ZBT18_BOVIN
ID ZBT18_BOVIN Reviewed; 522 AA.
AC A0JN76;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Zinc finger and BTB domain-containing protein 18;
DE AltName: Full=Zinc finger protein 238;
GN Name=ZBTB18; Synonyms=ZNF238;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal cerebellum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transcriptional repressor that plays a role in various
CC developmental processes such as myogenesis and brain development.
CC Specifically binds the consensus DNA sequence 5'-[AC]ACATCTG[GT][AC]-3'
CC which contains the E box core, and acts by recruiting chromatin
CC remodeling multiprotein complexes. Plays a key role in myogenesis by
CC directly repressing the expression of ID2 and ID3, 2 inhibitors of
CC skeletal myogenesis. Also involved in controlling cell division of
CC progenitor cells and regulating the survival of postmitotic cortical
CC neurons. May also play a role in the organization of chromosomes in the
CC nucleus (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with DNMT3A. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Associates with
CC condensed chromatin. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. ZBTB18 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI26551.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC126550; AAI26551.1; ALT_INIT; mRNA.
DR RefSeq; NP_001071484.1; NM_001078016.1.
DR AlphaFoldDB; A0JN76; -.
DR SMR; A0JN76; -.
DR STRING; 9913.ENSBTAP00000000497; -.
DR PaxDb; A0JN76; -.
DR PRIDE; A0JN76; -.
DR GeneID; 538793; -.
DR KEGG; bta:538793; -.
DR CTD; 10472; -.
DR eggNOG; KOG1721; Eukaryota.
DR HOGENOM; CLU_034521_0_0_1; -.
DR InParanoid; A0JN76; -.
DR OrthoDB; 1318335at2759; -.
DR TreeFam; TF337437; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
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 GO; GO:0007519; P:skeletal muscle tissue development; ISS:UniProtKB.
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; 3.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 2: Evidence at transcript level;
KW Developmental protein; 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..522
FT /note="Zinc finger and BTB domain-containing protein 18"
FT /id="PRO_0000391924"
FT DOMAIN 24..91
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 370..392
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 410..432
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 438..460
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 466..489
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 121..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 310..427
FT /note="Interaction with DNMT3A"
FT /evidence="ECO:0000250"
FT COMPBIAS 121..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JKY3"
FT MOD_RES 516
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99592"
FT MOD_RES 517
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99592"
FT CROSSLNK 273
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q99592"
SQ SEQUENCE 522 AA; 58356 MW; 1483EE21ACEAE14C CRC64;
MEFPDHSRHL LQCLSEQRHQ GFLCDCTVLV GDAQFRAHRA VLASCSMYFH LFYKDQLDKR
DIVHLNSDIV TAPAFALLLE FMYEGKLQFK DLPIEDVLAA ASYLHMYDIV KVCKKKLKEK
ATTEADSTKK EEDASSCSDK VESLSDGSSH MAGDLPSDED EGEDEKLNIL PSKRDLAAEP
GNMWMRLPSD SAGIPQAGGE AEPHATAAGK TVASPCSSTE SLSQRSVTSV RDSADVDCVL
DLSVKSSLSG VENLNSSYFS SQDVLRSNLV QVKVEKEASC DESDVGTNDY DMEHSTVKES
VSTNNRVQYE PAHLAPLRED SVLRELERED KASDDEMMTP ESERVQVEGG MESSLLPYVS
NILSPAGQIF MCPLCNKVFP SPHILQIHLS THFREQDGLR SKPAADVNVP TCSLCGKTFS
CMYTLKRHER THSGEKPYTC TQCGKSFQYS HNLSRHAVVH TREKPHACKW CERRFTQSGD
LYRHIRKFHC ELVNSLSVKS EALSLPAVRD WTLEDSSQEL WK
