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Far upstream element-binding protein 2 (FUSE-binding protein 2) (KH type-splicing regulatory protein) (KSRP) (MAP2 RNA trans-acting protein 1) (MARTA1)

 FUBP2_RAT               Reviewed;         721 AA.
Q99PF5;
26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
16-JAN-2019, 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;
AltName: Full=MAP2 RNA trans-acting protein 1;
Short=MARTA1;
Name=Khsrp; Synonyms=Fubp2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 73-87; 89-108 AND
475-486, SUBCELLULAR LOCATION, AND FUNCTION.
TISSUE=Brain;
PubMed=12358751; DOI=10.1046/j.1471-4159.2002.01058.x;
Rehbein M., Wege K., Buck F., Schweizer M., Richter D., Kindler S.;
"Molecular characterization of MARTA1, a protein interacting with the
dendritic targeting element of MAP2 mRNAs.";
J. Neurochem. 82:1039-1046(2002).
[2]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182 AND SER-185, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: 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).
Binds to the dendritic targeting element and may play a role in
mRNA trafficking. {ECO:0000250, ECO:0000269|PubMed:12358751}.
-!- 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:0000269|PubMed:12358751}.
Cytoplasm {ECO:0000269|PubMed:12358751}. Note=A small proportion
is also found in the cytoplasm of neuronal cell bodies and
dendrites.
-!- SIMILARITY: Belongs to the KHSRP family. {ECO:0000305}.
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EMBL; AF308818; AAG59811.1; -; mRNA.
RefSeq; NP_598286.1; NM_133602.1.
UniGene; Rn.92643; -.
ProteinModelPortal; Q99PF5; -.
SMR; Q99PF5; -.
CORUM; Q99PF5; -.
STRING; 10116.ENSRNOP00000066023; -.
iPTMnet; Q99PF5; -.
PhosphoSitePlus; Q99PF5; -.
SwissPalm; Q99PF5; -.
REPRODUCTION-2DPAGE; Q99PF5; -.
jPOST; Q99PF5; -.
PaxDb; Q99PF5; -.
PRIDE; Q99PF5; -.
GeneID; 171137; -.
KEGG; rno:171137; -.
CTD; 8570; -.
RGD; 621828; Khsrp.
eggNOG; KOG1676; Eukaryota.
eggNOG; ENOG410XZYE; LUCA.
HOVERGEN; HBG000625; -.
InParanoid; Q99PF5; -.
KO; K13210; -.
OrthoDB; 590738at2759; -.
PhylomeDB; Q99PF5; -.
PRO; PR:Q99PF5; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0030425; C:dendrite; IDA:RGD.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
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; IDA:RGD.
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:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
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:0043488; P:regulation of mRNA stability; ISS:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
GO; GO:0008380; P:RNA splicing; 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; PS50084; KH_TYPE_1; 4.
1: Evidence at protein level;
Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing;
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 2 721 Far upstream element-binding protein 2.
/FTId=PRO_0000050138.
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 69 498 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:0000250|UniProtKB:Q3U0V1}.
MOD_RES 88 88 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q3U0V1}.
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:22673903}.
MOD_RES 185 185 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
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:0000250|UniProtKB:Q92945}.
MOD_RES 414 414 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q92945}.
MOD_RES 416 416 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q92945}.
MOD_RES 443 443 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q92945}.
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}.
SEQUENCE 721 AA; 74226 MW; 482C7A765C60EE4A CRC64;
MSDYSTGGPP 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 GPAGPMGPFH PGPFNQGPPG APPHAGGPPP
HQYPPQGWGN TYPEWQPPAP HDPNKAAAAA TDPNAAWAAY YSHYYQQPPG PVPGPAPAPA
APPAQGEPPQ PPPTGQSDYT KAWEEYYKKI GQQPQQPGAP PQQDYTKAWE EYYKKQAQVA
TGGGPGAPPG SQPDYSAAWA EYYRQQAAYY GQTPGPGGPQ PPSTQQGQQQ ATEANGYELH
L


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Pathways :
WP731: Sterol regulatory element binding protein related
WP1531: Vitamin D synthesis
WP1616: ABC transporters
WP2292: Chemokine signaling pathway
WP1493: Carbon assimilation C4 pathway
WP1909: Signal regulatory protein (SIRP) family interactions
WP2272: Pathogenic Escherichia coli infection
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1502: Mitochondrial biogenesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination
WP1665: Limonene and pinene degradation
WP1672: Mismatch repair

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Bibliography :
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