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DescriptionRecName: Full=Zinc finger and BTB domain-containing protein 45 {ECO:0000303|PubMed:21131782}; AltName: Full=Zinc finger protein 499 {ECO:0000305};
MyHits logo
MyHits synonymsZBT45_MOUSE , Q52KG4 , Q3TLP9 , 3B239179EE6E92D3
match map segment
ipat:ZINC_FINGER_C2H2_1 iprf:ZINC_FINGER_C2H2_2 ismart:BTB iprf:ZINC_FINGER_C2H2_2 iprf:ZINC_FINGER_C2H2_2 ipfam:BTB iprf:ZINC_FINGER_C2H2_2 ipat:ZINC_FINGER_C2H2_1 ipat:ZINC_FINGER_C2H2_1 ismart:ZnF_C2H2 iprf:BTB ismart:ZnF_C2H2 ismart:ZnF_C2H2 ipat:ZINC_FINGER_C2H2_1 ismart:ZnF_C2H2  
Legends: 1, CONFLICT S -> G (in Ref. 1; BAE38743). {ECO:0000305}; 2, BTB. {ECO:0000255|PROSITE- ProRule:PRU00037}; 3, ZN_FING C2H2-type 1. {ECO:0000255|PROSITE- ProRule:PRU00042}; 4, ZN_FING C2H2-type 2. {ECO:0000255|PROSITE- ProRule:PRU00042}; 5, ZN_FING C2H2-type 3. {ECO:0000255|PROSITE- ProRule:PRU00042}; 6, ZN_FING C2H2-type 4. {ECO:0000255|PROSITE- ProRule:PRU00042}; 7, COMPBIAS Pro-rich. {ECO:0000255|PROSITE- ProRule:PRU00015}; 8, ipat:ZINC_FINGER_C2H2_1 [T]; 9, iprf:ZINC_FINGER_C2H2_2 [T]; 10, ismart:ZnF_C2H2 [T].
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   10-MAY-2017, entry version 118.
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,
GN   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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the 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
RT   project: 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
RT   proper glial differentiation of neural and oligodendrocyte progenitor
RT   cells.";
RL   Cell Cycle 9:4866-4875(2010).
CC   -!- FUNCTION: May be involved in transcriptional regulation
CC       (Probable). In the central nervous system, may play a role in
CC       glial cell differentiation (PubMed:21131782).
CC       {ECO:0000269|PubMed:21131782, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- DEVELOPMENTAL STAGE: Detected in embryonic forebrain at stages
CC       E12.5 and E14.5 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   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   UniGene; Mm.279272; -.
DR   SMR; Q52KG4; -.
DR   STRING; 10090.ENSMUSP00000056086; -.
DR   MaxQB; Q52KG4; -.
DR   PaxDb; Q3TLP9; -.
DR   PeptideAtlas; Q3TLP9; -.
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   eggNOG; KOG1721; Eukaryota.
DR   eggNOG; COG5048; LUCA.
DR   GeneTree; ENSGT00760000119063; -.
DR   HOGENOM; HOG000136747; -.
DR   HOVERGEN; HBG060183; -.
DR   KO; K10516; -.
DR   OMA; APPDCVL; -.
DR   OrthoDB; EOG091G0EMJ; -.
DR   TreeFam; TF335684; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   Bgee; ENSMUSG00000049600; -.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR000210; BTB/POZ_dom.
DR   InterPro; IPR011333; SKP1/BTB/POZ.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF00651; BTB; 1.
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   Complete proteome; DNA-binding; Metal-binding; Neurogenesis; Nucleus;
KW   Reference proteome; Repeat; Transcription; Transcription regulation;
KW   Zinc; Zinc-finger.
FT   CHAIN         1    520       Zinc finger and BTB domain-containing
FT                                protein 45.
FT                                /FTId=PRO_0000439879.
FT   DOMAIN       33     96       BTB. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00037}.
FT   ZN_FING     412    434       C2H2-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     440    462       C2H2-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     468    490       C2H2-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     495    517       C2H2-type 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   COMPBIAS    128    197       Pro-rich. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00015}.
FT   COMPBIAS    302    373       Pro-rich. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00015}.
FT   CONFLICT    304    304       S -> G (in Ref. 1; BAE38743).
FT                                {ECO:0000305}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       414    434       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       412    439       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT        33    126       ismart:BTB [T]
FT   MYHIT       495    520       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       468    495       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT        23    122       ipfam:BTB [T]
FT   MYHIT       440    467       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       470    490       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       442    462       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       440    462       ismart:ZnF_C2H2 [T]
FT   MYHIT        33     96       iprf:BTB [T]
FT   MYHIT       468    490       ismart:ZnF_C2H2 [T]
FT   MYHIT       495    517       ismart:ZnF_C2H2 [T]
FT   MYHIT       497    517       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       412    434       ismart:ZnF_C2H2 [T]
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
//