FUBP2_RAT
ID FUBP2_RAT Reviewed; 721 AA.
AC Q99PF5;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 121.
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;
DE AltName: Full=MAP2 RNA trans-acting protein 1;
DE Short=MARTA1;
GN Name=Khsrp; Synonyms=Fubp2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 73-87; 89-108 AND 475-486,
RP SUBCELLULAR LOCATION, AND FUNCTION.
RC TISSUE=Brain;
RX PubMed=12358751; DOI=10.1046/j.1471-4159.2002.01058.x;
RA Rehbein M., Wege K., Buck F., Schweizer M., Richter D., Kindler S.;
RT "Molecular characterization of MARTA1, a protein interacting with the
RT dendritic targeting element of MAP2 mRNAs.";
RL J. Neurochem. 82:1039-1046(2002).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182 AND SER-185, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Part of a ternary complex that binds to the downstream
CC control sequence (DCS) of the pre-mRNA. Mediates exon inclusion in
CC transcripts that are subject to tissue-specific alternative splicing.
CC May interact with single-stranded DNA from the far-upstream element
CC (FUSE). May activate gene expression. Also involved in degradation of
CC inherently unstable mRNAs that contain AU-rich elements (AREs) in their
CC 3'-UTR, possibly by recruiting degradation machinery to ARE-containing
CC mRNAs (By similarity). Binds to the dendritic targeting element and may
CC play a role in mRNA trafficking. {ECO:0000250,
CC ECO:0000269|PubMed:12358751}.
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:0000269|PubMed:12358751}. Cytoplasm
CC {ECO:0000269|PubMed:12358751}. Note=A small proportion is also found in
CC the cytoplasm of neuronal cell bodies and dendrites.
CC -!- SIMILARITY: Belongs to the KHSRP family. {ECO:0000305}.
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DR EMBL; AF308818; AAG59811.1; -; mRNA.
DR RefSeq; NP_598286.1; NM_133602.1.
DR AlphaFoldDB; Q99PF5; -.
DR SMR; Q99PF5; -.
DR BioGRID; 251142; 1.
DR CORUM; Q99PF5; -.
DR STRING; 10116.ENSRNOP00000066023; -.
DR iPTMnet; Q99PF5; -.
DR PhosphoSitePlus; Q99PF5; -.
DR SwissPalm; Q99PF5; -.
DR REPRODUCTION-2DPAGE; Q99PF5; -.
DR jPOST; Q99PF5; -.
DR PaxDb; Q99PF5; -.
DR PRIDE; Q99PF5; -.
DR GeneID; 171137; -.
DR KEGG; rno:171137; -.
DR CTD; 8570; -.
DR RGD; 621828; Khsrp.
DR eggNOG; KOG1676; Eukaryota.
DR InParanoid; Q99PF5; -.
DR PhylomeDB; Q99PF5; -.
DR Reactome; R-RNO-450604; KSRP (KHSRP) binds and destabilizes mRNA.
DR PRO; PR:Q99PF5; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISO:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
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; IDA:RGD.
DR GO; GO:0003729; F:mRNA binding; ISO:RGD.
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; ISO:RGD.
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:RGD.
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; ISO:RGD.
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; PS50084; KH_TYPE_1; 4.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; DNA-binding;
KW Isopeptide bond; Methylation; mRNA processing; mRNA splicing;
KW mRNA transport; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding; Transcription; Transcription regulation; Transport;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q92945"
FT CHAIN 2..721
FT /note="Far upstream element-binding protein 2"
FT /id="PRO_0000050138"
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..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 688..721
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:0000250|UniProtKB:Q3U0V1"
FT MOD_RES 88
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q3U0V1"
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:22673903"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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:0000250|UniProtKB:Q92945"
FT MOD_RES 414
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q92945"
FT MOD_RES 416
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q92945"
FT MOD_RES 443
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q92945"
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"
SQ 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
