YBOX1_MOUSE
ID YBOX1_MOUSE Reviewed; 322 AA.
AC P62960; P22568; P27817; P43482;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Y-box-binding protein 1 {ECO:0000303|Ref.1};
DE Short=YB-1 {ECO:0000303|Ref.1};
DE AltName: Full=CCAAT-binding transcription factor I subunit A;
DE Short=CBF-A;
DE AltName: Full=DNA-binding protein B {ECO:0000303|Ref.1};
DE Short=DBPB {ECO:0000303|Ref.1};
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:0000250|UniProtKB:P67809};
DE AltName: Full=Y-box transcription factor;
GN Name=Ybx1 {ECO:0000312|MGI:MGI:99146};
GN Synonyms=Msy-1 {ECO:0000303|PubMed:8505341},
GN Msy1 {ECO:0000303|PubMed:8505341}, Nsep1 {ECO:0000250|UniProtKB:P67809},
GN Yb1 {ECO:0000303|Ref.1};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lens;
RA Shaughnessy M., Wistow G.J.;
RT "Absence of MHC expression in lens and cloning of dbpB/YB-1, a DNA-binding
RT protein expressed in mouse lens.";
RL Curr. Eye Res. 11:171-181(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1622927;
RA Familari M., Sak D., Wolffe A.P., Tafuri S.R., Ranjan M.;
RT "The Y-box factors: a family of nucleic acid binding proteins conserved
RT from Escherichia coli to man.";
RL New Biol. 4:290-298(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=1741293; DOI=10.1093/nar/20.3.601;
RA Gai X., Lipson K.E., Prystowsky M.B.;
RT "Unusual DNA binding characteristics of an in vitro translation product of
RT the CCAAT binding protein mYB-1.";
RL Nucleic Acids Res. 20:601-606(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Oocyte;
RX PubMed=8505341; DOI=10.1016/s0021-9258(19)50328-3;
RA Tafuri S.R., Familari M., Wolffe A.P.;
RT "A mouse Y box protein, MSY1, is associated with paternal mRNA in
RT spermatocytes.";
RL J. Biol. Chem. 268:12213-12220(1993).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon, Mammary gland, and Salivary gland;
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 SUBUNIT.
RX PubMed=10318844; DOI=10.1074/jbc.274.20.14238;
RA Kelm R.J. Jr., Cogan J.G., Elder P.K., Strauch A.R., Getz M.J.;
RT "Molecular interactions between single-stranded DNA-binding proteins
RT associated with an essential MCAT element in the mouse smooth muscle alpha-
RT actin promoter.";
RL J. Biol. Chem. 274:14238-14245(1999).
RN [7]
RP INTERACTION WITH FMR1.
RX PubMed=11162447; DOI=10.1006/bbrc.2000.4035;
RA Ceman S., Nelson R., Warren S.T.;
RT "Identification of mouse YB1/p50 as a component of the FMRP-associated mRNP
RT particle.";
RL Biochem. Biophys. Res. Commun. 279:904-908(2000).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=15899865; DOI=10.1128/mcb.25.11.4625-4637.2005;
RA Lu Z.H., Books J.T., Ley T.J.;
RT "YB-1 is important for late-stage embryonic development, optimal cellular
RT stress responses, and the prevention of premature senescence.";
RL Mol. Cell. Biol. 25:4625-4637(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [11]
RP IDENTIFICATION IN A HISTONE PRE-MRNA COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=19470752; DOI=10.1128/mcb.00296-09;
RA Yang X.-C., Torres M.P., Marzluff W.F., Dominski Z.;
RT "Three proteins of the U7-specific Sm ring function as the molecular ruler
RT to determine the site of 3'-end processing in mammalian histone pre-mRNA.";
RL Mol. Cell. Biol. 29:4045-4056(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163; SER-172; SER-174 AND
RP SER-312, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [14]
RP INTERACTION WITH ZBTB7B.
RX PubMed=28784777; DOI=10.1073/pnas.1703494114;
RA Li S., Mi L., Yu L., Yu Q., Liu T., Wang G.X., Zhao X.Y., Wu J., Lin J.D.;
RT "Zbtb7b engages the long noncoding RNA Blnc1 to drive brown and beige fat
RT development and thermogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E7111-E7120(2017).
RN [15]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
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).
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:8505341, PubMed:29712925).
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) (By similarity).
CC Promotes mRNA stabilization: acts by binding to m5C-containing mRNAs
CC and recruiting the mRNA stability maintainer ELAVL1, thereby preventing
CC mRNA decay (By similarity). Component of the CRD-mediated complex that
CC promotes MYC mRNA stability (By similarity). Contributes to the
CC regulation of translation by modulating the interaction between the
CC mRNA and eukaryotic initiation factors (By similarity). Plays a key
CC role in RNA composition of extracellular exosomes by defining the
CC sorting of small non-coding RNAs, such as tRNAs, Y RNAs, Vault RNAs and
CC miRNAs (By similarity). Probably sorts RNAs in exosomes by recognizing
CC and binding C5-methylcytosine (m5C)-containing RNAs (By similarity).
CC Acts as a key effector of epidermal progenitors by preventing epidermal
CC progenitor senescence: acts by regulating the translation of a
CC senescence-associated subset of cytokine mRNAs, possibly by binding to
CC m5C-containing mRNAs (PubMed:29712925). Also involved in pre-mRNA
CC alternative splicing regulation: binds to splice sites in pre-mRNA and
CC regulates splice site selection (By similarity). Also able to bind DNA:
CC 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' (By similarity). Binds to promoters that contain a Y-box (5'-
CC CTGATTGGCCAA-3'), such as MDR1 and HLA class II genes (By similarity).
CC Promotes separation of DNA strands that contain mismatches or are
CC modified by cisplatin (By similarity). Has endonucleolytic activity and
CC can introduce nicks or breaks into double-stranded DNA, suggesting a
CC role in DNA repair (By similarity). The secreted form acts as an
CC extracellular mitogen and stimulates cell migration and proliferation
CC (By similarity). {ECO:0000250|UniProtKB:P67809,
CC ECO:0000250|UniProtKB:Q28618, ECO:0000269|PubMed:29712925,
CC ECO:0000269|PubMed:8505341}.
CC -!- SUBUNIT: Homodimer in the presence of ATP (PubMed:10318844,
CC PubMed:8505341). Component of the coding region determinant (CRD)-
CC mediated complex, composed of DHX9, HNRNPU, IGF2BP1, SYNCRIP and YBX1
CC (By similarity). Identified in a IGF2BP1-dependent mRNP granule complex
CC containing untranslated mRNAs (By similarity). Component of the U11/U12
CC snRNPs that are part of the U12-type spliceosome (By similarity).
CC Identified in a histone pre-mRNA complex, at least composed of ERI1,
CC LSM11, SLBP, SNRPB, SYNCRIP and YBX1 (PubMed:11162447). Interacts with
CC IGF2BP1 and RBBP6 (By similarity). Component of cytoplasmic messenger
CC ribonucleoprotein particles (mRNPs) (By similarity). Interacts with
CC AKT1, MBNL1, SFRS9, SFRS12, ALYREF/THOC4, MSH2, XRCC5, WRN and NCL (By
CC similarity). Interacts (via C-terminus) with APEX1 (via N-terminus);
CC the interaction is increased with APEX1 acetylated at 'Lys-6' and 'Lys-
CC 7' (By similarity). Interacts with AGO1 and AGO2 (By similarity).
CC Interacts with ANKRD2 (By similarity). Interacts with DERA (By
CC similarity). Interacts with FMR1; this interaction occurs in
CC association with polyribosome (PubMed:11162447). Interacts with ZBTB7B
CC (PubMed:28784777). Interacts with HDGF. Interacts with ELAVL1; leading
CC to ELAVL1 recruitment on C5-methylcytosine (m5C)-containing mRNAs and
CC subsequent mRNA stability (By similarity).
CC {ECO:0000250|UniProtKB:P67809, ECO:0000269|PubMed:10318844,
CC ECO:0000269|PubMed:11162447, ECO:0000269|PubMed:28784777,
CC ECO:0000269|PubMed:8505341}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P67809}. Nucleus
CC {ECO:0000250|UniProtKB:P67809}. Cytoplasmic granule
CC {ECO:0000250|UniProtKB:P67809}. Secreted
CC {ECO:0000250|UniProtKB:P67809}. Secreted, extracellular exosome
CC {ECO:0000250|UniProtKB:P67809}. Note=Predominantly cytoplasmic in
CC proliferating cells. Cytotoxic stress and DNA damage enhance
CC translocation to the nucleus. Localized in cytoplasmic mRNP granules
CC containing untranslated mRNAs. Shuttles between nucleus and cytoplasm.
CC Localized with DDX1, MBNL1 and TIAL1 in stress granules upon stress.
CC Secreted by mesangial and monocytic cells after inflammatory
CC challenges. {ECO:0000250|UniProtKB:P67809}.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in the testis
CC (PubMed:8505341). Present in the mRNP particles that mediate the
CC storage and masking of mRNAs during spermiogenesis (PubMed:8505341). In
CC epidermis, expression is restricted to the cycling keratinocyte
CC progenitors (PubMed:29712925). {ECO:0000269|PubMed:29712925,
CC ECO:0000269|PubMed:8505341}.
CC -!- DEVELOPMENTAL STAGE: Found at very low levels at day 10 and levels
CC increase at day 15 and persist throughout adulthood.
CC {ECO:0000269|PubMed:8505341}.
CC -!- DOMAIN: In the CSD domain, Trp-63 specifically recognizes C5-
CC methylcytosine (m5C) modification through its indole ring.
CC {ECO:0000250|UniProtKB:P67809}.
CC -!- PTM: Ubiquitinated by RBBP6; leading to a decrease of YBX1
CC transcactivational ability. {ECO:0000250|UniProtKB:P67809}.
CC -!- PTM: In the absence of phosphorylation the protein is retained in the
CC cytoplasm. {ECO:0000250|UniProtKB:P67809}.
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 -!- DISRUPTION PHENOTYPE: Perinatal lethality (PubMed:15899865). Embryos
CC develop normally up to embryonic day 13.5 dpc and then show progressive
CC mortality (PubMed:15899865). Embryos display severe growth retardation
CC caused by hypoplasia in multiple organs (PubMed:15899865). Fibroblasts
CC show a normal rate of protein synthesis and minimal alterations in the
CC transcriptome and proteome (PubMed:15899865). Mice show defects in the
CC architecture of the skin characterized by markedly reduced thickness of
CC the epidermis and delayed onset of the placodes to hair follicle
CC transition (PubMed:29712925). {ECO:0000269|PubMed:15899865,
CC ECO:0000269|PubMed:29712925}.
CC -!- SIMILARITY: Belongs to the YBX1 family. {ECO:0000305}.
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DR EMBL; M60419; AAA40577.1; -; mRNA.
DR EMBL; M62867; AAA63390.1; -; mRNA.
DR EMBL; X57621; CAA40847.1; -; mRNA.
DR EMBL; BC013450; AAH13450.1; -; mRNA.
DR EMBL; BC013620; AAH13620.1; -; mRNA.
DR EMBL; BC029747; AAH29747.1; -; mRNA.
DR EMBL; BC031472; AAH31472.1; -; mRNA.
DR EMBL; BC061634; AAH61634.1; -; mRNA.
DR CCDS; CCDS18579.1; -.
DR PIR; I58195; I58195.
DR RefSeq; NP_035862.2; NM_011732.2.
DR AlphaFoldDB; P62960; -.
DR BMRB; P62960; -.
DR SMR; P62960; -.
DR BioGRID; 204613; 143.
DR ComplexPortal; CPX-1089; CRD-mediated mRNA stability complex.
DR DIP; DIP-34256N; -.
DR IntAct; P62960; 72.
DR MINT; P62960; -.
DR STRING; 10090.ENSMUSP00000078589; -.
DR iPTMnet; P62960; -.
DR PhosphoSitePlus; P62960; -.
DR SwissPalm; P62960; -.
DR EPD; P62960; -.
DR jPOST; P62960; -.
DR PaxDb; P62960; -.
DR PeptideAtlas; P62960; -.
DR PRIDE; P62960; -.
DR ProteomicsDB; 299619; -.
DR DNASU; 22608; -.
DR Ensembl; ENSMUST00000079644; ENSMUSP00000078589; ENSMUSG00000028639.
DR GeneID; 22608; -.
DR KEGG; mmu:22608; -.
DR UCSC; uc008ulu.1; mouse.
DR CTD; 4904; -.
DR MGI; MGI:99146; Ybx1.
DR VEuPathDB; HostDB:ENSMUSG00000028639; -.
DR eggNOG; KOG3070; Eukaryota.
DR GeneTree; ENSGT00940000153341; -.
DR HOGENOM; CLU_063071_1_0_1; -.
DR InParanoid; P62960; -.
DR OMA; GDKKVIX; -.
DR OrthoDB; 1431946at2759; -.
DR PhylomeDB; P62960; -.
DR TreeFam; TF317306; -.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-MMU-72165; mRNA Splicing - Minor Pathway.
DR Reactome; R-MMU-9017802; Noncanonical activation of NOTCH3.
DR BioGRID-ORCS; 22608; 18 hits in 78 CRISPR screens.
DR ChiTaRS; Ybx1; mouse.
DR PRO; PR:P62960; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P62960; protein.
DR Bgee; ENSMUSG00000028639; Expressed in presomitic mesoderm and 261 other tissues.
DR ExpressionAtlas; P62960; baseline and differential.
DR Genevisible; P62960; MM.
DR GO; GO:0070937; C:CRD-mediated mRNA stability complex; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0070062; C:extracellular exosome; ISS:UniProtKB.
DR GO; GO:0071204; C:histone pre-mRNA 3'end processing complex; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:1990124; C:messenger ribonucleoprotein complex; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IGI:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0005689; C:U12-type spliceosomal complex; ISO:MGI.
DR GO; GO:0062153; F:C5-methylcytidine-containing RNA binding; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0051020; F:GTPase binding; ISO:MGI.
DR GO; GO:0035198; F:miRNA binding; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0003676; F:nucleic acid binding; IBA:GO_Central.
DR GO; GO:0002039; F:p53 binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:MGI.
DR GO; GO:0098761; P:cellular response to interleukin-7; IDA:MGI.
DR GO; GO:0070934; P:CRD-mediated mRNA stabilization; ISS:UniProtKB.
DR GO; GO:0048598; P:embryonic morphogenesis; ISS:UniProtKB.
DR GO; GO:0008544; P:epidermis development; IMP:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:1990428; P:miRNA transport; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0048255; P:mRNA stabilization; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:2000773; P:negative regulation of cellular senescence; IMP:UniProtKB.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; ISO:MGI.
DR GO; GO:1900152; P:negative regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; ISO:MGI.
DR GO; GO:0051154; P:negative regulation of striated muscle cell differentiation; IDA:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
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:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:2000767; P:positive regulation of cytoplasmic translation; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:1903608; P:protein localization to cytoplasmic stress granule; ISO:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR GO; GO:0050658; P:RNA transport; ISS:UniProtKB.
DR GO; GO:0051031; P:tRNA transport; ISS: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 Acetylation; Activator; Cytoplasm; DNA-binding; Isopeptide bond; Mitogen;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; RNA-binding; Secreted; Transcription;
KW Transcription regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P67809"
FT CHAIN 2..322
FT /note="Y-box-binding protein 1"
FT /id="PRO_0000100220"
FT DOMAIN 59..123
FT /note="CSD"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 16..69
FT /note="Interaction with ss-DNA"
FT /evidence="ECO:0000250|UniProtKB:P67809"
FT REGION 63..68
FT /note="C5-methylcytosine binding"
FT /evidence="ECO:0000250|UniProtKB:P67809"
FT REGION 118..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..304
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 63
FT /note="Important for C5-methylcytosine-recognition"
FT /evidence="ECO:0000250|UniProtKB:P67809"
FT SITE 217..218
FT /note="Cleavage; by 20S proteasomal protease"
FT /evidence="ECO:0000250|UniProtKB:Q28618"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P67809"
FT MOD_RES 100
FT /note="Phosphoserine; by PKB/AKT1"
FT /evidence="ECO:0000250|UniProtKB:P67809"
FT MOD_RES 160
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P67809"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P67809"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 299
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P67809"
FT MOD_RES 302
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P67809"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT CROSSLNK 24
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P67809"
FT CROSSLNK 135
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P67809"
FT CONFLICT 29
FT /note="G -> A (in Ref. 2; AAA63390)"
FT /evidence="ECO:0000305"
FT CONFLICT 43..45
FT /note="AAP -> RR (in Ref. 3; CAA40847)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="G -> P (in Ref. 3; CAA40847)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 322 AA; 35730 MW; C6667CF7CA10D45D CRC64;
MSSEAETQQP PAAPAAALSA ADTKPGSTGS GAGSGGPGGL TSAAPAGGDK KVIATKVLGT
VKWFNVRNGY GFINRNDTKE DVFVHQTAIK KNNPRKYLRS VGDGETVEFD VVEGEKGAEA
ANVTGPGGVP VQGSKYAADR NHYRRYPRRR GPPRNYQQNY QNSESGEKNE GSESAPEGQA
QQRRPYRRRR FPPYYMRRPY ARRPQYSNPP VQGEVMEGAD NQGAGEQGRP VRQNMYRGYR
PRFRRGPPRQ RQPREDGNEE DKENQGDETQ GQQPPQRRYR RNFNYRRRRP ENPKPQDGKE
TKAADPPAEN SSAPEAEQGG AE
