YBOX1_HUMAN
ID YBOX1_HUMAN Reviewed; 324 AA.
AC P67809; P16990; P16991; Q14972; Q15325; Q5FVF0;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Y-box-binding protein 1 {ECO:0000303|PubMed:10817758};
DE Short=YB-1 {ECO:0000303|PubMed:10817758};
DE AltName: Full=CCAAT-binding transcription factor I subunit A;
DE Short=CBF-A;
DE AltName: Full=DNA-binding protein B {ECO:0000250|UniProtKB:P62960};
DE Short=DBPB {ECO:0000250|UniProtKB:P62960};
DE AltName: Full=Enhancer factor I subunit A {ECO:0000250|UniProtKB:P62961};
DE Short=EFI-A {ECO:0000250|UniProtKB:P62961};
DE AltName: Full=Nuclease-sensitive element-binding protein 1 {ECO:0000303|PubMed:1891370};
DE AltName: Full=Y-box transcription factor;
GN Name=YBX1 {ECO:0000312|HGNC:HGNC:8014};
GN Synonyms=NSEP1 {ECO:0000303|PubMed:1891370},
GN YB1 {ECO:0000303|PubMed:10817758};
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].
RX PubMed=2977358; DOI=10.1016/0378-1119(88)90514-8;
RA Sakura H., Maekawa T., Imamoto F., Yasuda K., Ishii S.;
RT "Two human genes isolated by a novel method encode DNA-binding proteins
RT containing a common region of homology.";
RL Gene 73:499-507(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3174636; DOI=10.1073/pnas.85.19.7322;
RA Didier D.K., Schiffenbauer J., Woulfe S.L., Zacheis M., Schwartz B.D.;
RT "Characterization of the cDNA encoding a protein binding to the major
RT histocompatibility complex class II Y box.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:7322-7326(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1891370; DOI=10.1093/nar/19.17.4771;
RA Kolluri R., Kinniburgh A.J.;
RT "Full length cDNA sequence encoding a nuclease-sensitive element DNA
RT binding protein.";
RL Nucleic Acids Res. 19:4771-4771(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Bone marrow;
RX PubMed=8188694; DOI=10.1016/s0021-9258(17)36764-9;
RA Horwitz E.M., Maloney K.A., Ley T.J.;
RT "A human protein containing a 'cold shock' domain binds specifically to H-
RT DNA upstream from the human gamma-globin genes.";
RL J. Biol. Chem. 269:14130-14139(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Adrenal cortex, Eye, Kidney, Muscle, Placenta, Skin, Testis, and
RC Uterus;
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 [6]
RP PROTEIN SEQUENCE OF 2-53; 70-93; 102-137; 157-185; 205-231; 257-279 AND
RP 305-324, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2,
RP PHOSPHORYLATION AT SER-165, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V.;
RL Submitted (JAN-2010) to UniProtKB.
RN [7]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND SUBUNIT.
RX PubMed=10817758;
RA Chen C.-Y., Gherzi R., Andersen J.S., Gaietta G., Juerchott K.,
RA Royer H.-D., Mann M., Karin M.;
RT "Nucleolin and YB-1 are required for JNK-mediated interleukin-2 mRNA
RT stabilization during T-cell activation.";
RL Genes Dev. 14:1236-1248(2000).
RN [8]
RP FUNCTION.
RX PubMed=11698476; DOI=10.4049/jimmunol.167.10.5970;
RA Capowski E.E., Esnault S., Bhattacharya S., Malter J.S.;
RT "Y box-binding factor promotes eosinophil survival by stabilizing
RT granulocyte-macrophage colony-stimulating factor mRNA.";
RL J. Immunol. 167:5970-5976(2001).
RN [9]
RP FUNCTION, INTERACTION WITH SFRS9, AND SUBCELLULAR LOCATION.
RX PubMed=12604611; DOI=10.1074/jbc.m212518200;
RA Raffetseder U., Frye B., Rauen T., Juerchott K., Royer H.-D., Jansen P.L.,
RA Mertens P.R.;
RT "Splicing factor SRp30c interaction with Y-box protein-1 confers nuclear
RT YB-1 shuttling and alternative splice site selection.";
RL J. Biol. Chem. 278:18241-18248(2003).
RN [10]
RP INTERACTION WITH SFRS12.
RX PubMed=14559993; DOI=10.1128/mcb.23.21.7437-7447.2003;
RA Li J., Hawkins I.C., Harvey C.D., Jennings J.L., Link A.J., Patton J.G.;
RT "Regulation of alternative splicing by SRrp86 and its interacting
RT proteins.";
RL Mol. Cell. Biol. 23:7437-7447(2003).
RN [11]
RP INTERACTION WITH ANKRD2.
RX PubMed=15136035; DOI=10.1016/j.jmb.2004.03.071;
RA Kojic S., Medeot E., Guccione E., Krmac H., Zara I., Martinelli V.,
RA Valle G., Faulkner G.;
RT "The Ankrd2 protein, a link between the sarcomere and the nucleus in
RT skeletal muscle.";
RL J. Mol. Biol. 339:313-325(2004).
RN [12]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND INTERACTION WITH ALYREF/THOC4;
RP NCL; XRCC5; WRN AND MSH2.
RX PubMed=14718551; DOI=10.1093/nar/gkh170;
RA Gaudreault I., Guay D., Lebel M.;
RT "YB-1 promotes strand separation in vitro of duplex DNA containing either
RT mispaired bases or cisplatin modifications, exhibits endonucleolytic
RT activities and binds several DNA repair proteins.";
RL Nucleic Acids Res. 32:316-327(2004).
RN [13]
RP IDENTIFICATION IN A COMPLEX WITH THE U11/U12 SPLICEOSOME, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15146077; DOI=10.1261/rna.7320604;
RA Will C.L., Schneider C., Hossbach M., Urlaub H., Rauhut R., Elbashir S.,
RA Tuschl T., Luehrmann R.;
RT "The human 18S U11/U12 snRNP contains a set of novel proteins not found in
RT the U2-dependent spliceosome.";
RL RNA 10:929-941(2004).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-162, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [15]
RP PHOSPHORYLATION AT SER-102, INTERACTION WITH AKT1, SUBCELLULAR LOCATION,
RP AND MUTAGENESIS OF SER-102.
RX PubMed=15806160; DOI=10.1038/sj.onc.1208590;
RA Sutherland B.W., Kucab J., Wu J., Lee C., Cheang M.C.U., Yorida E.,
RA Turbin D., Dedhar S., Nelson C., Pollak M., Leighton Grimes H., Miller K.,
RA Badve S., Huntsman D., Blake-Gilks C., Chen M., Pallen C.J., Dunn S.E.;
RT "Akt phosphorylates the Y-box binding protein 1 at Ser102 located in the
RT cold shock domain and affects the anchorage-independent growth of breast
RT cancer cells.";
RL Oncogene 24:4281-4292(2005).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174 AND SER-176, AND
RP IDENTIFICATION BY 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 [17]
RP IDENTIFICATION BY 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 [18]
RP INTERACTION WITH AGO1 AND AGO2.
RX PubMed=17932509; DOI=10.1038/sj.embor.7401088;
RA Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M.,
RA Urlaub H., Meister G.;
RT "Proteomic and functional analysis of Argonaute-containing mRNA-protein
RT complexes in human cells.";
RL EMBO Rep. 8:1052-1060(2007).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Prostate cancer;
RX PubMed=17487921; DOI=10.1002/elps.200600782;
RA Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
RT "Toward a global characterization of the phosphoproteome in prostate cancer
RT cells: identification of phosphoproteins in the LNCaP cell line.";
RL Electrophoresis 28:2027-2034(2007).
RN [20]
RP IDENTIFICATION IN A MRNP GRANULE COMPLEX, INTERACTION WITH IGF2BP1,
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17289661; DOI=10.1074/mcp.m600346-mcp200;
RA Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R.,
RA Johnsen A.H., Christiansen J., Nielsen F.C.;
RT "Molecular composition of IMP1 ribonucleoprotein granules.";
RL Mol. Cell. Proteomics 6:798-811(2007).
RN [21]
RP INTERACTION WITH RBBP6, AND UBIQUITINATION.
RX PubMed=18851979; DOI=10.1016/j.jmb.2008.09.060;
RA Chibi M., Meyer M., Skepu A., Rees D.J.G., Moolman-Smook J.C., Pugh D.J.;
RT "RBBP6 interacts with multifunctional protein YB-1 through its RING finger
RT domain, leading to ubiquitination and proteosomal degradation of YB-1.";
RL J. Mol. Biol. 384:908-916(2008).
RN [22]
RP INTERACTION WITH MBNL1, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=18335541; DOI=10.1002/jnr.21655;
RA Onishi H., Kino Y., Morita T., Futai E., Sasagawa N., Ishiura S.;
RT "MBNL1 associates with YB-1 in cytoplasmic stress granules.";
RL J. Neurosci. Res. 86:1994-2002(2008).
RN [23]
RP FUNCTION, DNA-BINDING, AND INTERACTION WITH APEX1.
RX PubMed=18809583; DOI=10.1128/mcb.00244-08;
RA Chattopadhyay R., Das S., Maiti A.K., Boldogh I., Xie J., Hazra T.K.,
RA Kohno K., Mitra S., Bhakat K.K.;
RT "Regulatory role of human AP-endonuclease (APE1/Ref-1) in YB-1-mediated
RT activation of the multidrug resistance gene MDR1.";
RL Mol. Cell. Biol. 28:7066-7080(2008).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174 AND SER-176, 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 [25]
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 [26]
RP FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-301 AND LYS-304, AND
RP ACETYLATION AT LYS-301 AND LYS-304.
RX PubMed=19483673; DOI=10.1038/embor.2009.81;
RA Frye B.C., Halfter S., Djudjaj S., Muehlenberg P., Weber S.,
RA Raffetseder U., En-Nia A., Knott H., Baron J.M., Dooley S., Bernhagen J.,
RA Mertens P.R.;
RT "Y-box protein-1 is actively secreted through a non-classical pathway and
RT acts as an extracellular mitogen.";
RL EMBO Rep. 10:783-789(2009).
RN [27]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=19561594; DOI=10.1038/nbt.1550;
RA Ray D., Kazan H., Chan E.T., Pena Castillo L., Chaudhry S., Talukder S.,
RA Blencowe B.J., Morris Q., Hughes T.R.;
RT "Rapid and systematic analysis of the RNA recognition specificities of RNA-
RT binding proteins.";
RL Nat. Biotechnol. 27:667-670(2009).
RN [28]
RP FUNCTION, COMPONENT OF THE CRD-MEDIATED MRNA STABILIZATION COMPLEX,
RP IDENTIFICATION IN A MRNP COMPLEX, SUBCELLULAR LOCATION, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RX PubMed=19029303; DOI=10.1261/rna.1175909;
RA Weidensdorfer D., Stoehr N., Baude A., Lederer M., Koehn M., Schierhorn A.,
RA Buchmeier S., Wahle E., Huettelmaiery S.;
RT "Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic RNPs.";
RL RNA 15:104-115(2009).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102; SER-165; SER-167;
RP SER-174 AND SER-176, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165; SER-167; SER-174 AND
RP SER-176, AND 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 [31]
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 [32]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165; SER-167; SER-174;
RP SER-176 AND SER-314, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [33]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165; SER-174; SER-176 AND
RP SER-314, AND IDENTIFICATION 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 [34]
RP INTERACTION WITH DERA, AND SUBCELLULAR LOCATION.
RX PubMed=25229427; DOI=10.1016/j.bbamcr.2014.09.007;
RA Salleron L., Magistrelli G., Mary C., Fischer N., Bairoch A., Lane L.;
RT "DERA is the human deoxyribose phosphate aldolase and is involved in stress
RT response.";
RL Biochim. Biophys. Acta 1843:2913-2925(2014).
RN [35]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167; SER-174 AND SER-176, AND
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 [36]
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 [37]
RP INTERACTION WITH HDGF.
RX PubMed=26845719; DOI=10.1515/hsz-2015-0273;
RA Nuesse J., Mirastschijski U., Waespy M., Oetjen J., Brandes N., Rebello O.,
RA Paroni F., Kelm S., Dietz F.;
RT "Two new isoforms of the human hepatoma-derived growth factor interact with
RT components of the cytoskeleton.";
RL Biol. Chem. 397:417-436(2016).
RN [38]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=27559612; DOI=10.7554/elife.19276;
RA Shurtleff M.J., Temoche-Diaz M.M., Karfilis K.V., Ri S., Schekman R.;
RT "Y-box protein 1 is required to sort microRNAs into exosomes in cells and
RT in a cell-free reaction.";
RL Elife 5:0-0(2016).
RN [39]
RP FUNCTION, SUBCELLULAR LOCATION, AND RNA-BINDING.
RX PubMed=28341602; DOI=10.1016/j.bbapap.2017.03.010;
RA Kossinova O.A., Gopanenko A.V., Tamkovich S.N., Krasheninina O.A.,
RA Tupikin A.E., Kiseleva E., Yanshina D.D., Malygin A.A., Ven'yaminova A.G.,
RA Kabilov M.R., Karpova G.G.;
RT "Cytosolic YB-1 and NSUN2 are the only proteins recognizing specific motifs
RT present in mRNAs enriched in exosomes.";
RL Biochim. Biophys. Acta 1865:664-673(2017).
RN [40]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-26, 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 [41]
RP FUNCTION.
RX PubMed=29073095; DOI=10.1073/pnas.1712108114;
RA Shurtleff M.J., Yao J., Qin Y., Nottingham R.M., Temoche-Diaz M.M.,
RA Schekman R., Lambowitz A.M.;
RT "Broad role for YBX1 in defining the small noncoding RNA composition of
RT exosomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E8987-E8987(2017).
RN [42]
RP FUNCTION.
RX PubMed=29712925; DOI=10.1038/s41467-018-04092-0;
RA Kwon E., Todorova K., Wang J., Horos R., Lee K.K., Neel V.A., Negri G.L.,
RA Sorensen P.H., Lee S.W., Hentze M.W., Mandinova A.;
RT "The RNA-binding protein YBX1 regulates epidermal progenitors at a
RT posttranscriptional level.";
RL Nat. Commun. 9:1734-1734(2018).
RN [43]
RP STRUCTURE BY NMR OF 52-129, AND INTERACTION WITH SS-DNA.
RX PubMed=11851341; DOI=10.1006/jmbi.2001.5334;
RA Kloks C.P.A.M., Spronk C.A.E.M., Lasonder E., Hoffmann A., Vuister G.W.,
RA Grzesiek S., Hilbers C.W.;
RT "The solution structure and DNA-binding properties of the cold-shock domain
RT of the human Y-box protein YB-1.";
RL J. Mol. Biol. 316:317-326(2002).
RN [44] {ECO:0007744|PDB:6A6L}
RP X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) OF 50-130 IN COMPLEX WITH METHYLATED
RP RNA, FUNCTION, INTERACTION WITH ELAVL1, DOMAIN, AND MUTAGENESIS OF TRP-65.
RX PubMed=31358969; DOI=10.1038/s41556-019-0361-y;
RA Chen X., Li A., Sun B.F., Yang Y., Han Y.N., Yuan X., Chen R.X., Wei W.S.,
RA Liu Y., Gao C.C., Chen Y.S., Zhang M., Ma X.D., Liu Z.W., Luo J.H., Lyu C.,
RA Wang H.L., Ma J., Zhao Y.L., Zhou F.J., Huang Y., Xie D., Yang Y.G.;
RT "5-methylcytosine promotes pathogenesis of bladder cancer through
RT stabilizing mRNAs.";
RL Nat. Cell Biol. 21:978-990(2019).
CC -!- FUNCTION: DNA- and RNA-binding protein involved in various processes,
CC such as translational repression, RNA stabilization, mRNA splicing, DNA
CC repair and transcription regulation (PubMed:8188694, PubMed:10817758,
CC PubMed:11698476, PubMed:14718551, PubMed:18809583, PubMed:31358969).
CC Predominantly acts as a RNA-binding protein: binds preferentially to
CC the 5'-[CU]CUGCG-3' RNA motif and specifically recognizes mRNA
CC transcripts modified by C5-methylcytosine (m5C) (PubMed:19561594,
CC PubMed:31358969). Promotes mRNA stabilization: acts by binding to m5C-
CC containing mRNAs and recruiting the mRNA stability maintainer ELAVL1,
CC thereby preventing mRNA decay (PubMed:10817758, PubMed:11698476,
CC PubMed:31358969). Component of the CRD-mediated complex that promotes
CC MYC mRNA stability (PubMed:19029303). Contributes to the regulation of
CC translation by modulating the interaction between the mRNA and
CC eukaryotic initiation factors (By similarity). Plays a key role in RNA
CC composition of extracellular exosomes by defining the sorting of small
CC non-coding RNAs, such as tRNAs, Y RNAs, Vault RNAs and miRNAs
CC (PubMed:27559612, PubMed:29073095). Probably sorts RNAs in exosomes by
CC recognizing and binding C5-methylcytosine (m5C)-containing RNAs
CC (PubMed:28341602, PubMed:29073095). Acts as a key effector of epidermal
CC progenitors by preventing epidermal progenitor senescence: acts by
CC regulating the translation of a senescence-associated subset of
CC cytokine mRNAs, possibly by binding to m5C-containing mRNAs
CC (PubMed:29712925). Also involved in pre-mRNA alternative splicing
CC regulation: binds to splice sites in pre-mRNA and regulates splice site
CC selection (PubMed:12604611). Also able to bind DNA: regulates
CC transcription of the multidrug resistance gene MDR1 is enhanced in
CC presence of the APEX1 acetylated form at 'Lys-6' and 'Lys-7'
CC (PubMed:18809583). Binds to promoters that contain a Y-box (5'-
CC CTGATTGGCCAA-3'), such as MDR1 and HLA class II genes (PubMed:8188694,
CC PubMed:18809583). Promotes separation of DNA strands that contain
CC mismatches or are modified by cisplatin (PubMed:14718551). Has
CC endonucleolytic activity and can introduce nicks or breaks into double-
CC stranded DNA, suggesting a role in DNA repair (PubMed:14718551). The
CC secreted form acts as an extracellular mitogen and stimulates cell
CC migration and proliferation (PubMed:19483673).
CC {ECO:0000250|UniProtKB:Q28618, ECO:0000269|PubMed:10817758,
CC ECO:0000269|PubMed:11698476, ECO:0000269|PubMed:12604611,
CC ECO:0000269|PubMed:14718551, ECO:0000269|PubMed:18809583,
CC ECO:0000269|PubMed:19029303, ECO:0000269|PubMed:19483673,
CC ECO:0000269|PubMed:19561594, ECO:0000269|PubMed:27559612,
CC ECO:0000269|PubMed:28341602, ECO:0000269|PubMed:29073095,
CC ECO:0000269|PubMed:29712925, ECO:0000269|PubMed:31358969,
CC ECO:0000269|PubMed:8188694}.
CC -!- SUBUNIT: Homodimer in the presence of ATP (PubMed:10817758,
CC PubMed:11851341). Component of the coding region determinant (CRD)-
CC mediated complex, composed of DHX9, HNRNPU, IGF2BP1, SYNCRIP and YBX1
CC (PubMed:19029303). Identified in a IGF2BP1-dependent mRNP granule
CC complex containing untranslated mRNAs (PubMed:17289661). Component of
CC the U11/U12 snRNPs that are part of the U12-type spliceosome
CC (PubMed:15146077). Identified in a histone pre-mRNA complex, at least
CC composed of ERI1, LSM11, SLBP, SNRPB, SYNCRIP and YBX1 (By similarity).
CC Interacts with IGF2BP1 and RBBP6 (PubMed:17289661, PubMed:18851979).
CC Component of cytoplasmic messenger ribonucleoprotein particles (mRNPs)
CC (PubMed:19029303). Interacts with AKT1, MBNL1, SFRS9, SFRS12,
CC ALYREF/THOC4, MSH2, XRCC5, WRN and NCL (PubMed:12604611,
CC PubMed:14559993, PubMed:14718551, PubMed:15806160, PubMed:18335541).
CC Interacts (via C-terminus) with APEX1 (via N-terminus); the interaction
CC is increased with APEX1 acetylated at 'Lys-6' and 'Lys-7'
CC (PubMed:18809583). Interacts with AGO1 and AGO2 (PubMed:17932509).
CC Interacts with ANKRD2 (PubMed:15136035). Interacts with DERA
CC (PubMed:25229427). Interacts with FMR1; this interaction occurs in
CC association with polyribosome (By similarity). Interacts with ZBTB7B
CC (By similarity). Interacts with HDGF (isoform 1) (PubMed:26845719).
CC Interacts with ELAVL1; leading to ELAVL1 recruitment on C5-
CC methylcytosine (m5C)-containing mRNAs and subsequent mRNA stability
CC (PubMed:31358969). {ECO:0000250|UniProtKB:P62960,
CC ECO:0000269|PubMed:10817758, ECO:0000269|PubMed:11851341,
CC ECO:0000269|PubMed:12604611, ECO:0000269|PubMed:14559993,
CC ECO:0000269|PubMed:14718551, ECO:0000269|PubMed:15136035,
CC ECO:0000269|PubMed:15146077, ECO:0000269|PubMed:15806160,
CC ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:17932509,
CC ECO:0000269|PubMed:18335541, ECO:0000269|PubMed:18809583,
CC ECO:0000269|PubMed:18851979, ECO:0000269|PubMed:19029303,
CC ECO:0000269|PubMed:25229427, ECO:0000269|PubMed:26845719,
CC ECO:0000269|PubMed:31358969}.
CC -!- INTERACTION:
CC P67809; Q07021: C1QBP; NbExp=7; IntAct=EBI-354065, EBI-347528;
CC P67809; Q13616: CUL1; NbExp=2; IntAct=EBI-354065, EBI-359390;
CC P67809; Q08211: DHX9; NbExp=10; IntAct=EBI-354065, EBI-352022;
CC P67809; Q09472: EP300; NbExp=2; IntAct=EBI-354065, EBI-447295;
CC P67809; Q7Z6M2: FBXO33; NbExp=6; IntAct=EBI-354065, EBI-8555452;
CC P67809; Q14103-4: HNRNPD; NbExp=3; IntAct=EBI-354065, EBI-432545;
CC P67809; P62310: LSM3; NbExp=2; IntAct=EBI-354065, EBI-348239;
CC P67809; Q99697: PITX2; NbExp=3; IntAct=EBI-354065, EBI-1175211;
CC P67809; O15355: PPM1G; NbExp=2; IntAct=EBI-354065, EBI-725702;
CC P67809; Q13148: TARDBP; NbExp=6; IntAct=EBI-354065, EBI-372899;
CC P67809; P13693: TPT1; NbExp=4; IntAct=EBI-354065, EBI-1783169;
CC P67809; Q08705: CTCF; Xeno; NbExp=2; IntAct=EBI-354065, EBI-932806;
CC P67809; PRO_0000038050 [P19712]; Xeno; NbExp=4; IntAct=EBI-354065, EBI-10901281;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12604611,
CC ECO:0000269|PubMed:14718551, ECO:0000269|PubMed:15806160}. Nucleus
CC {ECO:0000269|PubMed:12604611, ECO:0000269|PubMed:14718551,
CC ECO:0000269|PubMed:15806160}. Cytoplasmic granule
CC {ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:18335541,
CC ECO:0000269|PubMed:19029303, ECO:0000269|PubMed:25229427}. Secreted
CC {ECO:0000269|PubMed:19483673}. Secreted, extracellular exosome
CC {ECO:0000269|PubMed:27559612, ECO:0000269|PubMed:28341602}.
CC Note=Predominantly cytoplasmic in proliferating cells
CC (PubMed:12604611). Cytotoxic stress and DNA damage enhance
CC translocation to the nucleus (PubMed:14718551). Localized in
CC cytoplasmic mRNP granules containing untranslated mRNAs
CC (PubMed:25229427). Shuttles between nucleus and cytoplasm
CC (PubMed:25229427). Localized with DDX1, MBNL1 and TIAL1 in stress
CC granules upon stress (PubMed:18335541). Secreted by mesangial and
CC monocytic cells after inflammatory challenges (PubMed:19483673).
CC {ECO:0000269|PubMed:12604611, ECO:0000269|PubMed:14718551,
CC ECO:0000269|PubMed:18335541, ECO:0000269|PubMed:19483673,
CC ECO:0000269|PubMed:25229427}.
CC -!- DOMAIN: In the CSD domain, Trp-65 specifically recognizes C5-
CC methylcytosine (m5C) modification through its indole ring.
CC {ECO:0000269|PubMed:31358969}.
CC -!- PTM: Ubiquitinated by RBBP6; leading to a decrease of YBX1
CC transcactivational ability. {ECO:0000269|PubMed:18851979}.
CC -!- PTM: In the absence of phosphorylation the protein is retained in the
CC cytoplasm. {ECO:0000269|PubMed:15806160, ECO:0000269|Ref.6}.
CC -!- PTM: Cleaved by a 20S proteasomal protease in response to agents that
CC damage DNA. Cleavage takes place in the absence of ubiquitination and
CC ATP. The resulting N-terminal fragment accumulates in the nucleus (By
CC similarity). {ECO:0000250|UniProtKB:Q28618}.
CC -!- SIMILARITY: Belongs to the YBX1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA35750.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAA59949.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAA61308.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/YBX1ID46554ch1p34.html";
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DR EMBL; M24070; AAA35750.1; ALT_INIT; mRNA.
DR EMBL; J03827; AAA61308.1; ALT_FRAME; mRNA.
DR EMBL; M83234; AAA59949.1; ALT_FRAME; mRNA.
DR EMBL; L28809; AAA20871.1; -; mRNA.
DR EMBL; BC002411; AAH02411.1; -; mRNA.
DR EMBL; BC010430; AAH10430.1; -; mRNA.
DR EMBL; BC015208; AAH15208.1; -; mRNA.
DR EMBL; BC038384; AAH38384.1; -; mRNA.
DR EMBL; BC065571; AAH65571.1; -; mRNA.
DR EMBL; BC070084; AAH70084.1; -; mRNA.
DR EMBL; BC071708; AAH71708.1; -; mRNA.
DR EMBL; BC090038; AAH90038.1; -; mRNA.
DR EMBL; BC098435; AAH98435.1; -; mRNA.
DR EMBL; BC106045; AAI06046.1; -; mRNA.
DR CCDS; CCDS470.1; -.
DR PIR; I39382; I39382.
DR PIR; S34426; S34426.
DR RefSeq; NP_004550.2; NM_004559.4.
DR PDB; 1H95; NMR; -; A=52-129.
DR PDB; 5YTS; X-ray; 1.77 A; A=50-130.
DR PDB; 5YTT; X-ray; 1.60 A; A=50-130.
DR PDB; 5YTV; X-ray; 1.70 A; A=50-130.
DR PDB; 5YTX; X-ray; 1.55 A; A=50-130.
DR PDB; 6A6L; X-ray; 1.78 A; A=50-130.
DR PDB; 6KTC; X-ray; 2.01 A; A=52-129.
DR PDB; 6KUG; X-ray; 1.40 A; A=52-129.
DR PDB; 6LMR; NMR; -; A=44-140.
DR PDB; 6LMS; NMR; -; A=51-140.
DR PDBsum; 1H95; -.
DR PDBsum; 5YTS; -.
DR PDBsum; 5YTT; -.
DR PDBsum; 5YTV; -.
DR PDBsum; 5YTX; -.
DR PDBsum; 6A6L; -.
DR PDBsum; 6KTC; -.
DR PDBsum; 6KUG; -.
DR PDBsum; 6LMR; -.
DR PDBsum; 6LMS; -.
DR AlphaFoldDB; P67809; -.
DR SMR; P67809; -.
DR BioGRID; 110959; 639.
DR ComplexPortal; CPX-1080; CRD-mediated mRNA stability complex.
DR CORUM; P67809; -.
DR DIP; DIP-29405N; -.
DR IntAct; P67809; 381.
DR MINT; P67809; -.
DR STRING; 9606.ENSP00000361626; -.
DR ChEMBL; CHEMBL4296006; -.
DR GlyGen; P67809; 4 sites, 1 O-linked glycan (4 sites).
DR iPTMnet; P67809; -.
DR MetOSite; P67809; -.
DR PhosphoSitePlus; P67809; -.
DR SwissPalm; P67809; -.
DR BioMuta; YBX1; -.
DR DMDM; 54040031; -.
DR EPD; P67809; -.
DR jPOST; P67809; -.
DR MassIVE; P67809; -.
DR MaxQB; P67809; -.
DR PaxDb; P67809; -.
DR PeptideAtlas; P67809; -.
DR PRIDE; P67809; -.
DR ProteomicsDB; 57522; -.
DR TopDownProteomics; P67809; -.
DR Antibodypedia; 32231; 596 antibodies from 36 providers.
DR DNASU; 4904; -.
DR Ensembl; ENST00000321358.12; ENSP00000361626.3; ENSG00000065978.19.
DR GeneID; 4904; -.
DR KEGG; hsa:4904; -.
DR MANE-Select; ENST00000321358.12; ENSP00000361626.3; NM_004559.5; NP_004550.2.
DR UCSC; uc001chs.4; human.
DR CTD; 4904; -.
DR DisGeNET; 4904; -.
DR GeneCards; YBX1; -.
DR HGNC; HGNC:8014; YBX1.
DR HPA; ENSG00000065978; Tissue enhanced (skeletal).
DR MIM; 154030; gene.
DR neXtProt; NX_P67809; -.
DR OpenTargets; ENSG00000065978; -.
DR PharmGKB; PA31791; -.
DR VEuPathDB; HostDB:ENSG00000065978; -.
DR eggNOG; KOG3070; Eukaryota.
DR GeneTree; ENSGT00940000153341; -.
DR HOGENOM; CLU_063071_1_0_1; -.
DR InParanoid; P67809; -.
DR OMA; GDKKVIX; -.
DR OrthoDB; 1431946at2759; -.
DR PhylomeDB; P67809; -.
DR TreeFam; TF317306; -.
DR PathwayCommons; P67809; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-HSA-72165; mRNA Splicing - Minor Pathway.
DR Reactome; R-HSA-9017802; Noncanonical activation of NOTCH3.
DR SignaLink; P67809; -.
DR SIGNOR; P67809; -.
DR BioGRID-ORCS; 4904; 720 hits in 1070 CRISPR screens.
DR ChiTaRS; YBX1; human.
DR EvolutionaryTrace; P67809; -.
DR GeneWiki; Y_box_binding_protein_1; -.
DR GenomeRNAi; 4904; -.
DR Pharos; P67809; Tbio.
DR PRO; PR:P67809; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P67809; protein.
DR Bgee; ENSG00000065978; Expressed in left testis and 103 other tissues.
DR ExpressionAtlas; P67809; baseline and differential.
DR Genevisible; P67809; HS.
DR GO; GO:0070937; C:CRD-mediated mRNA stability complex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:AgBase.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0071204; C:histone pre-mRNA 3'end processing complex; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:1990124; C:messenger ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0005689; C:U12-type spliceosomal complex; IDA:UniProtKB.
DR GO; GO:0062153; F:C5-methylcytidine-containing RNA binding; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; TAS:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; TAS:ProtInc.
DR GO; GO:0051020; F:GTPase binding; IPI:UniProtKB.
DR GO; GO:0035198; F:miRNA binding; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IEA:Ensembl.
DR GO; GO:0003676; F:nucleic acid binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:Ensembl.
DR GO; GO:0098761; P:cellular response to interleukin-7; IEA:Ensembl.
DR GO; GO:0070934; P:CRD-mediated mRNA stabilization; IDA:ComplexPortal.
DR GO; GO:0048598; P:embryonic morphogenesis; ISS:UniProtKB.
DR GO; GO:0008544; P:epidermis development; ISS:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:1990428; P:miRNA transport; IDA:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0048255; P:mRNA stabilization; IDA:UniProtKB.
DR GO; GO:2000773; P:negative regulation of cellular senescence; ISS:UniProtKB.
DR GO; GO:1900152; P:negative regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IDA:ComplexPortal.
DR GO; GO:0051154; P:negative regulation of striated muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0017148; P:negative regulation of translation; ISS:UniProtKB.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR GO; GO:2000767; P:positive regulation of cytoplasmic translation; IDA:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:1903608; P:protein localization to cytoplasmic stress granule; IMP:AgBase.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR GO; GO:0050658; P:RNA transport; IMP:UniProtKB.
DR GO; GO:0051031; P:tRNA transport; IMP:UniProtKB.
DR CDD; cd04458; CSP_CDS; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR011129; CSD.
DR InterPro; IPR019844; CSD_1.
DR InterPro; IPR002059; CSP_DNA-bd.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR Pfam; PF00313; CSD; 1.
DR PRINTS; PR00050; COLDSHOCK.
DR SMART; SM00357; CSP; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR PROSITE; PS00352; CSD_1; 1.
DR PROSITE; PS51857; CSD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Cytoplasm; Direct protein sequencing;
KW DNA-binding; Isopeptide bond; Mitogen; mRNA processing; mRNA splicing;
KW Nucleus; Phosphoprotein; Reference proteome; Repressor; RNA-binding;
KW Secreted; Transcription; Transcription regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330"
FT CHAIN 2..324
FT /note="Y-box-binding protein 1"
FT /id="PRO_0000100219"
FT DOMAIN 61..125
FT /note="CSD"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 15..71
FT /note="Interaction with ss-DNA"
FT /evidence="ECO:0000269|PubMed:11851341"
FT REGION 65..70
FT /note="C5-methylcytosine binding"
FT /evidence="ECO:0000269|PubMed:31358969,
FT ECO:0007744|PDB:6A6L"
FT REGION 120..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..269
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 65
FT /note="Important for C5-methylcytosine-recognition"
FT /evidence="ECO:0000269|PubMed:31358969"
FT SITE 219..220
FT /note="Cleavage; by 20S proteasomal protease"
FT /evidence="ECO:0000250|UniProtKB:Q28618"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330"
FT MOD_RES 102
FT /note="Phosphoserine; by PKB/AKT1"
FT /evidence="ECO:0000269|PubMed:15806160,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 162
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 301
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:19483673"
FT MOD_RES 304
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:19483673"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 26
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 137
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:18851979"
FT MUTAGEN 65
FT /note="W->A: Abolished binding to C5-methylcytosine (m5C)-
FT containing mRNAs."
FT /evidence="ECO:0000269|PubMed:31358969"
FT MUTAGEN 65
FT /note="W->F: Decreased binding to C5-methylcytosine (m5C)-
FT containing mRNAs. Decreased ability to discriminate between
FT m5C-containing and unmethylated mRNAs."
FT /evidence="ECO:0000269|PubMed:31358969"
FT MUTAGEN 102
FT /note="S->A: Loss of phosphorylation by PKB/AKT1. Inhibits
FT translocation to the nucleus and tumor cell growth."
FT /evidence="ECO:0000269|PubMed:15806160"
FT MUTAGEN 301
FT /note="K->A: Abrogates unconventional secretion."
FT /evidence="ECO:0000269|PubMed:19483673"
FT MUTAGEN 304
FT /note="K->A: Abrogates unconventional secretion."
FT /evidence="ECO:0000269|PubMed:19483673"
FT CONFLICT 120
FT /note="A -> E (in Ref. 2; AAA61308)"
FT /evidence="ECO:0000305"
FT STRAND 54..67
FT /evidence="ECO:0007829|PDB:6KUG"
FT TURN 68..71
FT /evidence="ECO:0007829|PDB:6KUG"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:6KUG"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:6KUG"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:6KUG"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:6KUG"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:6LMS"
FT STRAND 108..116
FT /evidence="ECO:0007829|PDB:6KUG"
FT STRAND 119..126
FT /evidence="ECO:0007829|PDB:6KUG"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:6LMR"
SQ SEQUENCE 324 AA; 35924 MW; DF0114BF974AEDB8 CRC64;
MSSEAETQQP PAAPPAAPAL SAADTKPGTT GSGAGSGGPG GLTSAAPAGG DKKVIATKVL
GTVKWFNVRN GYGFINRNDT KEDVFVHQTA IKKNNPRKYL RSVGDGETVE FDVVEGEKGA
EAANVTGPGG VPVQGSKYAA DRNHYRRYPR RRGPPRNYQQ NYQNSESGEK NEGSESAPEG
QAQQRRPYRR RRFPPYYMRR PYGRRPQYSN PPVQGEVMEG ADNQGAGEQG RPVRQNMYRG
YRPRFRRGPP RQRQPREDGN EEDKENQGDE TQGQQPPQRR YRRNFNYRRR RPENPKPQDG
KETKAADPPA ENSSAPEAEQ GGAE
