Full text data of NFIA
NFIA
(KIAA1439)
[Confidence: low (only semi-automatic identification from reviews)]
Nuclear factor 1 A-type; NF1-A; Nuclear factor 1/A (CCAAT-box-binding transcription factor; CTF; Nuclear factor I/A; NF-I/A; NFI-A; TGGCA-binding protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Nuclear factor 1 A-type; NF1-A; Nuclear factor 1/A (CCAAT-box-binding transcription factor; CTF; Nuclear factor I/A; NF-I/A; NFI-A; TGGCA-binding protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q12857
ID NFIA_HUMAN Reviewed; 509 AA.
AC Q12857; B4DRJ3; B4DS53; F5H0R0; F8W8W3; Q8TA97; Q9H3X9; Q9P2A9;
read moreDT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 22-JAN-2014, entry version 131.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.
RT The complete sequences of 150 new cDNA clones from brain which code
RT for large 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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
RT the human transcription factor nuclear factor I by FISH.";
RL Genomics 28:66-73(1995).
RN [7]
RP IDENTIFICATION BY 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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287, AND MASS
RP SPECTROMETRY.
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.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258; SER-265; SER-280;
RP SER-287; SER-300 AND SER-319, AND MASS SPECTROMETRY.
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280 AND SER-287, AND
RP MASS SPECTROMETRY.
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-265; SER-280; SER-287;
RP SER-300 AND SER-360, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
CC -!- FUNCTION: Recognizes and binds the palindromic sequence 5'-
CC TTGGCNNNNNGCCAA-3' present in viral and cellular promoters and in
CC the 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 -!- 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 -!- SIMILARITY: Belongs to the CTF/NF-I family.
CC -!- SIMILARITY: Contains 1 CTF/NF-I DNA-binding domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA92677.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR EMBL; AB037860; BAA92677.1; ALT_INIT; mRNA.
DR EMBL; AK299289; BAG61305.1; -; mRNA.
DR EMBL; AK299579; BAG61515.1; -; mRNA.
DR EMBL; AC092784; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC096534; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC096947; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC099792; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL096888; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL355795; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL445198; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL445432; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX06601.1; -; Genomic_DNA.
DR EMBL; BC022264; AAH22264.1; -; mRNA.
DR EMBL; U07809; AAA93124.1; -; mRNA.
DR RefSeq; NP_001128145.1; NM_001134673.3.
DR RefSeq; NP_001138983.1; NM_001145511.1.
DR RefSeq; NP_001138984.1; NM_001145512.1.
DR RefSeq; NP_005586.1; NM_005595.4.
DR UniGene; Hs.740757; -.
DR UniGene; Hs.744898; -.
DR ProteinModelPortal; Q12857; -.
DR IntAct; Q12857; 1.
DR MINT; MINT-6612489; -.
DR STRING; 9606.ENSP00000384523; -.
DR PhosphoSite; Q12857; -.
DR DMDM; 14194959; -.
DR PaxDb; Q12857; -.
DR PRIDE; Q12857; -.
DR DNASU; 4774; -.
DR Ensembl; ENST00000371187; ENSP00000360229; ENSG00000162599.
DR Ensembl; ENST00000371189; ENSP00000360231; ENSG00000162599.
DR Ensembl; ENST00000403491; ENSP00000384523; ENSG00000162599.
DR Ensembl; ENST00000407417; ENSP00000384680; ENSG00000162599.
DR GeneID; 4774; -.
DR KEGG; hsa:4774; -.
DR UCSC; uc001czy.3; human.
DR CTD; 4774; -.
DR GeneCards; GC01P061260; -.
DR HGNC; HGNC:7784; NFIA.
DR HPA; HPA006111; -.
DR HPA; HPA008884; -.
DR MIM; 600727; gene.
DR neXtProt; NX_Q12857; -.
DR PharmGKB; PA31590; -.
DR eggNOG; NOG252172; -.
DR HOGENOM; HOG000013028; -.
DR HOVERGEN; HBG006561; -.
DR KO; K09168; -.
DR OMA; KEQPENG; -.
DR OrthoDB; EOG7WDN2K; -.
DR ChiTaRS; NFIA; human.
DR GeneWiki; NFIA; -.
DR GenomeRNAi; 4774; -.
DR NextBio; 18406; -.
DR PRO; PR:Q12857; -.
DR ArrayExpress; Q12857; -.
DR Bgee; Q12857; -.
DR CleanEx; HS_NFIA; -.
DR Genevestigator; Q12857; -.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; NAS:UniProtKB.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
DR GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR GO; GO:0019079; P:viral genome replication; NAS:UniProtKB.
DR InterPro; IPR000647; CTF/NFI.
DR InterPro; IPR020604; CTF/NFI_DNA-bd-dom.
DR InterPro; IPR019739; CTF/NFI_DNA-bd_CS.
DR InterPro; IPR019548; CTF/NFI_DNA-bd_N.
DR InterPro; IPR003619; MAD_homology1_Dwarfin-type.
DR PANTHER; PTHR11492; PTHR11492; 1.
DR Pfam; PF00859; CTF_NFI; 1.
DR Pfam; PF03165; MH1; 1.
DR Pfam; PF10524; NfI_DNAbd_pre-N; 1.
DR SMART; SM00523; DWA; 1.
DR PROSITE; PS00349; CTF_NFI_1; 1.
DR PROSITE; PS51080; CTF_NFI_2; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Complete proteome; DNA replication;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1 509 Nuclear factor 1 A-type.
FT /FTId=PRO_0000100191.
FT DNA_BIND 1 194 CTF/NF-I.
FT MOD_RES 258 258 Phosphoserine.
FT MOD_RES 265 265 Phosphoserine.
FT MOD_RES 280 280 Phosphoserine.
FT MOD_RES 287 287 Phosphoserine.
FT MOD_RES 300 300 Phosphoserine.
FT MOD_RES 319 319 Phosphoserine.
FT MOD_RES 360 360 Phosphoserine.
FT VAR_SEQ 1 9 MYSPLCLTQ -> M (in isoform 3).
FT /FTId=VSP_046884.
FT VAR_SEQ 1 1 M -> MQMCRPASSSVLYVPTRWPGGCGATWQSCPSPPPRR
FT TRIPQRPAVM (in isoform 4).
FT /FTId=VSP_046883.
FT VAR_SEQ 474 509 TYSTPSTSPANRFVSVGPRDPSFVNIPQQTQSWYLG -> I
FT LVPGIKVAASHHPPDRPPDPFSTL (in isoform 2).
FT /FTId=VSP_036620.
FT CONFLICT 143 143 E -> G (in Ref. 2; BAG61305).
FT CONFLICT 186 186 A -> G (in Ref. 6; AAA93124).
FT CONFLICT 240 243 TGPN -> PAPT (in Ref. 6; AAA93124).
FT CONFLICT 274 274 S -> P (in Ref. 2; BAG61515).
FT CONFLICT 331 331 F -> L (in Ref. 2; BAG61305).
FT CONFLICT 358 358 R -> G (in Ref. 2; BAG61305).
FT CONFLICT 426 426 K -> R (in Ref. 2; BAG61305).
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
//
ID NFIA_HUMAN Reviewed; 509 AA.
AC Q12857; B4DRJ3; B4DS53; F5H0R0; F8W8W3; Q8TA97; Q9H3X9; Q9P2A9;
read moreDT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 22-JAN-2014, entry version 131.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.
RT The complete sequences of 150 new cDNA clones from brain which code
RT for large 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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
RT the human transcription factor nuclear factor I by FISH.";
RL Genomics 28:66-73(1995).
RN [7]
RP IDENTIFICATION BY 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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287, AND MASS
RP SPECTROMETRY.
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.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258; SER-265; SER-280;
RP SER-287; SER-300 AND SER-319, AND MASS SPECTROMETRY.
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280 AND SER-287, AND
RP MASS SPECTROMETRY.
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-265; SER-280; SER-287;
RP SER-300 AND SER-360, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
CC -!- FUNCTION: Recognizes and binds the palindromic sequence 5'-
CC TTGGCNNNNNGCCAA-3' present in viral and cellular promoters and in
CC the 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 -!- 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 -!- SIMILARITY: Belongs to the CTF/NF-I family.
CC -!- SIMILARITY: Contains 1 CTF/NF-I DNA-binding domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA92677.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs 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 RefSeq; NP_001128145.1; NM_001134673.3.
DR RefSeq; NP_001138983.1; NM_001145511.1.
DR RefSeq; NP_001138984.1; NM_001145512.1.
DR RefSeq; NP_005586.1; NM_005595.4.
DR UniGene; Hs.740757; -.
DR UniGene; Hs.744898; -.
DR ProteinModelPortal; Q12857; -.
DR IntAct; Q12857; 1.
DR MINT; MINT-6612489; -.
DR STRING; 9606.ENSP00000384523; -.
DR PhosphoSite; Q12857; -.
DR DMDM; 14194959; -.
DR PaxDb; Q12857; -.
DR PRIDE; Q12857; -.
DR DNASU; 4774; -.
DR Ensembl; ENST00000371187; ENSP00000360229; ENSG00000162599.
DR Ensembl; ENST00000371189; ENSP00000360231; ENSG00000162599.
DR Ensembl; ENST00000403491; ENSP00000384523; ENSG00000162599.
DR Ensembl; ENST00000407417; ENSP00000384680; ENSG00000162599.
DR GeneID; 4774; -.
DR KEGG; hsa:4774; -.
DR UCSC; uc001czy.3; human.
DR CTD; 4774; -.
DR GeneCards; GC01P061260; -.
DR HGNC; HGNC:7784; NFIA.
DR HPA; HPA006111; -.
DR HPA; HPA008884; -.
DR MIM; 600727; gene.
DR neXtProt; NX_Q12857; -.
DR PharmGKB; PA31590; -.
DR eggNOG; NOG252172; -.
DR HOGENOM; HOG000013028; -.
DR HOVERGEN; HBG006561; -.
DR KO; K09168; -.
DR OMA; KEQPENG; -.
DR OrthoDB; EOG7WDN2K; -.
DR ChiTaRS; NFIA; human.
DR GeneWiki; NFIA; -.
DR GenomeRNAi; 4774; -.
DR NextBio; 18406; -.
DR PRO; PR:Q12857; -.
DR ArrayExpress; Q12857; -.
DR Bgee; Q12857; -.
DR CleanEx; HS_NFIA; -.
DR Genevestigator; Q12857; -.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; NAS:UniProtKB.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
DR GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR GO; GO:0019079; P:viral genome replication; NAS:UniProtKB.
DR InterPro; IPR000647; CTF/NFI.
DR InterPro; IPR020604; CTF/NFI_DNA-bd-dom.
DR InterPro; IPR019739; CTF/NFI_DNA-bd_CS.
DR InterPro; IPR019548; CTF/NFI_DNA-bd_N.
DR InterPro; IPR003619; MAD_homology1_Dwarfin-type.
DR PANTHER; PTHR11492; PTHR11492; 1.
DR Pfam; PF00859; CTF_NFI; 1.
DR Pfam; PF03165; MH1; 1.
DR Pfam; PF10524; NfI_DNAbd_pre-N; 1.
DR SMART; SM00523; DWA; 1.
DR PROSITE; PS00349; CTF_NFI_1; 1.
DR PROSITE; PS51080; CTF_NFI_2; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Complete proteome; DNA replication;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1 509 Nuclear factor 1 A-type.
FT /FTId=PRO_0000100191.
FT DNA_BIND 1 194 CTF/NF-I.
FT MOD_RES 258 258 Phosphoserine.
FT MOD_RES 265 265 Phosphoserine.
FT MOD_RES 280 280 Phosphoserine.
FT MOD_RES 287 287 Phosphoserine.
FT MOD_RES 300 300 Phosphoserine.
FT MOD_RES 319 319 Phosphoserine.
FT MOD_RES 360 360 Phosphoserine.
FT VAR_SEQ 1 9 MYSPLCLTQ -> M (in isoform 3).
FT /FTId=VSP_046884.
FT VAR_SEQ 1 1 M -> MQMCRPASSSVLYVPTRWPGGCGATWQSCPSPPPRR
FT TRIPQRPAVM (in isoform 4).
FT /FTId=VSP_046883.
FT VAR_SEQ 474 509 TYSTPSTSPANRFVSVGPRDPSFVNIPQQTQSWYLG -> I
FT LVPGIKVAASHHPPDRPPDPFSTL (in isoform 2).
FT /FTId=VSP_036620.
FT CONFLICT 143 143 E -> G (in Ref. 2; BAG61305).
FT CONFLICT 186 186 A -> G (in Ref. 6; AAA93124).
FT CONFLICT 240 243 TGPN -> PAPT (in Ref. 6; AAA93124).
FT CONFLICT 274 274 S -> P (in Ref. 2; BAG61515).
FT CONFLICT 331 331 F -> L (in Ref. 2; BAG61305).
FT CONFLICT 358 358 R -> G (in Ref. 2; BAG61305).
FT CONFLICT 426 426 K -> R (in Ref. 2; BAG61305).
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
//
MIM
600727
*RECORD*
*FIELD* NO
600727
*FIELD* TI
*600727 NUCLEAR FACTOR I/A; NFIA
;;TRANSCRIPTION FACTOR NFIA;;
KIAA1439
*FIELD* TX
read more
DESCRIPTION
Nuclear factor I (NFI) proteins, such as NFIA, constitute a family of
dimeric DNA-binding proteins with similar, and possibly identical,
DNA-binding specificity. They function as cellular transcription factors
and as replication factors for adenovirus DNA replication. Diversity in
this protein family is generated by multiple genes, differential
splicing, and heterodimerization (summary by Qian et al., 1995).
CLONING
Qian et al. (1995) isolated partial cDNA sequences derived from 4
independent genes: NFIA, NFIB (600728), NFIC (600729), and NFIX
(164005).
By sequencing clones obtained from an adult brain cDNA library, Nagase
et al. (2000) cloned NFIA, which they designated KIAA1439. The deduced
protein contains 561 amino acids and shares complete sequence identity
with rat nuclear factor-1 over 509 amino acids. RT-PCR ELISA detected
moderate to high expression in all tissues examined. Highest expression
was detected in heart and liver, followed by brain, lung, ovary,
skeletal muscle, kidney, testis, fetal liver, fetal brain, pancreas, and
spleen. NFIA was expressed at moderate to high levels in all adult brain
regions tested, with highest expression in cerebellum and caudate
nucleus.
GENE STRUCTURE
Grunder et al. (2003) determined that the NFIA gene contains 11 exons.
By ortholog comparisons using protein sequences from 7 vertebrate
species, they identified 12 NFIA variants that are produced by
alternative splicing.
MAPPING
By FISH, Qian et al. (1995) mapped the NFIA and NFIB genes to
chromosomes 1p31.3-p31.2 and 9p24.1, respectively. They localized the
NFIC and NFIX genes to chromosome 19p13.3 in the order
cen--NFIX--NFIC--tel. Comparison of the position of NFI genes and JUN
genes (see JUNB, 165161) revealed a close physical linkage between
members of the NFI and JUN gene families in the human genome.
By FISH, Grunder et al. (2003) mapped the mouse Nfia and Nfib genes to
chromosome 4C4-C6.
GENE FUNCTION
Deneen et al. (2006) found that Nfia and Nfib were induced in the spinal
cord ventricular zone of mouse embryos concomitant with induction of
Glast (SLC1A3; 600111), a marker of gliogenesis. Using mouse and chicken
embryos and embryonic rat cortical progenitor cells, they showed that
Nfia and Nfib were necessary and sufficient to promote glial cell fate
specification. At later embryonic stages, Nfia and Nfib promoted
terminal astrocyte differentiation. Nfia also inhibited neurogenesis in
ventricular zone progenitors.
Rosa et al. (2007) identified a pathway by which PU.1 (SPI1; 165170)
regulated human monocyte/macrophage differentiation. PU.1 activated
transcription of MIR424 (300682), which translationally repressed NFIA,
resulting in activation of differentiation-specific genes, such as MCSFR
(CSF1R; 164770).
regulated human monocyte/macrophage differentiation. PU.1 activated
transcription of MIR424 (300682), which translationally repressed NFIA,
resulting in activation of differentiation-specific genes, such as MCSFR
(CSF1R; 164770).
MOLECULAR GENETICS
Lu et al. (2007) reported 5 patients, including 2 half sibs, with
balanced translocations or interstitial deletions of chromosome 1q31-q32
(613735) involving the NFIA gene confirmed by FISH and Southern blot
analysis. Three of the patients had been previously reported by Campbell
et al. (2002) and Shanske et al. (2004). The 2 half sibs had a 12-Mb
deletion involving approximately 47 additional genes, and another
patient had a 12-Mb deletion of chromosome 2q encompassing 39 additional
genes, as well as a translocation involving chromosome 1p. The remaining
2 patients had a translocation with a microdeletion and a translocation,
respectively. All 5 showed a similar phenotype characterized by
hypoplastic or absent corpus callosum, hydrocephalus or
ventriculomegaly, and developmental delay. Four patients had a tethered
spinal cord, 3 had Chiari type I malformation, and 3 had seizures. In
addition, 3 patients had urinary tract defects, including vesicoureteral
reflux and urinary incontinence. Although all 5 cases had
haploinsufficiency of NFIA, each case also had involvement of 1 or more
additional genes, which may have contributed to the phenotype.
Intragenic mutations in the NFIA gene were not identified in any of the
patients or in 219 additional patients with various neurologic
developmental abnormalities. Lu et al. (2007) noted the phenotypic
similarities to Nfia loss of function in the mouse and suggested that
haploinsufficiency of the NFIA gene contributed to the malformation
syndrome in these patients.
ANIMAL MODEL
Das Neves et al. (1999) found that disruption of the mouse Nfia gene
caused perinatal lethality. More than 95% of Nfia null animals died
within 2 weeks after birth. Newborn animals lacked a corpus callosum and
showed ventricular dilation indicating early hydrocephalus. Rare
surviving homozygous mice lacked a corpus callosum, showed severe
communicating hydrocephalus, a full-axial tremor indicative of
neurologic defects, male sterility, and low female fertility, but they
had near normal life spans.
*FIELD* RF
1. Campbell, C. G. N.; Wang, H.; Hunter, G. W.: Interstitial microdeletion
of chromosome 1p in two siblings. Am. J. Med. Genet. 111: 289-294,
2002.
2. das Neves, L.; Duchala, C. S.; Godinho, F.; Haxhiu, M. A.; Colmenares,
C.; Macklin, W. B.; Campbell, C. E.; Butz, K. G.; Gronostajski, R.
M.: Disruption of the murine nuclear factor I-A gene (Nfia) results
in perinatal lethality, hydrocephalus, and agenesis of the corpus
callosum. Proc. Nat. Acad. Sci. 96: 11946-11951, 1999. Note: Erratum:
Proc. Nat. Acad. Sci. 98: 4276 only, 2001.
3. Deneen, B.; Ho, R.; Lukaszewicz, A.; Hochstim, C. J.; Gronostajski,
R. M.; Anderson, D. J.: The transcription factor NFIA controls the
onset of gliogenesis in the developing spinal cord. Neuron 52: 953-968,
2006.
4. Grunder, A.; Qian, F.; Ebel, T. T.; Mincheva, A.; Lichter, P.;
Kruse, U.; Sippel, A. E.: Genomic organization, splice products and
mouse chromosomal localization of genes for transcription factor Nuclear
Factor One. Gene 304: 171-181, 2003.
5. Lu, W.; Quintero-Rivera, F.; Fan, Y.; Alkuraya, F. S.; Donovan,
D. J.; Xi, Q.; Turbe-Doan, A.; Li, Q.-G.; Campbell, C. G.; Shanske,
A. L.; Sherr, E. H.; Ahmad, A.; and 16 others: NFIA haploinsufficiency
is associated with a CNS malformation syndrome and urinary tract defects. PLoS
Genet. 3: e80, 2007. Note: Electronic Article.
6. Nagase, T.; Kikuno, R.; Ishikawa, K.; Hirosawa, M.; Ohara, O.:
Prediction of the coding sequences of unidentified human genes. XVI.
The complete sequences of 150 new cDNA clones from brain which code
for large proteins in vitro. DNA Res. 7: 65-73, 2000.
7. Qian, F.; Kruse, U.; Lichter, P.; Sippel, A. E.: Chromosomal localization
of the four genes (NFIA, B, C, and X) for the human transcription
factor nuclear factor I by FISH. Genomics 28: 66-73, 1995.
8. Rosa, A.; Ballarino, M.; Sorrentino, A.; Sthandier, O.; De Angelis,
F. G.; Marchioni, M.; Masella, B.; Guarini, A.; Fatica, A.; Peschle,
C.; Bozzoni, I.: The interplay between the master transcription factor
PU.1 and miR-424 regulates human monocyte/macrophage differentiation. Proc.
Nat. Acad. Sci. 104: 19849-19854, 2007.
9. Shanske, A. L.; Edelmann, L.; Kardon, N. B.; Gosset, P.; Levy,
B.: Detection of an interstitial deletion of 2q21-22 by high resolution
comparative genomic hybridization in a child with multiple congenital
anomalies and an apparent balanced translocation. Am. J. Med. Genet. 131A:
29-35, 2004.
*FIELD* CN
Patricia A. Hartz - updated: 2/4/2011
Paul J. Converse - updated: 2/7/2008
Cassandra L. Kniffin - updated: 7/10/2007
Patricia A. Hartz - updated: 4/1/2003
*FIELD* CD
Victor A. McKusick: 8/17/1995
*FIELD* ED
mgross: 02/08/2011
ckniffin: 2/8/2011
terry: 2/4/2011
terry: 1/20/2010
mgross: 2/7/2008
wwang: 7/16/2007
ckniffin: 7/10/2007
mgross: 4/3/2003
terry: 4/1/2003
mark: 8/17/1995
*RECORD*
*FIELD* NO
600727
*FIELD* TI
*600727 NUCLEAR FACTOR I/A; NFIA
;;TRANSCRIPTION FACTOR NFIA;;
KIAA1439
*FIELD* TX
read more
DESCRIPTION
Nuclear factor I (NFI) proteins, such as NFIA, constitute a family of
dimeric DNA-binding proteins with similar, and possibly identical,
DNA-binding specificity. They function as cellular transcription factors
and as replication factors for adenovirus DNA replication. Diversity in
this protein family is generated by multiple genes, differential
splicing, and heterodimerization (summary by Qian et al., 1995).
CLONING
Qian et al. (1995) isolated partial cDNA sequences derived from 4
independent genes: NFIA, NFIB (600728), NFIC (600729), and NFIX
(164005).
By sequencing clones obtained from an adult brain cDNA library, Nagase
et al. (2000) cloned NFIA, which they designated KIAA1439. The deduced
protein contains 561 amino acids and shares complete sequence identity
with rat nuclear factor-1 over 509 amino acids. RT-PCR ELISA detected
moderate to high expression in all tissues examined. Highest expression
was detected in heart and liver, followed by brain, lung, ovary,
skeletal muscle, kidney, testis, fetal liver, fetal brain, pancreas, and
spleen. NFIA was expressed at moderate to high levels in all adult brain
regions tested, with highest expression in cerebellum and caudate
nucleus.
GENE STRUCTURE
Grunder et al. (2003) determined that the NFIA gene contains 11 exons.
By ortholog comparisons using protein sequences from 7 vertebrate
species, they identified 12 NFIA variants that are produced by
alternative splicing.
MAPPING
By FISH, Qian et al. (1995) mapped the NFIA and NFIB genes to
chromosomes 1p31.3-p31.2 and 9p24.1, respectively. They localized the
NFIC and NFIX genes to chromosome 19p13.3 in the order
cen--NFIX--NFIC--tel. Comparison of the position of NFI genes and JUN
genes (see JUNB, 165161) revealed a close physical linkage between
members of the NFI and JUN gene families in the human genome.
By FISH, Grunder et al. (2003) mapped the mouse Nfia and Nfib genes to
chromosome 4C4-C6.
GENE FUNCTION
Deneen et al. (2006) found that Nfia and Nfib were induced in the spinal
cord ventricular zone of mouse embryos concomitant with induction of
Glast (SLC1A3; 600111), a marker of gliogenesis. Using mouse and chicken
embryos and embryonic rat cortical progenitor cells, they showed that
Nfia and Nfib were necessary and sufficient to promote glial cell fate
specification. At later embryonic stages, Nfia and Nfib promoted
terminal astrocyte differentiation. Nfia also inhibited neurogenesis in
ventricular zone progenitors.
Rosa et al. (2007) identified a pathway by which PU.1 (SPI1; 165170)
regulated human monocyte/macrophage differentiation. PU.1 activated
transcription of MIR424 (300682), which translationally repressed NFIA,
resulting in activation of differentiation-specific genes, such as MCSFR
(CSF1R; 164770).
regulated human monocyte/macrophage differentiation. PU.1 activated
transcription of MIR424 (300682), which translationally repressed NFIA,
resulting in activation of differentiation-specific genes, such as MCSFR
(CSF1R; 164770).
MOLECULAR GENETICS
Lu et al. (2007) reported 5 patients, including 2 half sibs, with
balanced translocations or interstitial deletions of chromosome 1q31-q32
(613735) involving the NFIA gene confirmed by FISH and Southern blot
analysis. Three of the patients had been previously reported by Campbell
et al. (2002) and Shanske et al. (2004). The 2 half sibs had a 12-Mb
deletion involving approximately 47 additional genes, and another
patient had a 12-Mb deletion of chromosome 2q encompassing 39 additional
genes, as well as a translocation involving chromosome 1p. The remaining
2 patients had a translocation with a microdeletion and a translocation,
respectively. All 5 showed a similar phenotype characterized by
hypoplastic or absent corpus callosum, hydrocephalus or
ventriculomegaly, and developmental delay. Four patients had a tethered
spinal cord, 3 had Chiari type I malformation, and 3 had seizures. In
addition, 3 patients had urinary tract defects, including vesicoureteral
reflux and urinary incontinence. Although all 5 cases had
haploinsufficiency of NFIA, each case also had involvement of 1 or more
additional genes, which may have contributed to the phenotype.
Intragenic mutations in the NFIA gene were not identified in any of the
patients or in 219 additional patients with various neurologic
developmental abnormalities. Lu et al. (2007) noted the phenotypic
similarities to Nfia loss of function in the mouse and suggested that
haploinsufficiency of the NFIA gene contributed to the malformation
syndrome in these patients.
ANIMAL MODEL
Das Neves et al. (1999) found that disruption of the mouse Nfia gene
caused perinatal lethality. More than 95% of Nfia null animals died
within 2 weeks after birth. Newborn animals lacked a corpus callosum and
showed ventricular dilation indicating early hydrocephalus. Rare
surviving homozygous mice lacked a corpus callosum, showed severe
communicating hydrocephalus, a full-axial tremor indicative of
neurologic defects, male sterility, and low female fertility, but they
had near normal life spans.
*FIELD* RF
1. Campbell, C. G. N.; Wang, H.; Hunter, G. W.: Interstitial microdeletion
of chromosome 1p in two siblings. Am. J. Med. Genet. 111: 289-294,
2002.
2. das Neves, L.; Duchala, C. S.; Godinho, F.; Haxhiu, M. A.; Colmenares,
C.; Macklin, W. B.; Campbell, C. E.; Butz, K. G.; Gronostajski, R.
M.: Disruption of the murine nuclear factor I-A gene (Nfia) results
in perinatal lethality, hydrocephalus, and agenesis of the corpus
callosum. Proc. Nat. Acad. Sci. 96: 11946-11951, 1999. Note: Erratum:
Proc. Nat. Acad. Sci. 98: 4276 only, 2001.
3. Deneen, B.; Ho, R.; Lukaszewicz, A.; Hochstim, C. J.; Gronostajski,
R. M.; Anderson, D. J.: The transcription factor NFIA controls the
onset of gliogenesis in the developing spinal cord. Neuron 52: 953-968,
2006.
4. Grunder, A.; Qian, F.; Ebel, T. T.; Mincheva, A.; Lichter, P.;
Kruse, U.; Sippel, A. E.: Genomic organization, splice products and
mouse chromosomal localization of genes for transcription factor Nuclear
Factor One. Gene 304: 171-181, 2003.
5. Lu, W.; Quintero-Rivera, F.; Fan, Y.; Alkuraya, F. S.; Donovan,
D. J.; Xi, Q.; Turbe-Doan, A.; Li, Q.-G.; Campbell, C. G.; Shanske,
A. L.; Sherr, E. H.; Ahmad, A.; and 16 others: NFIA haploinsufficiency
is associated with a CNS malformation syndrome and urinary tract defects. PLoS
Genet. 3: e80, 2007. Note: Electronic Article.
6. Nagase, T.; Kikuno, R.; Ishikawa, K.; Hirosawa, M.; Ohara, O.:
Prediction of the coding sequences of unidentified human genes. XVI.
The complete sequences of 150 new cDNA clones from brain which code
for large proteins in vitro. DNA Res. 7: 65-73, 2000.
7. Qian, F.; Kruse, U.; Lichter, P.; Sippel, A. E.: Chromosomal localization
of the four genes (NFIA, B, C, and X) for the human transcription
factor nuclear factor I by FISH. Genomics 28: 66-73, 1995.
8. Rosa, A.; Ballarino, M.; Sorrentino, A.; Sthandier, O.; De Angelis,
F. G.; Marchioni, M.; Masella, B.; Guarini, A.; Fatica, A.; Peschle,
C.; Bozzoni, I.: The interplay between the master transcription factor
PU.1 and miR-424 regulates human monocyte/macrophage differentiation. Proc.
Nat. Acad. Sci. 104: 19849-19854, 2007.
9. Shanske, A. L.; Edelmann, L.; Kardon, N. B.; Gosset, P.; Levy,
B.: Detection of an interstitial deletion of 2q21-22 by high resolution
comparative genomic hybridization in a child with multiple congenital
anomalies and an apparent balanced translocation. Am. J. Med. Genet. 131A:
29-35, 2004.
*FIELD* CN
Patricia A. Hartz - updated: 2/4/2011
Paul J. Converse - updated: 2/7/2008
Cassandra L. Kniffin - updated: 7/10/2007
Patricia A. Hartz - updated: 4/1/2003
*FIELD* CD
Victor A. McKusick: 8/17/1995
*FIELD* ED
mgross: 02/08/2011
ckniffin: 2/8/2011
terry: 2/4/2011
terry: 1/20/2010
mgross: 2/7/2008
wwang: 7/16/2007
ckniffin: 7/10/2007
mgross: 4/3/2003
terry: 4/1/2003
mark: 8/17/1995