ZBT18_MOUSE
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 03-AUG-2022, entry version 158.
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; Q9WUK6; -.
DR PRIDE; Q9WUK6; -.
DR ProteomicsDB; 298493; -.
DR Antibodypedia; 34710; 122 antibodies from 25 providers.
DR Ensembl; ENSMUST00000077225; ENSMUSP00000076463; ENSMUSG00000063659.
DR Ensembl; ENSMUST00000195612; ENSMUSP00000141724; ENSMUSG00000063659.
DR GeneID; 30928; -.
DR KEGG; mmu:30928; -.
DR UCSC; uc007dul.2; mouse.
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 PhylomeDB; Q9WUK6; -.
DR BioGRID-ORCS; 30928; 1 hit in 72 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 272 other tissues.
DR ExpressionAtlas; Q9WUK6; baseline and differential.
DR Genevisible; Q9WUK6; MM.
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: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: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:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; 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 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_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
