ID   143BB_XENLA             Reviewed;         244 AA.
AC   Q8AVQ3;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=14-3-3 protein beta/alpha-B;
GN   Name=ywhab-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 [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Adapter protein implicated in the regulation of a large
CC       spectrum of both general and specialized signaling pathways. Binds to a
CC       large number of partners, usually by recognition of a phosphoserine or
CC       phosphothreonine motif. Binding generally results in the modulation of
CC       the activity of the binding partner (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer, and heterodimer with other family members.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}.
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DR   EMBL; BC041526; AAH41526.1; -; mRNA.
DR   RefSeq; NP_001080764.1; NM_001087295.1.
DR   AlphaFoldDB; Q8AVQ3; -.
DR   SMR; Q8AVQ3; -.
DR   PRIDE; Q8AVQ3; -.
DR   DNASU; 380457; -.
DR   GeneID; 380457; -.
DR   KEGG; xla:380457; -.
DR   CTD; 380457; -.
DR   Xenbase; XB-GENE-1006032; ywhab.S.
DR   OMA; SMKAYQT; -.
DR   OrthoDB; 1176818at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10S.
DR   Bgee; 380457; Expressed in brain and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   Gene3D; 1.20.190.20; -; 1.
DR   InterPro; IPR000308; 14-3-3.
DR   InterPro; IPR023409; 14-3-3_CS.
DR   InterPro; IPR036815; 14-3-3_dom_sf.
DR   InterPro; IPR023410; 14-3-3_domain.
DR   PANTHER; PTHR18860; PTHR18860; 1.
DR   Pfam; PF00244; 14-3-3; 1.
DR   PIRSF; PIRSF000868; 14-3-3; 1.
DR   PRINTS; PR00305; 1433ZETA.
DR   SMART; SM00101; 14_3_3; 1.
DR   SUPFAM; SSF48445; SSF48445; 1.
DR   PROSITE; PS00796; 1433_1; 1.
DR   PROSITE; PS00797; 1433_2; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Reference proteome.
FT   CHAIN           1..244
FT                   /note="14-3-3 protein beta/alpha-B"
FT                   /id="PRO_0000058599"
FT   SITE            56
FT                   /note="Interaction with phosphoserine on interacting
FT                   protein"
FT                   /evidence="ECO:0000250"
FT   SITE            127
FT                   /note="Interaction with phosphoserine on interacting
FT                   protein"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   244 AA;  27759 MW;  9153B815F615BB99 CRC64;
     MDKSELVQKA KLSEQAERYD DMAASMKAVT ELGAELSNEE RNLLSVAYKN VVGARRSSWR
     VISSIEQKTE GNDKRQQMAR EYREKVETEL QDICKDVLDL LDRFLVPNAT PPESKVFYLK
     MKGDYYRYLS EVASGDSKQE TVANSQQAYQ EAFEISKSEM QPTHPIRLGL ALNFSVFYYE
     ILNSPDKACS LAKSAFDEAI AELDTLNEES YKDSTLIMQL LRDNLTLWTS ETQGEEADNV
     EGDN