YBX2B_XENLA
ID YBX2B_XENLA Reviewed; 324 AA.
AC P45441; A9JS45;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Y-box-binding protein 2-B;
DE AltName: Full=Cytoplasmic RNA-binding protein p54;
DE AltName: Full=Frog Y-box protein 2-B;
DE Short=FRGY2b;
DE AltName: Full=Messenger ribonucleoprotein particle 3;
DE Short=mRNP3;
GN Name=ybx2-b; Synonyms=frgy2-b;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 213-248, SUBUNIT,
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RC TISSUE=Ovary;
RX PubMed=1729676; DOI=10.1073/pnas.89.1.11;
RA Murray M.T., Schiller D.L., Franke W.W.;
RT "Sequence analysis of cytoplasmic mRNA-binding proteins of Xenopus oocytes
RT identifies a family of RNA-binding proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:11-15(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PARTIAL PROTEIN SEQUENCE, AND PHOSPHORYLATION.
RC TISSUE=Oocyte;
RX PubMed=1902800; DOI=10.1016/0014-5793(91)80456-d;
RA Deschamps S., Viel A., Denis H., le Maire M.;
RT "Purification of two thermostable components of messenger ribonucleoprotein
RT particles (mRNPs) from Xenopus laevis oocytes, belonging to a novel class
RT of RNA-binding proteins.";
RL FEBS Lett. 282:110-114(1991).
RN [4]
RP FUNCTION.
RX PubMed=1670777; DOI=10.1083/jcb.112.1.1;
RA Murray M.T., Krohne G., Franke W.W.;
RT "Different forms of soluble cytoplasmic mRNA binding proteins and particles
RT in Xenopus laevis oocytes and embryos.";
RL J. Cell Biol. 112:1-11(1991).
RN [5]
RP IDENTIFICATION IN A RIBONUCLEOPROTEIN COMPLEX WITH ELAVL1; ELAVL2; IGF2BP3;
RP STAU1; DDX6 AND LSM14B.
RX PubMed=19458392; DOI=10.1074/jbc.m109.009928;
RA Arthur P.K., Claussen M., Koch S., Tarbashevich K., Jahn O., Pieler T.;
RT "Participation of Xenopus Elr-type proteins in vegetal mRNA localization
RT during oogenesis.";
RL J. Biol. Chem. 284:19982-19992(2009).
CC -!- FUNCTION: Putative translation regulator. May be involved in the
CC developmental translational regulation of maternal mRNAs.
CC {ECO:0000269|PubMed:1670777}.
CC -!- SUBUNIT: Possibly forms a heterodimer with p54 in the 6S and 15S mRNA-
CC binding particles. Component of a ribonucleoprotein (RNP) complex,
CC composed at least of elavl1/elrA and/or elavl2/elrB, igf2bp3/vg1RBP,
CC ddx6/Xp54, ybx2/frgy2, lsm14b/rap55b and, in a subset of RNP complexes,
CC stau1/staufen. {ECO:0000269|PubMed:1729676,
CC ECO:0000269|PubMed:19458392}.
CC -!- INTERACTION:
CC P45441; O73932: igf2bp3-a; NbExp=2; IntAct=EBI-8486848, EBI-619004;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1729676}.
CC Note=Either free or associated with ribonucleoprotein particles.
CC -!- DEVELOPMENTAL STAGE: Expressed maternally. Expression peaks in the
CC early stage II oocyte and levels are maintained throughout oogenesis.
CC {ECO:0000269|PubMed:1729676}.
CC -!- PTM: Phosphorylation activates in vitro RNA binding.
CC {ECO:0000269|PubMed:1902800}.
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DR EMBL; M80257; AAA49924.1; -; mRNA.
DR EMBL; BC155913; AAI55914.1; -; mRNA.
DR PIR; A41786; A41786.
DR RefSeq; NP_001081167.1; NM_001087698.1.
DR AlphaFoldDB; P45441; -.
DR SMR; P45441; -.
DR BioGRID; 99031; 2.
DR IntAct; P45441; 1.
DR MINT; P45441; -.
DR GeneID; 394429; -.
DR KEGG; xla:394429; -.
DR CTD; 394429; -.
DR Xenbase; XB-GENE-6254213; ybx2.S.
DR OrthoDB; 1604809at2759; -.
DR Proteomes; UP000186698; Chromosome 3S.
DR Bgee; 394429; Expressed in testis and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
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 Cytoplasm; Direct protein sequencing; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; RNA-binding; Transcription; Transcription regulation;
KW Translation regulation.
FT CHAIN 1..324
FT /note="Y-box-binding protein 2-B"
FT /id="PRO_0000100228"
FT DOMAIN 44..108
FT /note="CSD"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 103..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..266
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 18
FT /note="A -> G (in Ref. 1; AAA49924)"
FT /evidence="ECO:0000305"
FT CONFLICT 125..126
FT /note="RR -> ST (in Ref. 1; AAA49924)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="R -> A (in Ref. 1; AAA49924)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 324 AA; 36176 MW; 8E86D15AE42B49F4 CRC64;
MSEAEPRETE AVTQPEPAPE IHKPDIVPPR NQINKKLLAT QVQGTVKWFN VRNGYGFINR
NDSKEDVFVH QTAIKKNNPR KFLRSVGDGE TVEFDVVEGE KGAEAANVTG PGGVPVKGSR
FAPNRRRFRR QFYRPRADTA GESGGEGVSP EQMSEGEKGE ETSPQQRPQR RRPPPFFYRR
RFRRGPRPNN QQNQGAEVTD QSENKDPAAP TSEALASGDG QQRPPPRRFQ QRFRRPFRPR
PPPPQTPEGG DGEAKAEGEP QRQRNRPYVQ RRRRQQPPTV QGESKAEPSE HPASEEGTPS
DAPTDDGAPV ETSEAGVEDT TAPE
