Entry sw: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   30-NOV-2016, entry version 150.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; 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-
RT   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
RT   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.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the 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.,
RA   Elsaesser H.-P., Moeroey T., Eilers M.;
RT   "Miz1 is required for early embryonic development during
RT   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
RT   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
RT   Miz-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
RT   transcription factor Miz1-mediated suppression on TNF-alpha-induced
RT   JNK activation and inflammation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:191-196(2012).
CC   -!- FUNCTION: Transcription factor that can function as an activator
CC       or repressor depending on its binding partners, and by targeting
CC       negative regulators of cell cycle progression. Has been shown to
CC       bind to the promoters of adenovirus major late protein and cyclin
CC       D1 and activate transcription. Required for early embryonic
CC       development during gastrulation. Plays a critical role in early
CC       lymphocyte development, where it is essential to prevent apoptosis
CC       in lymphoid precursors, allowing them to survive in response to
CC       IL7 and undergo proper lineage commitment. Represses RB1
CC       transcription; this repression can be blocked by interaction with
CC       ZBTB49 (By similarity). {ECO:0000250|UniProtKB:Q13105,
CC       ECO:0000269|PubMed:14560010, ECO:0000269|PubMed:20190815,
CC       ECO:0000269|PubMed:21258009}.
CC   -!- SUBUNIT: Homooligomerizes (via the BTB/POZ domain),
CC       multimerization is required for DNA binding. Binds to the C-
CC       terminal helix-loop-helix motif of MYC which inhibits ZBTB17
CC       transactivation and growth arrest activities and renders it
CC       insoluble in the nucleus. Also interacts with HCFC1, MAGEA4 and
CC       TMPRSS11A. Interacts (via the C-terminal zinc fingers) with GFI1;
CC       the interaction results in the recruitment of MYC to the
CC       CDKN1A/p21 and CDKN1B promoters and repression of transcription.
CC       Interacts with TRAF2, interfering with the binding of UBC13 to
CC       TRAF2, and inhibiting TRAF2 E3 ligase activity. Interacts with
CC       BCL6; the interaction inhibits ZBTB17 transactivation activity on
CC       target genes involved in cell cycle arrest. Interacts with ZBTB49;
CC       this interaction blocks ZBTB17-mediated repression of RB1 (By
CC       similarity). {ECO:0000250|UniProtKB:Q13105,
CC       ECO:0000269|PubMed:20190815, ECO:0000269|PubMed:22184250}.
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
CC       embryogenesis (6.5 dpc) to organogenesis, predominantly in neural
CC       and epithelial tissues. {ECO:0000269|PubMed:14560010}.
CC   -!- PTM: Undergoes 'Lys-48'-linked polyubiquitination at Lys-388 and
CC       Lys-472 and subsequent proteasomal degradation in a TRAF2-
CC       dependent manner and upon TNFA stimulation.
CC       {ECO:0000269|PubMed:22184250}.
CC   -!- DISRUPTION PHENOTYPE: Mice produce inviable embryos which are
CC       severely retarded in early development and do not undergo normal
CC       gastrulation due to massive apoptosis of ectodermal cells around
CC       day 7.5. {ECO:0000269|PubMed:14560010}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 BTB (POZ) domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00037}.
CC   -!- SIMILARITY: Contains 13 C2H2-type zinc fingers.
CC       {ECO:0000255|PROSITE-ProRule:PRU00042}.
DR   EMBL; U22396; AAA64848.1; -; mRNA.
DR   EMBL; U14556; AAA85493.1; -; mRNA.
DR   EMBL; AL670285; CAM20401.1; -; 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   UniGene; Mm.389590; -.
DR   ProteinModelPortal; Q60821; -.
DR   SMR; Q60821; -.
DR   BioGrid; 204631; 3.
DR   DIP; DIP-48690N; -.
DR   STRING; 10090.ENSMUSP00000006377; -.
DR   iPTMnet; Q60821; -.
DR   PhosphoSitePlus; Q60821; -.
DR   EPD; Q60821; -.
DR   MaxQB; Q60821; -.
DR   PaxDb; Q60821; -.
DR   PRIDE; Q60821; -.
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   eggNOG; KOG1721; Eukaryota.
DR   eggNOG; COG5048; LUCA.
DR   GeneTree; ENSGT00860000133719; -.
DR   HOGENOM; HOG000231298; -.
DR   HOVERGEN; HBG054919; -.
DR   InParanoid; Q60821; -.
DR   KO; K10500; -.
DR   OMA; CTHCQRQ; -.
DR   OrthoDB; EOG091G02KC; -.
DR   TreeFam; TF332047; -.
DR   PRO; PR:Q60821; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   Bgee; ENSMUSG00000006215; -.
DR   CleanEx; MM_ZBTB17; -.
DR   Genevisible; Q60821; MM.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; ISO:MGI.
DR   GO; GO:0007398; P:ectoderm development; IMP:MGI.
DR   GO; GO:0001702; P:gastrulation with mouth forming second; IMP:MGI.
DR   GO; GO:1903955; P:positive regulation of protein targeting to mitochondrion; ISO:MGI.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR   GO; GO:1903146; P:regulation of mitophagy; ISO:MGI.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.160.60; -; 13.
DR   InterPro; IPR000210; BTB/POZ_dom.
DR   InterPro; IPR011333; SKP1/BTB/POZ.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Pfam; PF00651; BTB; 1.
DR   Pfam; PF00096; zf-C2H2; 3.
DR   SMART; SM00225; BTB; 1.
DR   SMART; SM00355; ZnF_C2H2; 13.
DR   SUPFAM; SSF54695; SSF54695; 1.
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   Complete proteome; Developmental protein; DNA-binding;
KW   Isopeptide bond; Metal-binding; Nucleus; Reference proteome; Repeat;
KW   Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    794       Zinc finger and BTB domain-containing
FT                                protein 17.
FT                                /FTId=PRO_0000047731.
FT   DOMAIN        1    104       BTB. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00037}.
FT   ZN_FING     297    319       C2H2-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     325    347       C2H2-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     353    375       C2H2-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     381    403       C2H2-type 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     409    431       C2H2-type 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     437    459       C2H2-type 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     465    487       C2H2-type 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     493    515       C2H2-type 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     519    543       C2H2-type 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     549    571       C2H2-type 10. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     577    599       C2H2-type 11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     605    628       C2H2-type 12. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     708    730       C2H2-type 13. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   REGION      260    299       Interaction with MYC. {ECO:0000250}.
FT   REGION      628    794       Interaction with HCFC1. {ECO:0000250}.
FT   REGION      628    709       Interaction with MYC. {ECO:0000250}.
FT   CROSSLNK    388    388       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000269|PubMed:22184250}.
FT   CROSSLNK    472    472       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000269|PubMed:22184250}.
FT   CONFLICT    151    151       D -> G (in Ref. 1; AAA64848 and 2;
FT                                AAA85493). {ECO:0000305}.
FT   CONFLICT    507    507       A -> G (in Ref. 1; AAA64848).
FT                                {ECO:0000305}.
FT   CONFLICT    573    573       N -> K (in Ref. 2; AAA85493).
FT                                {ECO:0000305}.
FT   CONFLICT    577    577       H -> D (in Ref. 1; AAA64848 and 2;
FT                                AAA85493). {ECO:0000305}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT        14    110       ipfam:BTB [T]
FT   MYHIT       521    543       ismart:ZnF_C2H2 [T]
FT   MYHIT       551    571       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       297    319       ismart:ZnF_C2H2 [T]
FT   MYHIT       325    352       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       493    515       ismart:ZnF_C2H2 [T]
FT   MYHIT       409    436       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       549    576       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       577    604       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       493    520       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       467    487       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       465    492       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       437    464       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       521    548       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       465    487       ismart:ZnF_C2H2 [T]
FT   MYHIT        24    116       ismart:BTB [T]
FT   MYHIT       577    599       ismart:ZnF_C2H2 [T]
FT   MYHIT       411    431       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       605    633       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       381    408       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       607    628       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       297    324       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       383    403       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       355    375       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       353    375       ismart:ZnF_C2H2 [T]
FT   MYHIT       409    431       ismart:ZnF_C2H2 [T]
FT   MYHIT       579    599       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       327    347       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       299    319       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       549    571       ismart:ZnF_C2H2 [T]
FT   MYHIT        24     86       iprf:BTB [T]
FT   MYHIT       353    380       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       381    403       ismart:ZnF_C2H2 [T]
FT   MYHIT       437    459       ismart:ZnF_C2H2 [T]
FT   MYHIT       710    730       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       605    628       ismart:ZnF_C2H2 [T]
FT   MYHIT       325    347       ismart:ZnF_C2H2 [T]
FT   MYHIT       439    459       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       495    515       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       708    730       ismart:ZnF_C2H2 [T]
FT   MYHIT       708    735       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       521    543       ipat:ZINC_FINGER_C2H2_1 [T]
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
//