NFX1_HUMAN
ID NFX1_HUMAN Reviewed; 1120 AA.
AC Q12986; A8K6H8; Q5VXW6; Q96EL5; Q9BXI1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Transcriptional repressor NF-X1;
DE EC=2.3.2.-;
DE AltName: Full=Nuclear transcription factor, X box-binding protein 1;
GN Name=NFX1; Synonyms=NFX2;
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 2).
RC TISSUE=Testis;
RA Li J.M., Sah J.H., Zhou Z.M.;
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 48-1120 (ISOFORM 1).
RX PubMed=7964459; DOI=10.1084/jem.180.5.1763;
RA Song Z., Krishna S., Thanos D., Strominger J.L., Ono S.J.;
RT "A novel cysteine-rich sequence-specific DNA-binding protein interacts with
RT the conserved X-box motif of the human major histocompatibility complex
RT class II genes via a repeated Cys-His domain and functions as a
RT transcriptional repressor.";
RL J. Exp. Med. 180:1763-1774(1994).
RN [7]
RP FUNCTION AS AN E2-DEPENDENT UBIQUITIN-PROTEIN LIGASE.
RX PubMed=10500182; DOI=10.1073/pnas.96.20.11364;
RA Lorick K.L., Jensen J.P., Fang S., Ong A.M., Hatakeyama S., Weissman A.M.;
RT "RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent
RT ubiquitination.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:11364-11369(1999).
RN [8]
RP INTERACTION WITH HPV16 E6 (MICROBIAL INFECTION), AND FUNCTION.
RX PubMed=15371341; DOI=10.1101/gad.1214704;
RA Gewin L., Myers H., Kiyono T., Galloway D.A.;
RT "Identification of a novel telomerase repressor that interacts with the
RT human papillomavirus type-16 E6/E6-AP complex.";
RL Genes Dev. 18:2269-2282(2004).
RN [9]
RP FUNCTION, INTERACTION WITH PABPC1 AND PABPC4, AND MUTAGENESIS OF PHE-20.
RX PubMed=17267499; DOI=10.1128/jvi.02007-06;
RA Katzenellenbogen R.A., Egelkrout E.M., Vliet-Gregg P., Gewin L.C.,
RA Gafken P.R., Galloway D.A.;
RT "NFX1-123 and poly(A) binding proteins synergistically augment activation
RT of telomerase in human papillomavirus type 16 E6-expressing cells.";
RL J. Virol. 81:3786-3796(2007).
RN [10]
RP IDENTIFICATION BY 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND IDENTIFICATION BY
RP 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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-95; SER-150 AND
RP SER-326, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Binds to the X-box motif of MHC class II genes and represses
CC their expression. May play an important role in regulating the duration
CC of an inflammatory response by limiting the period in which MHC class
CC II molecules are induced by interferon-gamma. Isoform 3 binds to the X-
CC box motif of TERT promoter and represses its expression. Together with
CC PABPC1 or PABPC4, isoform 1 acts as a coactivator for TERT expression.
CC Mediates E2-dependent ubiquitination. {ECO:0000269|PubMed:10500182,
CC ECO:0000269|PubMed:15371341, ECO:0000269|PubMed:17267499}.
CC -!- SUBUNIT: Isoform 1 interacts with PABPC1 and PABPC4.
CC {ECO:0000269|PubMed:17267499}.
CC -!- SUBUNIT: (Microbial infection) Isoform 1 and isoform 3 interact with
CC human papillomavirus (HPV) type-16 E6 oncoprotein.
CC {ECO:0000269|PubMed:15371341}.
CC -!- INTERACTION:
CC Q12986; P54253: ATXN1; NbExp=3; IntAct=EBI-2130062, EBI-930964;
CC Q12986; G5E9A7: DMWD; NbExp=3; IntAct=EBI-2130062, EBI-10976677;
CC Q12986; P14136: GFAP; NbExp=3; IntAct=EBI-2130062, EBI-744302;
CC Q12986; P28799: GRN; NbExp=3; IntAct=EBI-2130062, EBI-747754;
CC Q12986; P02545: LMNA; NbExp=3; IntAct=EBI-2130062, EBI-351935;
CC Q12986; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-2130062, EBI-5235340;
CC Q12986; Q86WV8: TSC1; NbExp=3; IntAct=EBI-2130062, EBI-12806590;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=NFX-123;
CC IsoId=Q12986-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q12986-2; Sequence=VSP_033684, VSP_033685;
CC Name=3; Synonyms=NFX-91;
CC IsoId=Q12986-3; Sequence=VSP_033682, VSP_033683;
CC -!- INDUCTION: By IFNG/IFN-gamma.
CC -!- DOMAIN: The RING-type zinc finger domain interacts with an ubiquitin-
CC conjugating enzyme (E2) and facilitates ubiquitination.
CC -!- PTM: Isoform 3 is polyubiquitinated in the presence of HPV16 E6
CC protein; which leads to proteasomal degradation. Isoform 1 is not
CC polyubiquitinated.
CC -!- SIMILARITY: Belongs to the NFX1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA69517.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF332009; AAK16545.1; -; mRNA.
DR EMBL; AK291643; BAF84332.1; -; mRNA.
DR EMBL; AL356472; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL356218; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471071; EAW58510.1; -; Genomic_DNA.
DR EMBL; CH471071; EAW58511.1; -; Genomic_DNA.
DR EMBL; BC012151; AAH12151.1; -; mRNA.
DR EMBL; U15306; AAA69517.1; ALT_FRAME; mRNA.
DR CCDS; CCDS6538.1; -. [Q12986-1]
DR CCDS; CCDS6540.1; -. [Q12986-3]
DR PIR; I38869; I38869.
DR RefSeq; NP_002495.2; NM_002504.5. [Q12986-1]
DR RefSeq; NP_667345.1; NM_147134.3. [Q12986-3]
DR AlphaFoldDB; Q12986; -.
DR SMR; Q12986; -.
DR BioGRID; 110865; 442.
DR ELM; Q12986; -.
DR IntAct; Q12986; 23.
DR STRING; 9606.ENSP00000368856; -.
DR iPTMnet; Q12986; -.
DR PhosphoSitePlus; Q12986; -.
DR BioMuta; NFX1; -.
DR DMDM; 189047116; -.
DR EPD; Q12986; -.
DR jPOST; Q12986; -.
DR MassIVE; Q12986; -.
DR MaxQB; Q12986; -.
DR PaxDb; Q12986; -.
DR PeptideAtlas; Q12986; -.
DR PRIDE; Q12986; -.
DR ProteomicsDB; 59082; -. [Q12986-1]
DR ProteomicsDB; 59083; -. [Q12986-2]
DR ProteomicsDB; 59084; -. [Q12986-3]
DR Antibodypedia; 25201; 146 antibodies from 29 providers.
DR DNASU; 4799; -.
DR Ensembl; ENST00000318524.6; ENSP00000317695.6; ENSG00000086102.19. [Q12986-3]
DR Ensembl; ENST00000379540.8; ENSP00000368856.3; ENSG00000086102.19. [Q12986-1]
DR GeneID; 4799; -.
DR KEGG; hsa:4799; -.
DR MANE-Select; ENST00000379540.8; ENSP00000368856.3; NM_002504.6; NP_002495.2.
DR UCSC; uc003zso.4; human. [Q12986-1]
DR CTD; 4799; -.
DR DisGeNET; 4799; -.
DR GeneCards; NFX1; -.
DR HGNC; HGNC:7803; NFX1.
DR HPA; ENSG00000086102; Low tissue specificity.
DR MIM; 603255; gene.
DR neXtProt; NX_Q12986; -.
DR OpenTargets; ENSG00000086102; -.
DR PharmGKB; PA31608; -.
DR VEuPathDB; HostDB:ENSG00000086102; -.
DR eggNOG; KOG1952; Eukaryota.
DR GeneTree; ENSGT00940000156325; -.
DR HOGENOM; CLU_005714_1_2_1; -.
DR InParanoid; Q12986; -.
DR OMA; WCEKEVD; -.
DR OrthoDB; 299100at2759; -.
DR PhylomeDB; Q12986; -.
DR TreeFam; TF105889; -.
DR PathwayCommons; Q12986; -.
DR SignaLink; Q12986; -.
DR SIGNOR; Q12986; -.
DR BioGRID-ORCS; 4799; 19 hits in 1101 CRISPR screens.
DR ChiTaRS; NFX1; human.
DR GeneWiki; NFX1; -.
DR GenomeRNAi; 4799; -.
DR Pharos; Q12986; Tbio.
DR PRO; PR:Q12986; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q12986; protein.
DR Bgee; ENSG00000086102; Expressed in buccal mucosa cell and 190 other tissues.
DR Genevisible; Q12986; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:ARUK-UCL.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
DR GO; GO:0045347; P:negative regulation of MHC class II biosynthetic process; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0051865; P:protein autoubiquitination; IDA:ARUK-UCL.
DR GO; GO:0016567; P:protein ubiquitination; TAS:ARUK-UCL.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
DR CDD; cd02643; R3H_NF-X1; 1.
DR Gene3D; 3.30.1370.50; -; 1.
DR InterPro; IPR034078; NFX1_fam.
DR InterPro; IPR001374; R3H_dom.
DR InterPro; IPR036867; R3H_dom_sf.
DR InterPro; IPR034076; R3H_NF-X1.
DR InterPro; IPR000967; Znf_NFX1.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR001841; Znf_RING.
DR PANTHER; PTHR12360; PTHR12360; 1.
DR Pfam; PF01424; R3H; 1.
DR Pfam; PF01422; zf-NF-X1; 8.
DR SMART; SM00393; R3H; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00438; ZnF_NFX; 9.
DR SUPFAM; SSF82708; SSF82708; 1.
DR PROSITE; PS51061; R3H; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; DNA-binding; Host-virus interaction;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Transferase;
KW Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..1120
FT /note="Transcriptional repressor NF-X1"
FT /id="PRO_0000055979"
FT DOMAIN 994..1062
FT /note="R3H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00382"
FT ZN_FING 358..409
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 453..471
FT /note="NF-X1-type 1"
FT ZN_FING 506..525
FT /note="NF-X1-type 2"
FT ZN_FING 567..586
FT /note="NF-X1-type 3"
FT ZN_FING 632..655
FT /note="NF-X1-type 4"
FT ZN_FING 694..713
FT /note="NF-X1-type 5"
FT ZN_FING 721..740
FT /note="NF-X1-type 6"
FT ZN_FING 832..854
FT /note="NF-X1-type 7"
FT ZN_FING 863..884
FT /note="NF-X1-type 8"
FT REGION 9..26
FT /note="Interaction with PABPC1 and PABC4"
FT /evidence="ECO:0000269|PubMed:17267499"
FT REGION 22..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1081..1109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B1AY10"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B1AY10"
FT MOD_RES 150
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 809..833
FT /note="FRSNIPCHLVDISCGLPCSATLPCG -> QSHYWASTQKKRSHYMKKIPAHA
FT CL (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_033682"
FT VAR_SEQ 834..1120
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_033683"
FT VAR_SEQ 1014..1024
FT /note="GKNSKKSHSFP -> VEVETSHWTFL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.1"
FT /id="VSP_033684"
FT VAR_SEQ 1025..1120
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.1"
FT /id="VSP_033685"
FT VARIANT 731
FT /note="H -> Y (in dbSNP:rs5017299)"
FT /id="VAR_043380"
FT VARIANT 760
FT /note="P -> S (in dbSNP:rs2860036)"
FT /id="VAR_043381"
FT VARIANT 1086
FT /note="P -> Q (in dbSNP:rs2274866)"
FT /id="VAR_043382"
FT MUTAGEN 20
FT /note="F->A: Reduces PABPC1 and PABC4 binding."
FT /evidence="ECO:0000269|PubMed:17267499"
FT CONFLICT 179
FT /note="G -> A (in Ref. 1; AAA69517)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="G -> E (in Ref. 1; AAA69517)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="Q -> P (in Ref. 1; AAA69517)"
FT /evidence="ECO:0000305"
FT CONFLICT 419..420
FT /note="YT -> FS (in Ref. 1; AAA69517)"
FT /evidence="ECO:0000305"
FT CONFLICT 560
FT /note="I -> T (in Ref. 1; AAA69517)"
FT /evidence="ECO:0000305"
FT CONFLICT 653
FT /note="C -> V (in Ref. 1; AAA69517)"
FT /evidence="ECO:0000305"
FT CONFLICT 678
FT /note="E -> EA (in Ref. 2; BAF84332)"
FT /evidence="ECO:0000305"
FT CONFLICT 714
FT /note="I -> N (in Ref. 1; AAA69517)"
FT /evidence="ECO:0000305"
FT CONFLICT 786
FT /note="C -> G (in Ref. 1; AAA69517)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1120 AA; 124395 MW; F2203BE1DB6437E6 CRC64;
MAEAPPVSGT FKFNTDAAEF IPQEKKNSGL NCGTQRRLDS NRIGRRNYSS PPPCHLSRQV
PYDEISAVHQ HSYHPSGSKP KSQQTSFQSS PCNKSPKSHG LQNQPWQKLR NEKHHIRVKK
AQSLAEQTSD TAGLESSTRS ESGTDLREHS PSESEKEVVG ADPRGAKPKK ATQFVYSYGR
GPKVKGKLKC EWSNRTTPKP EDAGPESTKP VGVFHPDSSE ASSRKGVLDG YGARRNEQRR
YPQKRPPWEV EGARPRPGRN PPKQEGHRHT NAGHRNNMGP IPKDDLNERP AKSTCDSENL
AVINKSSRRV DQEKCTVRRQ DPQVVSPFSR GKQNHVLKNV ETHTGSLIEQ LTTEKYECMV
CCELVRVTAP VWSCQSCYHV FHLNCIKKWA RSPASQADGQ SGWRCPACQN VSAHVPNTYT
CFCGKVKNPE WSRNEIPHSC GEVCRKKQPG QDCPHSCNLL CHPGPCPPCP AFMTKTCECG
RTRHTVRCGQ AVSVHCSNPC ENILNCGQHQ CAELCHGGQC QPCQIILNQV CYCGSTSRDV
LCGTDVGKSD GFGDFSCLKI CGKDLKCGNH TCSQVCHPQP CQQCPRLPQL VRCCPCGQTP
LSQLLELGSS SRKTCMDPVP SCGKVCGKPL PCGSLDFIHT CEKLCHEGDC GPCSRTSVIS
CRCSFRTKEL PCTSLKSEDA TFMCDKRCNK KRLCGRHKCN EICCVDKEHK CPLICGRKLR
CGLHRCEEPC HRGNCQTCWQ ASFDELTCHC GASVIYPPVP CGTRPPECTQ TCARVHECDH
PVYHSCHSEE KCPPCTFLTQ KWCMGKHEFR SNIPCHLVDI SCGLPCSATL PCGMHKCQRL
CHKGECLVDE PCKQPCTTPR ADCGHPCMAP CHTSSPCPVT ACKAKVELQC ECGRRKEMVI
CSEASSTYQR IAAISMASKI TDMQLGGSVE ISKLITKKEV HQARLECDEE CSALERKKRL
AEAFHISEDS DPFNIRSSGS KFSDSLKEDA RKDLKFVSDV EKEMETLVEA VNKGKNSKKS
HSFPPMNRDH RRIIHDLAQV YGLESVSYDS EPKRNVVVTA IRGKSVCPPT TLTGVLEREM
QARPPPPIPH HRHQSDKNPG SSNLQKITKE PIIDYFDVQD
