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 24-JAN-2024, entry version 181. 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. 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; 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; 2. 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; 9606-ENSP00000307041; -. DR PeptideAtlas; Q01954; -. DR ProteomicsDB; 58015; -. DR Antibodypedia; 28194; 207 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 AGR; HGNC:1081; -. DR CTD; 646; -. DR DisGeNET; 646; -. DR GeneCards; BNC1; -. DR HGNC; HGNC:1081; BNC1. DR HPA; ENSG00000169594; Tissue enhanced (adipose tissue, 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; 5394049at2759; -. DR PhylomeDB; Q01954; -. DR TreeFam; TF350399; -. DR PathwayCommons; Q01954; -. DR SignaLink; Q01954; -. DR SIGNOR; Q01954; -. DR BioGRID-ORCS; 646; 9 hits in 1151 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 79 other cell types or tissues. DR ExpressionAtlas; Q01954; baseline and differential. 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:0007283; P:spermatogenesis; IEA:UniProtKB-KW. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 3. DR InterPro; IPR040436; Disconnected-like. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR PANTHER; PTHR15021; DISCONNECTED-RELATED; 1. DR PANTHER; PTHR15021:SF1; ZINC FINGER PROTEIN BASONUCLIN-1; 1. DR Pfam; PF12874; zf-met; 2. DR SMART; SM00355; ZnF_C2H2; 6. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3. DR Genevisible; Q01954; HS. 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; uncertain significance; affects FT nuclear localization; the mutant exhibits a punctate FT 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 //