NFIX_HUMAN
ID NFIX_HUMAN Reviewed; 502 AA.
AC Q14938; B4DM25; O60413; Q0VG09; Q12859; Q13050; Q13052; Q5U094; Q9UPH1;
AC Q9Y6R8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 196.
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 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 [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Foreskin;
RX PubMed=7937100; DOI=10.1093/nar/22.19.3825;
RA Apt D., Liu Y., Bernard H.U.;
RT "Cloning and functional analysis of spliced isoforms of human nuclear
RT factor I-X: interference with transcriptional activation by NFI/CTF in a
RT cell-type specific manner.";
RL Nucleic Acids Res. 22:3825-3833(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4 AND 5).
RC TISSUE=Brain;
RX PubMed=8799200; DOI=10.3109/13550289609146542;
RA Sumner C., Shinohara T., Durham L., Traub R., Major E.O., Amemiya K.;
RT "Expression of multiple classes of the nuclear factor-1 family in the
RT developing human brain: differential expression of two classes of NF-1
RT genes.";
RL J. Neurovirol. 2:87-100(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [6]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC TISSUE=Brain;
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 19-228.
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280, AND IDENTIFICATION BY
RP 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 INVOLVEMENT IN MALNS AND MRSHSS, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=20673863; DOI=10.1016/j.ajhg.2010.07.001;
RA Malan V., Rajan D., Thomas S., Shaw A.C., Louis Dit Picard H., Layet V.,
RA Till M., van Haeringen A., Mortier G., Nampoothiri S., Puseljic S.,
RA Legeai-Mallet L., Carter N.P., Vekemans M., Munnich A., Hennekam R.C.,
RA Colleaux L., Cormier-Daire V.;
RT "Distinct effects of allelic NFIX mutations on nonsense-mediated mRNA decay
RT engender either a Sotos-like or a Marshall-Smith syndrome.";
RL Am. J. Hum. Genet. 87:189-198(2010).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-265, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE 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 [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-279, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [14]
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).
RN [15]
RP VARIANTS MALNS PRO-60 AND PRO-121.
RX PubMed=22301465; DOI=10.1038/jhg.2012.7;
RA Yoneda Y., Saitsu H., Touyama M., Makita Y., Miyamoto A., Hamada K.,
RA Kurotaki N., Tomita H., Nishiyama K., Tsurusaki Y., Doi H., Miyake N.,
RA Ogata K., Naritomi K., Matsumoto N.;
RT "Missense mutations in the DNA-binding/dimerization domain of NFIX cause
RT Sotos-like features.";
RL J. Hum. Genet. 57:207-211(2012).
RN [16]
RP VARIANTS MALNS PRO-116 AND GLU-125.
RX PubMed=26193383; DOI=10.1016/j.ejmg.2015.06.009;
RA Gurrieri F., Cavaliere M.L., Wischmeijer A., Mammi C., Neri G.,
RA Pisanti M.A., Rodella G., Lagana C., Priolo M.;
RT "NFIX mutations affecting the DNA-binding domain cause a peculiar
RT overgrowth syndrome (Malan syndrome): a new patients series.";
RL Eur. J. Med. Genet. 58:488-491(2015).
RN [17]
RP INVOLVEMENT IN MRSHSS, AND VARIANTS MALNS CYS-38 AND PRO-54.
RX PubMed=26200704; DOI=10.1038/pr.2015.135;
RA Martinez F., Marin-Reina P., Sanchis-Calvo A., Perez-Aytes A., Oltra S.,
RA Rosello M., Mayo S., Monfort S., Pantoja J., Orellana C.;
RT "Novel mutations of NFIX gene causing Marshall-Smith syndrome or Sotos-like
RT syndrome: one gene, two phenotypes.";
RL Pediatr. Res. 78:533-539(2015).
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 Q14938; Q2TAL8: QRICH1; NbExp=3; IntAct=EBI-8476987, EBI-2798044;
CC Q14938; Q8N883: ZNF614; NbExp=3; IntAct=EBI-8476987, EBI-9675993;
CC Q14938-3; P40763: STAT3; NbExp=3; IntAct=EBI-20559045, EBI-518675;
CC Q14938-4; P40763: STAT3; NbExp=3; IntAct=EBI-20558886, EBI-518675;
CC Q14938-5; P40692: MLH1; NbExp=3; IntAct=EBI-12024662, EBI-744248;
CC Q14938-5; A0A0S2Z4H3: NFIB; NbExp=3; IntAct=EBI-12024662, EBI-16430952;
CC Q14938-5; Q2TAL8: QRICH1; NbExp=3; IntAct=EBI-12024662, EBI-2798044;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q14938-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14938-2; Sequence=VSP_003560;
CC Name=3;
CC IsoId=Q14938-3; Sequence=VSP_003561, VSP_003562;
CC Name=4;
CC IsoId=Q14938-4; Sequence=VSP_003558;
CC Name=5;
CC IsoId=Q14938-5; Sequence=VSP_003559, VSP_003561, VSP_003562;
CC Name=6;
CC IsoId=Q14938-6; Sequence=VSP_003558, VSP_003561, VSP_003562;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:20673863}.
CC -!- DEVELOPMENTAL STAGE: Prominent expression is observed in the central
CC and peripheral nervous system in the embryo at Carnagie stage 17 (CS17;
CC gestational day 42); at this stage it is also observed in the
CC mandibular arch, cartilage primordium of the humerus, scapula, and
CC vertebrae; in the limb expression is detected in the perichondrium.
CC Expressed in the cerebral cortex, hippocampus, and faintly in the
CC thalamus in fetal brain at 22 weeks of gestation,.
CC {ECO:0000269|PubMed:20673863}.
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: Malan syndrome (MALNS) [MIM:614753]: An autosomal dominant
CC syndrome characterized by overgrowth, advanced bone age, macrocephaly,
CC impaired intellectual development, behavior anomalies, and dysmorphic
CC facial features. Patients develop marfanoid habitus, with long and
CC slender body, very low body mass, long narrow face, and arachnodactyly.
CC {ECO:0000269|PubMed:20673863, ECO:0000269|PubMed:22301465,
CC ECO:0000269|PubMed:26193383, ECO:0000269|PubMed:26200704}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Marshall-Smith syndrome (MRSHSS) [MIM:602535]: A distinct
CC malformation syndrome characterized by accelerated skeletal maturation,
CC relative failure to thrive, respiratory difficulties, intellectual
CC disability, and unusual facies, including prominent forehead, shallow
CC orbits, blue sclerae, depressed nasal bridge, and micrognathia.
CC Additional skeletal findings include long and thin tubular bones, broad
CC middle phalanges with relatively narrow distal phalanges, and
CC scoliosis. Inheritance is autosomal dominant.
CC {ECO:0000269|PubMed:20673863, ECO:0000269|PubMed:26200704}. 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}.
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DR EMBL; L31881; AAA53422.1; -; mRNA.
DR EMBL; U18759; AAB52369.1; -; mRNA.
DR EMBL; U18761; AAB52371.1; -; mRNA.
DR EMBL; AK297261; BAG59737.1; -; mRNA.
DR EMBL; BT019732; AAV38537.1; -; mRNA.
DR EMBL; AC004660; AAC15752.1; -; Genomic_DNA.
DR EMBL; AC007787; AAD38240.1; -; Genomic_DNA.
DR EMBL; AC007787; AAD38241.1; -; Genomic_DNA.
DR EMBL; CH471106; EAW84340.1; -; Genomic_DNA.
DR EMBL; BC117113; AAI17114.1; -; mRNA.
DR EMBL; BC117115; AAI17116.1; -; mRNA.
DR EMBL; U07811; AAA93126.1; -; mRNA.
DR CCDS; CCDS45996.1; -. [Q14938-3]
DR CCDS; CCDS59359.1; -. [Q14938-6]
DR PIR; S50112; S50112.
DR RefSeq; NP_001257973.1; NM_001271044.2. [Q14938-6]
DR RefSeq; NP_002492.2; NM_002501.3. [Q14938-3]
DR RefSeq; XP_005259975.1; XM_005259918.4.
DR AlphaFoldDB; Q14938; -.
DR BioGRID; 110856; 196.
DR IntAct; Q14938; 173.
DR MINT; Q14938; -.
DR STRING; 9606.ENSP00000380781; -.
DR GlyGen; Q14938; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q14938; -.
DR PhosphoSitePlus; Q14938; -.
DR BioMuta; NFIX; -.
DR DMDM; 14195678; -.
DR EPD; Q14938; -.
DR jPOST; Q14938; -.
DR MassIVE; Q14938; -.
DR MaxQB; Q14938; -.
DR PaxDb; Q14938; -.
DR PeptideAtlas; Q14938; -.
DR PRIDE; Q14938; -.
DR ProteomicsDB; 60247; -. [Q14938-1]
DR ProteomicsDB; 60248; -. [Q14938-2]
DR ProteomicsDB; 60249; -. [Q14938-3]
DR ProteomicsDB; 60250; -. [Q14938-4]
DR ProteomicsDB; 60251; -. [Q14938-5]
DR Antibodypedia; 7151; 141 antibodies from 26 providers.
DR DNASU; 4784; -.
DR Ensembl; ENST00000397661.6; ENSP00000380781.2; ENSG00000008441.19. [Q14938-3]
DR Ensembl; ENST00000585575.5; ENSP00000468794.1; ENSG00000008441.19. [Q14938-4]
DR Ensembl; ENST00000587260.1; ENSP00000467785.1; ENSG00000008441.19. [Q14938-5]
DR Ensembl; ENST00000587760.5; ENSP00000466389.1; ENSG00000008441.19. [Q14938-6]
DR Ensembl; ENST00000592199.6; ENSP00000467512.1; ENSG00000008441.19. [Q14938-1]
DR GeneID; 4784; -.
DR KEGG; hsa:4784; -.
DR MANE-Select; ENST00000592199.6; ENSP00000467512.1; NM_001365902.3; NP_001352831.1.
DR UCSC; uc002mwd.4; human. [Q14938-1]
DR CTD; 4784; -.
DR DisGeNET; 4784; -.
DR GeneCards; NFIX; -.
DR HGNC; HGNC:7788; NFIX.
DR HPA; ENSG00000008441; Tissue enhanced (skeletal).
DR MalaCards; NFIX; -.
DR MIM; 164005; gene.
DR MIM; 602535; phenotype.
DR MIM; 614753; phenotype.
DR neXtProt; NX_Q14938; -.
DR OpenTargets; ENSG00000008441; -.
DR Orphanet; 447980; 19p13.3 microduplication syndrome.
DR Orphanet; 420179; Malan overgrowth syndrome.
DR Orphanet; 561; Marshall-Smith syndrome.
DR PharmGKB; PA31594; -.
DR VEuPathDB; HostDB:ENSG00000008441; -.
DR eggNOG; KOG3663; Eukaryota.
DR GeneTree; ENSGT00950000182916; -.
DR InParanoid; Q14938; -.
DR OMA; NDVDAGM; -.
DR OrthoDB; 967862at2759; -.
DR PhylomeDB; Q14938; -.
DR TreeFam; TF313889; -.
DR PathwayCommons; Q14938; -.
DR Reactome; R-HSA-73980; RNA Polymerase III Transcription Termination.
DR Reactome; R-HSA-749476; RNA Polymerase III Abortive And Retractive Initiation.
DR SignaLink; Q14938; -.
DR SIGNOR; Q14938; -.
DR BioGRID-ORCS; 4784; 15 hits in 1102 CRISPR screens.
DR ChiTaRS; NFIX; human.
DR GeneWiki; NFIX; -.
DR GenomeRNAi; 4784; -.
DR Pharos; Q14938; Tbio.
DR PRO; PR:Q14938; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q14938; protein.
DR Bgee; ENSG00000008441; Expressed in cortical plate and 186 other tissues.
DR ExpressionAtlas; Q14938; baseline and differential.
DR Genevisible; Q14938; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:ProtInc.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
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:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
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; Disease variant; DNA replication;
KW DNA-binding; Isopeptide bond; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..502
FT /note="Nuclear factor 1 X-type"
FT /id="PRO_0000100203"
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..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 398..406
FT /note="9aaTAD"
FT /evidence="ECO:0000269|PubMed:31375868"
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..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70257"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70257"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70257"
FT MOD_RES 343
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P70257"
FT MOD_RES 390
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P70257"
FT CROSSLNK 279
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..9
FT /note="MYSPYCLTQ -> M (in isoform 4 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:8799200"
FT /id="VSP_003558"
FT VAR_SEQ 1..8
FT /note="MYSPYCLT -> MLPACRL (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8799200"
FT /id="VSP_003559"
FT VAR_SEQ 318..359
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7937100"
FT /id="VSP_003560"
FT VAR_SEQ 419..441
FT /note="PNGSGQGKVPGSFLLPPPPPVAR -> HSQRQAPPLPTGLSASDPGTATF
FT (in isoform 3, isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8799200,
FT ECO:0000303|Ref.4"
FT /id="VSP_003561"
FT VAR_SEQ 442..502
FT /note="Missing (in isoform 3, isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8799200,
FT ECO:0000303|Ref.4"
FT /id="VSP_003562"
FT VARIANT 38
FT /note="R -> C (in MALNS)"
FT /evidence="ECO:0000269|PubMed:26200704"
FT /id="VAR_077571"
FT VARIANT 54
FT /note="R -> P (in MALNS)"
FT /evidence="ECO:0000269|PubMed:26200704"
FT /id="VAR_077572"
FT VARIANT 60
FT /note="L -> P (in MALNS; dbSNP:rs387907254)"
FT /evidence="ECO:0000269|PubMed:22301465"
FT /id="VAR_068720"
FT VARIANT 116
FT /note="R -> P (in MALNS)"
FT /evidence="ECO:0000269|PubMed:26193383"
FT /id="VAR_077573"
FT VARIANT 121
FT /note="R -> P (in MALNS; dbSNP:rs387907255)"
FT /evidence="ECO:0000269|PubMed:22301465"
FT /id="VAR_068721"
FT VARIANT 125
FT /note="K -> E (in MALNS)"
FT /evidence="ECO:0000269|PubMed:26193383"
FT /id="VAR_077574"
FT CONFLICT 91
FT /note="F -> Y (in Ref. 1; AAA53422)"
FT /evidence="ECO:0000305"
FT CONFLICT 399
FT /note="S -> P (in Ref. 3; BAG59737)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 502 AA; 55098 MW; 55B40A7DC505EA21 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 STSTTKRPKS IDDSEMESPV DDVFYPGTGR
SPAAGSSQSS GWPNDVDAGP ASLKKSGKLD FCSALSSQGS SPRMAFTHHP LPVLAGVRPG
SPRATASALH FPSTSIIQQS SPYFTHPTIR YHHHHGQDSL KEFVQFVCSD GSGQATGQPN
GSGQGKVPGS FLLPPPPPVA RPVPLPMPDS KSTSTAPDGA ALTPPSPSFA TTGASSANRF
VSIGPRDGNF LNIPQQSQSW FL
