ID FUBP2_HUMAN Reviewed; 711 AA. AC Q92945; O00301; Q59EZ9; Q5U4P6; Q9UNT5; Q9UQH5; DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot. DT 30-NOV-2010, sequence version 4. DT 27-MAR-2024, entry version 211. 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=p75; GN Name=KHSRP; Synonyms=FUBP2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 72-85; 123-128; 267-281; RP 283-291; 348-359; 474-488; 489-494; 621-627; 629-646 AND 647-653, AND RP FUNCTION. RC TISSUE=Neuroblastoma, and Retinoblastoma; RX PubMed=9136930; DOI=10.1101/gad.11.8.1023; RA Min H., Turck C.W., Nikolic J.M., Black D.L.; RT "A new regulatory protein, KSRP, mediates exon inclusion through an RT intronic splicing enhancer."; RL Genes Dev. 11:1023-1036(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Ovary; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-115 AND 573-711. RX PubMed=10087204; DOI=10.1006/geno.1998.5725; RA Ring H.Z., Vameghi-Meyers V., Nikolic J.M., Min H., Black D.L., Francke U.; RT "Mapping of the KHSRP gene to a region of conserved synteny on human RT chromosome 19p13.3 and mouse chromosome 17."; RL Genomics 56:350-352(1999). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 60-711, AND FUNCTION. RC TISSUE=B-cell lymphoma, and Skeletal muscle; RX PubMed=8940189; DOI=10.1074/jbc.271.49.31679; RA Davis-Smyth T., Duncan R.C., Zheng T., Michelotti G., Levens D.; RT "The far upstream element-binding proteins comprise an ancient family of RT single-strand DNA-binding transactivators."; RL J. Biol. Chem. 271:31679-31687(1996). RN [6] RP PROTEIN SEQUENCE OF 151-162; 321-331 AND 385-394, AND IDENTIFICATION BY RP MASS SPECTROMETRY. RC TISSUE=Fetal brain cortex; RA Lubec G., Chen W.-Q., Sun Y.; RL Submitted (DEC-2008) to UniProtKB. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 183-566. RC TISSUE=Brain; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., RA Ohara O., Nagase T., Kikuno R.F.; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP FUNCTION, AND INTERACTION WITH PTBP1; PTBP2 AND HNRPH1. RX PubMed=11003644; DOI=10.1128/mcb.20.20.7463-7479.2000; RA Markovtsov V., Nikolic J.M., Goldman J.A., Turck C.W., Chou M.-Y., RA Black D.L.; RT "Cooperative assembly of an hnRNP complex induced by a tissue-specific RT homolog of polypyrimidine tract binding protein."; RL Mol. Cell. Biol. 20:7463-7479(2000). RN [9] RP INTERACTION WITH PARN. RX PubMed=15175153; DOI=10.1016/j.molcel.2004.05.002; RA Gherzi R., Lee K.-Y., Briata P., Wegmueller D., Moroni C., Karin M., RA Chen C.-Y.; RT "A KH domain RNA binding protein, KSRP, promotes ARE-directed mRNA turnover RT by recruiting the degradation machinery."; RL Mol. Cell 14:571-583(2004). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-100; SER-181 AND SER-274, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 AND SER-480, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [19] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [20] RP INTERACTION WITH PQBP1. RX PubMed=21933836; DOI=10.1093/hmg/ddr430; RA Kunde S.A., Musante L., Grimme A., Fischer U., Mueller E., Wanker E.E., RA Kalscheuer V.M.; RT "The X-chromosome-linked intellectual disability protein PQBP1 is a RT component of neuronal RNA granules and regulates the appearance of stress RT granules."; RL Hum. Mol. Genet. 20:4916-4931(2011). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181; SER-274 AND SER-480, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [22] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [23] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [24] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99; SER-125; SER-129; RP SER-131; SER-181; SER-184; SER-193; SER-274 AND SER-480, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [25] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [26] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-411; ARG-413; ARG-415 AND RP ARG-442, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [27] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-121, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25114211; DOI=10.1073/pnas.1413825111; RA Impens F., Radoshevich L., Cossart P., Ribet D.; RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by RT external stimuli."; RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014). RN [28] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [29] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-121, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [30] RP STRUCTURE BY NMR OF 218-418 AND 423-525. RX PubMed=17437720; DOI=10.1016/j.str.2007.03.006; RA Garcia-Mayoral M.F., Hollingworth D., Masino L., Diaz-Moreno I., Kelly G., RA Gherzi R., Chou C.F., Chen C.Y., Ramos A.; RT "The structure of the C-terminal KH domains of KSRP reveals a noncanonical RT motif important for mRNA degradation."; RL Structure 15:485-498(2007). RN [31] RP STRUCTURE BY NMR OF 130-218 AND 221-305, PHOSPHORYLATION AT SER-193, AND RP SUBCELLULAR LOCATION. RX PubMed=19198587; DOI=10.1038/nsmb.1558; RA Diaz-Moreno I., Hollingworth D., Frenkiel T.A., Kelly G., Martin S., RA Howell S., Garcia-Mayoral M., Gherzi R., Briata P., Ramos A.; RT "Phosphorylation-mediated unfolding of a KH domain regulates KSRP RT localization via 14-3-3 binding."; RL Nat. Struct. Mol. Biol. 16:238-246(2009). CC -!- FUNCTION: Binds to the dendritic targeting element and may play a role CC in mRNA trafficking (By similarity). Part of a ternary complex that CC binds to the downstream control sequence (DCS) of the pre-mRNA. CC Mediates exon inclusion in transcripts that are subject to tissue- CC specific alternative splicing. May interact with single-stranded DNA CC from the far-upstream element (FUSE). May activate gene expression. CC Also involved in degradation of inherently unstable mRNAs that contain CC AU-rich elements (AREs) in their 3'-UTR, possibly by recruiting CC degradation machinery to ARE-containing mRNAs. {ECO:0000250, CC ECO:0000269|PubMed:11003644, ECO:0000269|PubMed:8940189, CC ECO:0000269|PubMed:9136930}. CC -!- SUBUNIT: Part of a ternary complex containing FUBP2, PTBP1, PTBP2 and CC HNRPH1 (PubMed:11003644). Interacts with PARN (PubMed:15175153). CC Interacts with PQBP1 (PubMed:21933836). {ECO:0000269|PubMed:11003644, CC ECO:0000269|PubMed:15175153, ECO:0000269|PubMed:21933836}. CC -!- INTERACTION: CC Q92945; Q9UPY3-1: DICER1; NbExp=3; IntAct=EBI-1049099, EBI-15569571; CC Q92945; P63101: Ywhaz; Xeno; NbExp=2; IntAct=EBI-1049099, EBI-354751; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19198587}. Cytoplasm CC {ECO:0000269|PubMed:19198587}. Note=A small proportion is also found in CC the cytoplasm of neuronal cell bodies and dendrites. {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Detected in neural and non-neural cell lines. CC -!- DOMAIN: KH domains KH 3 and KH 4 behave as independent binding modules CC and can interact with different regions of the AU-rich RNA targets of CC degradation. CC -!- PTM: Phosphorylation at Ser-193 leads to the unfolding of the unstable CC KH domain 1, creating a site for 14-3-3 YWHAZ binding, which promotes CC nuclear localization and impairs the RNA degradation function. CC {ECO:0000269|PubMed:19198587}. CC -!- SIMILARITY: Belongs to the KHSRP family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC50892.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=AAH85004.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U94832; AAB53222.1; -; mRNA. DR EMBL; AC011491; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC011539; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC085004; AAH85004.1; ALT_SEQ; mRNA. DR EMBL; AF093747; AAD29861.1; -; Genomic_DNA. DR EMBL; AF093745; AAD29861.1; JOINED; Genomic_DNA. DR EMBL; AF093748; AAD29862.1; -; Genomic_DNA. DR EMBL; U69126; AAC50892.1; ALT_FRAME; mRNA. DR EMBL; AB209662; BAD92899.1; -; mRNA. DR CCDS; CCDS45936.1; -. DR RefSeq; NP_003676.2; NM_003685.2. DR PDB; 2HH2; NMR; -; A=424-525. DR PDB; 2HH3; NMR; -; A=318-418. DR PDB; 2JVZ; NMR; -; A=233-396. DR PDB; 2OPU; NMR; -; A=130-218. DR PDB; 2OPV; NMR; -; A=221-305. DR PDB; 4B8T; NMR; -; A=317-418. DR PDBsum; 2HH2; -. DR PDBsum; 2HH3; -. DR PDBsum; 2JVZ; -. DR PDBsum; 2OPU; -. DR PDBsum; 2OPV; -. DR PDBsum; 4B8T; -. DR AlphaFoldDB; Q92945; -. DR SMR; Q92945; -. DR BioGRID; 114139; 264. DR CORUM; Q92945; -. DR DIP; DIP-48484N; -. DR ELM; Q92945; -. DR IntAct; Q92945; 76. DR MINT; Q92945; -. DR STRING; 9606.ENSP00000381216; -. DR ChEMBL; CHEMBL1795105; -. DR DrugBank; DB11638; Artenimol. DR DrugBank; DB02709; Resveratrol. DR GlyCosmos; Q92945; 5 sites, 1 glycan. DR GlyGen; Q92945; 8 sites, 1 O-linked glycan (8 sites). DR iPTMnet; Q92945; -. DR MetOSite; Q92945; -. DR PhosphoSitePlus; Q92945; -. DR SwissPalm; Q92945; -. DR BioMuta; KHSRP; -. DR DMDM; 313104306; -. DR REPRODUCTION-2DPAGE; Q92945; -. DR EPD; Q92945; -. DR jPOST; Q92945; -. DR MassIVE; Q92945; -. DR MaxQB; Q92945; -. DR PaxDb; 9606-ENSP00000381216; -. DR PeptideAtlas; Q92945; -. DR ProteomicsDB; 75616; -. DR Pumba; Q92945; -. DR Antibodypedia; 6316; 367 antibodies from 34 providers. DR DNASU; 8570; -. DR Ensembl; ENST00000398148.7; ENSP00000381216.2; ENSG00000088247.19. DR GeneID; 8570; -. DR KEGG; hsa:8570; -. DR UCSC; uc002mer.5; human. DR AGR; HGNC:6316; -. DR CTD; 8570; -. DR DisGeNET; 8570; -. DR GeneCards; KHSRP; -. DR HGNC; HGNC:6316; KHSRP. DR HPA; ENSG00000088247; Low tissue specificity. DR MIM; 603445; gene. DR neXtProt; NX_Q92945; -. DR OpenTargets; ENSG00000088247; -. DR PharmGKB; PA30097; -. DR VEuPathDB; HostDB:ENSG00000088247; -. DR eggNOG; KOG1676; Eukaryota. DR GeneTree; ENSGT00940000156051; -. DR HOGENOM; CLU_014285_1_0_1; -. DR InParanoid; Q92945; -. DR OMA; QPVHQWA; -. DR OrthoDB; 1662at2759; -. DR PhylomeDB; Q92945; -. DR TreeFam; TF313654; -. DR PathwayCommons; Q92945; -. DR Reactome; R-HSA-380994; ATF4 activates genes in response to endoplasmic reticulum stress. DR Reactome; R-HSA-450604; KSRP (KHSRP) binds and destabilizes mRNA. DR SignaLink; Q92945; -. DR SIGNOR; Q92945; -. DR BioGRID-ORCS; 8570; 79 hits in 1173 CRISPR screens. DR ChiTaRS; KHSRP; human. DR EvolutionaryTrace; Q92945; -. DR GeneWiki; KHSRP; -. DR GenomeRNAi; 8570; -. DR Pharos; Q92945; Tbio. DR PRO; PR:Q92945; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; Q92945; Protein. DR Bgee; ENSG00000088247; Expressed in ventricular zone and 213 other cell types or tissues. DR ExpressionAtlas; Q92945; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; IDA:UniProtKB. DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central. DR GO; GO:0044183; F:protein folding chaperone; EXP:DisProt. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; IDA:UniProtKB. DR GO; GO:0071345; P:cellular response to cytokine stimulus; IMP:UniProtKB. DR GO; GO:0010586; P:miRNA metabolic process; IMP:UniProtKB. DR GO; GO:0006397; P:mRNA processing; TAS:ProtInc. DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW. DR GO; GO:0010989; P:negative regulation of low-density lipoprotein particle clearance; IGI:BHF-UCL. DR GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; IDA:UniProtKB. DR GO; GO:0061014; P:positive regulation of mRNA catabolic process; IDA:UniProtKB. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro. DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central. DR GO; GO:0043488; P:regulation of mRNA stability; IDA:UniProtKB. DR GO; GO:0008380; P:RNA splicing; TAS:UniProtKB. DR GO; GO:0000375; P:RNA splicing, via transesterification reactions; TAS:UniProtKB. DR CDD; cd22479; KH-I_FUBP2_rpt1; 1. DR CDD; cd22482; KH-I_FUBP2_rpt2; 1. DR CDD; cd22485; KH-I_FUBP2_rpt3; 1. DR CDD; cd22488; KH-I_FUBP2_rpt4; 1. DR DisProt; DP01590; -. DR Gene3D; 3.30.1370.10; K Homology domain, type 1; 4. DR InterPro; IPR015096; FUBP_C. DR InterPro; IPR047372; KH-I_FUBP2_rpt1. DR InterPro; IPR047369; KH-I_FUBP2_rpt2. DR InterPro; IPR047370; KH-I_FUBP2_rpt3. DR InterPro; IPR047371; KH-I_FUBP2_rpt4. DR InterPro; IPR004087; KH_dom. DR InterPro; IPR004088; KH_dom_type_1. DR InterPro; IPR036612; KH_dom_type_1_sf. DR PANTHER; PTHR10288; KH DOMAIN CONTAINING RNA BINDING PROTEIN; 1. DR PANTHER; PTHR10288:SF171; P-ELEMENT SOMATIC INHIBITOR, ISOFORM C; 1. DR Pfam; PF09005; DUF1897; 2. DR Pfam; PF00013; KH_1; 4. DR SMART; SM00322; KH; 4. DR SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 4. DR PROSITE; PS50084; KH_TYPE_1; 4. DR Genevisible; Q92945; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; KW DNA-binding; 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:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378" FT CHAIN 2..711 FT /note="Far upstream element-binding protein 2" FT /id="PRO_0000050137" FT DOMAIN 144..208 FT /note="KH 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117" FT DOMAIN 233..299 FT /note="KH 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117" FT DOMAIN 322..386 FT /note="KH 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117" FT DOMAIN 424..491 FT /note="KH 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117" FT REPEAT 571..582 FT /note="1" FT REPEAT 617..628 FT /note="2" FT REPEAT 643..654 FT /note="3" FT REPEAT 673..684 FT /note="4" FT REGION 1..147 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 392..429 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 497..569 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 571..684 FT /note="4 X 12 AA imperfect repeats" FT REGION 583..711 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 122..139 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 502..545 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 587..614 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378" FT MOD_RES 40 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:Q3U0V1" FT MOD_RES 87 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q3U0V1" FT MOD_RES 99 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 100 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 125 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 129 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 131 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 181 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 184 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 193 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:19198587, FT ECO:0007744|PubMed:23186163" FT MOD_RES 274 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 411 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 413 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 415 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 442 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 480 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT CROSSLNK 121 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0007744|PubMed:25114211" FT CROSSLNK 121 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:28112733" FT CONFLICT 46 FT /note="G -> C (in Ref. 1; AAB53222 and 4; AAD29861)" FT /evidence="ECO:0000305" FT CONFLICT 96 FT /note="V -> G (in Ref. 5; AAC50892)" FT /evidence="ECO:0000305" FT CONFLICT 406..407 FT /note="MP -> I (in Ref. 5; AAC50892)" FT /evidence="ECO:0000305" FT CONFLICT 422 FT /note="Missing (in Ref. 5; AAC50892)" FT /evidence="ECO:0000305" FT CONFLICT 487..488 FT /note="AK -> CR (in Ref. 5; AAC50892)" FT /evidence="ECO:0000305" FT CONFLICT 694..696 FT /note="GPG -> VP (in Ref. 5; AAC50892)" FT /evidence="ECO:0000305" FT STRAND 132..134 FT /evidence="ECO:0007829|PDB:2OPU" FT HELIX 141..144 FT /evidence="ECO:0007829|PDB:2OPU" FT STRAND 146..151 FT /evidence="ECO:0007829|PDB:2OPU" FT HELIX 153..159 FT /evidence="ECO:0007829|PDB:2OPU" FT TURN 161..163 FT /evidence="ECO:0007829|PDB:2OPU" FT HELIX 165..174 FT /evidence="ECO:0007829|PDB:2OPU" FT STRAND 179..183 FT /evidence="ECO:0007829|PDB:2OPU" FT STRAND 188..194 FT /evidence="ECO:0007829|PDB:2OPU" FT HELIX 198..216 FT /evidence="ECO:0007829|PDB:2OPU" FT STRAND 234..240 FT /evidence="ECO:0007829|PDB:2JVZ" FT TURN 242..244 FT /evidence="ECO:0007829|PDB:2OPV" FT TURN 245..249 FT /evidence="ECO:0007829|PDB:2JVZ" FT TURN 251..253 FT /evidence="ECO:0007829|PDB:2JVZ" FT HELIX 254..261 FT /evidence="ECO:0007829|PDB:2JVZ" FT STRAND 265..269 FT /evidence="ECO:0007829|PDB:2JVZ" FT STRAND 271..273 FT /evidence="ECO:0007829|PDB:2OPV" FT STRAND 275..279 FT /evidence="ECO:0007829|PDB:2JVZ" FT STRAND 281..287 FT /evidence="ECO:0007829|PDB:2JVZ" FT HELIX 289..302 FT /evidence="ECO:0007829|PDB:2JVZ" FT STRAND 306..308 FT /evidence="ECO:0007829|PDB:2JVZ" FT TURN 317..319 FT /evidence="ECO:0007829|PDB:4B8T" FT STRAND 325..330 FT /evidence="ECO:0007829|PDB:2HH3" FT TURN 331..333 FT /evidence="ECO:0007829|PDB:2HH3" FT HELIX 334..338 FT /evidence="ECO:0007829|PDB:2HH3" FT STRAND 340..342 FT /evidence="ECO:0007829|PDB:2JVZ" FT HELIX 343..352 FT /evidence="ECO:0007829|PDB:2HH3" FT STRAND 355..358 FT /evidence="ECO:0007829|PDB:2HH3" FT STRAND 363..375 FT /evidence="ECO:0007829|PDB:2HH3" FT HELIX 376..393 FT /evidence="ECO:0007829|PDB:2HH3" FT STRAND 400..405 FT /evidence="ECO:0007829|PDB:4B8T" FT TURN 413..415 FT /evidence="ECO:0007829|PDB:4B8T" FT STRAND 427..432 FT /evidence="ECO:0007829|PDB:2HH2" FT HELIX 433..435 FT /evidence="ECO:0007829|PDB:2HH2" FT TURN 436..438 FT /evidence="ECO:0007829|PDB:2HH2" FT TURN 441..444 FT /evidence="ECO:0007829|PDB:2HH2" FT HELIX 446..453 FT /evidence="ECO:0007829|PDB:2HH2" FT STRAND 454..460 FT /evidence="ECO:0007829|PDB:2HH2" FT STRAND 472..479 FT /evidence="ECO:0007829|PDB:2HH2" FT HELIX 481..494 FT /evidence="ECO:0007829|PDB:2HH2" SQ SEQUENCE 711 AA; 73115 MW; AB0B7C0B5B938114 CRC64; MSDYSTGGPP PGPPPPAGGG GGAGGAGGGP PPGPPGAGDR GGGGPGGGGP GGGSAGGPSQ PPGGGGPGIR KDAFADAVQR ARQIAAKIGG DAATTVNNST PDFGFGGQKR QLEDGDQPES KKLASQGDSI SSQLGPIHPP PRTSMTEEYR VPDGMVGLII GRGGEQINKI QQDSGCKVQI SPDSGGLPER SVSLTGAPES VQKAKMMLDD IVSRGRGGPP GQFHDNANGG QNGTVQEIMI PAGKAGLVIG KGGETIKQLQ ERAGVKMILI QDGSQNTNVD KPLRIIGDPY KVQQACEMVM DILRERDQGG FGDRNEYGSR IGGGIDVPVP RHSVGVVIGR SGEMIKKIQN DAGVRIQFKQ DDGTGPEKIA HIMGPPDRCE HAARIINDLL QSLRSGPPGP PGGPGMPPGG RGRGRGQGNW GPPGGEMTFS IPTHKCGLVI GRGGENVKAI NQQTGAFVEI SRQLPPNGDP NFKLFIIRGS PQQIDHAKQL IEEKIEGPLC PVGPGPGGPG PAGPMGPFNP GPFNQGPPGA PPHAGGPPPH QYPPQGWGNT YPQWQPPAPH DPSKAAAAAA DPNAAWAAYY SHYYQQPPGP VPGPAPAPAA PPAQGEPPQP PPTGQSDYTK AWEEYYKKIG QQPQQPGAPP QQDYTKAWEE YYKKQAQVAT GGGPGAPPGS QPDYSAAWAE YYRQQAAYYG QTPGPGGPQP PPTQQGQQQA Q //