NFIA_HUMAN
ID NFIA_HUMAN Reviewed; 509 AA.
AC Q12857; B4DRJ3; B4DS53; F5H0R0; F8W8W3; Q8TA97; Q9H3X9; Q9P2A9;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Nuclear factor 1 A-type;
DE Short=NF1-A;
DE Short=Nuclear factor 1/A;
DE AltName: Full=CCAAT-box-binding transcription factor;
DE Short=CTF;
DE AltName: Full=Nuclear factor I/A;
DE Short=NF-I/A;
DE Short=NFI-A;
DE AltName: Full=TGGCA-binding protein;
GN Name=NFIA; Synonyms=KIAA1439;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Skeletal muscle;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 19-243.
RX PubMed=7590749; DOI=10.1006/geno.1995.1107;
RA Qian F., Kruse U., Lichter P., Sippel A.E.;
RT "Chromosomal localization of the four genes (NFIA, B, C, and X) for the
RT human transcription factor nuclear factor I by FISH.";
RL Genomics 28:66-73(1995).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258; SER-265; SER-280;
RP SER-287; SER-300 AND SER-319, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280 AND SER-287, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-265; SER-280; SER-287;
RP SER-300 AND SER-360, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280; SER-287 AND SER-300, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP INVOLVEMENT IN BRMUTD.
RX PubMed=24462883; DOI=10.1016/j.ejmg.2013.12.011;
RA Rao A., O'Donnell S., Bain N., Meldrum C., Shorter D., Goel H.;
RT "An intragenic deletion of the NFIA gene in a patient with a hypoplastic
RT corpus callosum, craniofacial abnormalities and urinary tract defects.";
RL Eur. J. Med. Genet. 57:65-70(2014).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-265; SER-280; SER-287;
RP SER-300; SER-469 AND THR-471, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT
RP SER-469 (ISOFORM 2), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP INVOLVEMENT IN BRMUTD.
RX PubMed=27081522; DOI=10.1038/hgv.2015.7;
RA Negishi Y., Miya F., Hattori A., Mizuno K., Hori I., Ando N., Okamoto N.,
RA Kato M., Tsunoda T., Yamasaki M., Kanemura Y., Kosaki K., Saitoh S.;
RT "Truncating mutation in NFIA causes brain malformation and urinary tract
RT defects.";
RL Hum. Genome Var. 2:15007-15007(2015).
RN [15]
RP 9AATAD MOTIF.
RX PubMed=31375868; DOI=10.1007/s00018-019-03251-w;
RA Piskacek M., Havelka M., Jendruchova K., Knight A., Keegan L.P.;
RT "The evolution of the 9aaTAD domain in Sp2 proteins: inactivation with
RT valines and intron reservoirs.";
RL Cell. Mol. Life Sci. 77:1793-1810(2020).
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 -!- SUBUNIT: Binds DNA as a homodimer.
CC -!- INTERACTION:
CC Q12857-2; Q9H0R8: GABARAPL1; NbExp=3; IntAct=EBI-12119652, EBI-746969;
CC Q12857-2; A0A0S2Z4H3: NFIB; NbExp=3; IntAct=EBI-12119652, EBI-16430952;
CC Q12857-2; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-12119652, EBI-742388;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q12857-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q12857-2; Sequence=VSP_036620;
CC Name=3;
CC IsoId=Q12857-3; Sequence=VSP_046884;
CC Name=4;
CC IsoId=Q12857-4; Sequence=VSP_046883;
CC -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC number of yeast and animal transcription factors.
CC {ECO:0000269|PubMed:31375868}.
CC -!- DISEASE: Brain malformations with or without urinary tract defects
CC (BRMUTD) [MIM:613735]: A syndrome characterized by corpus callosum
CC hypoplasia or agenesis, hydrocephalus or ventricular enlargement,
CC developmental delay, and urinary tract defects.
CC {ECO:0000269|PubMed:24462883, ECO:0000269|PubMed:27081522}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the CTF/NF-I family. {ECO:0000255|PROSITE-
CC ProRule:PRU00436}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA92677.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB037860; BAA92677.1; ALT_INIT; mRNA.
DR EMBL; AK299289; BAG61305.1; -; mRNA.
DR EMBL; AK299579; BAG61515.1; -; mRNA.
DR EMBL; AC092784; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC096534; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC096947; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC099792; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL096888; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL355795; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL445198; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL445432; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX06601.1; -; Genomic_DNA.
DR EMBL; BC022264; AAH22264.1; -; mRNA.
DR EMBL; U07809; AAA93124.1; -; mRNA.
DR CCDS; CCDS44156.1; -. [Q12857-1]
DR CCDS; CCDS53321.1; -. [Q12857-3]
DR CCDS; CCDS53322.1; -. [Q12857-4]
DR CCDS; CCDS615.1; -. [Q12857-2]
DR RefSeq; NP_001128145.1; NM_001134673.3. [Q12857-1]
DR RefSeq; NP_001138983.1; NM_001145511.1. [Q12857-3]
DR RefSeq; NP_001138984.1; NM_001145512.1. [Q12857-4]
DR RefSeq; NP_005586.1; NM_005595.4. [Q12857-2]
DR AlphaFoldDB; Q12857; -.
DR BioGRID; 110847; 179.
DR IntAct; Q12857; 134.
DR MINT; Q12857; -.
DR STRING; 9606.ENSP00000360231; -.
DR GlyGen; Q12857; 3 sites, 2 O-linked glycans (3 sites).
DR iPTMnet; Q12857; -.
DR PhosphoSitePlus; Q12857; -.
DR BioMuta; NFIA; -.
DR DMDM; 14194959; -.
DR EPD; Q12857; -.
DR jPOST; Q12857; -.
DR MassIVE; Q12857; -.
DR MaxQB; Q12857; -.
DR PaxDb; Q12857; -.
DR PeptideAtlas; Q12857; -.
DR PRIDE; Q12857; -.
DR ProteomicsDB; 25418; -.
DR ProteomicsDB; 30217; -.
DR ProteomicsDB; 58986; -. [Q12857-1]
DR ProteomicsDB; 58987; -. [Q12857-2]
DR Antibodypedia; 1812; 290 antibodies from 31 providers.
DR DNASU; 4774; -.
DR Ensembl; ENST00000371187.7; ENSP00000360229.3; ENSG00000162599.17. [Q12857-2]
DR Ensembl; ENST00000371189.8; ENSP00000360231.3; ENSG00000162599.17. [Q12857-4]
DR Ensembl; ENST00000403491.8; ENSP00000384523.3; ENSG00000162599.17. [Q12857-1]
DR Ensembl; ENST00000407417.7; ENSP00000384680.2; ENSG00000162599.17. [Q12857-3]
DR GeneID; 4774; -.
DR KEGG; hsa:4774; -.
DR MANE-Select; ENST00000403491.8; ENSP00000384523.3; NM_001134673.4; NP_001128145.1.
DR UCSC; uc001czv.4; human. [Q12857-1]
DR CTD; 4774; -.
DR DisGeNET; 4774; -.
DR GeneCards; NFIA; -.
DR GeneReviews; NFIA; -.
DR HGNC; HGNC:7784; NFIA.
DR HPA; ENSG00000162599; Tissue enhanced (brain).
DR MalaCards; NFIA; -.
DR MIM; 600727; gene.
DR MIM; 613735; phenotype.
DR neXtProt; NX_Q12857; -.
DR OpenTargets; ENSG00000162599; -.
DR Orphanet; 401986; 1p31p32 microdeletion syndrome.
DR PharmGKB; PA31590; -.
DR VEuPathDB; HostDB:ENSG00000162599; -.
DR eggNOG; KOG3663; Eukaryota.
DR GeneTree; ENSGT00950000182916; -.
DR InParanoid; Q12857; -.
DR OMA; XSPHATP; -.
DR OrthoDB; 967862at2759; -.
DR PhylomeDB; Q12857; -.
DR TreeFam; TF313889; -.
DR PathwayCommons; Q12857; -.
DR Reactome; R-HSA-73980; RNA Polymerase III Transcription Termination.
DR Reactome; R-HSA-749476; RNA Polymerase III Abortive And Retractive Initiation.
DR SignaLink; Q12857; -.
DR SIGNOR; Q12857; -.
DR BioGRID-ORCS; 4774; 15 hits in 1105 CRISPR screens.
DR ChiTaRS; NFIA; human.
DR GeneWiki; NFIA; -.
DR GenomeRNAi; 4774; -.
DR Pharos; Q12857; Tbio.
DR PRO; PR:Q12857; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q12857; protein.
DR Bgee; ENSG00000162599; Expressed in medial globus pallidus and 204 other tissues.
DR ExpressionAtlas; Q12857; baseline and differential.
DR Genevisible; Q12857; HS.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; NAS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
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 GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
DR GO; GO:0060074; P:synapse maturation; IEA:Ensembl.
DR GO; GO:0072189; P:ureter development; IEA:Ensembl.
DR GO; GO:0019079; P:viral genome replication; NAS: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; 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; Methylation;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..509
FT /note="Nuclear factor 1 A-type"
FT /id="PRO_0000100191"
FT DNA_BIND 1..194
FT /note="CTF/NF-I"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00436"
FT REGION 189..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 394..402
FT /note="9aaTAD"
FT /evidence="ECO:0000269|PubMed:31375868"
FT COMPBIAS 259..276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..457
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 287
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 305
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09414"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 389
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q02780"
FT MOD_RES 469
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 471
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..9
FT /note="MYSPLCLTQ -> M (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046884"
FT VAR_SEQ 1
FT /note="M -> MQMCRPASSSVLYVPTRWPGGCGATWQSCPSPPPRRTRIPQRPAVM
FT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046883"
FT VAR_SEQ 474..509
FT /note="TYSTPSTSPANRFVSVGPRDPSFVNIPQQTQSWYLG -> ILVPGIKVAASH
FT HPPDRPPDPFSTL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_036620"
FT CONFLICT 143
FT /note="E -> G (in Ref. 2; BAG61305)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="A -> G (in Ref. 6; AAA93124)"
FT /evidence="ECO:0000305"
FT CONFLICT 240..243
FT /note="TGPN -> PAPT (in Ref. 6; AAA93124)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="S -> P (in Ref. 2; BAG61515)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="F -> L (in Ref. 2; BAG61305)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="R -> G (in Ref. 2; BAG61305)"
FT /evidence="ECO:0000305"
FT CONFLICT 426
FT /note="K -> R (in Ref. 2; BAG61305)"
FT /evidence="ECO:0000305"
FT MOD_RES Q12857-2:469
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
SQ SEQUENCE 509 AA; 55944 MW; 42090C6B8B229F87 CRC64;
MYSPLCLTQD EFHPFIEALL PHVRAFAYTW FNLQARKRKY FKKHEKRMSK EEERAVKDEL
LSEKPEVKQK WASRLLAKLR KDIRPEYRED FVLTVTGKKP PCCVLSNPDQ KGKMRRIDCL
RQADKVWRLD LVMVILFKGI PLESTDGERL VKSPQCSNPG LCVQPHHIGV SVKELDLYLA
YFVHAADSSQ SESPSQPSDA DIKDQPENGH LGFQDSFVTS GVFSVTELVR VSQTPIAAGT
GPNFSLSDLE SSSYYSMSPG AMRRSLPSTS STSSTKRLKS VEDEMDSPGE EPFYTGQGRS
PGSGSQSSGW HEVEPGMPSP TTLKKSEKSG FSSPSPSQTS SLGTAFTQHH RPVITGPRAS
PHATPSTLHF PTSPIIQQPG PYFSHPAIRY HPQETLKEFV QLVCPDAGQQ AGQVGFLNPN
GSSQGKVHNP FLPTPMLPPP PPPPMARPVP LPVPDTKPPT TSTEGGAASP TSPTYSTPST
SPANRFVSVG PRDPSFVNIP QQTQSWYLG
