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Far upstream element-binding protein 2 (FUSE-binding protein 2) (KH type-splicing regulatory protein) (KSRP) (p75)

 FUBP2_HUMAN             Reviewed;         711 AA.
Q92945; O00301; Q59EZ9; Q5U4P6; Q9UNT5; Q9UQH5;
26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
30-NOV-2010, sequence version 4.
18-JUL-2018, entry version 176.
RecName: Full=Far upstream element-binding protein 2;
Short=FUSE-binding protein 2;
AltName: Full=KH type-splicing regulatory protein;
Short=KSRP;
AltName: Full=p75;
Name=KHSRP; Synonyms=FUBP2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 72-85; 123-128;
267-281; 283-291; 348-359; 474-488; 489-494; 621-627; 629-646 AND
647-653, AND FUNCTION.
TISSUE=Neuroblastoma, and Retinoblastoma;
PubMed=9136930; DOI=10.1101/gad.11.8.1023;
Min H., Turck C.W., Nikolic J.M., Black D.L.;
"A new regulatory protein, KSRP, mediates exon inclusion through an
intronic splicing enhancer.";
Genes Dev. 11:1023-1036(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Ovary;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-115 AND 573-711.
PubMed=10087204; DOI=10.1006/geno.1998.5725;
Ring H.Z., Vameghi-Meyers V., Nikolic J.M., Min H., Black D.L.,
Francke U.;
"Mapping of the KHSRP gene to a region of conserved synteny on human
chromosome 19p13.3 and mouse chromosome 17.";
Genomics 56:350-352(1999).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 60-711, AND FUNCTION.
TISSUE=B-cell lymphoma, and Skeletal muscle;
PubMed=8940189; DOI=10.1074/jbc.271.49.31679;
Davis-Smyth T., Duncan R.C., 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. 271:31679-31687(1996).
[6]
PROTEIN SEQUENCE OF 151-162; 321-331 AND 385-394, AND IDENTIFICATION
BY MASS SPECTROMETRY.
TISSUE=Fetal brain cortex;
Lubec G., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 183-566.
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[8]
FUNCTION, AND INTERACTION WITH PTBP1; PTBP2 AND HNRPH1.
PubMed=11003644; DOI=10.1128/MCB.20.20.7463-7479.2000;
Markovtsov V., Nikolic J.M., Goldman J.A., Turck C.W., Chou M.-Y.,
Black D.L.;
"Cooperative assembly of an hnRNP complex induced by a tissue-specific
homolog of polypyrimidine tract binding protein.";
Mol. Cell. Biol. 20:7463-7479(2000).
[9]
INTERACTION WITH PARN.
PubMed=15175153; DOI=10.1016/j.molcel.2004.05.002;
Gherzi R., Lee K.-Y., Briata P., Wegmueller D., Moroni C., Karin M.,
Chen C.-Y.;
"A KH domain RNA binding protein, KSRP, promotes ARE-directed mRNA
turnover by recruiting the degradation machinery.";
Mol. Cell 14:571-583(2004).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-100; SER-181 AND
SER-274, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 AND SER-480, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[20]
INTERACTION WITH PQBP1.
PubMed=21933836; DOI=10.1093/hmg/ddr430;
Kunde S.A., Musante L., Grimme A., Fischer U., Mueller E.,
Wanker E.E., Kalscheuer V.M.;
"The X-chromosome-linked intellectual disability protein PQBP1 is a
component of neuronal RNA granules and regulates the appearance of
stress granules.";
Hum. Mol. Genet. 20:4916-4931(2011).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181; SER-274 AND
SER-480, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[22]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[23]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99; SER-125; SER-129;
SER-131; SER-181; SER-184; SER-193; SER-274 AND SER-480, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[25]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[26]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-411; ARG-413; ARG-415 AND
ARG-442, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[27]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-121, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[28]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[29]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-121, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[30]
STRUCTURE BY NMR OF 218-418 AND 423-525.
PubMed=17437720; DOI=10.1016/j.str.2007.03.006;
Garcia-Mayoral M.F., Hollingworth D., Masino L., Diaz-Moreno I.,
Kelly G., Gherzi R., Chou C.F., Chen C.Y., Ramos A.;
"The structure of the C-terminal KH domains of KSRP reveals a
noncanonical motif important for mRNA degradation.";
Structure 15:485-498(2007).
[31]
STRUCTURE BY NMR OF 130-218 AND 221-305, PHOSPHORYLATION AT SER-193,
AND SUBCELLULAR LOCATION.
PubMed=19198587; DOI=10.1038/nsmb.1558;
Diaz-Moreno I., Hollingworth D., Frenkiel T.A., 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. 16:238-246(2009).
-!- 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. {ECO:0000250, ECO:0000269|PubMed:11003644,
ECO:0000269|PubMed:8940189, ECO:0000269|PubMed:9136930}.
-!- SUBUNIT: Part of a ternary complex containing FUBP2, PTBP1, PTBP2
and HNRPH1 (PubMed:11003644). Interacts with PARN
(PubMed:15175153). Interacts with PQBP1 (PubMed:21933836).
{ECO:0000269|PubMed:11003644, ECO:0000269|PubMed:15175153,
ECO:0000269|PubMed:21933836}.
-!- INTERACTION:
Q9UPY3-1:DICER1; NbExp=3; IntAct=EBI-1049099, EBI-15569571;
P60520:GABARAPL2; NbExp=2; IntAct=EBI-1049099, EBI-720116;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19198587}.
Cytoplasm {ECO:0000269|PubMed:19198587}. Note=A small proportion
is also found in the cytoplasm of neuronal cell bodies and
dendrites. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Detected in neural and non-neural cell lines.
-!- DOMAIN: KH domains KH 3 and KH 4 behave as independent binding
modules and can interact with different regions of the AU-rich RNA
targets of degradation.
-!- PTM: Phosphorylation at Ser-193 leads to the unfolding of the
unstable KH domain 1, creating a site for 14-3-3 YWHAZ binding,
which promotes nuclear localization and impairs the RNA
degradation function. {ECO:0000269|PubMed:19198587}.
-!- SIMILARITY: Belongs to the KHSRP family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC50892.1; Type=Frameshift; Positions=304, 309, 466, 473; Evidence={ECO:0000305};
Sequence=AAH85004.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
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EMBL; U94832; AAB53222.1; -; mRNA.
EMBL; AC011491; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC011539; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC085004; AAH85004.1; ALT_SEQ; mRNA.
EMBL; AF093747; AAD29861.1; -; Genomic_DNA.
EMBL; AF093745; AAD29861.1; JOINED; Genomic_DNA.
EMBL; AF093748; AAD29862.1; -; Genomic_DNA.
EMBL; U69126; AAC50892.1; ALT_FRAME; mRNA.
EMBL; AB209662; BAD92899.1; -; mRNA.
CCDS; CCDS45936.1; -.
RefSeq; NP_003676.2; NM_003685.2.
UniGene; Hs.727344; -.
PDB; 2HH2; NMR; -; A=424-525.
PDB; 2HH3; NMR; -; A=318-418.
PDB; 2JVZ; NMR; -; A=233-396.
PDB; 2OPU; NMR; -; A=130-218.
PDB; 2OPV; NMR; -; A=221-305.
PDB; 4B8T; NMR; -; A=317-418.
PDBsum; 2HH2; -.
PDBsum; 2HH3; -.
PDBsum; 2JVZ; -.
PDBsum; 2OPU; -.
PDBsum; 2OPV; -.
PDBsum; 4B8T; -.
ProteinModelPortal; Q92945; -.
SMR; Q92945; -.
BioGrid; 114139; 86.
DIP; DIP-48484N; -.
ELM; Q92945; -.
IntAct; Q92945; 37.
MINT; Q92945; -.
STRING; 9606.ENSP00000381216; -.
ChEMBL; CHEMBL1795105; -.
iPTMnet; Q92945; -.
PhosphoSitePlus; Q92945; -.
SwissPalm; Q92945; -.
BioMuta; KHSRP; -.
DMDM; 313104306; -.
REPRODUCTION-2DPAGE; Q92945; -.
EPD; Q92945; -.
MaxQB; Q92945; -.
PaxDb; Q92945; -.
PeptideAtlas; Q92945; -.
PRIDE; Q92945; -.
ProteomicsDB; 75616; -.
Ensembl; ENST00000398148; ENSP00000381216; ENSG00000088247.
GeneID; 8570; -.
KEGG; hsa:8570; -.
UCSC; uc002mer.5; human.
CTD; 8570; -.
DisGeNET; 8570; -.
EuPathDB; HostDB:ENSG00000088247.15; -.
GeneCards; KHSRP; -.
H-InvDB; HIX0040083; -.
HGNC; HGNC:6316; KHSRP.
HPA; HPA034739; -.
HPA; HPA056518; -.
MIM; 603445; gene.
neXtProt; NX_Q92945; -.
OpenTargets; ENSG00000088247; -.
PharmGKB; PA30097; -.
eggNOG; KOG1676; Eukaryota.
eggNOG; ENOG410XZYE; LUCA.
GeneTree; ENSGT00730000110664; -.
HOGENOM; HOG000231552; -.
HOVERGEN; HBG000625; -.
InParanoid; Q92945; -.
KO; K13210; -.
PhylomeDB; Q92945; -.
TreeFam; TF313654; -.
Reactome; R-HSA-380994; ATF4 activates genes.
Reactome; R-HSA-450604; KSRP (KHSRP) binds and destabilizes mRNA.
SIGNOR; Q92945; -.
ChiTaRS; KHSRP; human.
EvolutionaryTrace; Q92945; -.
GeneWiki; KHSRP; -.
GenomeRNAi; 8570; -.
PMAP-CutDB; Q92945; -.
PRO; PR:Q92945; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000088247; -.
CleanEx; HS_KHSRP; -.
ExpressionAtlas; Q92945; baseline and differential.
Genevisible; Q92945; HS.
GO; GO:0010494; C:cytoplasmic stress granule; IEA:Ensembl.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; IDA:UniProtKB.
GO; GO:0071345; P:cellular response to cytokine stimulus; IMP:UniProtKB.
GO; GO:0010586; P:miRNA metabolic process; IMP:UniProtKB.
GO; GO:0006402; P:mRNA catabolic process; IEA:Ensembl.
GO; GO:0006397; P:mRNA processing; TAS:ProtInc.
GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
GO; GO:0010989; P:negative regulation of low-density lipoprotein particle clearance; IGI:BHF-UCL.
GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; IDA:UniProtKB.
GO; GO:0061014; P:positive regulation of mRNA catabolic process; IDA:UniProtKB.
GO; GO:2000628; P:regulation of miRNA metabolic process; IEA:Ensembl.
GO; GO:0043488; P:regulation of mRNA stability; IDA:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0008380; P:RNA splicing; TAS:UniProtKB.
GO; GO:0000375; P:RNA splicing, via transesterification reactions; TAS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 3.30.1370.10; -; 4.
InterPro; IPR015096; FUBP_C.
InterPro; IPR004087; KH_dom.
InterPro; IPR004088; KH_dom_type_1.
InterPro; IPR036612; KH_dom_type_1_sf.
Pfam; PF09005; DUF1897; 2.
Pfam; PF00013; KH_1; 4.
SMART; SM00322; KH; 4.
SUPFAM; SSF54791; SSF54791; 4.
PROSITE; PS50084; KH_TYPE_1; 4.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Direct protein sequencing; DNA-binding; Isopeptide bond; Methylation;
mRNA processing; mRNA splicing; mRNA transport; Nucleus;
Phosphoprotein; Reference proteome; Repeat; RNA-binding;
Transcription; Transcription regulation; Transport; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
CHAIN 2 711 Far upstream element-binding protein 2.
/FTId=PRO_0000050137.
DOMAIN 144 208 KH 1. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
DOMAIN 233 299 KH 2. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
DOMAIN 322 386 KH 3. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
DOMAIN 424 491 KH 4. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
REPEAT 571 582 1.
REPEAT 617 628 2.
REPEAT 643 654 3.
REPEAT 673 684 4.
REGION 571 684 4 X 12 AA imperfect repeats.
COMPBIAS 7 67 Gly/Pro-rich.
COMPBIAS 68 496 Gly-rich.
COMPBIAS 498 612 Ala/Gly/Pro-rich.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
MOD_RES 40 40 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q3U0V1}.
MOD_RES 87 87 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q3U0V1}.
MOD_RES 99 99 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 100 100 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 125 125 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 129 129 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 131 131 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 181 181 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 184 184 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 193 193 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:19198587}.
MOD_RES 274 274 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 411 411 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 413 413 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 415 415 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 442 442 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 480 480 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
CROSSLNK 121 121 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate. {ECO:0000244|PubMed:25114211}.
CROSSLNK 121 121 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CONFLICT 46 46 G -> C (in Ref. 1; AAB53222 and 4;
AAD29861). {ECO:0000305}.
CONFLICT 96 96 V -> G (in Ref. 5; AAC50892).
{ECO:0000305}.
CONFLICT 406 407 MP -> I (in Ref. 5; AAC50892).
{ECO:0000305}.
CONFLICT 422 422 Missing (in Ref. 5; AAC50892).
{ECO:0000305}.
CONFLICT 487 488 AK -> CR (in Ref. 5; AAC50892).
{ECO:0000305}.
CONFLICT 694 696 GPG -> VP (in Ref. 5; AAC50892).
{ECO:0000305}.
STRAND 132 134 {ECO:0000244|PDB:2OPU}.
HELIX 141 144 {ECO:0000244|PDB:2OPU}.
STRAND 146 151 {ECO:0000244|PDB:2OPU}.
HELIX 153 159 {ECO:0000244|PDB:2OPU}.
TURN 161 163 {ECO:0000244|PDB:2OPU}.
HELIX 165 174 {ECO:0000244|PDB:2OPU}.
STRAND 179 183 {ECO:0000244|PDB:2OPU}.
STRAND 188 194 {ECO:0000244|PDB:2OPU}.
HELIX 198 216 {ECO:0000244|PDB:2OPU}.
STRAND 234 240 {ECO:0000244|PDB:2JVZ}.
TURN 242 244 {ECO:0000244|PDB:2OPV}.
TURN 245 249 {ECO:0000244|PDB:2JVZ}.
TURN 251 253 {ECO:0000244|PDB:2JVZ}.
HELIX 254 261 {ECO:0000244|PDB:2JVZ}.
STRAND 265 269 {ECO:0000244|PDB:2JVZ}.
STRAND 271 273 {ECO:0000244|PDB:2OPV}.
STRAND 275 279 {ECO:0000244|PDB:2JVZ}.
STRAND 281 287 {ECO:0000244|PDB:2JVZ}.
HELIX 289 302 {ECO:0000244|PDB:2JVZ}.
STRAND 306 308 {ECO:0000244|PDB:2JVZ}.
TURN 317 319 {ECO:0000244|PDB:4B8T}.
STRAND 325 330 {ECO:0000244|PDB:2HH3}.
TURN 331 333 {ECO:0000244|PDB:2HH3}.
HELIX 334 338 {ECO:0000244|PDB:2HH3}.
STRAND 340 342 {ECO:0000244|PDB:2JVZ}.
HELIX 343 352 {ECO:0000244|PDB:2HH3}.
STRAND 355 358 {ECO:0000244|PDB:2HH3}.
STRAND 363 375 {ECO:0000244|PDB:2HH3}.
HELIX 376 393 {ECO:0000244|PDB:2HH3}.
STRAND 400 405 {ECO:0000244|PDB:4B8T}.
TURN 413 415 {ECO:0000244|PDB:4B8T}.
STRAND 427 432 {ECO:0000244|PDB:2HH2}.
HELIX 433 435 {ECO:0000244|PDB:2HH2}.
TURN 436 438 {ECO:0000244|PDB:2HH2}.
TURN 441 444 {ECO:0000244|PDB:2HH2}.
HELIX 446 453 {ECO:0000244|PDB:2HH2}.
STRAND 454 460 {ECO:0000244|PDB:2HH2}.
STRAND 472 479 {ECO:0000244|PDB:2HH2}.
HELIX 481 494 {ECO:0000244|PDB:2HH2}.
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


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