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 27-MAR-2024, entry version 204. 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}; 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; 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 SMR; Q12857; -. DR BioGRID; 110847; 185. DR IntAct; Q12857; 135. DR MINT; Q12857; -. DR STRING; 9606.ENSP00000360231; -. DR GlyCosmos; Q12857; 3 sites, 2 glycans. DR GlyGen; Q12857; 13 sites, 2 O-linked glycans (13 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; 9606-ENSP00000360231; -. DR PeptideAtlas; Q12857; -. DR ProteomicsDB; 25418; -. DR ProteomicsDB; 30217; -. DR ProteomicsDB; 58986; -. [Q12857-1] DR ProteomicsDB; 58987; -. [Q12857-2] DR Pumba; Q12857; -. DR Antibodypedia; 1812; 321 antibodies from 31 providers. DR DNASU; 4774; -. DR Ensembl; ENST00000371187.7; ENSP00000360229.3; ENSG00000162599.18. [Q12857-2] DR Ensembl; ENST00000371189.8; ENSP00000360231.3; ENSG00000162599.18. [Q12857-4] DR Ensembl; ENST00000403491.8; ENSP00000384523.3; ENSG00000162599.18. [Q12857-1] DR Ensembl; ENST00000407417.7; ENSP00000384680.2; ENSG00000162599.18. [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 AGR; HGNC:7784; -. DR CTD; 4774; -. DR DisGeNET; 4774; -. DR GeneCards; NFIA; -. DR GeneReviews; NFIA; -. DR HGNC; HGNC:7784; NFIA. DR HPA; ENSG00000162599; Low tissue specificity. 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; 5392447at2759; -. 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; 23 hits in 1192 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 206 other cell types or tissues. DR ExpressionAtlas; Q12857; baseline and differential. 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:0030509; P:BMP signaling pathway; IEA:Ensembl. DR GO; GO:0051216; P:cartilage development; IEA:Ensembl. DR GO; GO:0000902; P:cell morphogenesis; IEA:Ensembl. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR GO; GO:0010458; P:exit from mitosis; IEA:Ensembl. DR GO; GO:0010467; P:gene expression; IEA:Ensembl. DR GO; GO:0021780; P:glial cell fate specification; IEA:Ensembl. DR GO; GO:0014009; P:glial cell proliferation; IEA:Ensembl. DR GO; GO:0035108; P:limb morphogenesis; IEA:Ensembl. DR GO; GO:0061351; P:neural precursor cell proliferation; IEA:Ensembl. DR GO; GO:0048665; P:neuron fate specification; IEA:Ensembl. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB. DR GO; GO:0006355; P:regulation of DNA-templated transcription; NAS:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0009611; P:response to wounding; IEA:Ensembl. DR GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl. 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:SF6; NUCLEAR FACTOR 1 A-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; Q12857; HS. 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 //