NFIC_HUMAN
ID NFIC_HUMAN Reviewed; 508 AA.
AC P08651; A8K1H0; B7Z4U5; B7Z9C3; K7EMU1; P08652; Q14932; Q9UPJ3; Q9UPJ9;
AC Q9UPK0; Q9UPK1;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=Nuclear factor 1 C-type;
DE Short=NF1-C;
DE Short=Nuclear factor 1/C;
DE AltName: Full=CCAAT-box-binding transcription factor;
DE Short=CTF;
DE AltName: Full=Nuclear factor I/C;
DE Short=NF-I/C;
DE Short=NFI-C;
DE AltName: Full=TGGCA-binding protein;
GN Name=NFIC; Synonyms=NFI;
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; 2 AND 3), AND PARTIAL PROTEIN
RP SEQUENCE.
RX PubMed=3398920; DOI=10.1038/334218a0;
RA Santoro C., Mermod N., Andrews P.C., Tjian R.;
RT "A family of human CCAAT-box-binding proteins active in transcription and
RT DNA replication: cloning and expression of multiple cDNAs.";
RL Nature 334:218-224(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
RX PubMed=8710515; DOI=10.1093/nar/24.12.2416;
RA Wenzelides S., Altmann S., Wendler W., Winnacker E.L.;
RT "CTF5 -- a new transcriptional activator of the NFI/CTF family.";
RL Nucleic Acids Res. 24:2416-2421(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 6).
RC TISSUE=Caudate nucleus, Heart, and Uterus;
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 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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC TISSUE=Uterus;
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343, 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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-294; SER-323; SER-333 AND
RP SER-339, AND IDENTIFICATION BY MASS SPECTROMETRY [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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333, 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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-194; SER-323; SER-333; SER-337; SER-339; SER-343 AND
RP SER-487, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-305; SER-323; SER-333;
RP SER-339 AND SER-343, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194; SER-304; SER-333;
RP SER-339; SER-343; SER-475 AND SER-477, AND IDENTIFICATION BY MASS
RP 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 [15]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-365; ARG-395 AND ARG-451, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
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).
RN [16]
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 P08651; O00712: NFIB; NbExp=5; IntAct=EBI-741360, EBI-10963452;
CC P08651-5; P07101-3: TH; NbExp=3; IntAct=EBI-18939222, EBI-12001016;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=4;
CC IsoId=P08651-1; Sequence=Displayed;
CC Name=1;
CC IsoId=P08651-2; Sequence=VSP_003552;
CC Name=2;
CC IsoId=P08651-3; Sequence=VSP_003552, VSP_003555, VSP_003556;
CC Name=3;
CC IsoId=P08651-4; Sequence=VSP_003552, VSP_003553, VSP_003555,
CC VSP_003556;
CC Name=5;
CC IsoId=P08651-5; Sequence=VSP_003554;
CC Name=6;
CC IsoId=P08651-6; Sequence=VSP_047539;
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 -!- SIMILARITY: Belongs to the CTF/NF-I family. {ECO:0000255|PROSITE-
CC ProRule:PRU00436}.
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DR EMBL; X12492; CAA31012.1; -; mRNA.
DR EMBL; X92857; CAA63440.1; -; mRNA.
DR EMBL; AK289885; BAF82574.1; -; mRNA.
DR EMBL; AK297867; BAH12681.1; -; mRNA.
DR EMBL; AK304816; BAH14259.1; -; mRNA.
DR EMBL; AC005514; AAC32593.1; -; Genomic_DNA.
DR EMBL; AC005514; AAC32594.1; -; Genomic_DNA.
DR EMBL; AC005551; AAC33190.1; -; Genomic_DNA.
DR EMBL; AC005551; AAC33191.1; -; Genomic_DNA.
DR EMBL; AC005551; AAC33192.1; -; Genomic_DNA.
DR EMBL; AC005778; AAC62842.1; -; Genomic_DNA.
DR EMBL; CH471139; EAW69325.1; -; Genomic_DNA.
DR EMBL; CH471139; EAW69326.1; -; Genomic_DNA.
DR EMBL; BC012120; AAH12120.1; -; mRNA.
DR CCDS; CCDS12107.1; -. [P08651-5]
DR CCDS; CCDS45914.1; -. [P08651-2]
DR CCDS; CCDS58640.1; -. [P08651-3]
DR CCDS; CCDS59330.1; -. [P08651-1]
DR CCDS; CCDS59331.1; -. [P08651-6]
DR PIR; B33416; B33416.
DR PIR; S01038; S01038.
DR RefSeq; NP_001231931.1; NM_001245002.1. [P08651-1]
DR RefSeq; NP_001231933.1; NM_001245004.1. [P08651-6]
DR RefSeq; NP_001231934.1; NM_001245005.1. [P08651-3]
DR RefSeq; NP_005588.2; NM_005597.3. [P08651-5]
DR RefSeq; NP_995315.1; NM_205843.2. [P08651-2]
DR RefSeq; XP_016882324.1; XM_017026835.1. [P08651-6]
DR AlphaFoldDB; P08651; -.
DR BioGRID; 110854; 175.
DR DIP; DIP-44692N; -.
DR IntAct; P08651; 143.
DR MINT; P08651; -.
DR STRING; 9606.ENSP00000396843; -.
DR GlyGen; P08651; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P08651; -.
DR PhosphoSitePlus; P08651; -.
DR BioMuta; NFIC; -.
DR DMDM; 14195672; -.
DR EPD; P08651; -.
DR jPOST; P08651; -.
DR MassIVE; P08651; -.
DR MaxQB; P08651; -.
DR PaxDb; P08651; -.
DR PeptideAtlas; P08651; -.
DR PRIDE; P08651; -.
DR ProteomicsDB; 52148; -. [P08651-1]
DR ProteomicsDB; 52149; -. [P08651-2]
DR ProteomicsDB; 52150; -. [P08651-3]
DR ProteomicsDB; 52151; -. [P08651-4]
DR ProteomicsDB; 52152; -. [P08651-5]
DR Antibodypedia; 23195; 306 antibodies from 31 providers.
DR DNASU; 4782; -.
DR Ensembl; ENST00000341919.7; ENSP00000342194.2; ENSG00000141905.19. [P08651-5]
DR Ensembl; ENST00000395111.7; ENSP00000378543.2; ENSG00000141905.19. [P08651-3]
DR Ensembl; ENST00000443272.3; ENSP00000396843.2; ENSG00000141905.19. [P08651-1]
DR Ensembl; ENST00000586919.5; ENSP00000465177.1; ENSG00000141905.19. [P08651-4]
DR Ensembl; ENST00000589123.5; ENSP00000465655.1; ENSG00000141905.19. [P08651-2]
DR Ensembl; ENST00000590282.5; ENSP00000466647.1; ENSG00000141905.19. [P08651-6]
DR GeneID; 4782; -.
DR KEGG; hsa:4782; -.
DR MANE-Select; ENST00000443272.3; ENSP00000396843.2; NM_001245002.2; NP_001231931.1.
DR UCSC; uc002lxo.3; human. [P08651-1]
DR CTD; 4782; -.
DR DisGeNET; 4782; -.
DR GeneCards; NFIC; -.
DR HGNC; HGNC:7786; NFIC.
DR HPA; ENSG00000141905; Tissue enriched (skeletal).
DR MIM; 600729; gene.
DR neXtProt; NX_P08651; -.
DR OpenTargets; ENSG00000141905; -.
DR PharmGKB; PA31592; -.
DR VEuPathDB; HostDB:ENSG00000141905; -.
DR eggNOG; KOG3663; Eukaryota.
DR GeneTree; ENSGT00950000182916; -.
DR HOGENOM; CLU_012576_3_0_1; -.
DR InParanoid; P08651; -.
DR OMA; AQDEFHP; -.
DR OrthoDB; 967862at2759; -.
DR PhylomeDB; P08651; -.
DR PathwayCommons; P08651; -.
DR Reactome; R-HSA-73980; RNA Polymerase III Transcription Termination.
DR Reactome; R-HSA-749476; RNA Polymerase III Abortive And Retractive Initiation.
DR SignaLink; P08651; -.
DR SIGNOR; P08651; -.
DR BioGRID-ORCS; 4782; 25 hits in 1104 CRISPR screens.
DR ChiTaRS; NFIC; human.
DR GeneWiki; NFIC_(gene); -.
DR GenomeRNAi; 4782; -.
DR Pharos; P08651; Tbio.
DR PRO; PR:P08651; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P08651; protein.
DR Bgee; ENSG00000141905; Expressed in nipple and 203 other tissues.
DR ExpressionAtlas; P08651; baseline and differential.
DR Genevisible; P08651; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
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; IDA:NTNU_SB.
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 Acetylation; Activator; Alternative splicing; Direct protein sequencing;
KW DNA replication; DNA-binding; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..508
FT /note="Nuclear factor 1 C-type"
FT /id="PRO_0000100199"
FT DNA_BIND 1..195
FT /note="CTF/NF-I"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00436"
FT REGION 190..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 438..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 404..412
FT /note="9aaTAD"
FT /evidence="ECO:0000269|PubMed:31375868"
FT COMPBIAS 194..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 300
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P70255"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70255"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 305
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
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 337
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 339
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 343
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 365
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 365
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 395
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 451
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 475
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 477
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 487
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT VAR_SEQ 1..10
FT /note="MYSSPLCLTQ -> M (in isoform 1, isoform 2 and isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:3398920"
FT /id="VSP_003552"
FT VAR_SEQ 188..211
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:3398920"
FT /id="VSP_003553"
FT VAR_SEQ 424..508
FT /note="LNGSGQLKMPSHCLSAQMLAPPPPGLPRLALPPATKPATTSEGGATSPTSPS
FT YSPPDTSPANRSFVGLGPRDPAGIYQAQSWYLG -> PTLRPTRPLQTVPLWD (in
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047539"
FT VAR_SEQ 424..503
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8710515"
FT /id="VSP_003554"
FT VAR_SEQ 424..439
FT /note="LNGSGQLKMPSHCLSA -> PTLRPTRPLQTVPLWD (in isoform 2
FT and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:3398920"
FT /id="VSP_003555"
FT VAR_SEQ 440..508
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:3398920"
FT /id="VSP_003556"
FT VARIANT 417
FT /note="A -> S (in dbSNP:rs10412720)"
FT /id="VAR_057656"
FT CONFLICT 130
FT /note="L -> P (in Ref. 3; BAH12681)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="D -> V (in Ref. 2; CAA63440)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="E -> K (in Ref. 3; BAH12681)"
FT /evidence="ECO:0000305"
FT CONFLICT 353
FT /note="H -> Y (in Ref. 3; BAH12681)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 508 AA; 55675 MW; 3D0F97DA0F3AF992 CRC64;
MYSSPLCLTQ DEFHPFIEAL LPHVRAFAYT WFNLQARKRK YFKKHEKRMS KDEERAVKDE
LLGEKPEVKQ KWASRLLAKL RKDIRPECRE DFVLSITGKK APGCVLSNPD QKGKMRRIDC
LRQADKVWRL DLVMVILFKG IPLESTDGER LVKAAQCGHP VLCVQPHHIG VAVKELDLYL
AYFVRERDAE QSGSPRTGMG SDQEDSKPIT LDTTDFQESF VTSGVFSVTE LIQVSRTPVV
TGTGPNFSLG ELQGHLAYDL NPASTGLRRT LPSTSSSGSK RHKSGSMEED VDTSPGGDYY
TSPSSPTSSS RNWTEDMEGG ISSPVKKTEM DKSPFNSPSP QDSPRLSSFT QHHRPVIAVH
SGIARSPHPS SALHFPTTSI LPQTASTYFP HTAIRYPPHL NPQDPLKDLV SLACDPASQQ
PGPLNGSGQL KMPSHCLSAQ MLAPPPPGLP RLALPPATKP ATTSEGGATS PTSPSYSPPD
TSPANRSFVG LGPRDPAGIY QAQSWYLG
