ID   1433B_XENTR             Reviewed;         244 AA.
AC   Q5XGC8; Q28HK2;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=14-3-3 protein beta/alpha;
GN   Name=ywhab; ORFNames=TTpA010k20.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Tadpole;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2004) 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; CR760847; CAJ82973.1; -; mRNA.
DR   EMBL; BC084514; AAH84514.1; -; mRNA.
DR   RefSeq; NP_001011116.1; NM_001011116.1.
DR   AlphaFoldDB; Q5XGC8; -.
DR   SMR; Q5XGC8; -.
DR   STRING; 8364.ENSXETP00000049381; -.
DR   PaxDb; Q5XGC8; -.
DR   GeneID; 496529; -.
DR   KEGG; xtr:496529; -.
DR   CTD; 7529; -.
DR   Xenbase; XB-GENE-1006026; ywhab.
DR   eggNOG; KOG0841; Eukaryota.
DR   HOGENOM; CLU_058290_1_0_1; -.
DR   InParanoid; Q5XGC8; -.
DR   OrthoDB; 1176818at2759; -.
DR   PhylomeDB; Q5XGC8; -.
DR   Reactome; R-XTR-111447; Activation of BAD and translocation to mitochondria.
DR   Reactome; R-XTR-165159; MTOR signalling.
DR   Reactome; R-XTR-166208; mTORC1-mediated signalling.
DR   Reactome; R-XTR-2028269; Signaling by Hippo.
DR   Reactome; R-XTR-392517; Rap1 signalling.
DR   Reactome; R-XTR-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
DR   Reactome; R-XTR-450513; Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA.
DR   Reactome; R-XTR-5625740; RHO GTPases activate PKNs.
DR   Reactome; R-XTR-5628897; TP53 Regulates Metabolic Genes.
DR   Reactome; R-XTR-5673000; RAF activation.
DR   Reactome; R-XTR-5674135; MAP2K and MAPK activation.
DR   Reactome; R-XTR-5675221; Negative regulation of MAPK pathway.
DR   Reactome; R-XTR-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
DR   Reactome; R-XTR-9614399; Regulation of localization of FOXO transcription factors.
DR   Proteomes; UP000008143; Chromosome 10.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000022830; Expressed in brain and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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"
FT                   /id="PRO_0000058600"
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;  27721 MW;  FF766793EA1CA9E5 CRC64;
     MDKSELVQKA KLSEQAERYD DMAASMKAVT ELGAELSNEE RNLLSVAYKN VVGARRSSWR
     VISSIEQKTE GNDKRQQMAR EYREKVETEL QDICKDVLGL LDKYLVPNAT PPESKVFYLK
     MKGDYYRYLS EVASGDSKQE TVTCSQQAYQ EAFEISKSEM QPTHPIRLGL ALNFSVFYYE
     ILNSPEKACS LAKSAFDEAI AELDTLNEES YKDSTLIMQL LRDNLTLWTS ENQGEEADNA
     EADN