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 04-NOV-2026, entry version 210. 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}, YB1 GN {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, RC and 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; DOI=10.1101/gad.14.10.1236; 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 IN COMPLEX WITH METHYLATED RNA, FUNCTION, INTERACTION RP 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:10817758, PubMed:11698476, CC PubMed:14718551, PubMed:18809583, PubMed:31358969, PubMed:8188694). 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). Binds to TSC22D1 transcripts, thereby CC inhibiting their translation and negatively regulating TGF-beta- CC mediated transcription of COL1A2 (By similarity). Also able to bind CC DNA: regulates transcription of the multidrug resistance gene MDR1 is CC enhanced in presence of the APEX1 acetylated form at 'Lys-6' and 'Lys- CC 7' (PubMed:18809583). Binds to promoters that contain a Y-box (5'- CC CTGATTGGCCAA-3'), such as MDR1 and HLA class II genes (PubMed:18809583, CC PubMed:8188694). 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:P62960, ECO:0000250|UniProtKB:Q28618, CC ECO:0000269|PubMed:10817758, ECO:0000269|PubMed:11698476, CC ECO:0000269|PubMed:12604611, ECO:0000269|PubMed:14718551, CC ECO:0000269|PubMed:18809583, ECO:0000269|PubMed:19029303, CC ECO:0000269|PubMed:19483673, ECO:0000269|PubMed:19561594, CC ECO:0000269|PubMed:27559612, ECO:0000269|PubMed:28341602, CC ECO:0000269|PubMed:29073095, ECO:0000269|PubMed:29712925, CC ECO:0000269|PubMed:31358969, 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). Interacts with PURB (By similarity). CC {ECO:0000250|UniProtKB:P62960, ECO:0000269|PubMed:10817758, CC ECO:0000269|PubMed:11851341, ECO:0000269|PubMed:12604611, CC ECO:0000269|PubMed:14559993, ECO:0000269|PubMed:14718551, CC ECO:0000269|PubMed:15136035, ECO:0000269|PubMed:15146077, CC ECO:0000269|PubMed:15806160, ECO:0000269|PubMed:17289661, CC ECO:0000269|PubMed:17932509, ECO:0000269|PubMed:18335541, CC ECO:0000269|PubMed:18809583, ECO:0000269|PubMed:18851979, CC ECO:0000269|PubMed:19029303, ECO:0000269|PubMed:25229427, CC ECO:0000269|PubMed:26845719, ECO:0000269|PubMed:31358969}. CC -!- INTERACTION: CC P67809; Q07021: C1QBP; NbExp=13; IntAct=EBI-354065, EBI-347528; CC P67809; Q13616: CUL1; NbExp=2; IntAct=EBI-354065, EBI-359390; CC P67809; Q08211: DHX9; NbExp=11; 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}. Cytoplasm, CC P-body {ECO:0000250|UniProtKB:P62960}. Note=Predominantly cytoplasmic CC in proliferating cells (PubMed:12604611). Cytotoxic stress and DNA CC damage enhance translocation to the nucleus (PubMed:14718551). CC Localized in 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 transactivational ability. {ECO:0000269|PubMed:18851979}. CC -!- PTM: Phosphorylated; increased by TGFB1 treatment (Ref.6). CC Phosphorylation by PKB/AKT1 reduces interaction with cytoplasmic mRNA CC (By similarity). In the absence of phosphorylation the protein is CC retained in the cytoplasm (PubMed:15806160). CC {ECO:0000250|UniProtKB:Q28618, ECO:0000269|PubMed:15806160, CC 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="https://atlasgeneticsoncology.org/gene/46554/YBX1"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; 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_004559.5. 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 SMR; P67809; -. DR BioGRID; 110959; 817. DR ComplexPortal; CPX-1080; CRD-mediated mRNA stability complex. DR CORUM; P67809; -. DR DIP; DIP-29405N; -. DR IntAct; P67809; 549. DR MINT; P67809; -. DR STRING; 9606.ENSP00000361626; -. DR NDEx; IQUERY-CP-YBX1; 2 NDEx IQuery Curated Pathways. DR BindingDB; P67809; -. DR ChEMBL; CHEMBL4296006; -. DR MoonProt; P67809; -. DR GlyCosmos; P67809; 8 sites, 2 glycans. DR GlyGen; P67809; 9 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (7 sites). DR iPTMnet; P67809; -. DR PhosphoSitePlus; P67809; -. DR SwissPalm; P67809; -. DR MetOSite; P67809; -. DR BioMuta; YBX1; -. DR DMDM; 54040031; -. DR PaxDb; 9606-ENSP00000361626; -. DR PeptideAtlas; P67809; -. DR ProteomicsDB; 57522; -. DR Pumba; P67809; -. DR TopDownProteomics; P67809; -. DR jPOST; P67809; -. DR MassIVE; P67809; -. DR DNASU; 4904; -. DR Ensembl; ENST00000321358.12; ENSP00000361626.3; ENSG00000065978.20. DR Ensembl; ENST00000886270.1; ENSP00000556329.1; ENSG00000065978.20. DR Ensembl; ENST00000886274.1; ENSP00000556333.1; ENSG00000065978.20. 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 VEuPathDB; HostDB:ENSG00000065978; -. DR GeneCards; YBX1; -. DR HGNC; HGNC:8014; YBX1. DR AGR; HGNC:8014; -. DR HPA; ENSG00000065978; Tissue enhanced (skeletal). DR MalaCards; YBX1; -. DR MIM; 154030; gene. DR OpenTargets; ENSG00000065978; -. DR ClinPGx; PA31791; -. DR eggNOG; KOG3070; Eukaryota. DR GeneTree; ENSGT00940000153341; -. DR HOGENOM; CLU_063071_1_0_1; -. DR InParanoid; P67809; -. DR OMA; AGGDXTK; -. DR OrthoDB; 9538680at2759; -. DR PhylomeDB; P67809; -. DR Reactome; R-HSA-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription. DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway. DR Reactome; R-HSA-72165; mRNA Splicing - Minor Pathway. DR Reactome; R-HSA-72203; Processing of Capped Intron-Containing Pre-mRNA. DR Reactome; R-HSA-877300; Interferon gamma signaling. DR Reactome; R-HSA-9017802; Noncanonical activation of NOTCH3. DR Reactome; R-HSA-9770562; mRNA Polyadenylation. DR Reactome; R-HSA-9918476; Assembly and Release of Dengue Virus Virions. DR Reactome; R-HSA-9918481; Dengue Virus-Host Interactions. DR Reactome; R-HSA-9918487; Dengue Virus Genome Translation and Replication. DR SignaLink; P67809; -. DR SIGNOR; P67809; -. DR ChiTaRS; YBX1; human. DR EvolutionaryTrace; P67809; -. DR Agora; ENSG00000065978; -. DR GeneWiki; Y_box_binding_protein_1; -. DR GenomeRNAi; 4904; -. DR PRO; PR:P67809; -. DR Bgee; ENSG00000065978; Expressed in left testis and 105 other cell types or tissues. DR ExpressionAtlas; P67809; baseline and differential. DR CDD; cd04458; CSP_CDS; 1. DR FunFam; 2.40.50.140:FF:000054; Nuclease-sensitive element-binding protein 1; 1. DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1. DR InterPro; IPR050181; Cold_shock_domain. DR InterPro; IPR011129; CSD. DR InterPro; IPR019844; CSD_CS. DR InterPro; IPR002059; CSD_DNA-bd. DR InterPro; IPR012340; NA-bd_OB-fold. DR PANTHER; PTHR11544; COLD SHOCK DOMAIN CONTAINING PROTEINS; 1. DR Pfam; PF00313; CSD; 1. DR PRINTS; PR00050; COLDSHOCK. DR SMART; SM00357; CSP; 1. DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1. DR PROSITE; PS00352; CSD_1; 1. DR PROSITE; PS51857; CSD_2; 1. 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:0070062; C:extracellular exosome; IDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; EXP:UniProtKB. DR GO; GO:0071204; C:histone pre-mRNA 3'end processing complex; ISS:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; EXP:UniProtKB. DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell. 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 reader activity; IDA:UniProtKB. 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: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:1990428; P:miRNA transport; IDA:UniProtKB. 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: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: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:0006355; P:regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central. DR GO; GO:0050658; P:RNA transport; IMP:UniProtKB. DR GO; GO:0051031; P:tRNA transport; IMP:UniProtKB. DR Proteomes; UP000005640; Chromosome 1. DR PathwayCommons; P67809; -. DR Pharos; P67809; Tbio. DR Antibodypedia; 32231; 715 antibodies from 40 providers. DR RNAct; P67809; protein. DR BioGRID-ORCS; 4904; 727 hits in 1144 CRISPR screens. DR AlphaFoldDB; P67809; -. DR MDposit; P67809; -. DR CD-CODE; 232F8A39; P-body. DR CD-CODE; 5253F164; YBX1 condensate. DR CD-CODE; DEE660B4; Stress granule. DR CD-CODE; F85A2E29; IMP1 RNP granule. DR FunCoup; P67809; 1907. DR PAN-GO; P67809; 3 GO annotations based on evolutionary models. 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; Proteomics identification; Reference proteome; KW Repressor; RNA-binding; Secreted; Transcription; Transcription regulation; KW 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 58..121 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 30..41 FT /note="Gly residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 144..154 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 155..166 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 194..208 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 241..250 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 279..291 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 292..305 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 FT (m5C)-containing mRNAs." FT /evidence="ECO:0000269|PubMed:31358969" FT MUTAGEN 65 FT /note="W->F: Decreased binding to C5-methylcytosine FT (m5C)-containing mRNAs. Decreased ability to discriminate FT between 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 //