ID  E2RU97;
PN  14-3-3 protein;
GN  GL50803_006430;
OS  184922;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:16368691, ECO:0000269|PubMed:19733174, ECO:0000269|PubMed:19861170, ECO:0000269|PubMed:21135098, ECO:0000269|PubMed:24147113, ECO:0000269|PubMed:24728194, ECO:0000269|PubMed:28932813}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:28932813}. Nucleus {ECO:0000269|PubMed:16368691, ECO:0000269|PubMed:19733174, ECO:0000269|PubMed:21135098, ECO:0000269|PubMed:22452640}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:28932813}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:28932813}. Nucleus envelope {ECO:0000269|PubMed:28932813}. Endoplasmic reticulum {ECO:0000269|PubMed:28932813}. Note=In trophozoites and cysts, localizes intensely in the cytoplasm. Not detected in the central area of the cell corresponding to the median body nor in flagella. Detected in the nuclei of the encysting cells. Nuclear localization increases during the transition of cells from the early to the late encysting stage. Does not localize to the encystation-specific vesicles of the encysting cells (PubMed:16368691, PubMed:19733174). In interphase cells, detected throughout the cell with somewhat enriched at the cortex and perinuclear region. Associates with the intracytoplasmic axonemes of all flagella, but it is most apparent in the anterior flagella of interphase cells. Localizes also to the nuclear envelope/endoplasmic reticulum and to the microtubule bare area of the ventral disc during interphase. In mitotic cells, disassociates from the intracytoplasmic axonemes and localizes around the spindle. During cytokinesis, localizes with the ingressing furrow, which does not utilize a contractile ring (PubMed:28932813). Does no colocalize with F-actin (PubMed:24728194, PubMed:28932813). {ECO:0000269|PubMed:16368691, ECO:0000269|PubMed:19733174, ECO:0000269|PubMed:24728194, ECO:0000269|PubMed:28932813}.
DR  UNIPROT: E2RU97;
DR  PDB: 4F7R;
DR  PDB: 4ZQ0;
DR  PDB: 5BY9;
DR  Pfam: PF00244;
DR  PROSITE: PS00796;
DE  Function: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner (By similarity). Binds with varying affinity to various synthetic phosphopeptides having a consensus binding motif RSX(pS/pT)XP, called mode-1, where X is any residue and pS/pT is a phosphorylated serine/threonine, and to synthetic phosphopeptides having a consensus binding motif Xp(S/T)X1-2-COOH, called mode-3, in which the phosphorylated residue occupies the penultimate C-terminal position in the target protein, but does not bind to their unphosphorylated counterparts (PubMed:19733174). Binds to synthetic human RAF1 phosphopeptides, but not to their unphosphorylated forms. Binds to difopein, a polypeptide containing a phosphorylation- independent binding motif (PubMed:16368691, PubMed:19733174). Involved in encystation (PubMed:19733174). Involved in cell proliferation. Required for actin and tubulin cytoskeletal organization. Regulates actin filament formation and nuclear size (PubMed:28932813). {ECO:0000250|UniProtKB:P62261, ECO:0000269|PubMed:16368691, ECO:0000269|PubMed:19733174, ECO:0000269|PubMed:28932813}.
DE  Reference Proteome: Yes;
GO  GO:0005930;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0005783;
GO  GO:0031514;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0005819;
GO  GO:0003779;
GO  GO:0042802;
GO  GO:0019900;
GO  GO:0051219;
GO  GO:0050815;
GO  GO:0042803;
GO  GO:0030036;
GO  GO:1990051;
GO  GO:0030010;
GO  GO:0000165;
GO  GO:0051495;
GO  GO:0051289;
GO  GO:0070207;
GO  GO:0008104;
GO  GO:0097298;
GO  GO:0007165;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAEAFTREDYVFMAQLNENAERYDEMVETMRKISGMEGELSDKERNLLSVAYKNVIGPRRAAWRIVSSIEAKEKGRQKPN
SQ  AKRIEQIRVYRQKIEKELSDICNDILKLLQEQFVPRSTNADAKVFYYKMQGDYYRYLAEYSSGEDKEKIAGSALNAYNSA
SQ  FEISQQLPPTHPIRLGLALNFSVFYYEILASPDRACELARKAFDAAITDLDKLTEESYKDSTLIMQLLRDNLNLWVTDSA
SQ  GDDNAEEK
//