BNC2_MOUSE
ID BNC2_MOUSE Reviewed; 1127 AA.
AC Q8BMQ3; H3BIU0; Q6T3A4;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 3.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Zinc finger protein basonuclin-2;
GN Name=Bnc2 {ECO:0000312|MGI:MGI:2443805};
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] {ECO:0000305, ECO:0000312|EMBL:BAC26901.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC26901.1};
RC TISSUE=Ovary {ECO:0000312|EMBL:BAC26901.1}, and
RC Uterus {ECO:0000312|EMBL:BAC26901.1};
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]
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] {ECO:0000305, ECO:0000312|EMBL:AAR99388.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 68-1127 (ISOFORM 1), SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=CD-1 {ECO:0000312|EMBL:AAR99388.1};
RX PubMed=15081112; DOI=10.1016/j.ygeno.2003.11.009;
RA Romano R.-A., Li H., Tummala R., Maul R., Sinha S.;
RT "Identification of Basonuclin2, a DNA-binding zinc-finger protein expressed
RT in germ tissues and skin keratinocytes.";
RL Genomics 83:821-833(2004).
RN [4] {ECO:0000305}
RP PROBABLE FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=14988505; DOI=10.1073/pnas.0400268101;
RA Vanhoutteghem A., Djian P.;
RT "Basonuclin 2: an extremely conserved homolog of the zinc finger protein
RT basonuclin.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:3468-3473(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
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).
RN [6]
RP DEVELOPMENTAL STAGE.
RX PubMed=31051115; DOI=10.1016/j.ajhg.2019.03.023;
RA Kolvenbach C.M., Dworschak G.C., Frese S., Japp A.S., Schuster P.,
RA Wenzlitschke N., Yilmaz O., Lopes F.M., Pryalukhin A., Schierbaum L.,
RA van der Zanden L.F.M., Kause F., Schneider R., Taranta-Janusz K.,
RA Szczepanska M., Pawlaczyk K., Newman W.G., Beaman G.M., Stuart H.M.,
RA Cervellione R.M., Feitz W.F.J., van Rooij I.A.L.M., Schreuder M.F.,
RA Steffens M., Weber S., Merz W.M., Feldkoetter M., Hoppe B., Thiele H.,
RA Altmueller J., Berg C., Kristiansen G., Ludwig M., Reutter H., Woolf A.S.,
RA Hildebrandt F., Grote P., Zaniew M., Odermatt B., Hilger A.C.;
RT "Rare variants in BNC2 are implicated in autosomal-dominant congenital
RT lower urinary-tract obstruction.";
RL Am. J. Hum. Genet. 104:994-1006(2019).
CC -!- FUNCTION: Probable transcription factor specific for skin
CC keratinocytes. May play a role in the differentiation of spermatozoa
CC and oocytes. May also play an important role in early urinary-tract
CC development. {ECO:0000250|UniProtKB:Q6ZN30}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15081112}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:15081112};
CC IsoId=Q8BMQ3-1; Sequence=Displayed;
CC Name=2 {ECO:0000305};
CC IsoId=Q8BMQ3-2; Sequence=VSP_051875;
CC -!- TISSUE SPECIFICITY: Highly expressed in ovary, testis and kidney.
CC Expressed at moderate levels in skin and small intestine, and at lower
CC levels in lung. Trace amounts of expression detected in liver and
CC colon. Not detected in brain, spleen or thymus.
CC {ECO:0000269|PubMed:14988505, ECO:0000269|PubMed:15081112}.
CC -!- DEVELOPMENTAL STAGE: Detected at embryonic days 15.5 and 17.5.
CC Expressed in the developing lower urinary-tract structures, with
CC emphasis on the genital tubercle above the phallic urethra and below
CC the pelvic urethra at as early as embryonic day 13.5 dpc, the critical
CC time point for urethral development. In embryos, expression is also
CC visible in the brain, in the mandibular region, and in dorsal parts
CC above the spinal cord. {ECO:0000269|PubMed:15081112,
CC ECO:0000269|PubMed:31051115}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAR99388.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL772261; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL805919; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX004826; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK030323; BAC26901.1; -; mRNA.
DR EMBL; AY438375; AAR99388.1; ALT_INIT; mRNA.
DR CCDS; CCDS18301.2; -. [Q8BMQ3-2]
DR RefSeq; NP_766458.3; NM_172870.4. [Q8BMQ3-2]
DR AlphaFoldDB; Q8BMQ3; -.
DR BioGRID; 232414; 1.
DR IntAct; Q8BMQ3; 1.
DR MINT; Q8BMQ3; -.
DR STRING; 10090.ENSMUSP00000135375; -.
DR iPTMnet; Q8BMQ3; -.
DR PhosphoSitePlus; Q8BMQ3; -.
DR jPOST; Q8BMQ3; -.
DR PaxDb; Q8BMQ3; -.
DR PeptideAtlas; Q8BMQ3; -.
DR PRIDE; Q8BMQ3; -.
DR ProteomicsDB; 273749; -. [Q8BMQ3-1]
DR ProteomicsDB; 273750; -. [Q8BMQ3-2]
DR Antibodypedia; 10169; 83 antibodies from 19 providers.
DR DNASU; 242509; -.
DR Ensembl; ENSMUST00000102820; ENSMUSP00000099884; ENSMUSG00000028487. [Q8BMQ3-1]
DR Ensembl; ENSMUST00000176691; ENSMUSP00000135375; ENSMUSG00000028487. [Q8BMQ3-2]
DR GeneID; 242509; -.
DR KEGG; mmu:242509; -.
DR UCSC; uc008tlg.2; mouse. [Q8BMQ3-1]
DR UCSC; uc008tli.2; mouse. [Q8BMQ3-2]
DR CTD; 54796; -.
DR MGI; MGI:2443805; Bnc2.
DR VEuPathDB; HostDB:ENSMUSG00000028487; -.
DR eggNOG; ENOG502QR8N; Eukaryota.
DR GeneTree; ENSGT00390000005844; -.
DR HOGENOM; CLU_010637_0_0_1; -.
DR InParanoid; Q8BMQ3; -.
DR OMA; KMDTPAI; -.
DR OrthoDB; 96985at2759; -.
DR PhylomeDB; Q8BMQ3; -.
DR TreeFam; TF350399; -.
DR BioGRID-ORCS; 242509; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Bnc2; mouse.
DR PRO; PR:Q8BMQ3; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8BMQ3; protein.
DR Bgee; ENSMUSG00000028487; Expressed in animal zygote and 178 other tissues.
DR ExpressionAtlas; Q8BMQ3; baseline and differential.
DR Genevisible; Q8BMQ3; MM.
DR GO; GO:0000785; C:chromatin; IDA:ARUK-UCL.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000182; F:rDNA binding; IDA:ARUK-UCL.
DR GO; GO:0003416; P:endochondral bone growth; IMP:MGI.
DR GO; GO:0060485; P:mesenchyme development; IMP:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0060021; P:roof of mouth development; IMP:MGI.
DR GO; GO:0043586; P:tongue development; IMP:MGI.
DR InterPro; IPR040436; Disconnected-like.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR15021; PTHR15021; 1.
DR Pfam; PF00096; zf-C2H2; 1.
DR SMART; SM00355; ZnF_C2H2; 6.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1127
FT /note="Zinc finger protein basonuclin-2"
FT /id="PRO_0000046935"
FT ZN_FING 469..492
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 861..884
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1063..1086
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1091..1118
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 44..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 675..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 955..976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 996..1041
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1107..1127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..691
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..745
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..772
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 589
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZN30"
FT CROSSLNK 305
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6ZN30"
FT CROSSLNK 424
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6ZN30"
FT CROSSLNK 444
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6ZN30"
FT CROSSLNK 449
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6ZN30"
FT CROSSLNK 669
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6ZN30"
FT CROSSLNK 922
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6ZN30"
FT CROSSLNK 947
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6ZN30"
FT VAR_SEQ 44..138
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_051875"
FT CONFLICT 257
FT /note="V -> I (in Ref. 1; BAC26901)"
FT /evidence="ECO:0000305"
FT CONFLICT 406
FT /note="S -> G (in Ref. 1; BAC26901)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1127 AA; 125335 MW; 94B2315C52776CEB CRC64;
MARFVPSPPP NCLSYKSEGR LGEQDWQAHF KVPCCGVDPS QLESEEAEVD VRERDTQRDR
EPKRARDLTL RDSCTDNSMQ FGTRTTAAEP GFMGTWQNAD TNLLFRMSQQ VPLACAGRVL
GADFCPNLEE PDQRLEVQAI RCTLVNCTCE CFQPGKINLR TCDQCKHGWV AHALDKLSTQ
HLYHPTQVEI VQSNVVFDIS SLMLYGTQAV PVRLKILLDR LFSVLKQEEV LHILHGLGWT
LRDYVRGYIL QDAAGKVLDR WAIMSREEEI ITLQQFLRFG ETKSIVELMA IQEKEGQAVA
VPSSKTDSDI RTFIESNNRT RSPSLLAHLE NSNPSSIHHF ENIPNSLAFL LPFQYINPVS
APLLGLPPNG LLLEQPGLRL REPSISTQNE YNESSESEVS PTPYKSDQTP NRNALTSITN
VEPKTEPACV SPIQNSAPVS DLSKTEHPKS SFRIHRMRRM GSASRKGRVF CNACGKTFYD
KGTLKIHYNA VHLKIKHRCT IEGCNMVFSS LRSRNRHSAN PNPRLHMPML RNNRDKDLIR
ATSGAATPVI ASTKSNLTLT SPGRPPMGFT TPPLDPVLQN PLPSQLVFSG LKTVQPVPPF
YRSLLTPGEM VSPPTSLPTS PIIPTSGTIE QHPPPPSEPI VPAVMMGTHE PSADLAPKKK
PRKSSMPVKI EKEIIDTADE FDDEDDDPND GGTVVNDMSH DNHCHSQDEM SPGMSVKDFS
KHNRTRCISR TEIRRADSMT SEDQEPERDY ENESESSEPK LGEESMEGDE HLHSEVSEKV
LMNSERPDEN HSEPSHQDVI KVKEEFTDPT YDMFYMSQYG LYNGGGASMA ALHESFTSSL
NYGSPQKFSP EGDLCSSPDP KICYVCKKSF KSSYSVKLHY RNVHLKEMHV CTVAGCNAAF
PSRRSRDRHS ANINLHRKLL TKELDDMSLD SSQPSLSKDL RDEFLMKIYG AQHPLGLDGR
EDASSPAGTE DSHLNGYGRG MAEDYMVLDL STTSSLQSSS SVHSSRESDA GSDEGILLDD
IDGASDSGES THKAEAPTLP GSLGAEVSGS LMFSSLSGSN GGIMCNICHK MYSNKGTLRV
HYKTVHLREM HKCKVPGCNM MFSSVRSRNR HSQNPNLHKN IPFTSID
