KHSRP

KH-type splicing regulatory protein
PDB rendering based on 2hh2.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 2HH2​, 2HH3​, 2JVZ​, 2OPU​, 2OPV​, 4B8T​
Identifiers
Symbols	KHSRP ; FBP2; FUBP2; KSRP
External IDs	OMIM: 603445 HomoloGene: 2734 ChEMBL: 1795105 GeneCards: KHSRP Gene
Gene ontology Molecular function • DNA binding • mRNA binding • poly(A) RNA binding Cellular component • nucleoplasm • cytosol • cytoplasmic stress granule • membrane Biological process • RNA splicing, via transesterification reactions • transcription, DNA-templated • regulation of transcription, DNA-templated • mRNA processing • mRNA catabolic process • RNA splicing • gene expression • mRNA transport • regulation of miRNA metabolic process Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	8570	16549
Ensembl	ENSG00000088247	ENSMUSG00000007670
UniProt	Q92945	Q3U0V1
RefSeq (mRNA)	NM_003685	NM_010613
RefSeq (protein)	NP_003676	NP_034743
Location (UCSC)	Chr 19: 6.41 – 6.42 Mb	Chr 17: 57.02 – 57.03 Mb
PubMed search

Far upstream element-binding protein 2 is a protein that in humans is encoded by the KHSRP gene.^[1][2][3]

References

1. Min H, Turck CW, Nikolic JM, Black DL (May 1997). "A new regulatory protein, KSRP, mediates exon inclusion through an intronic splicing enhancer". Genes Dev 11 (8): 1023–36. doi:10.1101/gad.11.8.1023. PMID 9136930.
2. Davis-Smyth T, Duncan RC, Zheng T, Michelotti G, Levens D (Jan 1997). "The far upstream element-binding proteins comprise an ancient family of single-strand DNA-binding transactivators". J Biol Chem 271 (49): 31679–87. doi:10.1074/jbc.271.49.31679. PMID 8940189.
3. "Entrez Gene: KHSRP KH-type splicing regulatory protein (FUSE binding protein 2)".

Further reading

• Dawson SJ, White LA (1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin.". J. Infect. 24 (3): 317–20. doi:10.1016/S0163-4453(05)80037-4. PMID 1602151.
• Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
• Chou MY, Rooke N, Turck CW, Black DL (1999). "hnRNP H is a component of a splicing enhancer complex that activates a c-src alternative exon in neuronal cells.". Mol. Cell. Biol. 19 (1): 69–77. PMC 83866. PMID 9858532.
• Ring HZ, Vameghi-Meyers V, Nikolic JM, et al. (1999). "Mapping of the KHSRP gene to a region of conserved synteny on human chromosome 19p13.3 and mouse chromosome 17.". Genomics 56 (3): 350–2. doi:10.1006/geno.1998.5725. PMID 10087204.
• Lellek H, Kirsten R, Diehl I, et al. (2000). "Purification and molecular cloning of a novel essential component of the apolipoprotein B mRNA editing enzyme-complex.". J. Biol. Chem. 275 (26): 19848–56. doi:10.1074/jbc.M001786200. PMID 10781591.
• Chou MY, Underwood JG, Nikolic J, et al. (2000). "Multisite RNA binding and release of polypyrimidine tract binding protein during the regulation of c-src neural-specific splicing.". Mol. Cell 5 (6): 949–57. doi:10.1016/S1097-2765(00)80260-9. PMID 10911989.
• Markovtsov V, Nikolic JM, Goldman JA, et al. (2000). "Cooperative assembly of an hnRNP complex induced by a tissue-specific homolog of polypyrimidine tract binding protein.". Mol. Cell. Biol. 20 (20): 7463–79. doi:10.1128/MCB.20.20.7463-7479.2000. PMC 86300. PMID 11003644.
• Chen CY, Gherzi R, Ong SE, et al. (2002). "AU binding proteins recruit the exosome to degrade ARE-containing mRNAs.". Cell 107 (4): 451–64. doi:10.1016/S0092-8674(01)00578-5. PMID 11719186.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Hall MP, Huang S, Black DL (2004). "Differentiation-induced colocalization of the KH-type splicing regulatory protein with polypyrimidine tract binding protein and the c-src pre-mRNA.". Mol. Biol. Cell 15 (2): 774–86. doi:10.1091/mbc.E03-09-0692. PMC 329392. PMID 14657238.
• Gherzi R, Lee KY, Briata P, et al. (2004). "A KH domain RNA binding protein, KSRP, promotes ARE-directed mRNA turnover by recruiting the degradation machinery.". Mol. Cell 14 (5): 571–83. doi:10.1016/j.molcel.2004.05.002. PMID 15175153.
• Suswam EA, Nabors LB, Huang Y, et al. (2005). "IL-1beta induces stabilization of IL-8 mRNA in malignant breast cancer cells via the 3' untranslated region: Involvement of divergent RNA-binding factors HuR, KSRP and TIAR.". Int. J. Cancer 113 (6): 911–9. doi:10.1002/ijc.20675. PMID 15514971.
• Wickham L, Benjannet S, Marcinkiewicz E, et al. (2005). "Beta-amyloid protein converting enzyme 1 and brain-specific type II membrane protein BRI3: binding partners processed by furin.". J. Neurochem. 92 (1): 93–102. doi:10.1111/j.1471-4159.2004.02840.x. PMID 15606899.
• Chou CF, Mulky A, Maitra S, et al. (2006). "Tethering KSRP, a decay-promoting AU-rich element-binding protein, to mRNAs elicits mRNA decay.". Mol. Cell. Biol. 26 (10): 3695–706. doi:10.1128/MCB.26.10.3695-3706.2006. PMC 1489004. PMID 16648466.
• Beausoleil SA, Villén J, Gerber SA, et al. (2006). "A probability-based approach for high-throughput protein phosphorylation analysis and site localization.". Nat. Biotechnol. 24 (10): 1285–92. doi:10.1038/nbt1240. PMID 16964243.
• Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.". Cell 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
• Gherzi R, Trabucchi M, Ponassi M, et al. (2007). "The RNA-binding protein KSRP promotes decay of beta-catenin mRNA and is inactivated by PI3K-AKT signaling.". PLoS Biol. 5 (1): e5. doi:10.1371/journal.pbio.0050005. PMC 1702562. PMID 17177604.
• Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry.". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.