ID FUBP1_HUMAN Reviewed; 644 AA.
AC Q96AE4; Q12828;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 3.
DT 27-MAR-2024, entry version 208.
DE RecName: Full=Far upstream element-binding protein 1;
DE Short=FBP;
DE Short=FUSE-binding protein 1;
DE AltName: Full=DNA helicase V;
DE Short=hDH V;
GN Name=FUBP1;
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), PROTEIN SEQUENCE OF 192-194;
RP 204-207; 273-280; 285-291; 301-315; 322-329; 395-398; 410-412; 431-439 AND
RP 441-444, AND FUNCTION.
RC TISSUE=Leukemia;
RX PubMed=8125259; DOI=10.1101/gad.8.4.465;
RA Duncan R., Bazar L., Michelotti G., Tomonaga T., Krutzsch H., Avigan M.,
RA Levens D.;
RT "A sequence-specific, single-strand binding protein activates the far
RT upstream element of c-myc and defines a new DNA-binding motif.";
RL Genes Dev. 8:465-480(1994).
RN [2]
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., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., 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., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., 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., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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 [4]
RP PROTEIN SEQUENCE OF 45-64; 134-146; 272-284; 309-322; 380-387; 415-425 AND
RP 431-440.
RX PubMed=11222755; DOI=10.1093/nar/29.5.1061;
RA Vindigni A., Ochem A., Triolo G., Falaschi A.;
RT "Identification of human DNA helicase V with the far upstream element-
RT binding protein.";
RL Nucleic Acids Res. 29:1061-1067(2001).
RN [5]
RP PROTEIN SEQUENCE OF 107-118; 134-146; 163-170; 249-256; 272-293 AND
RP 332-344, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [6]
RP PARTIAL PROTEIN SEQUENCE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=12176931; DOI=10.1101/gr.473902;
RA Rappsilber J., Ryder U., Lamond A.I., Mann M.;
RT "Large-scale proteomic analysis of the human spliceosome.";
RL Genome Res. 12:1231-1245(2002).
RN [7]
RP IDENTIFICATION IN A COMPLEX WITH PUF60 AND FUSE DNA, AND INTERACTION WITH
RP PUF60.
RX PubMed=10882074; DOI=10.1016/s1097-2765(00)80428-1;
RA Liu J., He L., Collins I., Ge H., Libutti D., Li J., Egly J.-M., Levens D.;
RT "The FBP interacting repressor targets TFIIH to inhibit activated
RT transcription.";
RL Mol. Cell 5:331-341(2000).
RN [8]
RP INTERACTION WITH JTV1, UBIQUITINATION, AND PROTEASOME-MEDIATED DEGRADATION.
RX PubMed=12819782; DOI=10.1038/ng1182;
RA Kim M.J., Park B.-J., Kang Y.-S., Kim H.J., Park J.-H., Kang J.W.,
RA Lee S.W., Han J.M., Lee H.-W., Kim S.;
RT "Downregulation of FUSE-binding protein and c-myc by tRNA synthetase
RT cofactor p38 is required for lung cell differentiation.";
RL Nat. Genet. 34:330-336(2003).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [10]
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., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-153 AND SER-630, 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 [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-630, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-153 AND SER-630, 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 [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140 AND SER-630, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-55; SER-140; THR-153
RP AND THR-432, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-359; ARG-361 AND ARG-363, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [20]
RP STRUCTURE BY NMR OF 278-447 IN COMPLEX WITH SINGLE-STRANDED FUSE DNA.
RX PubMed=11875576; DOI=10.1038/4151051a;
RA Braddock D.T., Louis J.M., Baber J.L., Levens D., Clore G.M.;
RT "Structure and dynamics of KH domains from FBP bound to single-stranded
RT DNA.";
RL Nature 415:1051-1056(2002).
CC -!- FUNCTION: Regulates MYC expression by binding to a single-stranded far-
CC upstream element (FUSE) upstream of the MYC promoter. May act both as
CC activator and repressor of transcription. {ECO:0000269|PubMed:8125259}.
CC -!- SUBUNIT: Found in a complex with PUF60 and far upstream element (FUSE)
CC DNA segment. Interacts with PUF60 and JTV1.
CC {ECO:0000269|PubMed:10882074, ECO:0000269|PubMed:11875576,
CC ECO:0000269|PubMed:12819782}.
CC -!- INTERACTION:
CC Q96AE4; Q13155: AIMP2; NbExp=4; IntAct=EBI-711404, EBI-745226;
CC Q96AE4; Q9UPT9: USP22; NbExp=3; IntAct=EBI-711404, EBI-723510;
CC Q96AE4-1; Q9UHX1-2: PUF60; NbExp=2; IntAct=EBI-5455665, EBI-11529177;
CC Q96AE4-2; P50995: ANXA11; NbExp=3; IntAct=EBI-12121668, EBI-715243;
CC Q96AE4-2; Q8NDC0: MAPK1IP1L; NbExp=3; IntAct=EBI-12121668, EBI-741424;
CC Q96AE4-2; Q96HR8: NAF1; NbExp=3; IntAct=EBI-12121668, EBI-2515597;
CC Q96AE4-2; Q6NWY9: PRPF40B; NbExp=3; IntAct=EBI-12121668, EBI-11285481;
CC Q96AE4-2; Q9NZ81: PRR13; NbExp=3; IntAct=EBI-12121668, EBI-740924;
CC Q96AE4-2; Q9UHX1-2: PUF60; NbExp=3; IntAct=EBI-12121668, EBI-11529177;
CC Q96AE4-2; P09012: SNRPA; NbExp=3; IntAct=EBI-12121668, EBI-607085;
CC Q96AE4-2; P14678-2: SNRPB; NbExp=3; IntAct=EBI-12121668, EBI-372475;
CC Q96AE4-2; P09234: SNRPC; NbExp=3; IntAct=EBI-12121668, EBI-766589;
CC Q96AE4-2; Q01085-2: TIAL1; NbExp=3; IntAct=EBI-12121668, EBI-11064654;
CC Q96AE4-2; P26368-2: U2AF2; NbExp=3; IntAct=EBI-12121668, EBI-11097439;
CC Q96AE4-2; A5D8V6: VPS37C; NbExp=3; IntAct=EBI-12121668, EBI-2559305;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96AE4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96AE4-2; Sequence=VSP_021107, VSP_008321;
CC -!- PTM: Ubiquitinated. This targets the protein for proteasome-mediated
CC degradation. {ECO:0000269|PubMed:12819782}.
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DR EMBL; U05040; AAA17976.2; -; mRNA.
DR EMBL; AC096948; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC017247; AAH17247.1; -; mRNA.
DR CCDS; CCDS683.1; -. [Q96AE4-1]
DR PIR; A53184; A53184.
DR RefSeq; NP_001290362.1; NM_001303433.1.
DR RefSeq; NP_003893.2; NM_003902.4. [Q96AE4-1]
DR RefSeq; XP_016858232.1; XM_017002743.1. [Q96AE4-2]
DR PDB; 1J4W; NMR; -; A=278-447.
DR PDB; 2KXH; NMR; -; B=27-52.
DR PDB; 4LIJ; X-ray; 1.80 A; A/B/C=86-175.
DR PDB; 6Y24; X-ray; 1.86 A; A=365-455.
DR PDB; 6Y2C; X-ray; 2.00 A; A/B=261-351.
DR PDB; 6Y2D; X-ray; 1.90 A; A/B/C/D=185-259.
DR PDB; 8P25; NMR; -; A=21-56.
DR PDBsum; 1J4W; -.
DR PDBsum; 2KXH; -.
DR PDBsum; 4LIJ; -.
DR PDBsum; 6Y24; -.
DR PDBsum; 6Y2C; -.
DR PDBsum; 6Y2D; -.
DR PDBsum; 8P25; -.
DR AlphaFoldDB; Q96AE4; -.
DR SMR; Q96AE4; -.
DR BioGRID; 114399; 205.
DR DIP; DIP-47273N; -.
DR ELM; Q96AE4; -.
DR IntAct; Q96AE4; 69.
DR MINT; Q96AE4; -.
DR STRING; 9606.ENSP00000359804; -.
DR BindingDB; Q96AE4; -.
DR ChEMBL; CHEMBL4295922; -.
DR DrugBank; DB05786; Irofulven.
DR DrugBank; DB12893; Sacituzumab govitecan.
DR GlyGen; Q96AE4; 9 sites, 1 O-linked glycan (9 sites).
DR iPTMnet; Q96AE4; -.
DR MetOSite; Q96AE4; -.
DR PhosphoSitePlus; Q96AE4; -.
DR SwissPalm; Q96AE4; -.
DR BioMuta; FUBP1; -.
DR DMDM; 116241370; -.
DR REPRODUCTION-2DPAGE; IPI00375441; -.
DR EPD; Q96AE4; -.
DR jPOST; Q96AE4; -.
DR MassIVE; Q96AE4; -.
DR MaxQB; Q96AE4; -.
DR PaxDb; 9606-ENSP00000359804; -.
DR PeptideAtlas; Q96AE4; -.
DR ProteomicsDB; 75958; -. [Q96AE4-1]
DR ProteomicsDB; 75959; -. [Q96AE4-2]
DR Pumba; Q96AE4; -.
DR TopDownProteomics; Q96AE4-1; -. [Q96AE4-1]
DR Antibodypedia; 1310; 381 antibodies from 35 providers.
DR DNASU; 8880; -.
DR Ensembl; ENST00000294623.8; ENSP00000294623.4; ENSG00000162613.18. [Q96AE4-2]
DR Ensembl; ENST00000370768.7; ENSP00000359804.2; ENSG00000162613.18. [Q96AE4-1]
DR GeneID; 8880; -.
DR KEGG; hsa:8880; -.
DR MANE-Select; ENST00000370768.7; ENSP00000359804.2; NM_003902.5; NP_003893.2.
DR UCSC; uc001dii.4; human. [Q96AE4-1]
DR AGR; HGNC:4004; -.
DR CTD; 8880; -.
DR DisGeNET; 8880; -.
DR GeneCards; FUBP1; -.
DR HGNC; HGNC:4004; FUBP1.
DR HPA; ENSG00000162613; Low tissue specificity.
DR MIM; 603444; gene.
DR neXtProt; NX_Q96AE4; -.
DR OpenTargets; ENSG00000162613; -.
DR PharmGKB; PA28420; -.
DR VEuPathDB; HostDB:ENSG00000162613; -.
DR eggNOG; KOG1676; Eukaryota.
DR GeneTree; ENSGT00940000160043; -.
DR HOGENOM; CLU_014285_1_0_1; -.
DR InParanoid; Q96AE4; -.
DR OMA; YGQQGSW; -.
DR OrthoDB; 1662at2759; -.
DR PhylomeDB; Q96AE4; -.
DR TreeFam; TF313654; -.
DR PathwayCommons; Q96AE4; -.
DR SignaLink; Q96AE4; -.
DR SIGNOR; Q96AE4; -.
DR BioGRID-ORCS; 8880; 165 hits in 1188 CRISPR screens.
DR ChiTaRS; FUBP1; human.
DR EvolutionaryTrace; Q96AE4; -.
DR GeneWiki; Far_upstream_element-binding_protein_1; -.
DR GenomeRNAi; 8880; -.
DR Pharos; Q96AE4; Tbio.
DR PRO; PR:Q96AE4; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q96AE4; Protein.
DR Bgee; ENSG00000162613; Expressed in ventricular zone and 212 other cell types or tissues.
DR ExpressionAtlas; Q96AE4; baseline and differential.
DR Genevisible; Q96AE4; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; TAS:ProtInc.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR CDD; cd22478; KH-I_FUBP1_rpt1; 1.
DR CDD; cd22481; KH-I_FUBP1_rpt2; 1.
DR CDD; cd22484; KH-I_FUBP1_rpt3; 1.
DR CDD; cd22487; KH-I_FUBP1_rpt4; 1.
DR Gene3D; 3.30.1370.10; K Homology domain, type 1; 4.
DR InterPro; IPR015096; FUBP_C.
DR InterPro; IPR048249; KH-I_FUBP1_dom1.
DR InterPro; IPR048250; KH-I_FUBP1_dom2.
DR InterPro; IPR048251; KH-I_FUBP1_dom3.
DR InterPro; IPR048252; KH-I_FUBP1_dom4.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR PANTHER; PTHR10288:SF99; FAR UPSTREAM ELEMENT-BINDING PROTEIN 1; 1.
DR PANTHER; PTHR10288; KH DOMAIN CONTAINING RNA BINDING PROTEIN; 1.
DR Pfam; PF09005; DUF1897; 2.
DR Pfam; PF00013; KH_1; 4.
DR SMART; SM00322; KH; 4.
DR SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 4.
DR PROSITE; PS50084; KH_TYPE_1; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Direct protein sequencing;
KW DNA-binding; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..644
FT /note="Far upstream element-binding protein 1"
FT /id="PRO_0000050135"
FT DOMAIN 100..164
FT /note="KH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 185..251
FT /note="KH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 275..339
FT /note="KH 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 376..443
FT /note="KH 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 44..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..505
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..578
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 153
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 321
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q91WJ8"
FT MOD_RES 359
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 361
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 363
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 432
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 630
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT VAR_SEQ 97
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021107"
FT VAR_SEQ 643..644
FT /note="GQ -> CRFDPASIELAL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_008321"
FT VARIANT 399
FT /note="I -> K (in dbSNP:rs12748509)"
FT /id="VAR_049679"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:8P25"
FT HELIX 30..44
FT /evidence="ECO:0007829|PDB:2KXH"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:8P25"
FT STRAND 101..108
FT /evidence="ECO:0007829|PDB:4LIJ"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:4LIJ"
FT HELIX 112..116
FT /evidence="ECO:0007829|PDB:4LIJ"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:4LIJ"
FT HELIX 121..130
FT /evidence="ECO:0007829|PDB:4LIJ"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:4LIJ"
FT STRAND 144..152
FT /evidence="ECO:0007829|PDB:4LIJ"
FT HELIX 154..168
FT /evidence="ECO:0007829|PDB:4LIJ"
FT STRAND 186..192
FT /evidence="ECO:0007829|PDB:6Y2D"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:6Y2D"
FT HELIX 197..201
FT /evidence="ECO:0007829|PDB:6Y2D"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:6Y2D"
FT HELIX 206..215
FT /evidence="ECO:0007829|PDB:6Y2D"
FT STRAND 217..221
FT /evidence="ECO:0007829|PDB:6Y2D"
FT STRAND 233..239
FT /evidence="ECO:0007829|PDB:6Y2D"
FT HELIX 241..255
FT /evidence="ECO:0007829|PDB:6Y2D"
FT HELIX 261..266
FT /evidence="ECO:0007829|PDB:6Y2C"
FT STRAND 278..283
FT /evidence="ECO:0007829|PDB:6Y2C"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:6Y2C"
FT HELIX 287..291
FT /evidence="ECO:0007829|PDB:6Y2C"
FT HELIX 293..295
FT /evidence="ECO:0007829|PDB:6Y2C"
FT HELIX 296..305
FT /evidence="ECO:0007829|PDB:6Y2C"
FT STRAND 308..311
FT /evidence="ECO:0007829|PDB:6Y2C"
FT STRAND 319..327
FT /evidence="ECO:0007829|PDB:6Y2C"
FT HELIX 329..345
FT /evidence="ECO:0007829|PDB:6Y2C"
FT STRAND 377..384
FT /evidence="ECO:0007829|PDB:6Y24"
FT HELIX 385..387
FT /evidence="ECO:0007829|PDB:6Y24"
FT HELIX 388..392
FT /evidence="ECO:0007829|PDB:6Y24"
FT HELIX 394..396
FT /evidence="ECO:0007829|PDB:6Y24"
FT HELIX 397..406
FT /evidence="ECO:0007829|PDB:6Y24"
FT STRAND 409..412
FT /evidence="ECO:0007829|PDB:6Y24"
FT TURN 417..419
FT /evidence="ECO:0007829|PDB:1J4W"
FT STRAND 424..431
FT /evidence="ECO:0007829|PDB:6Y24"
FT HELIX 433..447
FT /evidence="ECO:0007829|PDB:6Y24"
SQ SEQUENCE 644 AA; 67560 MW; 1FD422EA2FC49531 CRC64;
MADYSTVPPP SSGSAGGGGG GGGGGGVNDA FKDALQRARQ IAAKIGGDAG TSLNSNDYGY
GGQKRPLEDG DQPDAKKVAP QNDSFGTQLP PMHQQQSRSV MTEEYKVPDG MVGFIIGRGG
EQISRIQQES GCKIQIAPDS GGLPERSCML TGTPESVQSA KRLLDQIVEK GRPAPGFHHG
DGPGNAVQEI MIPASKAGLV IGKGGETIKQ LQERAGVKMV MIQDGPQNTG ADKPLRITGD
PYKVQQAKEM VLELIRDQGG FREVRNEYGS RIGGNEGIDV PIPRFAVGIV IGRNGEMIKK
IQNDAGVRIQ FKPDDGTTPE RIAQITGPPD RCQHAAEIIT DLLRSVQAGN PGGPGPGGRG
RGRGQGNWNM GPPGGLQEFN FIVPTGKTGL IIGKGGETIK SISQQSGARI ELQRNPPPNA
DPNMKLFTIR GTPQQIDYAR QLIEEKIGGP VNPLGPPVPH GPHGVPGPHG PPGPPGPGTP
MGPYNPAPYN PGPPGPAPHG PPAPYAPQGW GNAYPHWQQQ APPDPAKAGT DPNSAAWAAY
YAHYYQQQAQ PPPAAPAGAP TTTQTNGQGD QQNPAPAGQV DYTKAWEEYY KKMGQAVPAP
TGAPPGGQPD YSAAWAEYYR QQAAYYAQTS PQGMPQHPPA PQGQ
//
