Far upstream element-binding protein 2

Details

Name
Far upstream element-binding protein 2
Synonyms
  • FUBP2
  • FUSE-binding protein 2
  • KH type-splicing regulatory protein
  • KSRP
  • p75
Gene Name
KHSRP
Organism
Humans
Amino acid sequence
>lcl|BSEQ0049899|Far upstream element-binding protein 2
MSDYSTGGPPPGPPPPAGGGGGAGGAGGGPPPGPPGAGDRGGGGPGGGGPGGGSAGGPSQ
PPGGGGPGIRKDAFADAVQRARQIAAKIGGDAATTVNNSTPDFGFGGQKRQLEDGDQPES
KKLASQGDSISSQLGPIHPPPRTSMTEEYRVPDGMVGLIIGRGGEQINKIQQDSGCKVQI
SPDSGGLPERSVSLTGAPESVQKAKMMLDDIVSRGRGGPPGQFHDNANGGQNGTVQEIMI
PAGKAGLVIGKGGETIKQLQERAGVKMILIQDGSQNTNVDKPLRIIGDPYKVQQACEMVM
DILRERDQGGFGDRNEYGSRIGGGIDVPVPRHSVGVVIGRSGEMIKKIQNDAGVRIQFKQ
DDGTGPEKIAHIMGPPDRCEHAARIINDLLQSLRSGPPGPPGGPGMPPGGRGRGRGQGNW
GPPGGEMTFSIPTHKCGLVIGRGGENVKAINQQTGAFVEISRQLPPNGDPNFKLFIIRGS
PQQIDHAKQLIEEKIEGPLCPVGPGPGGPGPAGPMGPFNPGPFNQGPPGAPPHAGGPPPH
QYPPQGWGNTYPQWQPPAPHDPSKAAAAAADPNAAWAAYYSHYYQQPPGPVPGPAPAPAA
PPAQGEPPQPPPTGQSDYTKAWEEYYKKIGQQPQQPGAPPQQDYTKAWEEYYKKQAQVAT
GGGPGAPPGSQPDYSAAWAEYYRQQAAYYGQTPGPGGPQPPPTQQGQQQAQ
Number of residues
711
Molecular Weight
73115.16
Theoretical pI
Not Available
GO Classification
Functions
DNA binding / mRNA 3'-UTR AU-rich region binding / RNA binding
Processes
3'-UTR-mediated mRNA destabilization / cellular response to cytokine stimulus / miRNA metabolic process / mRNA catabolic process / mRNA processing / mRNA transport / negative regulation of nitric oxide biosynthetic process / positive regulation of mRNA catabolic process / regulation of miRNA metabolic process / regulation of mRNA stability / regulation of transcription, DNA-templated / RNA splicing / RNA splicing, via transesterification reactions / transcription, DNA-templated
Components
cytoplasmic stress granule / cytosol / membrane / nucleoplasm
General Function
Binds to the dendritic targeting element and may play a role in mRNA trafficking (By similarity). 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.
Specific Function
Dna binding
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Nucleus
Gene sequence
>lcl|BSEQ0049900|Far upstream element-binding protein 2 (KHSRP)
ATGTCGGACTACAGCACGGGAGGACCCCCGCCCGGGCCGCCGCCGCCCGCCGGCGGGGGC
GGGGGAGCCGGAGGCGCCGGGGGAGGCCCTCCGCCGGGCCCGCCAGGCGCGGGGGACCGG
GGCGGCGGCGGTCCCGGCGGCGGCGGCCCGGGCGGGGGGTCGGCCGGGGGCCCCTCTCAG
CCACCCGGCGGAGGCGGCCCGGGAATCCGCAAGGACGCTTTCGCCGACGCCGTGCAGCGG
GCCCGCCAGATTGCAGCCAAAATTGGAGGCGATGCTGCCACGACAGTGAATAACAGCACT
CCTGATTTTGGTTTTGGGGGCCAAAAGAGACAGTTGGAAGATGGAGATCAACCGGAGAGC
AAGAAGCTGGCTTCCCAGGGAGACTCAATCAGTTCTCAACTTGGACCCATCCATCCTCCC
CCAAGGACTTCAATGACAGAAGAGTACAGGGTCCCAGACGGCATGGTGGGCCTGATCATT
GGCAGAGGAGGTGAACAAATTAACAAAATCCAACAGGATTCAGGCTGCAAAGTACAGATT
TCTCCAGACAGCGGTGGCCTACCCGAGCGCAGTGTGTCCTTGACAGGAGCCCCAGAATCT
GTCCAGAAAGCCAAGATGATGCTGGATGACATTGTGTCTCGGGGTCGTGGGGGCCCCCCA
GGACAGTTCCACGACAACGCCAACGGGGGCCAGAACGGCACCGTGCAGGAGATCATGATC
CCCGCGGGCAAGGCCGGCCTGGTCATTGGCAAGGGCGGGGAGACCATTAAGCAGCTGCAG
GAACGCGCTGGAGTGAAGATGATCTTAATTCAGGACGGATCTCAGAATACGAATGTGGAC
AAACCTCTCCGCATCATTGGGGATCCTTACAAAGTGCAGCAAGCCTGTGAGATGGTGATG
GACATCCTCCGGGAACGTGACCAAGGCGGCTTTGGGGACCGGAATGAGTACGGATCTCGG
ATTGGCGGAGGCATCGATGTGCCAGTGCCCAGGCATTCTGTTGGCGTGGTCATTGGCCGG
AGTGGAGAGATGATCAAGAAGATCCAGAATGATGCTGGCGTGCGGATACAGTTCAAGCAA
GATGACGGGACAGGGCCCGAGAAGATTGCTCATATAATGGGGCCCCCAGACAGGTGCGAG
CACGCAGCCCGGATCATCAACGACCTCCTCCAGAGCCTCAGGAGTGGTCCCCCAGGTCCT
CCAGGGGGTCCAGGCATGCCCCCGGGGGGCCGAGGCCGAGGAAGAGGCCAAGGCAATTGG
GGTCCCCCTGGCGGGGAGATGACCTTCTCCATCCCCACTCACAAGTGTGGGCTGGTCATC
GGCCGAGGTGGCGAGAATGTGAAAGCCATAAACCAGCAGACGGGAGCCTTCGTAGAGATC
TCCCGGCAGCTGCCACCCAACGGGGACCCCAACTTCAAGTTGTTCATCATCCGGGGTTCA
CCCCAGCAGATTGACCACGCCAAGCAGCTTATCGAGGAAAAGATCGAGGGTCCTCTCTGC
CCAGTTGGACCAGGCCCAGGTGGCCCAGGCCCTGCTGGCCCAATGGGGCCCTTCAATCCT
GGGCCCTTCAACCAGGGGCCACCCGGGGCTCCCCCACATGCCGGGGGGCCCCCTCCTCAC
CAGTACCCACCCCAGGGCTGGGGCAATACCTACCCCCAGTGGCAGCCGCCTGCTCCTCAT
GACCCAAGCAAAGCAGCTGCAGCGGCCGCGGACCCCAACGCCGCGTGGGCCGCCTACTAC
TCACACTACTACCAGCAGCCCCCGGGCCCCGTCCCCGGCCCCGCACCGGCCCCTGCGGCC
CCACCGGCTCAGGGTGAGCCCCCTCAGCCCCCACCCACCGGCCAGTCGGACTACACTAAG
GCCTGGGAAGAGTATTACAAAAAGATCGGCCAGCAGCCCCAGCAGCCCGGAGCACCCCCA
CAGCAGGACTACACGAAGGCTTGGGAGGAGTACTACAAGAAGCAAGCGCAAGTGGCCACC
GGAGGGGGTCCAGGAGCTCCCCCAGGCTCCCAGCCAGACTACAGTGCCGCCTGGGCGGAA
TATTACAGACAGCAGGCCGCTTACTACGGACAGACCCCAGGTCCTGGCGGCCCCCAGCCG
CCGCCCACGCAGCAGGGACAGCAGCAGGCTCAATGA
Chromosome Location
19
Locus
19p13.3
External Identifiers
ResourceLink
UniProtKB IDQ92945
UniProtKB Entry NameFUBP2_HUMAN
HGNC IDHGNC:6316
General References
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  4. Ring HZ, Vameghi-Meyers V, Nikolic JM, Min H, Black DL, Francke U: Mapping of the KHSRP gene to a region of conserved synteny on human chromosome 19p13.3 and mouse chromosome 17. Genomics. 1999 Mar 15;56(3):350-2. [Article]
  5. Davis-Smyth T, Duncan RC, Zheng T, Michelotti G, Levens D: The far upstream element-binding proteins comprise an ancient family of single-strand DNA-binding transactivators. J Biol Chem. 1996 Dec 6;271(49):31679-87. [Article]
  6. Markovtsov V, Nikolic JM, Goldman JA, Turck CW, Chou MY, Black DL: Cooperative assembly of an hnRNP complex induced by a tissue-specific homolog of polypyrimidine tract binding protein. Mol Cell Biol. 2000 Oct;20(20):7463-79. [Article]
  7. Gherzi R, Lee KY, Briata P, Wegmuller D, Moroni C, Karin M, Chen CY: A KH domain RNA binding protein, KSRP, promotes ARE-directed mRNA turnover by recruiting the degradation machinery. Mol Cell. 2004 Jun 4;14(5):571-83. [Article]
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  27. Diaz-Moreno I, Hollingworth D, Frenkiel TA, Kelly G, Martin S, Howell S, Garcia-Mayoral M, Gherzi R, Briata P, Ramos A: Phosphorylation-mediated unfolding of a KH domain regulates KSRP localization via 14-3-3 binding. Nat Struct Mol Biol. 2009 Mar;16(3):238-46. doi: 10.1038/nsmb.1558. Epub 2009 Feb 8. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB02709ResveratrolinvestigationalunknownDetails
DB11638Artenimolapproved, experimental, investigationalunknownligandDetails