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 27-MAR-2024, entry version 211. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 451. DR ELM; Q12986; -. DR IntAct; Q12986; 23. DR STRING; 9606.ENSP00000368856; -. DR GlyGen; Q12986; 1 site, 1 O-linked glycan (1 site). 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; 9606-ENSP00000368856; -. DR PeptideAtlas; Q12986; -. DR ProteomicsDB; 59082; -. [Q12986-1] DR ProteomicsDB; 59083; -. [Q12986-2] DR ProteomicsDB; 59084; -. [Q12986-3] DR Pumba; Q12986; -. DR Antibodypedia; 25201; 163 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 AGR; HGNC:7803; -. 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; PRTSCED; -. DR OrthoDB; 1412at2759; -. DR PhylomeDB; Q12986; -. DR TreeFam; TF105889; -. DR PathwayCommons; Q12986; -. DR SignaLink; Q12986; -. DR SIGNOR; Q12986; -. DR BioGRID-ORCS; 4799; 19 hits in 1177 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 192 other cell types or tissues. 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:0006366; P:transcription by RNA polymerase II; TAS:ProtInc. DR CDD; cd06008; NF-X1-zinc-finger; 6. DR CDD; cd02643; R3H_NF-X1; 1. DR CDD; cd16696; RING-CH-C4HC3_NFX1; 1. DR Gene3D; 3.30.1370.50; R3H-like domain; 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; NUCLEAR TRANSCRIPTION FACTOR, X-BOX BINDING 1 NFX1; 1. DR PANTHER; PTHR12360:SF12; TRANSCRIPTIONAL REPRESSOR NF-X1; 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; R3H domain; 1. DR SUPFAM; SSF57850; RING/U-box; 1. DR PROSITE; PS51061; R3H; 1. DR PROSITE; PS50089; ZF_RING_2; 1. DR Genevisible; Q12986; HS. 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 //