ZBTB3_MOUSE
ID ZBTB3_MOUSE Reviewed; 518 AA.
AC Q91X45; Q3UQP3; Q8BIJ4;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Zinc finger and BTB domain-containing protein 3;
GN Name=Zbtb3;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Heart;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Colon;
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).
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH12410.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; AK049258; BAC33640.1; -; mRNA.
DR EMBL; AK142256; BAE24996.1; -; mRNA.
DR EMBL; AC129217; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC012410; AAH12410.1; ALT_INIT; mRNA.
DR EMBL; BC119186; AAI19187.1; -; mRNA.
DR EMBL; BC119188; AAI19189.1; -; mRNA.
DR CCDS; CCDS29548.1; -.
DR RefSeq; NP_001091707.1; NM_001098237.1.
DR RefSeq; NP_598520.1; NM_133759.3.
DR RefSeq; XP_006527482.1; XM_006527419.2.
DR AlphaFoldDB; Q91X45; -.
DR SMR; Q91X45; -.
DR BioGRID; 217367; 5.
DR IntAct; Q91X45; 5.
DR STRING; 10090.ENSMUSP00000127746; -.
DR iPTMnet; Q91X45; -.
DR PhosphoSitePlus; Q91X45; -.
DR EPD; Q91X45; -.
DR jPOST; Q91X45; -.
DR PaxDb; Q91X45; -.
DR PRIDE; Q91X45; -.
DR ProteomicsDB; 302039; -.
DR Antibodypedia; 14959; 153 antibodies from 22 providers.
DR DNASU; 75291; -.
DR Ensembl; ENSMUST00000172175; ENSMUSP00000127746; ENSMUSG00000071661.
DR GeneID; 75291; -.
DR KEGG; mmu:75291; -.
DR UCSC; uc008gnb.1; mouse.
DR CTD; 79842; -.
DR MGI; MGI:1922541; Zbtb3.
DR VEuPathDB; HostDB:ENSMUSG00000071661; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000161486; -.
DR HOGENOM; CLU_034521_0_0_1; -.
DR InParanoid; Q91X45; -.
DR OMA; ALLQMTH; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q91X45; -.
DR TreeFam; TF330979; -.
DR BioGRID-ORCS; 75291; 1 hit in 74 CRISPR screens.
DR PRO; PR:Q91X45; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q91X45; protein.
DR Bgee; ENSMUSG00000071661; Expressed in seminiferous tubule of testis and 92 other tissues.
DR Genevisible; Q91X45; MM.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor 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: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; 1.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE 2: Evidence at transcript level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..518
FT /note="Zinc finger and BTB domain-containing protein 3"
FT /id="PRO_0000047711"
FT DOMAIN 24..92
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 418..440
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 446..469
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 126..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 310..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..503
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 308
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H5J0"
FT MOD_RES 495
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H5J0"
FT CROSSLNK 131
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H5J0"
FT CROSSLNK 132
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H5J0"
FT CROSSLNK 478
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H5J0"
FT CONFLICT 321
FT /note="R -> G (in Ref. 3; AAH12410)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 518 AA; 55901 MW; 79D62A5BB424E081 CRC64;
MEFPEHSQQL LQSLREQRSQ GFLCDCTVMV GSTQFLAHRA VLASCSPFFQ LFYKERELDK
RDLVCIHNEI VTAPAFGLLL DFMYAGQLAL RGDTPLEDVL AAASYLHMND IVKVCKQRLQ
ARALAEADST KKEEETNPAS LEFLSGSSRG PQPLLASVEP SARWNKEEWK GPATPLPIAH
PADEPPVSGG ADTTQPSMEV DSSHLRAPPP PVADVSVSLA SPSSSTETIP VNYFSSGLPG
VSVEPLTPLD VVPESLRVVE PRDTGGPLQG FYPPAPAPPP APAPVLSQAP APVEAELVQV
KVEAIVISDE EADLSEEQPH RSEGLFPPGG AVYGGQPSQA EAFEEPGATG LEEVGPSDHF
LPPESHLPYH LLPGPGQYHR GLVTSPLPAP AALHEPLYPP PEYEAAQGSF GNFTEDVPTC
KTCGKTFSCS YTLRRHATVH TRERPYECRY CLRSYTQSGD LYRHIRKAHN EDLAKRSKPD
PEASTILGVQ PLSGSQTTER HSSGGGGPPK EFALGPKN