ID A0A140T894_BOVIN Unreviewed; 246 AA.
AC A0A140T894;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=14-3-3 protein beta/alpha {ECO:0000256|ARBA:ARBA00039305};
GN Name=YWHAB {ECO:0000313|Ensembl:ENSBTAP00000022411.2,
GN ECO:0000313|VGNC:VGNC:37044};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000022411.2, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000022411.2, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000022411.2,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000022411.2}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000022411.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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. Negative regulator of
CC osteogenesis. Blocks the nuclear translocation of the phosphorylated
CC form (by AKT1) of SRPK2 and antagonizes its stimulatory effect on
CC cyclin D1 expression resulting in blockage of neuronal apoptosis
CC elicited by SRPK2. Negative regulator of signaling cascades that
CC mediate activation of MAP kinases via AKAP13.
CC {ECO:0000256|ARBA:ARBA00037038}.
CC -!- SIMILARITY: Belongs to the 14-3-3 family.
CC {ECO:0000256|ARBA:ARBA00006141, ECO:0000256|RuleBase:RU003466}.
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DR RefSeq; NP_777219.2; NM_174794.2.
DR AlphaFoldDB; A0A140T894; -.
DR SMR; A0A140T894; -.
DR Ensembl; ENSBTAT00000022411.3; ENSBTAP00000022411.2; ENSBTAG00000016846.3.
DR GeneID; 286863; -.
DR KEGG; bta:286863; -.
DR CTD; 7529; -.
DR VEuPathDB; HostDB:ENSBTAG00000016846; -.
DR VGNC; VGNC:37044; YWHAB.
DR GeneTree; ENSGT01090000260040; -.
DR InParanoid; A0A140T894; -.
DR OMA; EQHVTII; -.
DR OrthoDB; 920089at2759; -.
DR Reactome; R-BTA-111447; Activation of BAD and translocation to mitochondria.
DR Reactome; R-BTA-165159; MTOR signalling.
DR Reactome; R-BTA-166208; mTORC1-mediated signalling.
DR Reactome; R-BTA-170968; Frs2-mediated activation.
DR Reactome; R-BTA-2028269; Signaling by Hippo.
DR Reactome; R-BTA-392517; Rap1 signalling.
DR Reactome; R-BTA-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
DR Reactome; R-BTA-450513; Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA.
DR Reactome; R-BTA-5625740; RHO GTPases activate PKNs.
DR Reactome; R-BTA-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-BTA-5673000; RAF activation.
DR Reactome; R-BTA-5674135; MAP2K and MAPK activation.
DR Reactome; R-BTA-5675221; Negative regulation of MAPK pathway.
DR Reactome; R-BTA-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
DR Reactome; R-BTA-9614399; Regulation of localization of FOXO transcription factors.
DR Proteomes; UP000009136; Chromosome 13.
DR Bgee; ENSBTAG00000016846; Expressed in occipital lobe and 102 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0050815; F:phosphoserine residue binding; IEA:Ensembl.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0004860; F:protein kinase inhibitor activity; IEA:Ensembl.
DR GO; GO:0051220; P:cytoplasmic sequestering of protein; IEA:Ensembl.
DR GO; GO:0045744; P:negative regulation of G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0035308; P:negative regulation of protein dephosphorylation; IEA:Ensembl.
DR GO; GO:0006605; P:protein targeting; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd10022; 14-3-3_beta_zeta; 1.
DR Gene3D; 1.20.190.20; 14-3-3 domain; 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; 14-3-3 PROTEIN; 1.
DR PANTHER; PTHR18860:SF28; 14-3-3 PROTEIN BETA_ALPHA; 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; 14-3-3 protein; 1.
DR PROSITE; PS00796; 1433_1; 1.
DR PROSITE; PS00797; 1433_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136}.
FT DOMAIN 5..244
FT /note="14-3-3"
FT /evidence="ECO:0000259|SMART:SM00101"
FT COILED 67..105
FT /evidence="ECO:0000256|SAM:Coils"
FT SITE 58
FT /note="Interaction with phosphoserine on interacting
FT protein"
FT /evidence="ECO:0000256|PIRSR:PIRSR000868-1"
FT SITE 129
FT /note="Interaction with phosphoserine on interacting
FT protein"
FT /evidence="ECO:0000256|PIRSR:PIRSR000868-1"
SQ SEQUENCE 246 AA; 28082 MW; 6BE1A9BF97468017 CRC64;
MTMDKSELVQ KAKLAEQAER YDDMAAAMKA VTEQGHELSN EERNLLSVAY KNVVGARRSS
WRVISSIEQK TERNEKKQQM GKEYREKIEA ELQDICNDVL ELLDKYLIPN ATQPESKVFY
LKMKGDYFRY LSEVASGDNK QTTVSNSQQA YQEAFEISKK EMQPTHPIRL GLALNFSVFY
YEILNSPEKA CSLAKTAFDE AIAELDTLNE ESYKDSTLIM QLLRDNLTLW TSENQGDEGD
AGEGEN
//
