YBOX2_MOUSE
ID YBOX2_MOUSE Reviewed; 360 AA.
AC Q9Z2C8; Q5NCW8; Q5NCW9; Q9Z2C7;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=Y-box-binding protein 2;
DE AltName: Full=FRGY2 homolog;
DE AltName: Full=Germ cell-specific Y-box-binding protein;
GN Name=Ybx2; Synonyms=Msy2;
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] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RC STRAIN=CD-1; TISSUE=Testis;
RX PubMed=9780336; DOI=10.1095/biolreprod59.5.1266;
RA Gu W., Tekur S., Reinbold R., Eppig J.J., Choi Y.-C., Zheng J.Z.,
RA Murray M.T., Hecht N.B.;
RT "Mammalian male and female germ cells express a germ cell-specific Y-box
RT protein, MSY2.";
RL Biol. Reprod. 59:1266-1274(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP FUNCTION IN MRNA TRANSLATION, PHOSPHORYLATION, RNA-BINDING, AND
RP IDENTIFICATION IN A MRNP COMPLEX WITH PABPC1.
RX PubMed=10076007; DOI=10.1093/nar/27.7.1747;
RA Herbert T.P., Hecht N.B.;
RT "The mouse Y-box protein, MSY2, is associated with a kinase on non-
RT polysomal mouse testicular mRNAs.";
RL Nucleic Acids Res. 27:1747-1753(1999).
RN [4]
RP IDENTIFICATION IN A MRNP COMPLEX WITH YBX3.
RC TISSUE=Testis;
RX PubMed=10772793; DOI=10.1006/dbio.2000.9658;
RA Davies H.G., Giorgini F., Fajardo M.A., Braun R.E.;
RT "A sequence-specific RNA binding complex expressed in murine germ cells
RT contains MSY2 and MSY4.";
RL Dev. Biol. 221:87-100(2000).
RN [5]
RP PHOSPHORYLATION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11566752; DOI=10.1095/biolreprod65.4.1260;
RA Yu J., Hecht N.B., Schultz R.M.;
RT "Expression of MSY2 in mouse oocytes and preimplantation embryos.";
RL Biol. Reprod. 65:1260-1270(2001).
RN [6]
RP RNA-BINDING.
RX PubMed=11564883; DOI=10.1128/mcb.21.20.7010-7019.2001;
RA Giorgini F., Davies H.G., Braun R.E.;
RT "MSY2 and MSY4 bind a conserved sequence in the 3' untranslated region of
RT protamine 1 mRNA in vitro and in vivo.";
RL Mol. Cell. Biol. 21:7010-7019(2001).
RN [7]
RP FUNCTION IN MRNA TRANSLATION, AND RNA-BINDING.
RX PubMed=12297523; DOI=10.1095/biolreprod67.4.1093;
RA Yu J., Hecht N.B., Schultz R.M.;
RT "RNA-binding properties and translation repression in vitro by germ cell-
RT specific MSY2 protein.";
RL Biol. Reprod. 67:1093-1098(2002).
RN [8]
RP FUNCTION IN MATERNAL MRNA CYTOPLASMIC RETENTION, RNA-BINDING, AND
RP MUTAGENESIS OF TYR-109 AND PHE-111.
RX PubMed=12648488; DOI=10.1016/s0012-1606(02)00094-5;
RA Yu J., Hecht N.B., Schultz R.M.;
RT "Requirement for RNA-binding activity of MSY2 for cytoplasmic localization
RT and retention in mouse oocytes.";
RL Dev. Biol. 255:249-262(2003).
RN [9]
RP FUNCTION IN MRNA STABILITY.
RX PubMed=15031116; DOI=10.1016/j.ydbio.2003.12.020;
RA Yu J., Deng M., Medvedev S., Yang J., Hecht N.B., Schultz R.M.;
RT "Transgenic RNAi-mediated reduction of MSY2 in mouse oocytes results in
RT reduced fertility.";
RL Dev. Biol. 268:195-206(2004).
RN [10]
RP FUNCTION IN CYTOPLASMIC MRNA STORAGE, RNA-BINDING, AND DNA-BINDING.
RX PubMed=15665108; DOI=10.1073/pnas.0404685102;
RA Yang J., Medvedev S., Reddi P.P., Schultz R.M., Hecht N.B.;
RT "The DNA/RNA-binding protein MSY2 marks specific transcripts for
RT cytoplasmic storage in mouse male germ cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:1513-1518(2005).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-67; THR-78 AND SER-252, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, 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).
CC -!- FUNCTION: Major constituent of messenger ribonucleoprotein particles
CC (mRNPs). Involved in the regulation of the stability and/or translation
CC of germ cell mRNAs. Binds to Y-box consensus promoter element. Binds to
CC full-length mRNA with high affinity in a sequence-independent manner.
CC Binds to short RNA sequences containing the consensus site 5'-UCCAUCA-
CC 3' with low affinity and limited sequence specificity. Its binding with
CC maternal mRNAs is necessary for its cytoplasmic retention. May mark
CC specific mRNAs (those transcribed from Y-box promoters) in the nucleus
CC for cytoplasmic storage, thereby linking transcription and mRNA
CC storage/translational delay. {ECO:0000269|PubMed:10076007,
CC ECO:0000269|PubMed:12297523, ECO:0000269|PubMed:12648488,
CC ECO:0000269|PubMed:15031116, ECO:0000269|PubMed:15665108}.
CC -!- SUBUNIT: Found in a mRNP complex with PABPC1 and YBX3.
CC {ECO:0000269|PubMed:10076007, ECO:0000269|PubMed:10772793}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11566752}. Nucleus
CC {ECO:0000269|PubMed:11566752}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Msy2;
CC IsoId=Q9Z2C8-1; Sequence=Displayed;
CC Name=2; Synonyms=Msy2a;
CC IsoId=Q9Z2C8-2; Sequence=VSP_013052, VSP_013053;
CC -!- TISSUE SPECIFICITY: Expressed in meiotic and postmeiotic male germ
CC cells and oocytes; poorly expressed in two cell stage embryos (at
CC protein level). Not detected in preimplantation embryos.
CC {ECO:0000269|PubMed:11566752, ECO:0000269|PubMed:9780336}.
CC -!- PTM: Phosphorylated during oocyte maturation and dephosphorylated
CC following egg activation. Phosphorylated in vitro by a kinase activity
CC associated with testicular mRNPs. Dephosphorylation leads to a decrease
CC in its affinity to bind RNA in vitro. {ECO:0000269|PubMed:10076007,
CC ECO:0000269|PubMed:11566752}.
CC -!- MISCELLANEOUS: Knockout mice for this gene exhibited reduced level of
CC mRNA and protein synthesis in fully grown oocytes and decrease
CC fertility.
CC -!- MISCELLANEOUS: [Isoform 2]: In PubMed:10772793 isoform 2 not detected
CC in oocytes.
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DR EMBL; AF073954; AAC98673.1; -; mRNA.
DR EMBL; AF073955; AAC98674.1; -; mRNA.
DR EMBL; AL596185; CAI35155.1; -; Genomic_DNA.
DR EMBL; AL596185; CAI35156.1; -; Genomic_DNA.
DR CCDS; CCDS83830.1; -. [Q9Z2C8-2]
DR AlphaFoldDB; Q9Z2C8; -.
DR SMR; Q9Z2C8; -.
DR DIP; DIP-59783N; -.
DR IntAct; Q9Z2C8; 2.
DR STRING; 10090.ENSMUSP00000018698; -.
DR iPTMnet; Q9Z2C8; -.
DR REPRODUCTION-2DPAGE; Q9Z2C8; -.
DR jPOST; Q9Z2C8; -.
DR MaxQB; Q9Z2C8; -.
DR PaxDb; Q9Z2C8; -.
DR PeptideAtlas; Q9Z2C8; -.
DR PRIDE; Q9Z2C8; -.
DR ProteomicsDB; 299804; -. [Q9Z2C8-1]
DR ProteomicsDB; 299805; -. [Q9Z2C8-2]
DR MGI; MGI:1096372; Ybx2.
DR eggNOG; KOG3070; Eukaryota.
DR InParanoid; Q9Z2C8; -.
DR PhylomeDB; Q9Z2C8; -.
DR ChiTaRS; Ybx2; mouse.
DR PRO; PR:Q9Z2C8; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9Z2C8; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005844; C:polysome; IDA:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; IDA:MGI.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:MGI.
DR GO; GO:0003729; F:mRNA binding; IDA:MGI.
DR GO; GO:0003676; F:nucleic acid binding; IBA:GO_Central.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; IDA:MGI.
DR GO; GO:0045182; F:translation regulator activity; IDA:MGI.
DR GO; GO:0048255; P:mRNA stabilization; IMP:MGI.
DR GO; GO:0051100; P:negative regulation of binding; IMP:MGI.
DR GO; GO:0017148; P:negative regulation of translation; IDA:MGI.
DR GO; GO:0048477; P:oogenesis; IMP:MGI.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0007286; P:spermatid development; IMP:MGI.
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 Alternative splicing; Cytoplasm; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding.
FT CHAIN 1..360
FT /note="Y-box-binding protein 2"
FT /id="PRO_0000100226"
FT DOMAIN 95..165
FT /note="CSD"
FT REGION 34..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..171
FT /note="Required for cytoplasmic retention"
FT REGION 159..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..360
FT /note="Required for mRNA-binding"
FT COMPBIAS 210..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 67
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 78
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..78
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9780336"
FT /id="VSP_013052"
FT VAR_SEQ 79..91
FT /note="PAPPARSQADKPV -> MSRRAGQAGSAKA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9780336"
FT /id="VSP_013053"
FT MUTAGEN 109
FT /note="Y->A: Abolishes cytoplasmic retention and mRNA-
FT binding affinity; when associated with A-111."
FT /evidence="ECO:0000269|PubMed:12648488"
FT MUTAGEN 111
FT /note="F->A: Abolishes cytoplasmic retention and mRNA-
FT binding affinity; when associated with A-109."
FT /evidence="ECO:0000269|PubMed:12648488"
FT CONFLICT 60..61
FT /note="LH -> S (in Ref. 2; CAI35155)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="R -> E (in Ref. 2; CAI35155/CAI35156)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 360 AA; 38271 MW; DFCAAE7F936731BF CRC64;
MSEAEASVVA TAAPAATVPA TAAGVVAVVV PVPAGEPQKA GGGAGGGGGA ASGPAAGTPL
HAPGPRTPGN QATAASGTPA PPARSQADKP VLAIQVLGTV KWFNVRNGYG FINRNDTKED
VFVHQTAIKR NNPRKFLRSV GDGETVEFDV VEGEKGARAA NVTGPGGVPV KGSRYAPNRR
RFRRFIPRPR PAAPPPMVAE APSGGTEPGS EGERAEDSGQ RPRRRRPPPF FYRRRFVRGP
RPPNQQQPIE GSDGVEPKET APLEGDQQQG DERVPPPRFR PRYRRPFRPR PPQQPTTEGG
DGETKPSQGP TDGSRPEPQR PRNRPYFQRR RQQPPGPRQP IAAETSAPIN SGDPPTTILE
