BNC1_HUMAN
ID BNC1_HUMAN Reviewed; 994 AA.
AC Q01954; Q15840;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Zinc finger protein basonuclin-1;
GN Name=BNC1; Synonyms=BNC;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Keratinocyte;
RX PubMed=1332044; DOI=10.1073/pnas.89.21.10311;
RA Tseng H., Green H.;
RT "Basonuclin: a keratinocyte protein with multiple paired zinc fingers.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:10311-10315(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9099851; DOI=10.1016/s0378-1119(96)00659-2;
RA Teumer J., Tseng H., Green H.;
RT "The human basonuclin gene.";
RL Gene 188:1-7(1997).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=8034748; DOI=10.1083/jcb.126.2.495;
RA Tseng H., Green H.;
RT "Association of basonuclin with ability of keratinocytes to multiply and
RT with absence of terminal differentiation.";
RL J. Cell Biol. 126:495-506(1994).
RN [4]
RP SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL, PHOSPHORYLATION AT
RP SER-537 AND SER-541, AND MUTAGENESIS OF SER-537; SER-540 AND SER-541.
RX PubMed=9223293; DOI=10.1073/pnas.94.15.7948;
RA Iuchi S., Green H.;
RT "Nuclear localization of basonuclin in human keratinocytes and the role of
RT phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:7948-7953(1997).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=9687312; DOI=10.1095/biolreprod59.2.388;
RA Mahoney M.G., Tang W., Xiang M.M., Moss S.B., Gerton G.L., Stanley J.R.,
RA Tseng H.;
RT "Translocation of the zinc finger protein basonuclin from the mouse germ
RT cell nucleus to the midpiece of the spermatozoon during spermiogenesis.";
RL Biol. Reprod. 59:388-394(1998).
RN [6]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16891417; DOI=10.1073/pnas.0605086103;
RA Vanhoutteghem A., Djian P.;
RT "Basonuclins 1 and 2, whose genes share a common origin, are proteins with
RT widely different properties and functions.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:12423-12428(2006).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INVOLVEMENT IN POF16,
RP VARIANT POF16 PRO-532, AND CHARACTERIZATION OF VARIANT POF16 PRO-532.
RX PubMed=30010909; DOI=10.1093/hmg/ddy261;
RA Zhang D., Liu Y., Zhang Z., Lv P., Liu Y., Li J., Wu Y., Zhang R.,
RA Huang Y., Xu G., Qian Y., Qian Y., Chen S., Xu C., Shen J., Zhu L.,
RA Chen K., Zhu B., Ye X., Mao Y., Bo X., Zhou C., Wang T., Chen D., Yang W.,
RA Tan Y., Song Y., Zhou D., Sheng J., Gao H., Zhu Y., Li M., Wu L., He L.,
RA Huang H.;
RT "Basonuclin 1 deficiency is a cause of primary ovarian insufficiency.";
RL Hum. Mol. Genet. 27:3787-3800(2018).
CC -!- FUNCTION: Transcriptional activator (By similarity). It is likely
CC involved in the regulation of keratinocytes terminal differentiation in
CC squamous epithelia and hair follicles (PubMed:8034748). Required for
CC the maintenance of spermatogenesis (By similarity). It is involved in
CC the positive regulation of oocyte maturation, probably acting through
CC the control of BMP15 levels and regulation of AKT signaling cascade
CC (PubMed:30010909). May also play a role in the early development of
CC embryos (By similarity). {ECO:0000250|UniProtKB:O35914,
CC ECO:0000269|PubMed:30010909, ECO:0000269|PubMed:8034748}.
CC -!- SUBUNIT: Interacts with HSF2BP (via C-terminus).
CC {ECO:0000250|UniProtKB:O35914}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16891417,
CC ECO:0000269|PubMed:30010909, ECO:0000269|PubMed:8034748,
CC ECO:0000269|PubMed:9223293}. Cytoplasm {ECO:0000269|PubMed:9223293}.
CC Nucleus, nucleoplasm {ECO:0000269|PubMed:16891417}. Note=Relocates to
CC the midpiece of the flagellum during late spermiogenesis in spermatids.
CC {ECO:0000250|UniProtKB:O35914}.
CC -!- TISSUE SPECIFICITY: In epidermis, primarily detected in cells of the
CC basal or immediately suprabasal layers (at protein level)
CC (PubMed:16891417). In hair follicles, mainly expressed in the outer
CC root sheath (at protein level) (PubMed:8034748). Expressed in
CC epidermis, testis and foreskin, and to a lower extent in thymus,
CC spleen, mammary glands, placenta, brain and heart (PubMed:9687312).
CC Expressed in the ovary, notably in oocytes (PubMed:30010909).
CC {ECO:0000269|PubMed:16891417, ECO:0000269|PubMed:30010909,
CC ECO:0000269|PubMed:8034748, ECO:0000269|PubMed:9687312}.
CC -!- PTM: Phosphorylation on Ser-537 and Ser-541 leads to cytoplasmic
CC localization. {ECO:0000269|PubMed:9223293}.
CC -!- DISEASE: Premature ovarian failure 16 (POF16) [MIM:618723]: An
CC autosomal dominant form of premature ovarian failure, an ovarian
CC disorder defined as the cessation of ovarian function under the age of
CC 40 years. It is characterized by oligomenorrhea or amenorrhea, in the
CC presence of elevated levels of serum gonadotropins and low estradiol.
CC {ECO:0000269|PubMed:30010909}. Note=The disease may be caused by
CC variants affecting the gene represented in this entry.
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DR EMBL; L03427; AAA35584.1; -; mRNA.
DR EMBL; U59694; AAB53028.1; -; Genomic_DNA.
DR EMBL; U59692; AAB53028.1; JOINED; Genomic_DNA.
DR EMBL; U59693; AAB53028.1; JOINED; Genomic_DNA.
DR CCDS; CCDS10324.1; -.
DR PIR; A46415; A46415.
DR RefSeq; NP_001288135.1; NM_001301206.1.
DR RefSeq; NP_001708.3; NM_001717.3.
DR AlphaFoldDB; Q01954; -.
DR BioGRID; 107115; 5.
DR IntAct; Q01954; 1.
DR STRING; 9606.ENSP00000307041; -.
DR iPTMnet; Q01954; -.
DR PhosphoSitePlus; Q01954; -.
DR BioMuta; BNC1; -.
DR DMDM; 12644377; -.
DR EPD; Q01954; -.
DR MassIVE; Q01954; -.
DR MaxQB; Q01954; -.
DR PaxDb; Q01954; -.
DR PeptideAtlas; Q01954; -.
DR PRIDE; Q01954; -.
DR ProteomicsDB; 58015; -.
DR Antibodypedia; 28194; 186 antibodies from 26 providers.
DR DNASU; 646; -.
DR Ensembl; ENST00000345382.7; ENSP00000307041.2; ENSG00000169594.14.
DR GeneID; 646; -.
DR KEGG; hsa:646; -.
DR MANE-Select; ENST00000345382.7; ENSP00000307041.2; NM_001717.4; NP_001708.3.
DR UCSC; uc002bjt.2; human.
DR CTD; 646; -.
DR DisGeNET; 646; -.
DR GeneCards; BNC1; -.
DR HGNC; HGNC:1081; BNC1.
DR HPA; ENSG00000169594; Tissue enhanced (esophagus, testis).
DR MalaCards; BNC1; -.
DR MIM; 601930; gene.
DR MIM; 618723; phenotype.
DR neXtProt; NX_Q01954; -.
DR OpenTargets; ENSG00000169594; -.
DR Orphanet; 243; 46,XX gonadal dysgenesis.
DR PharmGKB; PA25391; -.
DR VEuPathDB; HostDB:ENSG00000169594; -.
DR eggNOG; ENOG502QR8N; Eukaryota.
DR GeneTree; ENSGT00390000005844; -.
DR InParanoid; Q01954; -.
DR OMA; MEPRVPF; -.
DR OrthoDB; 96985at2759; -.
DR PhylomeDB; Q01954; -.
DR TreeFam; TF350399; -.
DR PathwayCommons; Q01954; -.
DR SignaLink; Q01954; -.
DR SIGNOR; Q01954; -.
DR BioGRID-ORCS; 646; 8 hits in 1075 CRISPR screens.
DR GeneWiki; BNC1; -.
DR GenomeRNAi; 646; -.
DR Pharos; Q01954; Tbio.
DR PRO; PR:Q01954; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q01954; protein.
DR Bgee; ENSG00000169594; Expressed in germinal epithelium of ovary and 77 other tissues.
DR ExpressionAtlas; Q01954; baseline and differential.
DR Genevisible; Q01954; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; ISS:ARUK-UCL.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; IDA:ARUK-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000182; F:rDNA binding; IDA:ARUK-UCL.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0008544; P:epidermis development; TAS:ProtInc.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; TAS:ProtInc.
DR GO; GO:1900195; P:positive regulation of oocyte maturation; IMP:UniProtKB.
DR GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; IDA:ARUK-UCL.
DR GO; GO:0006356; P:regulation of transcription by RNA polymerase I; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR InterPro; IPR040436; Disconnected-like.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR15021; PTHR15021; 1.
DR SMART; SM00355; ZnF_C2H2; 6.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 1: Evidence at protein level;
KW Cytoplasm; Differentiation; Disease variant; DNA-binding; Metal-binding;
KW Nucleus; Phosphoprotein; Premature ovarian failure; Reference proteome;
KW Repeat; Spermatogenesis; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..994
FT /note="Zinc finger protein basonuclin-1"
FT /id="PRO_0000046932"
FT ZN_FING 357..380
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 385..414
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 720..743
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 748..775
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 928..951
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 956..983
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..249
FT /note="Hydrophobic"
FT REGION 402..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 555..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 859..881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 970..994
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 533..539
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:9223293"
FT COMPBIAS 616..638
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 859..879
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 537
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:9223293"
FT MOD_RES 541
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:9223293"
FT VARIANT 532
FT /note="L -> P (in POF16; unknown pathological significance;
FT affects nuclear localization; the mutant exhibits a
FT punctate localization in the nucleus; dbSNP:rs149100994)"
FT /evidence="ECO:0000269|PubMed:30010909"
FT /id="VAR_083487"
FT MUTAGEN 537
FT /note="S->A: No effect on phosphorylation. Abolishes
FT phosphorylation and induces nuclear restriction; when
FT associated with A-541."
FT /evidence="ECO:0000269|PubMed:9223293"
FT MUTAGEN 537
FT /note="S->D: Reduces phosphorylation and induces partial
FT relocation into the cytoplasm."
FT /evidence="ECO:0000269|PubMed:9223293"
FT MUTAGEN 540
FT /note="S->D: No effect on phosphorylation, no effect on
FT subcellular location."
FT /evidence="ECO:0000269|PubMed:9223293"
FT MUTAGEN 541
FT /note="S->A: Strongly reduces phosphorylation. Abolishes
FT phosphorylation and induces nuclear restriction; when
FT associated with A-537."
FT /evidence="ECO:0000269|PubMed:9223293"
FT MUTAGEN 541
FT /note="S->D: Strongly reduces phosphorylation and induces
FT partial relocation into the cytoplasm."
FT /evidence="ECO:0000269|PubMed:9223293"
FT CONFLICT 6..14
FT /note="PSRGGRGAA -> EPGRTRGG (in Ref. 1; AAA35584)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="S -> C (in Ref. 1; AAA35584)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="F -> N (in Ref. 1; AAA35584)"
FT /evidence="ECO:0000305"
FT CONFLICT 401
FT /note="S -> T (in Ref. 1; AAA35584)"
FT /evidence="ECO:0000305"
FT CONFLICT 638
FT /note="Q -> H (in Ref. 1; AAA35584)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 994 AA; 110972 MW; 7DF13EE782E20ED5 CRC64;
MRRRPPSRGG RGAARARETR RQPRHRSGRR MAEAISCTLN CSCQSFKPGK INHRQCDQCK
HGWVAHALSK LRIPPMYPTS QVEIVQSNVV FDISSLMLYG TQAIPVRLKI LLDRLFSVLK
QDEVLQILHA LDWTLQDYIR GYVLQDASGK VLDHWSIMTS EEEVATLQQF LRFGETKSIV
ELMAIQEKEE QSIIIPPSTA NVDIRAFIES CSHRSSSLPT PVDKGNPSSI HPFENLISNM
TFMLPFQFFN PLPPALIGSL PEQYMLEQGH DQSQDPKQEV HGPFPDSSFL TSSSTPFQVE
KDQCLNCPDA ITKKEDSTHL SDSSSYNIVT KFERTQLSPE AKVKPERNSL GTKKGRVFCT
ACEKTFYDKG TLKIHYNAVH LKIKHKCTIE GCNMVFSSLR SRNRHSANPN PRLHMPMNRN
NRDKDLRNSL NLASSENYKC PGFTVTSPDC RPPPSYPGSG EDSKGQPAFP NIGQNGVLFP
NLKTVQPVLP FYRSPATPAE VANTPGILPS LPLLSSSIPE QLISNEMPFD ALPKKKSRKS
SMPIKIEKEA VEIANEKRHN LSSDEDMPLQ VVSEDEQEAC SPQSHRVSEE QHVQSGGLGK
PFPEGERPCH RESVIESSGA ISQTPEQATH NSERETEQTP ALIMVPREVE DGGHEHYFTP
GMEPQVPFSD YMELQQRLLA GGLFSALSNR GMAFPCLEDS KELEHVGQHA LARQIEENRF
QCDICKKTFK NACSVKIHHK NMHVKEMHTC TVEGCNATFP SRRSRDRHSS NLNLHQKALS
QEALESSEDH FRAAYLLKDV AKEAYQDVAF TQQASQTSVI FKGTSRMGSL VYPITQVHSA
SLESYNSGPL SEGTILDLST TSSMKSESSS HSSWDSDGVS EEGTVLMEDS DGNCEGSSLV
PGEDEYPICV LMEKADQSLA SLPSGLPITC HLCQKTYSNK GTFRAHYKTV HLRQLHKCKV
PGCNTMFSSV RSRNRHSQNP NLHKSLASSP SHLQ
