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NFIB_HUMAN
ID   NFIB_HUMAN              Reviewed;         420 AA.
AC   O00712; G3V1P1; H7BYE8; O00166; Q12858; Q5VW29; Q63HM5; Q6ZNF9; Q96J45;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2004, sequence version 2.
DT   03-AUG-2022, entry version 190.
DE   RecName: Full=Nuclear factor 1 B-type;
DE            Short=NF1-B;
DE            Short=Nuclear factor 1/B;
DE   AltName: Full=CCAAT-box-binding transcription factor;
DE            Short=CTF;
DE   AltName: Full=Nuclear factor I/B;
DE            Short=NF-I/B;
DE            Short=NFI-B;
DE   AltName: Full=TGGCA-binding protein;
GN   Name=NFIB;
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] (ISOFORM 1).
RX   PubMed=9484777; DOI=10.1038/sj.onc.1201609;
RA   Geurts J.M.W., Schoenmakers E.F.P.M., Roijer E., Astroem A.-K., Stenman G.,
RA   van de Ven W.J.M.;
RT   "Identification of NFIB as recurrent translocation partner gene of HMGIC in
RT   pleomorphic adenomas.";
RL   Oncogene 16:865-872(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC   TISSUE=Foreskin;
RX   PubMed=9099724; DOI=10.1074/jbc.272.16.10739;
RA   Liu Y., Bernard H.U., Apt D.;
RT   "NFI-B3, a novel transcriptional repressor of the nuclear factor I family,
RT   is generated by alternative RNA processing.";
RL   J. Biol. Chem. 272:10739-10745(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   TISSUE=Amygdala;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 6).
RC   TISSUE=Colon epithelium;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA   Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA   Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA   Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA   Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA   Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA   Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA   Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA   Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA   Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA   McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA   Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA   Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA   Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA   Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA   West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA   Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA   Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton 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   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Cervix;
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   [9]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 20-283.
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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264 AND SER-328, AND
RP   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-312; SER-328 AND SER-333, AND
RP   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   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312; SER-328 AND SER-333, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
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   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-292 AND SER-295, AND
RP   IDENTIFICATION BY 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   [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   FUNCTION, INVOLVEMENT IN MACID, VARIANTS MACID 37-ARG--GLY-420 DEL;
RP   89-ARG--GLY-420 DEL; THR-114; GLU-126; PRO-132 AND LEU-356, AND
RP   CHARACTERIZATION OF VARIANTS MACID THR-114; GLU-126; PRO-132 AND LEU-356.
RX   PubMed=30388402; DOI=10.1016/j.ajhg.2018.10.006;
RA   Schanze I., Bunt J., Lim J.W.C., Schanze D., Dean R.J., Alders M.,
RA   Blanchet P., Attie-Bitach T., Berland S., Boogert S., Boppudi S.,
RA   Bridges C.J., Cho M.T., Dobyns W.B., Donnai D., Douglas J., Earl D.L.,
RA   Edwards T.J., Faivre L., Fregeau B., Genevieve D., Gerard M., Gatinois V.,
RA   Holder-Espinasse M., Huth S.F., Izumi K., Kerr B., Lacaze E., Lakeman P.,
RA   Mahida S., Mirzaa G.M., Morgan S.M., Nowak C., Peeters H., Petit F.,
RA   Pilz D.T., Puechberty J., Reinstein E., Riviere J.B., Santani A.B.,
RA   Schneider A., Sherr E.H., Smith-Hicks C., Wieland I., Zackai E., Zhao X.,
RA   Gronostajski R.M., Zenker M., Richards L.J.;
RT   "NFIB haploinsufficiency is associated with intellectual disability and
RT   macrocephaly.";
RL   Am. J. Hum. Genet. 103:752-768(2018).
CC   -!- FUNCTION: Transcriptional activator of GFAP, essential for proper brain
CC       development (PubMed:30388402). Recognizes and binds the palindromic
CC       sequence 5'-TTGGCNNNNNGCCAA-3' present in viral and cellular promoters
CC       and in the origin of replication of adenovirus type 2. These proteins
CC       are individually capable of activating transcription and replication.
CC       {ECO:0000269|PubMed:30388402}.
CC   -!- SUBUNIT: Binds DNA as a homodimer.
CC   -!- INTERACTION:
CC       O00712; P08651: NFIC; NbExp=5; IntAct=EBI-10963452, EBI-741360;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC         Comment=Additional isoforms seem to exist.;
CC       Name=1;
CC         IsoId=O00712-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O00712-3; Sequence=Not described;
CC       Name=3; Synonyms=NFI-B3;
CC         IsoId=O00712-2; Sequence=VSP_003545, VSP_003546;
CC       Name=4;
CC         IsoId=O00712-4; Sequence=VSP_044462;
CC       Name=5;
CC         IsoId=O00712-5; Sequence=VSP_045065;
CC       Name=6;
CC         IsoId=O00712-6; Sequence=VSP_054713, VSP_054714;
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: Macrocephaly, acquired, with impaired intellectual development
CC       (MACID) [MIM:618286]: An autosomal dominant disorder characterized by
CC       postnatal macrocephaly and borderline to mild intellectual disability.
CC       Additional variable neurodevelopmental features include muscular
CC       hypotonia, motor and speech delay, attention deficit disorder, autism
CC       spectrum disorder, and behavioral abnormalities. Some patients present
CC       corpus callosum dysgenesis. {ECO:0000269|PubMed:30388402}. 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; U85193; AAB41899.1; -; mRNA.
DR   EMBL; U70862; AAB51197.1; -; mRNA.
DR   EMBL; BT007266; AAP35930.1; -; mRNA.
DR   EMBL; AK131233; BAD18416.1; -; mRNA.
DR   EMBL; BX648416; CAH56156.1; -; mRNA.
DR   EMBL; BX648845; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AL136366; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL441963; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL137017; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL449443; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471071; EAW58697.1; -; Genomic_DNA.
DR   EMBL; CH471071; EAW58699.1; -; Genomic_DNA.
DR   EMBL; BC001283; AAH01283.1; -; mRNA.
DR   EMBL; U07810; AAA93125.1; -; mRNA.
DR   CCDS; CCDS55291.1; -. [O00712-5]
DR   CCDS; CCDS6474.1; -. [O00712-1]
DR   CCDS; CCDS65007.1; -. [O00712-6]
DR   RefSeq; NP_001177666.1; NM_001190737.1. [O00712-5]
DR   RefSeq; NP_001177667.1; NM_001190738.1.
DR   RefSeq; NP_001269716.1; NM_001282787.1. [O00712-6]
DR   RefSeq; NP_005587.2; NM_005596.3. [O00712-1]
DR   AlphaFoldDB; O00712; -.
DR   SMR; O00712; -.
DR   BioGRID; 110853; 135.
DR   DIP; DIP-61433N; -.
DR   IntAct; O00712; 119.
DR   STRING; 9606.ENSP00000370340; -.
DR   GlyGen; O00712; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; O00712; -.
DR   PhosphoSitePlus; O00712; -.
DR   BioMuta; NFIB; -.
DR   EPD; O00712; -.
DR   jPOST; O00712; -.
DR   MassIVE; O00712; -.
DR   MaxQB; O00712; -.
DR   PaxDb; O00712; -.
DR   PeptideAtlas; O00712; -.
DR   PRIDE; O00712; -.
DR   ProteomicsDB; 32394; -.
DR   ProteomicsDB; 43594; -.
DR   ProteomicsDB; 48006; -. [O00712-1]
DR   ProteomicsDB; 48007; -. [O00712-2]
DR   ProteomicsDB; 65511; -.
DR   Antibodypedia; 1309; 221 antibodies from 30 providers.
DR   DNASU; 4781; -.
DR   Ensembl; ENST00000380953.6; ENSP00000370340.1; ENSG00000147862.18. [O00712-5]
DR   Ensembl; ENST00000380959.7; ENSP00000370346.3; ENSG00000147862.18. [O00712-1]
DR   Ensembl; ENST00000543693.5; ENSP00000442888.1; ENSG00000147862.18. [O00712-6]
DR   GeneID; 4781; -.
DR   KEGG; hsa:4781; -.
DR   MANE-Select; ENST00000380953.6; ENSP00000370340.1; NM_001190737.2; NP_001177666.1. [O00712-5]
DR   UCSC; uc003zld.4; human. [O00712-1]
DR   CTD; 4781; -.
DR   DisGeNET; 4781; -.
DR   GeneCards; NFIB; -.
DR   HGNC; HGNC:7785; NFIB.
DR   HPA; ENSG00000147862; Low tissue specificity.
DR   MalaCards; NFIB; -.
DR   MIM; 600728; gene.
DR   MIM; 618286; phenotype.
DR   neXtProt; NX_O00712; -.
DR   OpenTargets; ENSG00000147862; -.
DR   PharmGKB; PA31591; -.
DR   VEuPathDB; HostDB:ENSG00000147862; -.
DR   eggNOG; KOG3663; Eukaryota.
DR   GeneTree; ENSGT00950000182916; -.
DR   HOGENOM; CLU_061490_0_0_1; -.
DR   InParanoid; O00712; -.
DR   PhylomeDB; O00712; -.
DR   TreeFam; TF313889; -.
DR   PathwayCommons; O00712; -.
DR   Reactome; R-HSA-73980; RNA Polymerase III Transcription Termination.
DR   Reactome; R-HSA-749476; RNA Polymerase III Abortive And Retractive Initiation.
DR   SignaLink; O00712; -.
DR   SIGNOR; O00712; -.
DR   BioGRID-ORCS; 4781; 25 hits in 1093 CRISPR screens.
DR   ChiTaRS; NFIB; human.
DR   GeneWiki; NFIB_(gene); -.
DR   GenomeRNAi; 4781; -.
DR   Pharos; O00712; Tbio.
DR   PRO; PR:O00712; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   RNAct; O00712; protein.
DR   Bgee; ENSG00000147862; Expressed in pericardium and 209 other tissues.
DR   ExpressionAtlas; O00712; baseline and differential.
DR   Genevisible; O00712; HS.
DR   GO; GO:0044300; C:cerebellar mossy fiber; ISS:UniProtKB.
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; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
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; IDA:UniProtKB.
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:0140416; F:transcription regulator inhibitor activity; IDA:GO_Central.
DR   GO; GO:0021960; P:anterior commissure morphogenesis; ISS:UniProtKB.
DR   GO; GO:0007420; P:brain development; IMP:UniProtKB.
DR   GO; GO:0060689; P:cell differentiation involved in salivary gland development; IEA:Ensembl.
DR   GO; GO:0002062; P:chondrocyte differentiation; ISS:UniProtKB.
DR   GO; GO:0060486; P:club cell differentiation; ISS:UniProtKB.
DR   GO; GO:0071679; P:commissural neuron axon guidance; ISS:UniProtKB.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0002067; P:glandular epithelial cell differentiation; IEA:Ensembl.
DR   GO; GO:0010001; P:glial cell differentiation; ISS:UniProtKB.
DR   GO; GO:0030902; P:hindbrain development; IEA:Ensembl.
DR   GO; GO:0061141; P:lung ciliated cell differentiation; ISS:UniProtKB.
DR   GO; GO:0043392; P:negative regulation of DNA binding; IDA:UniProtKB.
DR   GO; GO:2000795; P:negative regulation of epithelial cell proliferation involved in lung morphogenesis; ISS:UniProtKB.
DR   GO; GO:2000791; P:negative regulation of mesenchymal cell proliferation involved in lung development; ISS:UniProtKB.
DR   GO; GO:1902894; P:negative regulation of miRNA transcription; IMP:BHF-UCL.
DR   GO; GO:2000647; P:negative regulation of stem cell proliferation; IEA:Ensembl.
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:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0021740; P:principal sensory nucleus of trigeminal nerve development; ISS:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR   GO; GO:0060662; P:salivary gland cavitation; IEA:Ensembl.
DR   GO; GO:0072089; P:stem cell proliferation; IEA:Ensembl.
DR   GO; GO:0060509; P:type I pneumocyte differentiation; ISS:UniProtKB.
DR   GO; GO:0060510; P:type II pneumocyte differentiation; ISS: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; Disease variant; DNA replication;
KW   DNA-binding; Intellectual disability; Methylation; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..420
FT                   /note="Nuclear factor 1 B-type"
FT                   /id="PRO_0000100195"
FT   DNA_BIND        1..195
FT                   /note="CTF/NF-I"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00436"
FT   REGION          189..208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          252..364
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          377..420
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           397..405
FT                   /note="9aaTAD"
FT                   /evidence="ECO:0000269|PubMed:31375868"
FT   COMPBIAS        252..274
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        287..301
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        318..339
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        398..420
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         264
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         286
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P97863"
FT   MOD_RES         292
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         295
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         312
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         328
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:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         335
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:P97863"
FT   MOD_RES         388
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:P97863"
FT   VAR_SEQ         1..252
FT                   /note="Missing (in isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_054713"
FT   VAR_SEQ         1..10
FT                   /note="MMYSPICLTQ -> MERIPVSVDFWVVCCAVLKCNPGIPMERIPVSVDFWVV
FT                   CCAVLKCNPGIPKRMSTLCFGFS (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_044462"
FT   VAR_SEQ         187..188
FT                   /note="QD -> AR (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:9099724"
FT                   /id="VSP_003545"
FT   VAR_SEQ         189..420
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:9099724"
FT                   /id="VSP_003546"
FT   VAR_SEQ         416..420
FT                   /note="SWYLG -> PNGSGQVVGKVPGHFTPVLAPSPHPSAVRPVTLSMTDTKPITT
FT                   STEAYTASGTSQANRYVGLSPRDPSFLHQQQLRICDWTMNQNGRHLYPSTSEDTLGITW
FT                   QSPGTWASLVPFQVSNRTPILPANVQNYGLNIIGEPFLQAETSN (in isoform
FT                   6)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_054714"
FT   VAR_SEQ         416
FT                   /note="S -> PNGSGQVVGKVPGHFTPVLAPSPHPSAVRPVTLSMTDTKPITTSTEA
FT                   YTASGTSQANRYVGLSPRDPSFLHQQQS (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_045065"
FT   VARIANT         37..420
FT                   /note="Missing (in MACID)"
FT                   /evidence="ECO:0000269|PubMed:30388402"
FT                   /id="VAR_081859"
FT   VARIANT         89..420
FT                   /note="Missing (in MACID)"
FT                   /evidence="ECO:0000269|PubMed:30388402"
FT                   /id="VAR_081860"
FT   VARIANT         114
FT                   /note="K -> T (in MACID; significant decrease of GFAP
FT                   transcriptional activation; dbSNP:rs1554709683)"
FT                   /evidence="ECO:0000269|PubMed:30388402"
FT                   /id="VAR_081861"
FT   VARIANT         126
FT                   /note="K -> E (in MACID; significant decrease of GFAP
FT                   transcriptional activation; dbSNP:rs1554709662)"
FT                   /evidence="ECO:0000269|PubMed:30388402"
FT                   /id="VAR_081862"
FT   VARIANT         132
FT                   /note="L -> P (in MACID; significant decrease of GFAP
FT                   transcriptional activation; dbSNP:rs1554709654)"
FT                   /evidence="ECO:0000269|PubMed:30388402"
FT                   /id="VAR_081863"
FT   VARIANT         356
FT                   /note="S -> L (in MACID; likely benign variant; does not
FT                   affect GFAP transcriptional activation;
FT                   dbSNP:rs1554639196)"
FT                   /evidence="ECO:0000269|PubMed:30388402"
FT                   /id="VAR_081864"
FT   CONFLICT        17
FT                   /note="I -> M (in Ref. 1; AAB41899)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        37
FT                   /note="R -> G (in Ref. 4; BAD18416)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        74
FT                   /note="S -> F (in Ref. 5; BX648845)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        198
FT                   /note="N -> S (in Ref. 4; BAD18416)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        284
FT                   /note="S -> R (in Ref. 5; BX648845)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   420 AA;  47442 MW;  0F71635FE9D64FA4 CRC64;
     MMYSPICLTQ DEFHPFIEAL LPHVRAIAYT WFNLQARKRK YFKKHEKRMS KDEERAVKDE
     LLSEKPEIKQ KWASRLLAKL RKDIRQEYRE DFVLTVTGKK HPCCVLSNPD QKGKIRRIDC
     LRQADKVWRL DLVMVILFKG IPLESTDGER LMKSPHCTNP ALCVQPHHIT VSVKELDLFL
     AYYVQEQDSG QSGSPSHNDP AKNPPGYLED SFVKSGVFNV SELVRVSRTP ITQGTGVNFP
     IGEIPSQPYY HDMNSGVNLQ RSLSSPPSSK RPKTISIDEN MEPSPTGDFY PSPSSPAAGS
     RTWHERDQDM SSPTTMKKPE KPLFSSASPQ DSSPRLSTFP QHHHPGIPGV AHSVISTRTP
     PPPSPLPFPT QAILPPAPSS YFSHPTIRYP PHLNPQDTLK NYVPSYDPSS PQTSQSWYLG
 
 
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