ID   ZBT18_MOUSE             Reviewed;         522 AA.
AC   Q9WUK6; Q3UHU9; Q7TMA6; Q80YQ4;
DT   21-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   24-JAN-2024, entry version 166.
DE   RecName: Full=Zinc finger and BTB domain-containing protein 18;
DE   AltName: Full=58 kDa repressor protein;
DE   AltName: Full=Transcriptional repressor RP58;
DE   AltName: Full=Zinc finger protein 238;
DE            Short=Zfp-238;
GN   Name=Zbtb18; Synonyms=Rp58, Zfp238, Znf238;
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].
RC   TISSUE=Liver, and Thymus;
RX   PubMed=10721697; DOI=10.1016/s0378-1119(99)00477-1;
RA   Meng G., Inazawa J., Ishida R., Tokura K., Nakahara K., Aoki K., Kasai M.;
RT   "Structural analysis of the gene encoding RP58, a sequence-specific
RT   transrepressor associated with heterochromatin.";
RL   Gene 242:59-64(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
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).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=17447250; DOI=10.1002/cne.21350;
RA   Ohtaka-Maruyama C., Miwa A., Kawano H., Kasai M., Okado H.;
RT   "Spatial and temporal expression of RP58, a novel zinc finger
RT   transcriptional repressor, in mouse brain.";
RL   J. Comp. Neurol. 502:1098-1108(2007).
RN   [5]
RP   FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX   PubMed=19409883; DOI=10.1016/j.ydbio.2009.04.030;
RA   Okado H., Ohtaka-Maruyama C., Sugitani Y., Fukuda Y., Ishida R., Hirai S.,
RA   Miwa A., Takahashi A., Aoki K., Mochida K., Suzuki O., Honda T.,
RA   Nakajima K., Ogawa M., Terashima T., Matsuda J., Kawano H., Kasai M.;
RT   "The transcriptional repressor RP58 is crucial for cell-division patterning
RT   and neuronal survival in the developing cortex.";
RL   Dev. Biol. 331:140-151(2009).
RN   [6]
RP   FUNCTION.
RX   PubMed=20059953; DOI=10.1016/j.devcel.2009.10.011;
RA   Yokoyama S., Ito Y., Ueno-Kudoh H., Shimizu H., Uchibe K., Albini S.,
RA   Mitsuoka K., Miyaki S., Kiso M., Nagai A., Hikata T., Osada T., Fukuda N.,
RA   Yamashita S., Harada D., Mezzano V., Kasai M., Puri P.L., Hayashizaki Y.,
RA   Okado H., Hashimoto M., Asahara H.;
RT   "A systems approach reveals that the myogenesis genome network is regulated
RT   by the transcriptional repressor RP58.";
RL   Dev. Cell 17:836-848(2009).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Lung;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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. {ECO:0000269|PubMed:19409883, ECO:0000269|PubMed:20059953}.
CC   -!- SUBUNIT: Interacts with DNMT3A. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Note=Associates with condensed
CC       chromatin.
CC   -!- DEVELOPMENTAL STAGE: In the developing brain, expression is detected at
CC       embryonic day (E) 10 in the neuroepithelium, and subsequently in the
CC       ventricular zones of the cerebral cortex in the 12 dpc embryo. Strong
CC       expression is observed in the preplate in the cerebral cortex from this
CC       stage onward. High levels of expression continue to be detected in the
CC       cortical plate and subventricular zone of the neocortex, hippocampus,
CC       and parts of the amygdala, but not in the thalamus or striatum. In the
CC       developing cerebral cortex, it is expressed both in postmitotic
CC       glutamatergic projection neurons and in their progenitor cells, but not
CC       in GABAergic interneurons. Also expressed in the adult neocortex,
CC       hippocampus, parts of the amygdala and granule cells in the cerebellum.
CC       {ECO:0000269|PubMed:19409883}.
CC   -!- DISRUPTION PHENOTYPE: Death shortly after birth. Brain of mutant mice
CC       display dysplasia of the neocortex and of the hippocampus, reduction of
CC       the number of mature cortical neurons and defects of laminar
CC       organization. In the cortex, an impaired cell-division patterning
CC       during the late embryonic stage and an enhancement of apoptosis of the
CC       postmitotic neurons are observed. {ECO:0000269|PubMed:19409883}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. ZBTB18 subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH50909.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF140224; AAD34547.1; -; mRNA.
DR   EMBL; AK147200; BAE27758.1; -; mRNA.
DR   EMBL; BC050909; AAH50909.1; ALT_INIT; mRNA.
DR   EMBL; BC054529; AAH54529.1; -; mRNA.
DR   EMBL; BC054742; AAH54742.1; -; mRNA.
DR   CCDS; CCDS15553.1; -.
DR   RefSeq; NP_001012330.1; NM_001012330.1.
DR   RefSeq; NP_038943.3; NM_013915.3.
DR   RefSeq; XP_006496956.1; XM_006496893.1.
DR   RefSeq; XP_006496957.1; XM_006496894.1.
DR   RefSeq; XP_006496958.1; XM_006496895.1.
DR   RefSeq; XP_006496959.1; XM_006496896.3.
DR   AlphaFoldDB; Q9WUK6; -.
DR   SMR; Q9WUK6; -.
DR   BioGRID; 206006; 2.
DR   STRING; 10090.ENSMUSP00000091831; -.
DR   iPTMnet; Q9WUK6; -.
DR   PhosphoSitePlus; Q9WUK6; -.
DR   MaxQB; Q9WUK6; -.
DR   PaxDb; 10090-ENSMUSP00000091831; -.
DR   ProteomicsDB; 298493; -.
DR   Antibodypedia; 34710; 144 antibodies from 25 providers.
DR   Ensembl; ENSMUST00000077225.8; ENSMUSP00000076463.7; ENSMUSG00000063659.12.
DR   Ensembl; ENSMUST00000195612.2; ENSMUSP00000141724.2; ENSMUSG00000063659.12.
DR   GeneID; 30928; -.
DR   KEGG; mmu:30928; -.
DR   UCSC; uc007dul.2; mouse.
DR   AGR; MGI:1353609; -.
DR   CTD; 10472; -.
DR   MGI; MGI:1353609; Zbtb18.
DR   VEuPathDB; HostDB:ENSMUSG00000063659; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000155092; -.
DR   HOGENOM; CLU_034521_0_0_1; -.
DR   InParanoid; Q9WUK6; -.
DR   OrthoDB; 783166at2759; -.
DR   PhylomeDB; Q9WUK6; -.
DR   BioGRID-ORCS; 30928; 1 hit in 77 CRISPR screens.
DR   ChiTaRS; Zbtb18; mouse.
DR   PRO; PR:Q9WUK6; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q9WUK6; Protein.
DR   Bgee; ENSMUSG00000063659; Expressed in cerebellum lobe and 275 other cell types or tissues.
DR   ExpressionAtlas; Q9WUK6; baseline and differential.
DR   GO; GO:0000792; C:heterochromatin; ISO:MGI.
DR   GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
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:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0021549; P:cerebellum development; IMP:MGI.
DR   GO; GO:0021987; P:cerebral cortex development; IMP:MGI.
DR   GO; GO:0021766; P:hippocampus development; IMP:MGI.
DR   GO; GO:0048872; P:homeostasis of number of cells; IMP:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR   GO; GO:0048666; P:neuron development; IMP:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0051302; P:regulation of cell division; IMP:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0007519; P:skeletal muscle tissue development; IMP:UniProtKB.
DR   CDD; cd18324; BTB_POZ_ZBTB18_RP58; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 3.
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   PANTHER; PTHR24394:SF18; ZINC FINGER AND BTB DOMAIN-CONTAINING PROTEIN 18; 1.
DR   PANTHER; PTHR24394; ZINC FINGER PROTEIN; 1.
DR   Pfam; PF00651; BTB; 1.
DR   Pfam; PF00096; zf-C2H2; 3.
DR   Pfam; PF13894; zf-C2H2_4; 1.
DR   SMART; SM00225; BTB; 1.
DR   SMART; SM00355; ZnF_C2H2; 4.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 3.
DR   SUPFAM; SSF54695; POZ domain; 1.
DR   PROSITE; PS50097; BTB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
DR   Genevisible; Q9WUK6; MM.
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_0000047478"
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: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"
FT   CONFLICT        42
FT                   /note="L -> V (in Ref. 3; AAH54742/AAH54529)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   522 AA;  58385 MW;  41E169E690D8B849 CRC64;
     MEFPDHSRHL LQCLSEQRHQ GFLCDCTVLV GDAQFRAHRA VLASCSMYFH LFYKDQLDKR
     DIVHLNSDIV TAPAFALLLE FMYEGKLQFK DLPIEDVLAA ASYLHMYDIV KVCKKKLKEK
     ATTEADSTKK EEDASSCSDK VESLSDGSSH MAGDLPSDED EGEDDKLNIL PSKRDLAAEP
     GNMWMRLPSD SAGIPQAGGE AEPHATAAGK TVASPCSSTE SLSQRSVTSV RDSADVDCVL
     DLSVKSSLSG VENLNSSYFS SQDVLRSNLV QVKVEKEASC DESDVGTNDY DMEHSTVKES
     VSTNNRVQYE PAHLAPLRED SVLRELDRED KASDDEMMTP ESERVQVEGG MENSLLPYVS
     NILSPAGQIF MCPLCNKVFP SPHILQIHLS THFREQDGIR SKPAADVNVP TCSLCGKTFS
     CMYTLKRHER THSGEKPYTC TQCGKSFQYS HNLSRHAVVH TREKPHACKW CERRFTQSGD
     LYRHIRKFHC ELVNSLSVKS EALSLPTVRD WTLEDSSQEL WK
//