FUBP2_MOUSE
ID FUBP2_MOUSE Reviewed; 748 AA.
AC Q3U0V1; E9QKH3; Q2VPQ6; Q6P2L2;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Far upstream element-binding protein 2;
DE Short=FUSE-binding protein 2;
DE AltName: Full=KH type-splicing regulatory protein;
DE Short=KSRP;
GN Name=Khsrp; Synonyms=Fubp2;
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].
RC STRAIN=NOD; TISSUE=Spleen;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 198-748.
RC STRAIN=C57BL/6J; 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182, AND IDENTIFICATION BY
RP 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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-88, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [8]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-40; ARG-412; ARG-414; ARG-416 AND
RP ARG-443, 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).
CC -!- FUNCTION: Binds to the dendritic targeting element and may play a role
CC in mRNA trafficking. Part of a ternary complex that binds to the
CC downstream control sequence (DCS) of the pre-mRNA. Mediates exon
CC inclusion in transcripts that are subject to tissue-specific
CC alternative splicing. May interact with single-stranded DNA from the
CC far-upstream element (FUSE). May activate gene expression. Also
CC involved in degradation of inherently unstable mRNAs that contain AU-
CC rich elements (AREs) in their 3'-UTR, possibly by recruiting
CC degradation machinery to ARE-containing mRNAs (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Part of a ternary complex containing FUBP2, PTBP1, PTBP2 and
CC HNRPH1. Interacts with PARN. Interacts with PQBP1.
CC {ECO:0000250|UniProtKB:Q92945}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Note=A small proportion is also found in the cytoplasm of neuronal cell
CC bodies and dendrites. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the KHSRP family. {ECO:0000305}.
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DR EMBL; AK156541; BAE33750.1; -; mRNA.
DR EMBL; CT571247; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC064454; AAH64454.1; -; mRNA.
DR EMBL; BC108414; AAI08415.1; -; mRNA.
DR CCDS; CCDS50157.1; -.
DR RefSeq; NP_034743.3; NM_010613.3.
DR AlphaFoldDB; Q3U0V1; -.
DR SMR; Q3U0V1; -.
DR BioGRID; 200927; 25.
DR IntAct; Q3U0V1; 8.
DR MINT; Q3U0V1; -.
DR STRING; 10090.ENSMUSP00000007814; -.
DR iPTMnet; Q3U0V1; -.
DR PhosphoSitePlus; Q3U0V1; -.
DR SwissPalm; Q3U0V1; -.
DR EPD; Q3U0V1; -.
DR jPOST; Q3U0V1; -.
DR MaxQB; Q3U0V1; -.
DR PaxDb; Q3U0V1; -.
DR PeptideAtlas; Q3U0V1; -.
DR PRIDE; Q3U0V1; -.
DR ProteomicsDB; 266885; -.
DR Antibodypedia; 6316; 321 antibodies from 34 providers.
DR DNASU; 16549; -.
DR Ensembl; ENSMUST00000007814; ENSMUSP00000007814; ENSMUSG00000007670.
DR GeneID; 16549; -.
DR KEGG; mmu:16549; -.
DR UCSC; uc008ddr.2; mouse.
DR CTD; 8570; -.
DR MGI; MGI:1336214; Khsrp.
DR VEuPathDB; HostDB:ENSMUSG00000007670; -.
DR eggNOG; KOG1676; Eukaryota.
DR GeneTree; ENSGT00940000156051; -.
DR HOGENOM; CLU_014285_1_0_1; -.
DR InParanoid; Q3U0V1; -.
DR OMA; QPVHQWA; -.
DR OrthoDB; 590738at2759; -.
DR PhylomeDB; Q3U0V1; -.
DR TreeFam; TF313654; -.
DR Reactome; R-MMU-450604; KSRP (KHSRP) binds and destabilizes mRNA.
DR BioGRID-ORCS; 16549; 5 hits in 75 CRISPR screens.
DR ChiTaRS; Khsrp; mouse.
DR PRO; PR:Q3U0V1; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q3U0V1; protein.
DR Bgee; ENSMUSG00000007670; Expressed in ventricular zone and 224 other tissues.
DR ExpressionAtlas; Q3U0V1; baseline and differential.
DR Genevisible; Q3U0V1; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; ISS:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISO:MGI.
DR GO; GO:0003729; F:mRNA binding; IDA:MGI.
DR GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; ISS:UniProtKB.
DR GO; GO:0071345; P:cellular response to cytokine stimulus; ISS:UniProtKB.
DR GO; GO:0010586; P:miRNA metabolic process; ISS:UniProtKB.
DR GO; GO:0006402; P:mRNA catabolic process; IDA:MGI.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0010989; P:negative regulation of low-density lipoprotein particle clearance; ISO:MGI.
DR GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; ISS:UniProtKB.
DR GO; GO:0061014; P:positive regulation of mRNA catabolic process; ISS:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:2000628; P:regulation of miRNA metabolic process; IDA:MGI.
DR GO; GO:0043488; P:regulation of mRNA stability; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
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; PS00178; AA_TRNA_LIGASE_I; 1.
DR PROSITE; PS50084; KH_TYPE_1; 4.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; DNA-binding; Isopeptide bond; Methylation;
KW mRNA processing; mRNA splicing; mRNA transport; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; Transcription;
KW Transcription regulation; Transport; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q92945"
FT CHAIN 2..748
FT /note="Far upstream element-binding protein 2"
FT /id="PRO_0000298678"
FT DOMAIN 145..209
FT /note="KH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 234..300
FT /note="KH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 323..387
FT /note="KH 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 425..492
FT /note="KH 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT REPEAT 572..583
FT /note="1"
FT REPEAT 618..629
FT /note="2"
FT REPEAT 644..655
FT /note="3"
FT REPEAT 674..685
FT /note="4"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 90..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..685
FT /note="4 X 12 AA imperfect repeats"
FT REGION 588..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 659..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 689..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..546
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..615
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q92945"
FT MOD_RES 40
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 88
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 101
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q92945"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92945"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92945"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92945"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92945"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92945"
FT MOD_RES 412
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 414
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 416
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 443
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 481
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92945"
FT CROSSLNK 122
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q92945"
FT CROSSLNK 122
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q92945"
FT CONFLICT 387
FT /note="I -> F (in Ref. 1; BAE33750)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 748 AA; 76775 MW; 0699217B3E1E54A9 CRC64;
MSDYNTGGPP PGPPPPAGGG GGAAGAGGGP PPGPPGAGDR GGGGPGGGGP GGGGASGGPS
QPPGGGGPGI RKDAFADAVQ RARQIAAKIG GDAATTVNNN TPDFGFGGQK RQLEDGDQPD
SKKLASQGDS IGSQLGPIHP PPRTSMTEEY RVPDGMVGLI IGRGGEQINK IQQDSGCKVQ
ISPDSGGLPE RSVSLTGAPE SVQKAKMMLD DIVSRGRGGP PGQFHDNANG GQNGTVQEIM
IPAGKAGLVI GKGGETIKQL QERAGVKMIL IQDGSQNTNV DKPLRIIGDP YKVQQACEMV
MDILRERDQG GFGDRNEYGS RVGGGIDVPV PRHSVGVVIG RSGEMIKKIQ NDAGVRIQFK
QDDGTGPEKI AHIMGPPDRC EHAARIINDL LQSLRSGPPG PPGAPGMPPG GRGRGRGQGN
WGPPGGEMTF SIPTHKCGLV IGRGGENVKA INQQTGAFVE ISRQLPPNGD PNFKLFVIRG
SPQQIDHAKQ LIEEKIEGPL CPVGPGPGGP GPAGPMGPFN PGPFNQGPPG APPHAGGPPP
HQYPPQGWGN TYPQWQPPAP HDPNKAAAAA TDPNAAWAAY YSHYYQQPPG PVPGPAPAPA
APPAQGEPPQ PPPTGQSDYT KAWEEYYKKI GQQPQQPGAP PQQDYTKAWE EYYKKQAQVA
TGGGPGAPPG SQPDYSAAWA EYYRQQAAYY GQTPGPGGPQ PPPTQQGQQQ ASGNCHPPPP
PFSFQPPATV HPALVGSAGN PFPCGVCP
