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Far upstream element-binding protein 2 (FUSE-binding protein 2) (KH type-splicing regulatory protein) (KSRP)

 FUBP2_MOUSE             Reviewed;         748 AA.
Q3U0V1; E9QKH3; Q2VPQ6; Q6P2L2;
21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
20-JUN-2018, entry version 113.
RecName: Full=Far upstream element-binding protein 2;
Short=FUSE-binding protein 2;
AltName: Full=KH type-splicing regulatory protein;
Short=KSRP;
Name=Khsrp; Synonyms=Fubp2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=NOD; TISSUE=Spleen;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 198-748.
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[7]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-88, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[8]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-40; ARG-412; ARG-414;
ARG-416 AND ARG-443, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Brain, and Embryo;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- FUNCTION: Binds to the dendritic targeting element and may play a
role in mRNA trafficking. Part of a ternary complex that binds to
the downstream control sequence (DCS) of the pre-mRNA. Mediates
exon inclusion in transcripts that are subject to tissue-specific
alternative splicing. May interact with single-stranded DNA from
the far-upstream element (FUSE). May activate gene expression.
Also involved in degradation of inherently unstable mRNAs that
contain AU-rich elements (AREs) in their 3'-UTR, possibly by
recruiting degradation machinery to ARE-containing mRNAs (By
similarity). {ECO:0000250}.
-!- SUBUNIT: Part of a ternary complex containing FUBP2, PTBP1, PTBP2
and HNRPH1. Interacts with PARN. Interacts with PQBP1.
{ECO:0000250|UniProtKB:Q92945}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm
{ECO:0000250}. Note=A small proportion is also found in the
cytoplasm of neuronal cell bodies and dendrites. {ECO:0000250}.
-!- SIMILARITY: Belongs to the KHSRP family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AK156541; BAE33750.1; -; mRNA.
EMBL; CT571247; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC064454; AAH64454.1; -; mRNA.
EMBL; BC108414; AAI08415.1; -; mRNA.
CCDS; CCDS50157.1; -.
RefSeq; NP_034743.3; NM_010613.3.
UniGene; Mm.34296; -.
ProteinModelPortal; Q3U0V1; -.
SMR; Q3U0V1; -.
BioGrid; 200927; 3.
IntAct; Q3U0V1; 4.
STRING; 10090.ENSMUSP00000007814; -.
iPTMnet; Q3U0V1; -.
PhosphoSitePlus; Q3U0V1; -.
SwissPalm; Q3U0V1; -.
EPD; Q3U0V1; -.
MaxQB; Q3U0V1; -.
PaxDb; Q3U0V1; -.
PeptideAtlas; Q3U0V1; -.
PRIDE; Q3U0V1; -.
DNASU; 16549; -.
Ensembl; ENSMUST00000007814; ENSMUSP00000007814; ENSMUSG00000007670.
GeneID; 16549; -.
KEGG; mmu:16549; -.
UCSC; uc008ddr.2; mouse.
CTD; 8570; -.
MGI; MGI:1336214; Khsrp.
eggNOG; KOG1676; Eukaryota.
eggNOG; ENOG410XZYE; LUCA.
GeneTree; ENSGT00730000110664; -.
HOGENOM; HOG000231552; -.
HOVERGEN; HBG000625; -.
InParanoid; Q3U0V1; -.
KO; K13210; -.
OMA; PAGQSDY; -.
OrthoDB; EOG091G073X; -.
TreeFam; TF313654; -.
Reactome; R-MMU-450604; KSRP (KHSRP) binds and destabilizes mRNA.
PRO; PR:Q3U0V1; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000007670; -.
CleanEx; MM_KHSRP; -.
Genevisible; Q3U0V1; MM.
GO; GO:0010494; C:cytoplasmic stress granule; IDA:MGI.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0030425; C:dendrite; ISO:MGI.
GO; GO:0043025; C:neuronal cell body; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; ISS:UniProtKB.
GO; GO:0003730; F:mRNA 3'-UTR binding; ISO:MGI.
GO; GO:0003729; F:mRNA binding; IDA:MGI.
GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; ISS:UniProtKB.
GO; GO:0071345; P:cellular response to cytokine stimulus; ISS:UniProtKB.
GO; GO:0010586; P:miRNA metabolic process; ISS:UniProtKB.
GO; GO:0006402; P:mRNA catabolic process; IDA:MGI.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
GO; GO:0010989; P:negative regulation of low-density lipoprotein particle clearance; ISO:MGI.
GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; ISS:UniProtKB.
GO; GO:0061014; P:positive regulation of mRNA catabolic process; ISS:UniProtKB.
GO; GO:2000628; P:regulation of miRNA metabolic process; IDA:MGI.
GO; GO:0043488; P:regulation of mRNA stability; ISS:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 3.30.1370.10; -; 4.
InterPro; IPR015096; FUBP_C.
InterPro; IPR004087; KH_dom.
InterPro; IPR004088; KH_dom_type_1.
InterPro; IPR036612; KH_dom_type_1_sf.
Pfam; PF09005; DUF1897; 2.
Pfam; PF00013; KH_1; 4.
SMART; SM00322; KH; 4.
SUPFAM; SSF54791; SSF54791; 4.
PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PROSITE; PS50084; KH_TYPE_1; 4.
1: Evidence at protein level;
Acetylation; Complete proteome; Cytoplasm; DNA-binding;
Isopeptide bond; Methylation; mRNA processing; mRNA splicing;
mRNA transport; Nucleus; Phosphoprotein; Reference proteome; Repeat;
RNA-binding; Transcription; Transcription regulation; Transport;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q92945}.
CHAIN 2 748 Far upstream element-binding protein 2.
/FTId=PRO_0000298678.
DOMAIN 145 209 KH 1. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
DOMAIN 234 300 KH 2. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
DOMAIN 323 387 KH 3. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
DOMAIN 425 492 KH 4. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
REPEAT 572 583 1.
REPEAT 618 629 2.
REPEAT 644 655 3.
REPEAT 674 685 4.
REGION 572 685 4 X 12 AA imperfect repeats.
COMPBIAS 7 68 Gly/Pro-rich.
COMPBIAS 69 497 Gly-rich.
COMPBIAS 499 613 Ala/Gly/Pro-rich.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:Q92945}.
MOD_RES 40 40 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 88 88 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 101 101 Phosphothreonine.
{ECO:0000250|UniProtKB:Q92945}.
MOD_RES 126 126 Phosphoserine.
{ECO:0000250|UniProtKB:Q92945}.
MOD_RES 130 130 Phosphoserine.
{ECO:0000250|UniProtKB:Q92945}.
MOD_RES 182 182 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 185 185 Phosphoserine.
{ECO:0000250|UniProtKB:Q92945}.
MOD_RES 194 194 Phosphoserine.
{ECO:0000250|UniProtKB:Q92945}.
MOD_RES 275 275 Phosphoserine.
{ECO:0000250|UniProtKB:Q92945}.
MOD_RES 412 412 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 414 414 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 416 416 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 443 443 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 481 481 Phosphoserine.
{ECO:0000250|UniProtKB:Q92945}.
CROSSLNK 122 122 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:Q92945}.
CROSSLNK 122 122 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q92945}.
CONFLICT 387 387 I -> F (in Ref. 1; BAE33750).
{ECO:0000305}.
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


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