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ZBT45_MOUSE
ID   ZBT45_MOUSE             Reviewed;         520 AA.
AC   Q52KG4; Q3TLP9;
DT   10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Zinc finger and BTB domain-containing protein 45 {ECO:0000303|PubMed:21131782};
DE   AltName: Full=Zinc finger protein 499 {ECO:0000305};
GN   Name=Zbtb45 {ECO:0000303|PubMed:21131782, ECO:0000312|MGI:MGI:2685003};
GN   Synonyms=Gm157 {ECO:0000312|MGI:MGI:2685003},
GN   Zfp499 {ECO:0000312|MGI:MGI:2685003};
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 {ECO:0000312|EMBL:AAH94359.1};
RN   [1] {ECO:0000312|EMBL:BAE38743.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary gland {ECO:0000312|EMBL:BAE38743.1};
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   [2] {ECO:0000312|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3] {ECO:0000312|EMBL:EDL38083.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000312|EMBL:AAH94359.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH94359.1};
RC   TISSUE=Brain {ECO:0000312|EMBL:AAH94359.1};
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] {ECO:0000305}
RP   FUNCTION, AND DEVELOPMENTAL STAGE.
RX   PubMed=21131782; DOI=10.4161/cc.9.24.14154;
RA   Soedersten E., Lilja T., Hermanson O.;
RT   "The novel BTB/POZ and zinc finger factor Zbtb45 is essential for proper
RT   glial differentiation of neural and oligodendrocyte progenitor cells.";
RL   Cell Cycle 9:4866-4875(2010).
CC   -!- FUNCTION: May be involved in transcriptional regulation (Probable). In
CC       the central nervous system, may play a role in glial cell
CC       differentiation (PubMed:21131782). {ECO:0000269|PubMed:21131782,
CC       ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- DEVELOPMENTAL STAGE: Detected in embryonic forebrain at stages 12.5 dpc
CC       and 14.5 dpc where it is ubiquitously expressed.
CC       {ECO:0000269|PubMed:21131782}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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DR   EMBL; AK166382; BAE38743.1; -; mRNA.
DR   EMBL; AC121301; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466634; EDL38083.1; -; Genomic_DNA.
DR   EMBL; CH466634; EDL38084.1; -; Genomic_DNA.
DR   EMBL; BC094359; AAH94359.1; -; mRNA.
DR   CCDS; CCDS20822.1; -.
DR   RefSeq; NP_001019870.1; NM_001024699.1.
DR   RefSeq; XP_006539865.1; XM_006539802.1.
DR   RefSeq; XP_006539866.1; XM_006539803.1.
DR   RefSeq; XP_006539867.1; XM_006539804.2.
DR   AlphaFoldDB; Q52KG4; -.
DR   SMR; Q52KG4; -.
DR   STRING; 10090.ENSMUSP00000130439; -.
DR   iPTMnet; Q52KG4; -.
DR   PhosphoSitePlus; Q52KG4; -.
DR   EPD; Q52KG4; -.
DR   MaxQB; Q52KG4; -.
DR   PaxDb; Q52KG4; -.
DR   PRIDE; Q52KG4; -.
DR   ProteomicsDB; 298497; -.
DR   Antibodypedia; 19698; 78 antibodies from 20 providers.
DR   Ensembl; ENSMUST00000051390; ENSMUSP00000056086; ENSMUSG00000049600.
DR   Ensembl; ENSMUST00000172240; ENSMUSP00000130439; ENSMUSG00000049600.
DR   Ensembl; ENSMUST00000210282; ENSMUSP00000147298; ENSMUSG00000049600.
DR   GeneID; 232879; -.
DR   KEGG; mmu:232879; -.
DR   UCSC; uc009fez.1; mouse.
DR   CTD; 84878; -.
DR   MGI; MGI:2685003; Zbtb45.
DR   VEuPathDB; HostDB:ENSMUSG00000049600; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000160859; -.
DR   HOGENOM; CLU_019055_1_0_1; -.
DR   InParanoid; Q52KG4; -.
DR   OMA; THTAWKG; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; Q52KG4; -.
DR   TreeFam; TF335684; -.
DR   BioGRID-ORCS; 232879; 1 hit in 72 CRISPR screens.
DR   PRO; PR:Q52KG4; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q52KG4; protein.
DR   Bgee; ENSMUSG00000049600; Expressed in embryonic brain and 205 other tissues.
DR   ExpressionAtlas; Q52KG4; baseline and differential.
DR   GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
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:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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; 4.
DR   SMART; SM00225; BTB; 1.
DR   SMART; SM00355; ZnF_C2H2; 4.
DR   SUPFAM; SSF54695; SSF54695; 1.
DR   SUPFAM; SSF57667; SSF57667; 2.
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   DNA-binding; Metal-binding; Neurogenesis; Nucleus; Reference proteome;
KW   Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..520
FT                   /note="Zinc finger and BTB domain-containing protein 45"
FT                   /id="PRO_0000439879"
FT   DOMAIN          33..96
FT                   /note="BTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT   ZN_FING         412..434
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         440..462
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         468..490
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         495..517
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          182..272
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          337..372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        205..224
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        337..367
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        304
FT                   /note="S -> G (in Ref. 1; BAE38743)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   520 AA;  55012 MW;  3B239179EE6E92D3 CRC64;
     MAATEAVHHI HLQNFSRSLL ETLNGQRLGG HFCDVTVRIR EASLRAHRCV LAAGSPFFQD
     KLLLGHSEIR VPPVVPAQTV RQLVEFLYSG SLVVAQGEAL QVLTAASVLR IQTVIDECTQ
     IIARARVPNT PAPAPLPPPV PPPLAPAQLR HRLRHLLAAR PPGHPNAAHS RKQRQPARLQ
     LPAPPAPIKA EGPDAEPALT AAPEDRGEED DDEETDEETD AEEGEGGGGG PGEGQAPPAF
     PDCAGGFLTT AADSAREDPP ASTGITDYGG AGRDFLRGTG VTEDVFPDSY VSAWHEESSG
     GPESCPVETS APPDCALAGP RPTGVKTPGP PVALFPFHLG APGPPAPTPP TPSGPAPAPP
     PTFYPTLQPD AAPSAQLGET QAVPAAPAAQ ATAISGTPVR APGGQGAEQP AYECSHCRKT
     FSSRKNYTKH MFIHSGEKPH QCAVCWRSFS LRDYLLKHMV THTGVRAFQC AVCAKRFTQK
     SSLNVHMRTH RPERAPCPAC GKVFSHRALL ERHLAAHPAP
 
 
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