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FUBP1_HUMAN
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   03-AUG-2022, entry version 199.
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   PDBsum; 1J4W; -.
DR   PDBsum; 2KXH; -.
DR   PDBsum; 4LIJ; -.
DR   PDBsum; 6Y24; -.
DR   PDBsum; 6Y2C; -.
DR   PDBsum; 6Y2D; -.
DR   AlphaFoldDB; Q96AE4; -.
DR   SMR; Q96AE4; -.
DR   BioGRID; 114399; 167.
DR   DIP; DIP-47273N; -.
DR   ELM; Q96AE4; -.
DR   IntAct; Q96AE4; 66.
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; 1 site, 1 O-linked glycan (1 site).
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; Q96AE4; -.
DR   PeptideAtlas; Q96AE4; -.
DR   PRIDE; Q96AE4; -.
DR   ProteomicsDB; 75958; -. [Q96AE4-1]
DR   ProteomicsDB; 75959; -. [Q96AE4-2]
DR   TopDownProteomics; Q96AE4-1; -. [Q96AE4-1]
DR   Antibodypedia; 1310; 318 antibodies from 35 providers.
DR   DNASU; 8880; -.
DR   Ensembl; ENST00000294623.8; ENSP00000294623.4; ENSG00000162613.17. [Q96AE4-2]
DR   Ensembl; ENST00000370768.7; ENSP00000359804.2; ENSG00000162613.17. [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   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; HAKQLVY; -.
DR   OrthoDB; 590738at2759; -.
DR   PhylomeDB; Q96AE4; -.
DR   TreeFam; TF313654; -.
DR   PathwayCommons; Q96AE4; -.
DR   SignaLink; Q96AE4; -.
DR   SIGNOR; Q96AE4; -.
DR   BioGRID-ORCS; 8880; 149 hits in 1102 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 210 other 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   Gene3D; 3.30.1370.10; -; 4.
DR   InterPro; IPR015096; FUBP_C.
DR   InterPro; IPR004087; KH_dom.
DR   InterPro; IPR004088; KH_dom_type_1.
DR   InterPro; IPR036612; KH_dom_type_1_sf.
DR   Pfam; PF09005; DUF1897; 2.
DR   Pfam; PF00013; KH_1; 4.
DR   SMART; SM00322; KH; 4.
DR   SUPFAM; SSF54791; SSF54791; 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   HELIX           30..44
FT                   /evidence="ECO:0007829|PDB:2KXH"
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
 
 
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