ID NFIB_MOUSE Reviewed; 570 AA. AC P97863; P70252; P70253; P70254; Q9R1G4; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 2. DT 02-SEP-2026, entry version 203. DE RecName: Full=Nuclear factor 1 B-type; DE Short=NF1-B; DE Short=Nuclear factor 1/B; DE AltName: Full=CCAAT-box-binding transcription factor; DE Short=CTF; DE AltName: Full=Nuclear factor I/B; DE Short=NF-I/B; DE Short=NFI-B; DE AltName: Full=TGGCA-binding protein; GN Name=Nfib; 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 [MRNA] (ISOFORM 3). RC STRAIN=BALB/cJ; TISSUE=Liver, and Skeletal muscle; RX PubMed=9056636; RX DOI=10.1002/(sici)1097-0177(199703)208:3<313::aid-aja3>3.0.co;2-l; RA Chaudhry A.Z., Lyons G.E., Gronostajski R.M.; RT "Expression patterns of the four nuclear factor I genes during mouse RT embryogenesis indicate a potential role in development."; RL Dev. Dyn. 208:313-325(1997). RN [2] RP NUCLEOTIDE SEQUENCE (ISOFORMS 1; 2 AND 3). RC STRAIN=NIH Swiss; RX PubMed=12568726; DOI=10.1016/s0378-1119(02)01204-0; RA Gruender A., Qian F., Ebel T.T., Mincheva A., Lichter P., Kruse U., RA Sippel A.E.; RT "Genomic organization, splice products and mouse chromosomal localization RT of genes for transcription factor Nuclear Factor One."; RL Gene 304:171-181(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 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 project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-187. RC STRAIN=129; RX PubMed=10087299; DOI=10.1007/s003359901008; RA Fletcher C.F., Jenkins N.A., Copeland N.G., Chaudhry A.Z., RA Gronostajski R.M.; RT "Exon structure of the nuclear factor I DNA-binding domain from C. elegans RT to mammals."; RL Mamm. Genome 10:390-396(1999). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic brain; RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200; RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.; RT "Phosphoproteomic analysis of the developing mouse brain."; RL Mol. Cell. Proteomics 3:1093-1101(2004). RN [6] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=15632069; DOI=10.1128/mcb.25.2.685-698.2005; RA Steele-Perkins G., Plachez C., Butz K.G., Yang G., Bachurski C.J., RA Kinsman S.L., Litwack E.D., Richards L.J., Gronostajski R.M.; RT "The transcription factor gene Nfib is essential for both lung maturation RT and brain development."; RL Mol. Cell. Biol. 25:685-698(2005). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-292 AND SER-295, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-286; SER-292; SER-295 AND RP SER-312, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, and Testis; 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 [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [10] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-335 AND ARG-388, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryo; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [11] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=30388402; DOI=10.1016/j.ajhg.2018.10.006; RA Schanze I., Bunt J., Lim J.W.C., Schanze D., Dean R.J., Alders M., RA Blanchet P., Attie-Bitach T., Berland S., Boogert S., Boppudi S., RA Bridges C.J., Cho M.T., Dobyns W.B., Donnai D., Douglas J., Earl D.L., RA Edwards T.J., Faivre L., Fregeau B., Genevieve D., Gerard M., Gatinois V., RA Holder-Espinasse M., Huth S.F., Izumi K., Kerr B., Lacaze E., Lakeman P., RA Mahida S., Mirzaa G.M., Morgan S.M., Nowak C., Peeters H., Petit F., RA Pilz D.T., Puechberty J., Reinstein E., Riviere J.B., Santani A.B., RA Schneider A., Sherr E.H., Smith-Hicks C., Wieland I., Zackai E., Zhao X., RA Gronostajski R.M., Zenker M., Richards L.J.; RT "NFIB haploinsufficiency is associated with intellectual disability and RT macrocephaly."; RL Am. J. Hum. Genet. 103:752-768(2018). CC -!- FUNCTION: Transcriptional activator of GFAP, essential for proper brain CC development (PubMed:15632069, PubMed:30388402). Recognizes and binds CC the palindromic sequence 5'-TTGGCNNNNNGCCAA-3' present in viral and CC cellular promoters and in the origin of replication of adenovirus type CC 2. These proteins are individually capable of activating transcription CC and replication (PubMed:30388402). {ECO:0000269|PubMed:15632069, CC ECO:0000269|PubMed:30388402}. CC -!- SUBUNIT: Binds DNA as a homodimer. CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P97863-1; Sequence=Displayed; CC Name=2; CC IsoId=P97863-2; Sequence=VSP_003547; CC Name=3; CC IsoId=P97863-3; Sequence=VSP_003548, VSP_003549; CC -!- TISSUE SPECIFICITY: Highest expression in lung, skeletal muscle and CC heart. Lower levels in liver, kidney and brain. Very low levels in CC testis and spleen. CC -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large CC number of yeast and animal transcription factors. CC {ECO:0000250|UniProtKB:O00712}. CC -!- DISRUPTION PHENOTYPE: NFIB knockout results in failure of lung CC maturation, and severe defects in development of the corpus callosum, CC specific midline glial populations, the hippocampus and the pons. GFAP CC expression is reduced in brains of NFIB-null mice (PubMed:15632069). CC Conditional NFIB knockdown in the telencephalon results in significant CC enlargement of the cerebral cortex with preservation of overall brain CC structure and inter-hemispheric connectivity (PubMed:30388402). CC {ECO:0000269|PubMed:15632069, ECO:0000269|PubMed:30388402}. CC -!- SIMILARITY: Belongs to the CTF/NF-I family. {ECO:0000255|PROSITE- CC ProRule:PRU00436}. 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; U57634; AAB49929.1; -; mRNA. DR EMBL; Y07685; CAA68949.1; -; mRNA. DR EMBL; Y07686; CAA68950.1; -; mRNA. DR EMBL; Y07687; CAA68951.1; -; mRNA. DR EMBL; BC014290; AAH14290.1; -; mRNA. DR EMBL; AF111264; AAD39099.1; -; Genomic_DNA. DR CCDS; CCDS38790.1; -. [P97863-3] DR CCDS; CCDS51213.1; -. [P97863-1] DR RefSeq; NP_001106680.1; NM_001113209.3. [P97863-1] DR RefSeq; NP_001273060.1; NM_001286131.2. [P97863-2] DR RefSeq; NP_032713.3; NM_008687.7. [P97863-3] DR AlphaFoldDB; P97863; -. DR SMR; P97863; -. DR BioGRID; 201747; 4. DR FunCoup; P97863; 1611. DR IntAct; P97863; 2. DR MINT; P97863; -. DR STRING; 10090.ENSMUSP00000052863; -. DR iPTMnet; P97863; -. DR PhosphoSitePlus; P97863; -. DR jPOST; P97863; -. DR PaxDb; 10090-ENSMUSP00000052863; -. DR ProteomicsDB; 287497; -. [P97863-1] DR ProteomicsDB; 287498; -. [P97863-2] DR ProteomicsDB; 287499; -. [P97863-3] DR Pumba; P97863; -. DR Antibodypedia; 1309; 242 antibodies from 33 providers. DR DNASU; 18028; -. DR Ensembl; ENSMUST00000050872.15; ENSMUSP00000052863.9; ENSMUSG00000008575.18. [P97863-1] DR Ensembl; ENSMUST00000064770.9; ENSMUSP00000067629.3; ENSMUSG00000008575.18. [P97863-3] DR GeneID; 18028; -. DR KEGG; mmu:18028; -. DR UCSC; uc008tjz.2; mouse. [P97863-1] DR UCSC; uc008tkd.3; mouse. [P97863-2] DR AGR; MGI:103188; -. DR CTD; 4781; -. DR MGI; MGI:103188; Nfib. DR VEuPathDB; HostDB:ENSMUSG00000008575; -. DR eggNOG; KOG3663; Eukaryota. DR GeneTree; ENSGT00950000182916; -. DR HOGENOM; CLU_012576_3_0_1; -. DR InParanoid; P97863; -. DR OMA; WHERDQX; -. DR OrthoDB; 10055441at2759; -. DR PhylomeDB; P97863; -. DR BioGRID-ORCS; 18028; 5 hits in 81 CRISPR screens. DR PRO; PR:P97863; -. DR Proteomes; UP000000589; Chromosome 4. DR RNAct; P97863; protein. DR Bgee; ENSMUSG00000008575; Expressed in rostral migratory stream and 287 other cell types or tissues. DR ExpressionAtlas; P97863; baseline and differential. DR GO; GO:0044300; C:cerebellar mossy fiber; IDA:UniProtKB. DR GO; GO:0001650; C:fibrillar center; ISO:GO_Central. DR GO; GO:0005654; C:nucleoplasm; ISO:GO_Central. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:UniProtKB. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:UniProtKB. DR GO; GO:0003690; F:double-stranded DNA binding; ISO:GO_Central. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI. DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:GO_Central. DR GO; GO:0021960; P:anterior commissure morphogenesis; IMP:UniProtKB. DR GO; GO:0007420; P:brain development; ISO:GO_Central. DR GO; GO:0060689; P:cell differentiation involved in salivary gland development; IMP:MGI. DR GO; GO:0021846; P:cell proliferation in forebrain; IMP:MGI. DR GO; GO:0002062; P:chondrocyte differentiation; IMP:UniProtKB. DR GO; GO:0060486; P:club cell differentiation; IMP:UniProtKB. DR GO; GO:0071679; P:commissural neuron axon guidance; IMP:UniProtKB. DR GO; GO:0010458; P:exit from mitosis; IMP:MGI. DR GO; GO:0030900; P:forebrain development; IMP:MGI. DR GO; GO:0010467; P:gene expression; IMP:MGI. DR GO; GO:0048699; P:generation of neurons; IMP:MGI. DR GO; GO:0010001; P:glial cell differentiation; IMP:UniProtKB. DR GO; GO:0021780; P:glial cell fate specification; IMP:MGI. DR GO; GO:0014009; P:glial cell proliferation; IMP:MGI. DR GO; GO:0030902; P:hindbrain development; IMP:MGI. DR GO; GO:0061141; P:lung ciliated cell differentiation; IMP:UniProtKB. DR GO; GO:0030324; P:lung development; IMP:MGI. DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:MGI. DR GO; GO:2000795; P:negative regulation of epithelial cell proliferation involved in lung morphogenesis; IMP:UniProtKB. DR GO; GO:2000791; P:negative regulation of mesenchymal cell proliferation involved in lung development; IMP:UniProtKB. DR GO; GO:1902894; P:negative regulation of miRNA transcription; ISO:GO_Central. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:GO_Central. DR GO; GO:0061351; P:neural precursor cell proliferation; IMP:MGI. DR GO; GO:0022008; P:neurogenesis; IMP:MGI. DR GO; GO:0048665; P:neuron fate specification; IMP:MGI. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISO:GO_Central. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0021740; P:principal sensory nucleus of trigeminal nerve development; IMP:UniProtKB. DR GO; GO:0031099; P:regeneration; IMP:MGI. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0009617; P:response to bacterium; IEP:MGI. DR GO; GO:0009611; P:response to wounding; IMP:MGI. DR GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI. DR GO; GO:0060662; P:salivary gland cavitation; IMP:MGI. DR GO; GO:0019827; P:stem cell population maintenance; IMP:MGI. DR GO; GO:0001894; P:tissue homeostasis; IMP:MGI. DR GO; GO:0060509; P:type I pneumocyte differentiation; IMP:UniProtKB. DR GO; GO:0060510; P:type II pneumocyte differentiation; IMP:UniProtKB. DR InterPro; IPR000647; CTF/NFI. DR InterPro; IPR020604; CTF/NFI_DNA-bd-dom. DR InterPro; IPR019739; CTF/NFI_DNA-bd_CS. DR InterPro; IPR019548; CTF/NFI_DNA-bd_N. DR InterPro; IPR003619; MAD_homology1_Dwarfin-type. DR PANTHER; PTHR11492:SF4; NUCLEAR FACTOR 1 B-TYPE; 1. DR PANTHER; PTHR11492; NUCLEAR FACTOR I; 1. DR Pfam; PF00859; CTF_NFI; 1. DR Pfam; PF03165; MH1; 1. DR Pfam; PF10524; NfI_DNAbd_pre-N; 1. DR SMART; SM00523; DWA; 1. DR PROSITE; PS00349; CTF_NFI_1; 1. DR PROSITE; PS51080; CTF_NFI_2; 1. PE 1: Evidence at protein level; KW Activator; Alternative splicing; DNA replication; DNA-binding; Methylation; KW Nucleus; Phosphoprotein; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1..570 FT /note="Nuclear factor 1 B-type" FT /id="PRO_0000100197" FT DNA_BIND 1..195 FT /note="CTF/NF-I" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00436" FT REGION 252..446 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 455..474 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 397..405 FT /note="9aaTAD" FT /evidence="ECO:0000250|UniProtKB:O00712" FT COMPBIAS 324..340 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 359..368 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 408..421 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 464..474 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 264 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O00712" FT MOD_RES 286 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 292 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:21183079" FT MOD_RES 295 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:15345747, FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079" FT MOD_RES 312 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 328 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O00712" FT MOD_RES 333 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O00712" FT MOD_RES 335 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 388 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT VAR_SEQ 416..498 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_003547" FT VAR_SEQ 416..420 FT /note="PNSSG -> SWYLG (in isoform 3)" FT /evidence="ECO:0000303|PubMed:9056636" FT /id="VSP_003548" FT VAR_SEQ 421..570 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:9056636" FT /id="VSP_003549" FT VARIANT 131 FT /note="D -> G (in strain: NIHSwiss)" SQ SEQUENCE 570 AA; 63507 MW; D94AB4400A2811CC CRC64; MMYSPICLTQ DEFHPFIEAL LPHVRAIAYT WFNLQARKRK YFKKHEKRMS KDEERAVKDE LLSEKPEIKQ KWASRLLAKL RKDIRQEYRE DFVLTVTGKK HPCCVLSNPD QKGKIRRIDC LRQADKVWRL DLVMVILFKG IPLESTDGER LMKSPHCTNP ALCVQPHHIT VSVKELDLFL AYYVQEQDSG QSGSPSHSDP AKNPPGYLED SFVKSGVFNV SELVRVSRTP ITQGTGVNFP IGEIPSQPYY HDMNSGVNLQ RSLSSPPSSK RPKTISIDEN MEPSPTGDFY PSPNSPAAGS RTWHERDQDM SSPTTMKKPE KPLFSSTSPQ DSSPRLSTFP QHHHPGIPGV AHSVISTRTP PPPSPLPFPT QAILPPAPSS YFSHPTIRYP PHLNPQDTLK NYVPSYDPSS PQTSQPNSSG QVVGKVPGHF TPVLAPSPHP SAVRPVTLTM TDTKPITTST EGEAASPTAT TYTASGTSQA NRYVGLSPRD PSFLHQQQLR ICDWTMNQNG RHLYPSTSED TLGITWQSPG TWASLVPFQV SNRTPILPAN VQNYGLNIIG EPFLQAETSN //