MGI.
DR GO; GO:0070314; P:G1 to G0 transition; ISO:MGI.
DR GO; GO:0001702; P:gastrulation with mouth forming second; IMP:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
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; 10.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 13.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 9.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 13.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 13.
PE 1: Evidence at protein level;
KW Developmental protein; DNA-binding; Isopeptide bond; Metal-binding;
KW Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..794
FT /note="Zinc finger and BTB domain-containing protein 17"
FT /id="PRO_0000047731"
FT DOMAIN 1..104
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 297..319
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 325..347
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 353..375
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 381..403
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 409..431
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 437..459
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 465..487
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 493..515
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 519..543
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 549..571
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 577..599
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 605..628
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 708..730
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 116..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..299
FT /note="Interaction with MYC"
FT /evidence="ECO:0000250"
FT REGION 628..794
FT /note="Interaction with HCFC1"
FT /evidence="ECO:0000250"
FT REGION 628..709
FT /note="Interaction with MYC"
FT /evidence="ECO:0000250"
FT REGION 769..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 388
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:22184250"
FT CROSSLNK 472
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:22184250"
FT CONFLICT 151
FT /note="D -> G (in Ref. 1; AAA64848 and 2; AAA85493)"
FT /evidence="ECO:0000305"
FT CONFLICT 507
FT /note="A -> G (in Ref. 1; AAA64848)"
FT /evidence="ECO:0000305"
FT CONFLICT 573
FT /note="N -> K (in Ref. 2; AAA85493)"
FT /evidence="ECO:0000305"
FT CONFLICT 577
FT /note="H -> D (in Ref. 1; AAA64848 and 2; AAA85493)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 794 AA; 86758 MW; 54CF6CF0D2C60303 CRC64;
MDFPQHSQRV LEQLNQQRQL GLLCDCTFVV DGVDFKAHKA VLAACSEYFK MLFVDQKDVV
HLDISNAAGL GQVLEFMYTA KLSLSPENVD DVLAVASFLQ MQDIVTACHT LKSLAEPSST
TGESADASAV EGGDKRAKDE KAAATMLSRL DQARGSSSTG PGRELKEERG GQAESASSGA
EQTEKADAPR EPPPVELKPD PTSSMAAAEA EALSESSEQE MEVEPASKGE DGQEEEGAGP
ATVKEEGMHL DNGEPPEENE ESAGTDSGQE LGMEGQNLRS GTYGDRTESK AYGSIIHKCE
DCGKEFTHTG NFKRHIRIHT GEKPFSCREC SKAFSDPAAC KAHEKTHSPL KPYGCEECGK
SYRLISLLNL HKKRHSGEAR YRCGDCGKLF TTSGNLKRHQ LVHSGQKPYQ CDYCGRSFSD
PTSKMRHLET HDTDKEHKCP HCDKKFNQVG NLKAHLKIHI ADGPLKCREC GKQFTTSGNL
KRHLRIHSGE KPYVCTHCQR QFADPGALQR HVRIHTGEKP CQCVICGKAF TQASSLIAHV
RQHTGEKPYV CERCGKRFVQ SSQLANHIRH HDNIRPHKCS VCSKAFVNVG DLSKHIIIHT
GEKPYLCDKC GRGFNRVDNL RSHVKTVHQG KAGIKILEPE EGGEVSVVTV DDMVTLATEA
LAATAVTQLT VVPVGAAVTA DETEVLKAEI SKAVKQVQEE DPNTHILYAC DSCGDKFLDA
NSLAQHVRIH TAQALVMFQT DADFYQQYGP GSTWPAGQML QAGELVFRPR DGTEGQPTLA
ESPPTAPDCL PPAE
