143BA_DANRE
ID 143BA_DANRE Reviewed; 244 AA.
AC Q5PRD0; A3KNI9;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=14-3-3 protein beta/alpha-A;
GN Name=ywhaba; Synonyms=ywhab1; ORFNames=wu:fb80c08;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo, and Testis;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2007) 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH86710.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC086710; AAH86710.1; ALT_INIT; mRNA.
DR EMBL; BC133863; AAI33864.1; -; mRNA.
DR RefSeq; NP_001076267.1; NM_001082798.1.
DR AlphaFoldDB; Q5PRD0; -.
DR SMR; Q5PRD0; -.
DR IntAct; Q5PRD0; 1.
DR MINT; Q5PRD0; -.
DR STRING; 7955.ENSDARP00000027118; -.
DR PaxDb; Q5PRD0; -.
DR PRIDE; Q5PRD0; -.
DR Ensembl; ENSDART00000025940; ENSDARP00000027118; ENSDARG00000013078.
DR GeneID; 323055; -.
DR KEGG; dre:323055; -.
DR CTD; 323055; -.
DR ZFIN; ZDB-GENE-030131-6583; ywhaba.
DR eggNOG; KOG0841; Eukaryota.
DR GeneTree; ENSGT01050000244817; -.
DR InParanoid; Q5PRD0; -.
DR OrthoDB; 1176818at2759; -.
DR PhylomeDB; Q5PRD0; -.
DR TreeFam; TF102003; -.
DR Reactome; R-DRE-111447; Activation of BAD and translocation to mitochondria.
DR Reactome; R-DRE-165159; MTOR signalling.
DR Reactome; R-DRE-166208; mTORC1-mediated signalling.
DR Reactome; R-DRE-170968; Frs2-mediated activation.
DR Reactome; R-DRE-2028269; Signaling by Hippo.
DR Reactome; R-DRE-392517; Rap1 signalling.
DR Reactome; R-DRE-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
DR Reactome; R-DRE-450513; Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA.
DR Reactome; R-DRE-5625740; RHO GTPases activate PKNs.
DR Reactome; R-DRE-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-DRE-5673000; RAF activation.
DR Reactome; R-DRE-5674135; MAP2K and MAPK activation.
DR Reactome; R-DRE-5675221; Negative regulation of MAPK pathway.
DR Reactome; R-DRE-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
DR Reactome; R-DRE-9614399; Regulation of localization of FOXO transcription factors.
DR PRO; PR:Q5PRD0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 6.
DR Bgee; ENSDARG00000013078; Expressed in brain and 40 other tissues.
DR ExpressionAtlas; Q5PRD0; baseline.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0006911; P:phagocytosis, engulfment; IMP:ZFIN.
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-A"
FT /id="PRO_0000058602"
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; 27647 MW; D8421934B4BF17EA CRC64;
MDKSDLVQKA KLAEQAERYD DMAASMKAVT EGGVELSNEE RNLLSVAYKN VVGARRSSWR
VISSIEQKTE GNEKKQQMAR EYREKIEAEL QEICNDVLGL LEKYLIPNAS QAESKVFYLK
MKGDYYRYLS EVASGDSKRT TVENSQKAYQ DAFEISKKEM QPTHPIRLGL ALNFSVFYYE
ILNTPEQACS LAKTAFDEAI AELDTLNEDS YKDSTLIMQL LRDNLTLWTS ENQGDEGDAG
EGEN