ZBT24_MOUSE
ID ZBT24_MOUSE Reviewed; 710 AA.
AC Q80X44; Q3UIB7; Q7TPC4; Q8CJC9;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Zinc finger and BTB domain-containing protein 24;
DE AltName: Full=Bone morphogenetic protein-induced factor 1;
DE AltName: Full=Brain-specific protein 1;
DE AltName: Full=Zinc finger protein 450;
GN Name=Zbtb24; Synonyms=Bif1, Bsg1, Znf450;
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] (ISOFORMS 1 AND 3), TISSUE SPECIFICITY, AND
RP INDUCTION.
RX PubMed=15526281; DOI=10.1002/jcb.20299;
RA Edgar A.J., Dover S.L., Lodrick M.N., McKay I.J., Hughes F.J., Turner W.;
RT "Bone morphogenetic protein-2 induces expression of murine zinc finger
RT transcription factor ZNF450.";
RL J. Cell. Biochem. 94:202-215(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
RA Chen W., Ci H., Wu T., Liang Y., Shimizu K., Li Y.-P.;
RT "Cloning and characterization of a novel mouse gene BSG1 cDNA specifically
RT expressed in brain and hippocampus.";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Amnion, and Oviduct;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C3H/He, and C57BL/6J; TISSUE=Brain, and Osteoblast;
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 [5]
RP PROTEIN SEQUENCE OF 441-453 AND 506-515, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
CC -!- FUNCTION: May be involved in BMP2-induced transcription.
CC -!- SUBUNIT: Interacts with MN1. {ECO:0000250|UniProtKB:O43167}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q80X44-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80X44-2; Sequence=VSP_016225;
CC Name=3;
CC IsoId=Q80X44-3; Sequence=VSP_016223, VSP_016224;
CC -!- TISSUE SPECIFICITY: Widely expressed. Highest level in liver, testis
CC and kidney. {ECO:0000269|PubMed:15526281}.
CC -!- INDUCTION: By BMP2 in fibroblast, myoblast and preosteoblast cell
CC lines. {ECO:0000269|PubMed:15526281}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF263010; AAK91811.2; -; mRNA.
DR EMBL; AY210402; AAO42998.1; -; mRNA.
DR EMBL; AY210403; AAO42999.1; -; Genomic_DNA.
DR EMBL; AK054097; BAE20695.1; -; mRNA.
DR EMBL; AK146986; BAE27589.1; -; mRNA.
DR EMBL; BC050933; AAH50933.1; -; mRNA.
DR EMBL; BC055367; AAH55367.1; -; mRNA.
DR CCDS; CCDS23804.1; -. [Q80X44-1]
DR CCDS; CCDS87996.1; -. [Q80X44-2]
DR CCDS; CCDS87997.1; -. [Q80X44-3]
DR RefSeq; NP_001264158.1; NM_001277229.1. [Q80X44-2]
DR RefSeq; NP_001264159.1; NM_001277230.1. [Q80X44-3]
DR RefSeq; NP_700447.2; NM_153398.3. [Q80X44-1]
DR PDB; 6ML2; X-ray; 1.87 A; A=375-519.
DR PDB; 6ML3; X-ray; 1.68 A; A=375-519.
DR PDB; 6ML4; X-ray; 1.48 A; A=375-519.
DR PDB; 6ML5; X-ray; 1.65 A; A=375-519.
DR PDB; 6ML6; X-ray; 1.54 A; A=375-519.
DR PDB; 6ML7; X-ray; 1.75 A; A=375-519.
DR PDBsum; 6ML2; -.
DR PDBsum; 6ML3; -.
DR PDBsum; 6ML4; -.
DR PDBsum; 6ML5; -.
DR PDBsum; 6ML6; -.
DR PDBsum; 6ML7; -.
DR AlphaFoldDB; Q80X44; -.
DR SMR; Q80X44; -.
DR BioGRID; 234478; 2.
DR IntAct; Q80X44; 2.
DR MINT; Q80X44; -.
DR STRING; 10090.ENSMUSP00000079592; -.
DR iPTMnet; Q80X44; -.
DR PhosphoSitePlus; Q80X44; -.
DR EPD; Q80X44; -.
DR MaxQB; Q80X44; -.
DR PaxDb; Q80X44; -.
DR PRIDE; Q80X44; -.
DR ProteomicsDB; 275124; -. [Q80X44-1]
DR ProteomicsDB; 275125; -. [Q80X44-2]
DR ProteomicsDB; 275126; -. [Q80X44-3]
DR Antibodypedia; 56124; 121 antibodies from 25 providers.
DR DNASU; 268294; -.
DR Ensembl; ENSMUST00000080771; ENSMUSP00000079592; ENSMUSG00000019826. [Q80X44-1]
DR Ensembl; ENSMUST00000213797; ENSMUSP00000148861; ENSMUSG00000019826. [Q80X44-2]
DR Ensembl; ENSMUST00000216656; ENSMUSP00000150197; ENSMUSG00000019826. [Q80X44-3]
DR GeneID; 268294; -.
DR KEGG; mmu:268294; -.
DR UCSC; uc007exl.2; mouse. [Q80X44-3]
DR UCSC; uc007exm.2; mouse. [Q80X44-1]
DR UCSC; uc011xdb.2; mouse. [Q80X44-2]
DR CTD; 9841; -.
DR MGI; MGI:3039618; Zbtb24.
DR VEuPathDB; HostDB:ENSMUSG00000019826; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000159373; -.
DR HOGENOM; CLU_024445_0_0_1; -.
DR InParanoid; Q80X44; -.
DR OMA; QAEQMHV; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q80X44; -.
DR TreeFam; TF332049; -.
DR BioGRID-ORCS; 268294; 6 hits in 70 CRISPR screens.
DR ChiTaRS; Zbtb24; mouse.
DR PRO; PR:Q80X44; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q80X44; protein.
DR Bgee; ENSMUSG00000019826; Expressed in granulocyte and 223 other tissues.
DR Genevisible; Q80X44; MM.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; NAS:UniProtKB.
DR GO; GO:0001227; F:DNA-binding transcription repressor 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:0002244; P:hematopoietic progenitor cell differentiation; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS: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; 6.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 8.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 4.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 8.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Direct protein sequencing; DNA-binding;
KW Metal-binding; Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..710
FT /note="Zinc finger and BTB domain-containing protein 24"
FT /id="PRO_0000047735"
FT DOMAIN 37..103
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT DNA_BIND 159..171
FT /note="A.T hook"
FT ZN_FING 293..315
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 321..343
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 349..371
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 377..399
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 405..427
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 433..455
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 461..483
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 489..511
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 134..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 651..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..254
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 318..354
FT /note="ERPFKCNECGKGFAQKHSLQVHTRMHTGERPYTCTVC -> NFDFQTWCDWL
FT GSLELWLGRLCCFYMVDMAIKPSCCV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15526281"
FT /id="VSP_016223"
FT VAR_SEQ 355..710
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15526281"
FT /id="VSP_016224"
FT VAR_SEQ 402..454
FT /note="HSLPECSHCHRKFMDVSQLKKHLRTHTGEKPFTCEICGKSFTAKSSLQTHIR
FT I -> TIPIRPLTTRMQPLPPKVYGRVPAEEAPADT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016225"
FT TURN 380..382
FT /evidence="ECO:0007829|PDB:6ML4"
FT STRAND 385..388
FT /evidence="ECO:0007829|PDB:6ML4"
FT HELIX 389..395
FT /evidence="ECO:0007829|PDB:6ML4"
FT HELIX 397..400
FT /evidence="ECO:0007829|PDB:6ML4"
FT TURN 408..410
FT /evidence="ECO:0007829|PDB:6ML4"
FT HELIX 417..428
FT /evidence="ECO:0007829|PDB:6ML4"
FT TURN 436..438
FT /evidence="ECO:0007829|PDB:6ML4"
FT STRAND 441..444
FT /evidence="ECO:0007829|PDB:6ML4"
FT HELIX 445..455
FT /evidence="ECO:0007829|PDB:6ML4"
FT TURN 464..466
FT /evidence="ECO:0007829|PDB:6ML4"
FT STRAND 469..472
FT /evidence="ECO:0007829|PDB:6ML4"
FT HELIX 473..480
FT /evidence="ECO:0007829|PDB:6ML4"
FT HELIX 481..484
FT /evidence="ECO:0007829|PDB:6ML4"
FT TURN 492..494
FT /evidence="ECO:0007829|PDB:6ML4"
FT STRAND 497..499
FT /evidence="ECO:0007829|PDB:6ML4"
FT HELIX 501..514
FT /evidence="ECO:0007829|PDB:6ML4"
SQ SEQUENCE 710 AA; 78751 MW; BB0533A274AFFF2D CRC64;
MADTTPEPCG QLMVHSDTHS DTVLASLEDQ RKKGFLCDIT LIVENVHFRA HKALLAASSE
YFSMMFAEEG EIGQSIYMLE GMVADTFGIL LEFIYTGYLH ASEKTTEQIL ATAQFLKVYD
LVKAYADFQD NHSAPKPPAL NCTGTPVVVI SNKKNDPLKR KRGRPRKANG LQEGRSELAA
EGELQLRVNN SVQNRQNFVF KEEDSVKLSE QTPEDKESEP AGEPGSVEEV PAEKDENFDP
KAGDGQESQS RCSRRRIRRS VKLKDYKLLG DEDDQSTAKR LCGRKKRSSG PEARCKDCDR
VFKYSHFLAI HQRRHTGERP FKCNECGKGF AQKHSLQVHT RMHTGERPYT CTVCGKALTT
KHSLLEHMSL HSGQKSFTCD QCGKYFSQKR QLKSHYRVHT GHSLPECSHC HRKFMDVSQL
KKHLRTHTGE KPFTCEICGK SFTAKSSLQT HIRIHRGEKP YSCSICGKCF SDSSAKRRHC
ILHTGKKPFS CPECGLQFAR LDNLKAHLKI HSKEKHTADS SSVSGSNVDE GRNILQLQPY
QLSTSGEQEI QLLVTDSVHN INFMPGPSQG VSIVAAESPQ SMATDPAANI TLLTQQPEQL
QGLILSAQQE QAEHIQSLSV IGGQMESSQT EPVHVITLSK ETLEHLHAHQ EQTTSSVPAA
DTGARATPVP STRPGAELTQ APLAVPLDPS PGATVAGWPF GPSSYRSLKM
