KHSRP

KHSRP
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2HH2, 2HH3, 2JVZ, 2OPU, 2OPV, 4B8T
Identifiers
Aliases	KHSRP, FBP2, FUBP2, KSRP, KH-type splicing regulatory protein, p75
External IDs	OMIM: 603445; MGI: 1336214; HomoloGene: 2734; GeneCards: KHSRP; OMA:KHSRP - orthologs
Gene location (Human) Chr. Chromosome 19 (human)[1] Band 19p13.3 Start 6,413,102 bp[1] End 6,424,811 bp[1]
Gene location (Mouse) Chr. Chromosome 17 (mouse)[2] Band 17 D|17 29.63 cM Start 57,328,051 bp[2] End 57,338,522 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in ventricular zone ganglionic eminence body of uterus right hemisphere of cerebellum left ovary right ovary canal of the cervix right testis right uterine tube left testis Top expressed in ventricular zone zygote tail of embryo hand neural layer of retina yolk sac genital tubercle secondary oocyte lip primary visual cortex More reference expression data BioGPS More reference expression data
Gene ontology Molecular function DNA binding protein binding nucleic acid binding mRNA binding mRNA 3'-UTR AU-rich region binding RNA binding Cellular component cytoplasm cytosol membrane nucleoplasm cytoplasmic stress granule nucleus exosome (RNase complex) Biological process mRNA transport regulation of transcription, DNA-templated mRNA catabolic process RNA splicing, via transesterification reactions mRNA processing transcription, DNA-templated regulation of miRNA metabolic process RNA splicing cellular response to cytokine stimulus negative regulation of nitric oxide biosynthetic process positive regulation of mRNA catabolic process 3'-UTR-mediated mRNA destabilization regulation of mRNA stability miRNA metabolic process transport negative regulation of low-density lipoprotein particle clearance Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 8570 16549 Ensembl ENSG00000088247 ENSMUSG00000007670 UniProt Q92945 Q3U0V1 RefSeq (mRNA) NM_003685 NM_001366299 NM_001366300 NM_010613 RefSeq (protein) NP_003676 NP_001353228 NP_001353229 NP_034743 Location (UCSC) Chr 19: 6.41 – 6.42 Mb Chr 17: 57.33 – 57.34 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Far upstream element-binding protein 2 is a protein that in humans is encoded by the KHSRP gene.[5][6][7]

References

1. GRCh38: Ensembl release 89: ENSG00000088247 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000007670 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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.
6. 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.
7. "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. doi:10.1128/MCB.19.1.69. 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. S2CID 14817671.
• 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. Bibcode:2002PNAS...9916899M. 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. S2CID 33272692.
• 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. S2CID 36799858.
• 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. S2CID 14294292.
• 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. S2CID 7827573.
• 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.