NFIX_MOUSE
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 03-AUG-2022, entry version 178.
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, Pancreas,
RC 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}.
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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 BioGRID; 201750; 32.
DR IntAct; P70257; 5.
DR MINT; P70257; -.
DR STRING; 10090.ENSMUSP00000105386; -.
DR iPTMnet; P70257; -.
DR PhosphoSitePlus; P70257; -.
DR jPOST; P70257; -.
DR MaxQB; P70257; -.
DR PaxDb; P70257; -.
DR PeptideAtlas; P70257; -.
DR PRIDE; P70257; -.
DR ProteomicsDB; 287408; -. [P70257-3]
DR ProteomicsDB; 287409; -. [P70257-1]
DR ProteomicsDB; 287410; -. [P70257-2]
DR Antibodypedia; 7151; 141 antibodies from 26 providers.
DR DNASU; 18032; -.
DR Ensembl; ENSMUST00000076715; ENSMUSP00000076005; ENSMUSG00000001911. [P70257-2]
DR Ensembl; ENSMUST00000099070; ENSMUSP00000096669; ENSMUSG00000001911. [P70257-1]
DR GeneID; 18032; -.
DR KEGG; mmu:18032; -.
DR UCSC; uc009mne.2; mouse. [P70257-1]
DR UCSC; uc009mnf.2; mouse. [P70257-2]
DR CTD; 4784; -.
DR MGI; MGI:97311; Nfix.
DR VEuPathDB; HostDB:ENSMUSG00000001911; -.
DR eggNOG; KOG3663; Eukaryota.
DR GeneTree; ENSGT00950000182916; -.
DR InParanoid; P70257; -.
DR OrthoDB; 967862at2759; -.
DR PhylomeDB; P70257; -.
DR BioGRID-ORCS; 18032; 6 hits in 74 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 251 other tissues.
DR ExpressionAtlas; P70257; baseline and differential.
DR Genevisible; P70257; MM.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IBA:GO_Central.
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: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:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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; PTHR11492; 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;
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
