Full text data of FUBP1
FUBP1
[Confidence: low (only semi-automatic identification from reviews)]
Far upstream element-binding protein 1; FBP; FUSE-binding protein 1 (DNA helicase V; hDH V)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Far upstream element-binding protein 1; FBP; FUSE-binding protein 1 (DNA helicase V; hDH V)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q96AE4
ID FUBP1_HUMAN Reviewed; 644 AA.
AC Q96AE4; Q12828;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 17-OCT-2006, sequence version 3.
DT 22-JAN-2014, entry version 128.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RP AND 441-444, AND FUNCTION.
RC TISSUE=Leukemia;
RX PubMed=8125259;
RA Duncan R., Bazar L., Michelotti G., Tomonaga T., Krutzsch H.,
RA Avigan M., 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.,
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 [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
RT project: 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
RP AND 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 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 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
RP WITH 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.,
RA 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
RP 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
RT 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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling 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
RT phosphorylation 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 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 [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-630, AND MASS
RP 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-153 AND SER-630, AND
RP 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).
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.,
RA Buerckstuemmer T., 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 MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [18]
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-
RT stranded DNA.";
RL Nature 415:1051-1056(2002).
CC -!- FUNCTION: Regulates MYC expression by binding to a single-stranded
CC far-upstream element (FUSE) upstream of the MYC promoter. May act
CC both as activator and repressor of transcription.
CC -!- SUBUNIT: Found in a complex with PUF60 and far upstream element
CC (FUSE) DNA segment. Interacts with PUF60 and JTV1.
CC -!- INTERACTION:
CC Q13155:AIMP2; NbExp=4; IntAct=EBI-711404, EBI-745226;
CC Q9UPT9:USP22; NbExp=3; IntAct=EBI-711404, EBI-723510;
CC -!- SUBCELLULAR LOCATION: Nucleus (Probable).
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 Note=No experimental confirmation available;
CC -!- PTM: Ubiquitinated. This targets the protein for proteasome-
CC mediated degradation.
CC -!- SIMILARITY: Contains 4 KH domains.
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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 PIR; A53184; A53184.
DR RefSeq; NP_003893.2; NM_003902.3.
DR RefSeq; XP_005271367.1; XM_005271310.1.
DR UniGene; Hs.567380; -.
DR PDB; 1J4W; NMR; -; A=278-447.
DR PDB; 2KXH; NMR; -; B=27-52.
DR PDBsum; 1J4W; -.
DR PDBsum; 2KXH; -.
DR ProteinModelPortal; Q96AE4; -.
DR SMR; Q96AE4; 22-52, 94-447.
DR DIP; DIP-47273N; -.
DR IntAct; Q96AE4; 25.
DR MINT; MINT-1374324; -.
DR STRING; 9606.ENSP00000359804; -.
DR PhosphoSite; Q96AE4; -.
DR DMDM; 116241370; -.
DR REPRODUCTION-2DPAGE; IPI00375441; -.
DR PaxDb; Q96AE4; -.
DR PRIDE; Q96AE4; -.
DR DNASU; 8880; -.
DR Ensembl; ENST00000294623; ENSP00000294623; ENSG00000162613.
DR Ensembl; ENST00000370768; ENSP00000359804; ENSG00000162613.
DR GeneID; 8880; -.
DR KEGG; hsa:8880; -.
DR UCSC; uc001dii.3; human.
DR CTD; 8880; -.
DR GeneCards; GC01M078400; -.
DR HGNC; HGNC:4004; FUBP1.
DR HPA; HPA006149; -.
DR MIM; 603444; gene.
DR neXtProt; NX_Q96AE4; -.
DR PharmGKB; PA28420; -.
DR eggNOG; NOG300923; -.
DR HOGENOM; HOG000231552; -.
DR HOVERGEN; HBG000625; -.
DR KO; K13210; -.
DR OrthoDB; EOG77Q4WB; -.
DR ChiTaRS; FUBP1; human.
DR EvolutionaryTrace; Q96AE4; -.
DR GeneWiki; Far_upstream_element-binding_protein_1; -.
DR GenomeRNAi; 8880; -.
DR NextBio; 33343; -.
DR PRO; PR:Q96AE4; -.
DR ArrayExpress; Q96AE4; -.
DR Bgee; Q96AE4; -.
DR CleanEx; HS_FUBP1; -.
DR Genevestigator; Q96AE4; -.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; TAS:ProtInc.
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:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc.
DR InterPro; IPR015096; DUF1897.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR Pfam; PF09005; DUF1897; 2.
DR Pfam; PF00013; KH_1; 4.
DR SMART; SM00322; KH; 4.
DR PROSITE; PS50084; KH_TYPE_1; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Direct protein sequencing; DNA-binding; Nucleus; Phosphoprotein;
KW Polymorphism; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 644 Far upstream element-binding protein 1.
FT /FTId=PRO_0000050135.
FT DOMAIN 100 164 KH 1.
FT DOMAIN 185 251 KH 2.
FT DOMAIN 275 339 KH 3.
FT DOMAIN 376 443 KH 4.
FT COMPBIAS 13 26 Gly-rich.
FT COMPBIAS 349 396 Gly-rich.
FT COMPBIAS 450 560 Pro-rich.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 140 140 Phosphoserine.
FT MOD_RES 153 153 Phosphothreonine.
FT MOD_RES 630 630 Phosphoserine.
FT VAR_SEQ 97 97 Missing (in isoform 2).
FT /FTId=VSP_021107.
FT VAR_SEQ 643 644 GQ -> CRFDPASIELAL (in isoform 2).
FT /FTId=VSP_008321.
FT VARIANT 399 399 I -> K (in dbSNP:rs12748509).
FT /FTId=VAR_049679.
FT HELIX 30 44
FT STRAND 278 283
FT HELIX 284 291
FT HELIX 293 295
FT HELIX 296 305
FT STRAND 308 312
FT STRAND 319 327
FT HELIX 329 346
FT STRAND 378 384
FT TURN 385 387
FT HELIX 388 392
FT HELIX 394 396
FT HELIX 397 406
FT STRAND 409 413
FT TURN 417 419
FT STRAND 424 430
FT HELIX 433 446
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
//
ID FUBP1_HUMAN Reviewed; 644 AA.
AC Q96AE4; Q12828;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 17-OCT-2006, sequence version 3.
DT 22-JAN-2014, entry version 128.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RP AND 441-444, AND FUNCTION.
RC TISSUE=Leukemia;
RX PubMed=8125259;
RA Duncan R., Bazar L., Michelotti G., Tomonaga T., Krutzsch H.,
RA Avigan M., 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.,
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 [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
RT project: 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
RP AND 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 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 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
RP WITH 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.,
RA 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
RP 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
RT 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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling 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
RT phosphorylation 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 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 [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-630, AND MASS
RP 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-153 AND SER-630, AND
RP 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).
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.,
RA Buerckstuemmer T., 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 MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [18]
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-
RT stranded DNA.";
RL Nature 415:1051-1056(2002).
CC -!- FUNCTION: Regulates MYC expression by binding to a single-stranded
CC far-upstream element (FUSE) upstream of the MYC promoter. May act
CC both as activator and repressor of transcription.
CC -!- SUBUNIT: Found in a complex with PUF60 and far upstream element
CC (FUSE) DNA segment. Interacts with PUF60 and JTV1.
CC -!- INTERACTION:
CC Q13155:AIMP2; NbExp=4; IntAct=EBI-711404, EBI-745226;
CC Q9UPT9:USP22; NbExp=3; IntAct=EBI-711404, EBI-723510;
CC -!- SUBCELLULAR LOCATION: Nucleus (Probable).
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 Note=No experimental confirmation available;
CC -!- PTM: Ubiquitinated. This targets the protein for proteasome-
CC mediated degradation.
CC -!- SIMILARITY: Contains 4 KH domains.
CC -----------------------------------------------------------------------
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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 PIR; A53184; A53184.
DR RefSeq; NP_003893.2; NM_003902.3.
DR RefSeq; XP_005271367.1; XM_005271310.1.
DR UniGene; Hs.567380; -.
DR PDB; 1J4W; NMR; -; A=278-447.
DR PDB; 2KXH; NMR; -; B=27-52.
DR PDBsum; 1J4W; -.
DR PDBsum; 2KXH; -.
DR ProteinModelPortal; Q96AE4; -.
DR SMR; Q96AE4; 22-52, 94-447.
DR DIP; DIP-47273N; -.
DR IntAct; Q96AE4; 25.
DR MINT; MINT-1374324; -.
DR STRING; 9606.ENSP00000359804; -.
DR PhosphoSite; Q96AE4; -.
DR DMDM; 116241370; -.
DR REPRODUCTION-2DPAGE; IPI00375441; -.
DR PaxDb; Q96AE4; -.
DR PRIDE; Q96AE4; -.
DR DNASU; 8880; -.
DR Ensembl; ENST00000294623; ENSP00000294623; ENSG00000162613.
DR Ensembl; ENST00000370768; ENSP00000359804; ENSG00000162613.
DR GeneID; 8880; -.
DR KEGG; hsa:8880; -.
DR UCSC; uc001dii.3; human.
DR CTD; 8880; -.
DR GeneCards; GC01M078400; -.
DR HGNC; HGNC:4004; FUBP1.
DR HPA; HPA006149; -.
DR MIM; 603444; gene.
DR neXtProt; NX_Q96AE4; -.
DR PharmGKB; PA28420; -.
DR eggNOG; NOG300923; -.
DR HOGENOM; HOG000231552; -.
DR HOVERGEN; HBG000625; -.
DR KO; K13210; -.
DR OrthoDB; EOG77Q4WB; -.
DR ChiTaRS; FUBP1; human.
DR EvolutionaryTrace; Q96AE4; -.
DR GeneWiki; Far_upstream_element-binding_protein_1; -.
DR GenomeRNAi; 8880; -.
DR NextBio; 33343; -.
DR PRO; PR:Q96AE4; -.
DR ArrayExpress; Q96AE4; -.
DR Bgee; Q96AE4; -.
DR CleanEx; HS_FUBP1; -.
DR Genevestigator; Q96AE4; -.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; TAS:ProtInc.
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:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc.
DR InterPro; IPR015096; DUF1897.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR Pfam; PF09005; DUF1897; 2.
DR Pfam; PF00013; KH_1; 4.
DR SMART; SM00322; KH; 4.
DR PROSITE; PS50084; KH_TYPE_1; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Direct protein sequencing; DNA-binding; Nucleus; Phosphoprotein;
KW Polymorphism; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 644 Far upstream element-binding protein 1.
FT /FTId=PRO_0000050135.
FT DOMAIN 100 164 KH 1.
FT DOMAIN 185 251 KH 2.
FT DOMAIN 275 339 KH 3.
FT DOMAIN 376 443 KH 4.
FT COMPBIAS 13 26 Gly-rich.
FT COMPBIAS 349 396 Gly-rich.
FT COMPBIAS 450 560 Pro-rich.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 140 140 Phosphoserine.
FT MOD_RES 153 153 Phosphothreonine.
FT MOD_RES 630 630 Phosphoserine.
FT VAR_SEQ 97 97 Missing (in isoform 2).
FT /FTId=VSP_021107.
FT VAR_SEQ 643 644 GQ -> CRFDPASIELAL (in isoform 2).
FT /FTId=VSP_008321.
FT VARIANT 399 399 I -> K (in dbSNP:rs12748509).
FT /FTId=VAR_049679.
FT HELIX 30 44
FT STRAND 278 283
FT HELIX 284 291
FT HELIX 293 295
FT HELIX 296 305
FT STRAND 308 312
FT STRAND 319 327
FT HELIX 329 346
FT STRAND 378 384
FT TURN 385 387
FT HELIX 388 392
FT HELIX 394 396
FT HELIX 397 406
FT STRAND 409 413
FT TURN 417 419
FT STRAND 424 430
FT HELIX 433 446
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
//
MIM
603444
*RECORD*
*FIELD* NO
603444
*FIELD* TI
*603444 FAR UPSTREAM ELEMENT-BINDING PROTEIN 1; FUBP1
;;FAR UPSTREAM ELEMENT-BINDING PROTEIN; FUBP;;
read moreFUSE-BINDING PROTEIN; FBP
*FIELD* TX
CLONING
The far upstream element (FUSE) of the human MYC (190080) protooncogene
stimulates expression in undifferentiated cells. Duncan et al. (1994)
purified a 70-kD FUSE-binding protein, or FBP, that is present in
undifferentiated but not differentiated cells. FBP exhibited DNA binding
specificity for the noncoding strand of the FUSE site in vitro. By PCR
of human cell line cDNA with degenerate primers based on a partial FBP
protein sequence, the authors isolated partial FBP cDNAs. They recovered
additional cDNAs from several libraries and used them to assemble a
full-length FBP cDNA sequence. The central region of the predicted
644-amino acid protein contains 4 copies of a repeat unit. In vitro
binding assays with mutant protein constructs indicated that the third
and fourth copies constituted the minimum single-stranded DNA-binding
domain. Using potassium permanganate to probe DNA conformation in vivo,
Duncan et al. (1994) determined that the pattern of sensitivity of
genomic DNA was consistent with the binding of FBP to the noncoding
strand of FUSE, which displaced the coding strand. Expression of FBP in
human leukemia cells stimulated the activity of a MYC promoter in a
FUSE-dependent manner. Northern blot analysis revealed that expression
of the 2.6-kb FBP mRNA declined upon differentiation, suggesting that
FUSE-binding activity may be regulated transcriptionally. In addition,
by sequence analysis of FBP cDNAs, the authors found evidence that FBP
activity may also be regulated by alternative splicing, translation
efficiency, and posttranslational modification.
GENE FUNCTION
Inherited mutations of the transcription factor IIH (TFIIH) helicase
subunits XPB (133510) or XPD (278730) yield overlapping DNA repair and
transcription syndromes. The high risk of cancer in these patients is
not fully explained by the repair defect. The transcription defect,
however, is subtle and more difficult to evaluate. Liu et al. (2001)
showed that XPB and XPD mutations block transcription activation by FBP,
a regulator of MYC expression, and block repression by the
FBP-interacting repressor (FIR; 604819). Through TFIIH, FBP facilitates
transcription until promoter escape, whereas after initiation, FIR uses
TFIIH to delay promoter escape. Mutations in TFIIH that impair
regulation by FBP and FIR affect proper regulation of MYC expression and
have implications in the development of malignancy.
MOLECULAR GENETICS
Bettegowda et al. (2011) performed exonic sequencing of 7
oligodendrogliomas. Among other changes, they found that the CIC gene
(612082) (homolog of the Drosophila gene capicua) on chromosome 19q was
somatically mutated in 6 cases and that the FUBP1 gene on chromosome 1p
was somatically mutated in 2 tumors. Examination of 27 additional
oligodendrogliomas revealed 12 and 3 more tumors with mutations of CIC
and FUBP1, respectively, 58% of which were predicted to result in
truncations of the encoded proteins. Bettegowda et al. (2011) concluded
that their results suggested a critical role for these genes in the
biology and pathology of oligodendrocytes.
*FIELD* RF
1. Bettegowda, C.; Agrawal, N.; Jiao, Y.; Sausen, M.; Wood, L. D.;
Hruban, R. H.; Rodriguez, F. J.; Cahill, D. P.; McLendon, R.; Riggins,
G.; Velculescu, V. E.; Oba-Shinjo, S. M.; Marie, S. K. N.; Vogelstein,
B.; Bigner, D.; Yan, H.; Papadopoulos, N.; Kinzler, K. W.: Mutations
in CIC and FUBP1 contribute to human oligodendroglioma. Science 333:
1453-1455, 2011.
2. Duncan, R.; Bazar, L.; Michelotti, G.; Tomonaga, T.; Krutzsch,
H.; Avigan, M.; Levens, D.: A sequence-specific, single-strand binding
protein activates the far upstream element of c-myc and defines a
new DNA-binding motif. Genes Dev. 8: 465-480, 1994.
3. Liu, J.; Akoulitchev, S.; Weber, A.; Ge, H.; Chuikov, S.; Libutti,
D.; Wang, X. W.; Conaway, J. W.; Harris, C. C.; Conaway, R. C.; Reinberg,
D.; Levens, D.: Defective interplay of activators and repressors
with TFIIH in xeroderma pigmentosum. Cell 104: 353-363, 2001.
*FIELD* CN
Ada Hamosh - updated: 11/22/2011
Stylianos E. Antonarakis - updated: 3/8/2001
*FIELD* CD
Rebekah S. Rasooly: 1/19/1999
*FIELD* ED
alopez: 11/29/2011
terry: 11/22/2011
mgross: 3/8/2001
psherman: 7/21/1999
alopez: 1/19/1999
*RECORD*
*FIELD* NO
603444
*FIELD* TI
*603444 FAR UPSTREAM ELEMENT-BINDING PROTEIN 1; FUBP1
;;FAR UPSTREAM ELEMENT-BINDING PROTEIN; FUBP;;
read moreFUSE-BINDING PROTEIN; FBP
*FIELD* TX
CLONING
The far upstream element (FUSE) of the human MYC (190080) protooncogene
stimulates expression in undifferentiated cells. Duncan et al. (1994)
purified a 70-kD FUSE-binding protein, or FBP, that is present in
undifferentiated but not differentiated cells. FBP exhibited DNA binding
specificity for the noncoding strand of the FUSE site in vitro. By PCR
of human cell line cDNA with degenerate primers based on a partial FBP
protein sequence, the authors isolated partial FBP cDNAs. They recovered
additional cDNAs from several libraries and used them to assemble a
full-length FBP cDNA sequence. The central region of the predicted
644-amino acid protein contains 4 copies of a repeat unit. In vitro
binding assays with mutant protein constructs indicated that the third
and fourth copies constituted the minimum single-stranded DNA-binding
domain. Using potassium permanganate to probe DNA conformation in vivo,
Duncan et al. (1994) determined that the pattern of sensitivity of
genomic DNA was consistent with the binding of FBP to the noncoding
strand of FUSE, which displaced the coding strand. Expression of FBP in
human leukemia cells stimulated the activity of a MYC promoter in a
FUSE-dependent manner. Northern blot analysis revealed that expression
of the 2.6-kb FBP mRNA declined upon differentiation, suggesting that
FUSE-binding activity may be regulated transcriptionally. In addition,
by sequence analysis of FBP cDNAs, the authors found evidence that FBP
activity may also be regulated by alternative splicing, translation
efficiency, and posttranslational modification.
GENE FUNCTION
Inherited mutations of the transcription factor IIH (TFIIH) helicase
subunits XPB (133510) or XPD (278730) yield overlapping DNA repair and
transcription syndromes. The high risk of cancer in these patients is
not fully explained by the repair defect. The transcription defect,
however, is subtle and more difficult to evaluate. Liu et al. (2001)
showed that XPB and XPD mutations block transcription activation by FBP,
a regulator of MYC expression, and block repression by the
FBP-interacting repressor (FIR; 604819). Through TFIIH, FBP facilitates
transcription until promoter escape, whereas after initiation, FIR uses
TFIIH to delay promoter escape. Mutations in TFIIH that impair
regulation by FBP and FIR affect proper regulation of MYC expression and
have implications in the development of malignancy.
MOLECULAR GENETICS
Bettegowda et al. (2011) performed exonic sequencing of 7
oligodendrogliomas. Among other changes, they found that the CIC gene
(612082) (homolog of the Drosophila gene capicua) on chromosome 19q was
somatically mutated in 6 cases and that the FUBP1 gene on chromosome 1p
was somatically mutated in 2 tumors. Examination of 27 additional
oligodendrogliomas revealed 12 and 3 more tumors with mutations of CIC
and FUBP1, respectively, 58% of which were predicted to result in
truncations of the encoded proteins. Bettegowda et al. (2011) concluded
that their results suggested a critical role for these genes in the
biology and pathology of oligodendrocytes.
*FIELD* RF
1. Bettegowda, C.; Agrawal, N.; Jiao, Y.; Sausen, M.; Wood, L. D.;
Hruban, R. H.; Rodriguez, F. J.; Cahill, D. P.; McLendon, R.; Riggins,
G.; Velculescu, V. E.; Oba-Shinjo, S. M.; Marie, S. K. N.; Vogelstein,
B.; Bigner, D.; Yan, H.; Papadopoulos, N.; Kinzler, K. W.: Mutations
in CIC and FUBP1 contribute to human oligodendroglioma. Science 333:
1453-1455, 2011.
2. Duncan, R.; Bazar, L.; Michelotti, G.; Tomonaga, T.; Krutzsch,
H.; Avigan, M.; Levens, D.: A sequence-specific, single-strand binding
protein activates the far upstream element of c-myc and defines a
new DNA-binding motif. Genes Dev. 8: 465-480, 1994.
3. Liu, J.; Akoulitchev, S.; Weber, A.; Ge, H.; Chuikov, S.; Libutti,
D.; Wang, X. W.; Conaway, J. W.; Harris, C. C.; Conaway, R. C.; Reinberg,
D.; Levens, D.: Defective interplay of activators and repressors
with TFIIH in xeroderma pigmentosum. Cell 104: 353-363, 2001.
*FIELD* CN
Ada Hamosh - updated: 11/22/2011
Stylianos E. Antonarakis - updated: 3/8/2001
*FIELD* CD
Rebekah S. Rasooly: 1/19/1999
*FIELD* ED
alopez: 11/29/2011
terry: 11/22/2011
mgross: 3/8/2001
psherman: 7/21/1999
alopez: 1/19/1999