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1433B_CHICK
ID   1433B_CHICK             Reviewed;         244 AA.
AC   Q5ZLQ6;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=14-3-3 protein beta/alpha;
GN   Name=YWHAB; ORFNames=RCJMB04_5d11;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
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   -!- PTM: Phosphorylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}.
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DR   EMBL; AJ719678; CAG31337.1; -; mRNA.
DR   RefSeq; NP_001006289.1; NM_001006289.1.
DR   AlphaFoldDB; Q5ZLQ6; -.
DR   SMR; Q5ZLQ6; -.
DR   BioGRID; 680338; 2.
DR   IntAct; Q5ZLQ6; 1.
DR   STRING; 9031.ENSGALP00000043305; -.
DR   PaxDb; Q5ZLQ6; -.
DR   PRIDE; Q5ZLQ6; -.
DR   Ensembl; ENSGALT00000044506; ENSGALP00000043305; ENSGALG00000004143.
DR   Ensembl; ENSGALT00000091201; ENSGALP00000071615; ENSGALG00000004143.
DR   Ensembl; ENSGALT00000107000; ENSGALP00000066011; ENSGALG00000004143.
DR   GeneID; 419190; -.
DR   KEGG; gga:419190; -.
DR   CTD; 7529; -.
DR   VEuPathDB; HostDB:geneid_419190; -.
DR   eggNOG; KOG0841; Eukaryota.
DR   GeneTree; ENSGT01050000244817; -.
DR   HOGENOM; CLU_058290_1_0_1; -.
DR   InParanoid; Q5ZLQ6; -.
DR   OMA; KGCQLAR; -.
DR   OrthoDB; 1176818at2759; -.
DR   PhylomeDB; Q5ZLQ6; -.
DR   TreeFam; TF102003; -.
DR   Reactome; R-GGA-165159; MTOR signalling.
DR   Reactome; R-GGA-166208; mTORC1-mediated signalling.
DR   Reactome; R-GGA-170968; Frs2-mediated activation.
DR   Reactome; R-GGA-2028269; Signaling by Hippo.
DR   Reactome; R-GGA-392517; Rap1 signalling.
DR   Reactome; R-GGA-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
DR   Reactome; R-GGA-5628897; TP53 Regulates Metabolic Genes.
DR   Reactome; R-GGA-5673000; RAF activation.
DR   Reactome; R-GGA-5674135; MAP2K and MAPK activation.
DR   Reactome; R-GGA-5675221; Negative regulation of MAPK pathway.
DR   Reactome; R-GGA-9614399; Regulation of localization of FOXO transcription factors.
DR   PRO; PR:Q5ZLQ6; -.
DR   Proteomes; UP000000539; Chromosome 20.
DR   Bgee; ENSGALG00000004143; Expressed in brain and 14 other 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:0043085; P:positive regulation of catalytic activity; IEA:Ensembl.
DR   GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR   GO; GO:0006605; P:protein targeting; IEA:Ensembl.
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; Phosphoprotein; Reference proteome.
FT   CHAIN           1..244
FT                   /note="14-3-3 protein beta/alpha"
FT                   /id="PRO_0000058597"
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"
FT   MOD_RES         184
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   244 AA;  27907 MW;  200272F6434A5254 CRC64;
     MDKSELVQKA KLAEQAERYD DMAAAMKAVT EQGHELSNEE RNLLSVAYKN VVGARRSSWR
     VISSIEQKTE RNEKKQQMGR EYREKIEAEL QDICNDVLEL LDKYLIVNAT QPESKVFYLK
     MKGDYYRYLS EVASGDNKQT TVANSQQAYQ EAFEISKKEM QPTHPIRLGL ALNFSVFYYE
     ILNSPEKACN LAKTAFDEAI AELDTLNEES YKDSTLIMQL LRDNLTLWTS ENQGDEGDAG
     EGEN
 
 
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