FUBP2_HUMAN
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 03-AUG-2022, entry version 202.
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};
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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; 202.
DR CORUM; Q92945; -.
DR DIP; DIP-48484N; -.
DR ELM; Q92945; -.
DR IntAct; Q92945; 73.
DR MINT; Q92945; -.
DR STRING; 9606.ENSP00000381216; -.
DR ChEMBL; CHEMBL1795105; -.
DR DrugBank; DB11638; Artenimol.
DR DrugBank; DB02709; Resveratrol.
DR GlyGen; Q92945; 5 sites, 1 O-linked glycan (5 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; Q92945; -.
DR PeptideAtlas; Q92945; -.
DR PRIDE; Q92945; -.
DR ProteomicsDB; 75616; -.
DR Antibodypedia; 6316; 321 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 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; 590738at2759; -.
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; 77 hits in 1095 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 211 other tissues.
DR ExpressionAtlas; Q92945; baseline and differential.
DR Genevisible; Q92945; HS.
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: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:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0043488; P:regulation of mRNA stability; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0008380; P:RNA splicing; TAS:UniProtKB.
DR GO; GO:0000375; P:RNA splicing, via transesterification reactions; TAS:UniProtKB.
DR DisProt; DP01590; -.
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 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
