FUBP1_MOUSE
ID FUBP1_MOUSE Reviewed; 651 AA.
AC Q91WJ8; Q8C0Y8;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Far upstream element-binding protein 1;
DE Short=FBP;
DE Short=FUSE-binding protein 1;
GN Name=Fubp1; Synonyms=D3Ertd330e;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Retina;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-286 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP PROTEIN SEQUENCE OF 103-114.
RC TISSUE=Brain;
RA Lubec G., Yang J.W., Zigmond M.;
RL Submitted (JUL-2007) to UniProtKB.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-149 AND SER-411, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-317; ARG-355; ARG-357 AND
RP ARG-359, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
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 [6]
RP STRUCTURE BY NMR OF 91-255.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of KH domains in FUSE binding protein 1.";
RL Submitted (NOV-2005) to the PDB data bank.
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Found in a complex with PUF60 and far upstream element (FUSE)
CC DNA segment. Interacts with PUF60 and JTV1 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q91WJ8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q91WJ8-2; Sequence=VSP_008322;
CC -!- PTM: Ubiquitinated. This targets the protein for proteasome-mediated
CC degradation (By similarity). {ECO:0000250}.
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DR EMBL; BC014763; AAH14763.1; -; mRNA.
DR EMBL; AK029458; BAC26457.1; -; mRNA.
DR CCDS; CCDS89707.1; -. [Q91WJ8-1]
DR RefSeq; XP_006501734.1; XM_006501671.1.
DR PDB; 1X4M; NMR; -; A=175-255.
DR PDB; 1X4N; NMR; -; A=91-168.
DR PDBsum; 1X4M; -.
DR PDBsum; 1X4N; -.
DR AlphaFoldDB; Q91WJ8; -.
DR SMR; Q91WJ8; -.
DR BioGRID; 206245; 15.
DR IntAct; Q91WJ8; 2.
DR STRING; 10090.ENSMUSP00000130145; -.
DR iPTMnet; Q91WJ8; -.
DR PhosphoSitePlus; Q91WJ8; -.
DR SwissPalm; Q91WJ8; -.
DR REPRODUCTION-2DPAGE; Q91WJ8; -.
DR EPD; Q91WJ8; -.
DR jPOST; Q91WJ8; -.
DR MaxQB; Q91WJ8; -.
DR PaxDb; Q91WJ8; -.
DR PeptideAtlas; Q91WJ8; -.
DR PRIDE; Q91WJ8; -.
DR ProteomicsDB; 266883; -. [Q91WJ8-1]
DR ProteomicsDB; 266884; -. [Q91WJ8-2]
DR Antibodypedia; 1310; 318 antibodies from 35 providers.
DR Ensembl; ENSMUST00000196739; ENSMUSP00000143101; ENSMUSG00000028034. [Q91WJ8-1]
DR UCSC; uc008rsv.1; mouse. [Q91WJ8-1]
DR MGI; MGI:1196294; Fubp1.
DR VEuPathDB; HostDB:ENSMUSG00000028034; -.
DR eggNOG; KOG1676; Eukaryota.
DR GeneTree; ENSGT00940000160043; -.
DR InParanoid; Q91WJ8; -.
DR OrthoDB; 590738at2759; -.
DR PhylomeDB; Q91WJ8; -.
DR BioGRID-ORCS; 51886; 5 hits in 75 CRISPR screens.
DR ChiTaRS; Fubp1; mouse.
DR EvolutionaryTrace; Q91WJ8; -.
DR PRO; PR:Q91WJ8; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q91WJ8; protein.
DR Bgee; ENSMUSG00000028034; Expressed in undifferentiated genital tubercle and 266 other tissues.
DR ExpressionAtlas; Q91WJ8; baseline and differential.
DR Genevisible; Q91WJ8; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0048588; P:developmental cell growth; IMP:MGI.
DR GO; GO:0071425; P:hematopoietic stem cell proliferation; IMP:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:1900149; P:positive regulation of Schwann cell migration; ISO:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0048103; P:somatic stem cell division; IMP:MGI.
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:0000250|UniProtKB:Q96AE4"
FT CHAIN 2..651
FT /note="Far upstream element-binding protein 1"
FT /id="PRO_0000050136"
FT DOMAIN 96..160
FT /note="KH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 181..247
FT /note="KH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 271..335
FT /note="KH 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 372..439
FT /note="KH 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 40..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 625..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..501
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..569
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q96AE4"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96AE4"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96AE4"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96AE4"
FT MOD_RES 149
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 317
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 355
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 357
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 359
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 428
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96AE4"
FT MOD_RES 626
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96AE4"
FT VAR_SEQ 67
FT /note="D -> DGSWTNPSSTTHWEGMPSPFKD (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_008322"
FT CONFLICT 93
FT /note="Missing (in Ref. 2; BAC26457)"
FT /evidence="ECO:0000305"
FT STRAND 97..104
FT /evidence="ECO:0007829|PDB:1X4N"
FT HELIX 105..112
FT /evidence="ECO:0007829|PDB:1X4N"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:1X4N"
FT HELIX 117..125
FT /evidence="ECO:0007829|PDB:1X4N"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:1X4N"
FT STRAND 140..148
FT /evidence="ECO:0007829|PDB:1X4N"
FT HELIX 150..166
FT /evidence="ECO:0007829|PDB:1X4N"
FT STRAND 182..188
FT /evidence="ECO:0007829|PDB:1X4M"
FT HELIX 190..196
FT /evidence="ECO:0007829|PDB:1X4M"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:1X4M"
FT HELIX 203..211
FT /evidence="ECO:0007829|PDB:1X4M"
FT STRAND 213..217
FT /evidence="ECO:0007829|PDB:1X4M"
FT STRAND 229..235
FT /evidence="ECO:0007829|PDB:1X4M"
FT TURN 237..239
FT /evidence="ECO:0007829|PDB:1X4M"
FT HELIX 240..251
FT /evidence="ECO:0007829|PDB:1X4M"
SQ SEQUENCE 651 AA; 68540 MW; F4EECA62FD9FA0D5 CRC64;
MADYSTVPPP SSGSAGGGGG GVVNDAFKDA LQRARQIAAK IGGDAGTSLN SNDYGYGGQK
RPLEDGDQPD AKKVPPQNDS FGAQLPPMHQ QQSRSVMTEE YKVPDGMVGF IIGRGGEQIS
RIQQESGCKI QIAPDSGGLP ERSCMLTGTP ESVQSAKRLL DQIVEKGRPA PGFHHGDGPG
NAVQEIMIPA SKAGLVIGKG GETIKQLQER AGVKMVMIQD GPQNTGADKP LRITGDPYKV
QQAKEMVLEL IRDQGGFREV RNEYGSRIGG NEGIDVPIPR FAVGIVIGRN GEMIKKIQND
AGVRIQFKPD DGTTPDRIAQ ITGPPDRCQH AAEIITDLLR SVQAGNPGGP GPGGRGRGRG
QGNWNMGPPG GLQEFNFIVP TGKTGLIIGK GGETIKSISQ QSGARIELQR SPPPNADPNM
KLFTIRGTPQ QIDYARQLIE EKIGGPVNPL GPPVPHGPHG VPGPHGPPGP PGPGTPMGPY
NPAPYNPGPP GPAPHGPPAP YAPQGWGNAY PHWQQQAPPD PAKAGADPNS AAWAAYYAHY
YQQQAQPPPA APAGAPATTQ TNGQGDQQAP APAGQVDYTK AWEEYYKKMG QAVPAPAGAP
PGGQPDYSAA WAEYYRQQAA YYAQTSPQGM PQHPPAPQGF ANHARSHHHL Y
