ZBT14_MOUSE
ID ZBT14_MOUSE Reviewed; 449 AA.
AC Q08376;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Zinc finger and BTB domain-containing protein 14;
DE AltName: Full=Zinc finger protein 161;
DE Short=Zfp-161;
DE AltName: Full=Zinc finger protein 5;
DE Short=ZF5;
GN Name=Zbtb14; Synonyms=Zfp-5, Zfp161, Zfp5;
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], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Plasmacytoma;
RX PubMed=8367294; DOI=10.1093/nar/21.16.3767;
RA Numoto M., Niwa O., Kaplan J., Wong K.-K., Merrell K., Kamiya K.,
RA Yanagihara K., Calame K.;
RT "Transcriptional repressor ZF5 identifies a new conserved domain in zinc
RT finger proteins.";
RL Nucleic Acids Res. 21:3767-3775(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain, and Ovary;
RX PubMed=9244432; DOI=10.1006/geno.1997.4784;
RA Sobek-Klocke I., Disque-Kochem C., Ronsiek M., Klocke R., Jockusch H.,
RA Breuning A., Ponstingl H., Rojas K., Overhauser J., Eichenlaub-Ritter U.;
RT "The human gene ZFP161 on 18p11.21-pter encodes a putative c-myc repressor
RT and is homologous to murine Zfp161 (Chr 17) and Zfp161-rs1 (X Chr).";
RL Genomics 43:156-164(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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).
CC -!- FUNCTION: Transcriptional activator of the dopamine transporter (DAT),
CC binding it's promoter at the consensus sequence 5'-CCTGCACAGTTCACGGA-
CC 3'. Binds to 5'-d(GCC)(n)-3' trinucleotide repeats in promoter regions
CC and acts as a repressor of the FMR1 gene (By similarity).
CC Transcriptional repressor of MYC and thymidine kinase promoters.
CC {ECO:0000250, ECO:0000269|PubMed:8367294}.
CC -!- SUBUNIT: Interacts with ZBTB21. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:8367294}.
CC -!- DOMAIN: The BTB/POZ domain seems to direct the protein to discrete
CC regions in the nucleus. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; L15325; AAA02940.1; -; mRNA.
DR EMBL; BC052017; AAH52017.1; -; mRNA.
DR CCDS; CCDS37682.1; -.
DR PIR; S41647; S41647.
DR RefSeq; NP_033573.1; NM_009547.2.
DR RefSeq; XP_006524275.1; XM_006524212.2.
DR RefSeq; XP_011244726.1; XM_011246424.2.
DR AlphaFoldDB; Q08376; -.
DR SMR; Q08376; -.
DR BioGRID; 204642; 25.
DR STRING; 10090.ENSMUSP00000108296; -.
DR iPTMnet; Q08376; -.
DR PhosphoSitePlus; Q08376; -.
DR EPD; Q08376; -.
DR jPOST; Q08376; -.
DR PaxDb; Q08376; -.
DR PeptideAtlas; Q08376; -.
DR PRIDE; Q08376; -.
DR ProteomicsDB; 275121; -.
DR Antibodypedia; 21919; 64 antibodies from 18 providers.
DR DNASU; 22666; -.
DR Ensembl; ENSMUST00000062369; ENSMUSP00000054897; ENSMUSG00000049672.
DR Ensembl; ENSMUST00000112674; ENSMUSP00000108294; ENSMUSG00000049672.
DR Ensembl; ENSMUST00000112676; ENSMUSP00000108296; ENSMUSG00000049672.
DR GeneID; 22666; -.
DR KEGG; mmu:22666; -.
DR UCSC; uc008dkt.1; mouse.
DR CTD; 7541; -.
DR MGI; MGI:1195345; Zbtb14.
DR VEuPathDB; HostDB:ENSMUSG00000049672; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000158052; -.
DR HOGENOM; CLU_697455_0_0_1; -.
DR InParanoid; Q08376; -.
DR OMA; KMIEHMG; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q08376; -.
DR TreeFam; TF333100; -.
DR BioGRID-ORCS; 22666; 8 hits in 73 CRISPR screens.
DR ChiTaRS; Zbtb14; mouse.
DR PRO; PR:Q08376; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q08376; protein.
DR Bgee; ENSMUSG00000049672; Expressed in floor plate of midbrain and 253 other tissues.
DR ExpressionAtlas; Q08376; baseline and differential.
DR Genevisible; Q08376; MM.
DR GO; GO:0016235; C:aggresome; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
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; IDA:NTNU_SB.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0003279; P:cardiac septum development; IMP:MGI.
DR GO; GO:0060976; P:coronary vasculature development; IMP:MGI.
DR GO; GO:0003170; P:heart valve development; IMP:MGI.
DR GO; GO:0001822; P:kidney development; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
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; 4.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE 2: Evidence at transcript level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Reference proteome;
KW Repeat; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..449
FT /note="Zinc finger and BTB domain-containing protein 14"
FT /id="PRO_0000047318"
FT DOMAIN 36..102
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 277..304
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 305..332
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 333..360
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 361..388
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 389..417
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 156..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 50..66
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 158..175
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 46
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O43829"
FT CROSSLNK 203
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O43829"
FT CROSSLNK 249
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O43829"
SQ SEQUENCE 449 AA; 50899 MW; 288E76CB689948D3 CRC64;
MEFFISMSET IKYNDDDHKT LFLKTLNEQR LEGEFCDIAI VVEDVKFRAH RCVLAACSTY
FKKLFKKLEV DSSSVIEIDF LRSDIFEEVL NYMYTAKISV KKEDVNLMMS SGQILGIRFL
DKLCSQKRDV SSPDESNGQS KSKYCLKLNR PIGDAADAQD DDVEEIGDQD DSPSDDTVEG
TPPSQEDGKS PTTTLRVQEA ILKELGSEEV RKVNCYGQEV ESMETPESKD LGSQTPQALT
FNDGMSEVKD EQTPGWTTAA SDMKFEYLLY GHHREQIACQ ACGKTFSDEG RLRKHEKLHT
ADRPFVCEMC TKGFTTQAHL KEHLKIHTGY KPYSCEVCGK SFIRAPDLKK HERVHSNERP
FACHMCDKAF KHKSHLKDHE RRHRGEKPFV CGSCTKAFAK ASDLKRHENN MHSERKQVTP
SAIQSETEQL QAAAMAAEAE QQLETIACS
