ID NFIX_MOUSE Reviewed; 488 AA. AC P70257; O08519; P70258; Q64192; Q99L78; Q9R1G2; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 16-JUN-2003, sequence version 2. DT 24-JAN-2024, entry version 186. DE RecName: Full=Nuclear factor 1 X-type; DE Short=NF1-X; DE Short=Nuclear factor 1/X; DE AltName: Full=CCAAT-box-binding transcription factor; DE Short=CTF; DE AltName: Full=Nuclear factor I/X; DE Short=NF-I/X; DE Short=NFI-X; DE AltName: Full=TGGCA-binding protein; GN Name=Nfix; 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] (ISOFORMS NFIX1; NFIX2 AND NFIX3), AND FUNCTION. RX PubMed=8581067; RA Nebl G., Cato A.C.B.; RT "NFI/X proteins: a class of NFI family of transcription factors with RT positive and negative regulatory domains."; RL Cell. Mol. Biol. Res. 41:85-95(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS NFIX1 AND NFIX2). 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 NFIX1). RC TISSUE=Mammary gland; 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 [MRNA] OF 4-488 (ISOFORM NFIX2). RC STRAIN=BALB/cJ; 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 [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 10-186. 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 [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280 AND SER-288, AND RP IDENTIFICATION BY 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 [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280; SER-301 AND SER-341, 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 SER-265; SER-280; SER-288; RP SER-301 AND SER-341, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301 AND RP SER-320 (ISOFORM NFIX2), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE RP 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 METHYLATION [LARGE SCALE ANALYSIS] AT ARG-343 AND ARG-390, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, and 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). CC -!- FUNCTION: Recognizes and binds the palindromic sequence 5'- CC TTGGCNNNNNGCCAA-3' present in viral and cellular promoters and in the CC origin of replication of adenovirus type 2. These proteins are CC individually capable of activating transcription and replication. CC Isoform NFIX1 acts as a transcriptional activator while isoform NFIX3 CC acts as a repressor. {ECO:0000269|PubMed:8581067}. CC -!- SUBUNIT: Binds DNA as a homodimer. CC -!- INTERACTION: CC P70257-2; Q60929: Mef2a; NbExp=2; IntAct=EBI-2639084, EBI-2639094; CC P70257-2; Q02111: Prkcq; NbExp=3; IntAct=EBI-2639084, EBI-2639157; CC P70257-2; Q02078: MEF2A; Xeno; NbExp=2; IntAct=EBI-2639084, EBI-2656305; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=NFIX3; CC IsoId=P70257-3; Sequence=Displayed; CC Name=NFIX1; CC IsoId=P70257-1; Sequence=VSP_007546, VSP_007547; CC Name=NFIX2; CC IsoId=P70257-2; Sequence=VSP_003563, VSP_007546, VSP_007547; 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:Q14938}. 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; S81451; AAB36083.2; -; mRNA. DR EMBL; Y07688; CAA68952.1; -; mRNA. DR EMBL; Y07689; CAA68953.1; -; mRNA. DR EMBL; BC003766; AAH03766.1; -; mRNA. DR EMBL; U57636; AAB49931.1; -; mRNA. DR EMBL; AF111266; AAD39101.1; -; Genomic_DNA. DR CCDS; CCDS40412.1; -. [P70257-2] DR CCDS; CCDS40413.1; -. [P70257-1] DR RefSeq; NP_001075451.1; NM_001081982.2. [P70257-1] DR RefSeq; NP_035036.1; NM_010906.3. [P70257-2] DR AlphaFoldDB; P70257; -. DR SMR; P70257; -. DR BioGRID; 201750; 32. DR IntAct; P70257; 5. DR MINT; P70257; -. DR STRING; 10090.ENSMUSP00000105386; -. DR GlyGen; P70257; 6 sites, 1 O-linked glycan (6 sites). DR iPTMnet; P70257; -. DR PhosphoSitePlus; P70257; -. DR jPOST; P70257; -. DR MaxQB; P70257; -. DR PaxDb; 10090-ENSMUSP00000105386; -. DR PeptideAtlas; P70257; -. DR ProteomicsDB; 287408; -. [P70257-3] DR ProteomicsDB; 287409; -. [P70257-1] DR ProteomicsDB; 287410; -. [P70257-2] DR Pumba; P70257; -. DR Antibodypedia; 7151; 161 antibodies from 26 providers. DR DNASU; 18032; -. DR Ensembl; ENSMUST00000076715.13; ENSMUSP00000076005.7; ENSMUSG00000001911.17. [P70257-2] DR Ensembl; ENSMUST00000099070.10; ENSMUSP00000096669.4; ENSMUSG00000001911.17. [P70257-1] DR GeneID; 18032; -. DR KEGG; mmu:18032; -. DR UCSC; uc009mne.2; mouse. [P70257-1] DR UCSC; uc009mnf.2; mouse. [P70257-2] DR AGR; MGI:97311; -. DR CTD; 4784; -. DR MGI; MGI:97311; Nfix. DR VEuPathDB; HostDB:ENSMUSG00000001911; -. DR eggNOG; KOG3663; Eukaryota. DR GeneTree; ENSGT00950000182916; -. DR InParanoid; P70257; -. DR OrthoDB; 5392447at2759; -. DR PhylomeDB; P70257; -. DR BioGRID-ORCS; 18032; 6 hits in 79 CRISPR screens. DR ChiTaRS; Nfix; mouse. DR PRO; PR:P70257; -. DR Proteomes; UP000000589; Chromosome 8. DR RNAct; P70257; Protein. DR Bgee; ENSMUSG00000001911; Expressed in rostral migratory stream and 253 other cell types or tissues. DR ExpressionAtlas; P70257; baseline and differential. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0003682; F:chromatin binding; IDA:MGI. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI. DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB. DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI. DR GO; GO:0048708; P:astrocyte differentiation; IMP:MGI. DR GO; GO:1905222; P:atrioventricular canal morphogenesis; IMP:MGI. DR GO; GO:0030282; P:bone mineralization; IMP:MGI. DR GO; GO:0007420; P:brain development; IMP:MGI. DR GO; GO:0048854; P:brain morphogenesis; IMP:MGI. DR GO; GO:0043010; P:camera-type eye development; IMP:MGI. DR GO; GO:0048469; P:cell maturation; IMP:MGI. DR GO; GO:0000902; P:cell morphogenesis; IMP:MGI. DR GO; GO:0021846; P:cell proliferation in forebrain; IDA:MGI. DR GO; GO:0071773; P:cellular response to BMP stimulus; IMP:MGI. DR GO; GO:0021696; P:cerebellar cortex morphogenesis; IMP:MGI. DR GO; GO:0021707; P:cerebellar granule cell differentiation; IMP:MGI. DR GO; GO:0021680; P:cerebellar Purkinje cell layer development; IMP:MGI. DR GO; GO:0021549; P:cerebellum development; IMP:MGI. DR GO; GO:0021987; P:cerebral cortex development; IMP:MGI. DR GO; GO:0048668; P:collateral sprouting; IMP:MGI. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR GO; GO:0043583; P:ear development; IMP:MGI. DR GO; GO:0001958; P:endochondral ossification; IMP:MGI. DR GO; GO:0060429; P:epithelium development; IMP:MGI. DR GO; GO:0010458; P:exit from mitosis; IMP:MGI. DR GO; GO:0030900; P:forebrain development; IMP:MGI. DR GO; GO:0021861; P:forebrain radial glial cell differentiation; IMP:MGI. DR GO; GO:0010467; P:gene expression; IDA:MGI. DR GO; GO:0048699; P:generation of neurons; IMP:MGI. DR GO; GO:0021782; P:glial cell development; IMP:MGI. DR GO; GO:0021780; P:glial cell fate specification; IMP:MGI. DR GO; GO:0014009; P:glial cell proliferation; IMP:MGI. DR GO; GO:0042063; P:gliogenesis; IDA:MGI. DR GO; GO:0021766; P:hippocampus development; IMP:MGI. DR GO; GO:0048873; P:homeostasis of number of cells within a tissue; IMP:MGI. DR GO; GO:0006954; P:inflammatory response; IMP:MGI. DR GO; GO:0021670; P:lateral ventricle development; IMP:MGI. DR GO; GO:0007612; P:learning; IMP:MGI. DR GO; GO:0030225; P:macrophage differentiation; IMP:MGI. DR GO; GO:0007613; P:memory; IMP:MGI. DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI. DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:MGI. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0061351; P:neural precursor cell proliferation; IMP:MGI. DR GO; GO:0014016; P:neuroblast differentiation; IMP:MGI. DR GO; GO:0097402; P:neuroblast migration; IMP:MGI. DR GO; GO:0007405; P:neuroblast proliferation; IMP:MGI. DR GO; GO:0022008; P:neurogenesis; IMP:MGI. DR GO; GO:0030182; P:neuron differentiation; IMP:MGI. DR GO; GO:0048665; P:neuron fate specification; IMP:MGI. DR GO; GO:0021772; P:olfactory bulb development; IMP:MGI. DR GO; GO:0048709; P:oligodendrocyte differentiation; IMP:MGI. DR GO; GO:0030316; P:osteoclast differentiation; IDA:MGI. DR GO; GO:0002158; P:osteoclast proliferation; IDA:MGI. DR GO; GO:0006909; P:phagocytosis; IMP:MGI. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB. 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:0009611; P:response to wounding; IMP:MGI. DR GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI. DR GO; GO:0007266; P:Rho protein signal transduction; IMP:MGI. DR GO; GO:0014816; P:skeletal muscle satellite cell differentiation; IMP:MGI. DR GO; GO:0007519; P:skeletal muscle tissue development; IMP:MGI. DR GO; GO:0043403; P:skeletal muscle tissue regeneration; IMP:MGI. DR GO; GO:0001501; P:skeletal system development; IMP:MGI. DR GO; GO:0035176; P:social behavior; IMP:MGI. DR GO; GO:0021510; P:spinal cord development; 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:0006366; P:transcription by RNA polymerase II; IDA:MGI. 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:SF3; NUCLEAR FACTOR 1 X-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. DR Genevisible; P70257; MM. PE 1: Evidence at protein level; KW Activator; Alternative splicing; DNA replication; DNA-binding; KW Isopeptide bond; Methylation; Nucleus; Phosphoprotein; Reference proteome; KW Repressor; Transcription; Transcription regulation; Ubl conjugation. FT CHAIN 1..488 FT /note="Nuclear factor 1 X-type" FT /id="PRO_0000100205" FT DNA_BIND 1..194 FT /note="CTF/NF-I" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00436" FT REGION 264..320 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 411..488 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 398..406 FT /note="9aaTAD" FT /evidence="ECO:0000250|UniProtKB:Q14938" FT COMPBIAS 301..315 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 411..425 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 430..445 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 448..478 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 265 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 280 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:15345747, FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079" FT MOD_RES 288 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:15345747, FT ECO:0007744|PubMed:21183079" FT MOD_RES 301 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:21183079" FT MOD_RES 341 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:21183079" FT MOD_RES 343 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 390 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT CROSSLNK 279 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q14938" FT VAR_SEQ 320..360 FT /note="Missing (in isoform NFIX2)" FT /evidence="ECO:0000303|PubMed:12568726, FT ECO:0000303|PubMed:8581067, ECO:0000303|PubMed:9056636" FT /id="VSP_003563" FT VAR_SEQ 419..441 FT /note="PNGSGQGKVPGSFLLPPPPPVAR -> HSQRQAPPLPTGLSASDPGTATF FT (in isoform NFIX1 and isoform NFIX2)" FT /evidence="ECO:0000303|PubMed:12568726, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8581067, FT ECO:0000303|PubMed:9056636" FT /id="VSP_007546" FT VAR_SEQ 442..488 FT /note="Missing (in isoform NFIX1 and isoform NFIX2)" FT /evidence="ECO:0000303|PubMed:12568726, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8581067, FT ECO:0000303|PubMed:9056636" FT /id="VSP_007547" FT CONFLICT 353 FT /note="V -> L (in Ref. 2; CAA68952)" FT /evidence="ECO:0000305" FT MOD_RES P70257-2:301 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES P70257-2:320 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" SQ SEQUENCE 488 AA; 53394 MW; 157F67EC17C96AD0 CRC64; MYSPYCLTQD EFHPFIEALL PHVRAFSYTW FNLQARKRKY FKKHEKRMSK DEERAVKDEL LGEKPEIKQK WASRLLAKLR KDIRPEFRED FVLTITGKKP PCCVLSNPDQ KGKIRRIDCL RQADKVWRLD LVMVILFKGI PLESTDGERL YKSPQCSNPG LCVQPHHIGV TIKELDLYLA YFVHTPESGQ SDSSNQQGDA DIKPLPNGHL SFQDCFVTSG VWNVTELVRV SQTPVATASG PNFSLADLES PSYYNINQVT LGRRSITSPP STSSTKRPKS IDDSEMESPV DDVFYPGTGR SPAAGSSQSS GWPNDVDAGP ASLKKSGKLD FCSALSSQGS SPRMAFTHHP LPVLAGVRPG SPRATASALH FPSTSIIQQS SPYFTHPTIR YHHHHGQDSL KEFVQFVCSD GSGQATGQPN GSGQGKVPGS FLLPPPPPVA RPVPLPMPDS KTTSTAPDGA ALTPPSPSFT TTGASSANRF VGIGPRDG //