ZBT18_RAT
ID ZBT18_RAT Reviewed; 522 AA.
AC Q9JKY3;
DT 21-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 131.
DE RecName: Full=Zinc finger and BTB domain-containing protein 18;
DE AltName: Full=58 kDa repressor protein;
DE Short=rRP58;
DE AltName: Full=Transcriptional repressor RP58;
DE AltName: Full=Zinc finger protein 238;
GN Name=Zbtb18; Synonyms=Rp58, Zfp238, Znf238;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=12040400;
RA Kang J.S., Yang Y.C., Liu H.L., Li Y.H., Du Y.C., Li R.X.;
RT "Cloning and distribution of rRP58, a novel neuronal gene.";
RL Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 33:563-568(2001).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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}.
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DR EMBL; AF221838; AAF34655.1; -; mRNA.
DR RefSeq; NP_073169.1; NM_022678.1.
DR AlphaFoldDB; Q9JKY3; -.
DR SMR; Q9JKY3; -.
DR STRING; 10116.ENSRNOP00000005849; -.
DR iPTMnet; Q9JKY3; -.
DR PhosphoSitePlus; Q9JKY3; -.
DR PaxDb; Q9JKY3; -.
DR GeneID; 64619; -.
DR KEGG; rno:64619; -.
DR UCSC; RGD:621548; rat.
DR CTD; 10472; -.
DR RGD; 621548; Zbtb18.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; Q9JKY3; -.
DR PhylomeDB; Q9JKY3; -.
DR PRO; PR:Q9JKY3; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0000792; C:heterochromatin; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
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:RGD.
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:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0021549; P:cerebellum development; ISO:RGD.
DR GO; GO:0021987; P:cerebral cortex development; ISO:RGD.
DR GO; GO:0021766; P:hippocampus development; ISO:RGD.
DR GO; GO:0048872; P:homeostasis of number of cells; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
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:0048666; P:neuron development; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0051302; P:regulation of cell division; ISO:RGD.
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 1: Evidence at protein 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_0000047479"
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..166
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:0007744|PubMed:22673903"
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; 58310 MW; 855504D57A6DF980 CRC64;
MEFPDHSRHL LQCLSEQRHQ GFLCDCTVLV GDAQFRAHRA VLASCSMYFH LFYKDQLDKR
DIVHLNSDIV TAPAFALLLE FMYEGKLQFK DLPIEDVLAA ASYLHMYDIV KVCKKKLKEK
ATTEADSTKK EEDASSCSDK VESLSDGSSH MAGDLPSDED EGEDDKLNIL PSKRDLAAEP
GNMWMRLPSD AAGIPQAGGE AEPHATAAGK TVASPCSSTE SLSQRSVTSV RDSADVDCVL
DLSVKSSLSG VENLNSSYFS SQDVLRGNLV QVKVEKEASC DESDVGTNDY DMEHSTVKES
VSANNRVQYE PAHLAPLRED SVLRELDRED KASDDEMMTP ESERVQVEGG MESSLLPYVS
NILSPAGQIF MCPLCNKVFP SPHILQIHLS THFREQDGIR SKPAADVNVP TCSLCGKTFS
CMYTLKRHER THSGEKPYTC TQCGKSFQYS HNLSRHAVVH TREKPHACKW CERRFTQSGD
LYRHIRKFHC ELVNSLSVKS EALSLPTVRD WTLEDSSQEL WR
