ID 143T_HUMAN STANDARD; PRT; 245 AA. AC P27348; DT 01-AUG-1992 (Rel. 23, Created) DT 01-AUG-1992 (Rel. 23, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE 14-3-3 PROTEIN TAU (14-3-3 PROTEIN THETA) (14-3-3 PROTEIN T-CELL) DE (HS1 PROTEIN). GN YWHAQ. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Mammalia; OC Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=T-CELL; RX MEDLINE; 91198149. RA NIELSEN P.J.; RT "Primary structure of a human protein kinase regulator protein."; RL Biochim. Biophys. Acta 1088:425-428(1991). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=KERATINOCYTES; RX MEDLINE; 93294871. RA LEFFERS H., MADSEN P., RASMUSSEN H.H., HONORE B., ANDERSEN A.H., RA WALBUM E., VANDEKERCKHOVE J., CELIS J.E.; RT "Molecular cloning and expression of the transformation sensitive RT epithelial marker stratifin. A member of a protein family that has RT been involved in the protein kinase C signalling pathway."; RL J. Mol. Biol. 231:982-998(1993). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS). RX MEDLINE; 95327195. RA XIAO B., SMERDON S.J., JONES D.H., DODSON G.G., SONEJI Y., RA AITKEN A., GAMBLIN S.J.; RT "Structure of a 14-3-3 protein and implications for coordination of RT multiple signalling pathways."; RL Nature 376:188-191(1995). CC -!- FUNCTION: ACTIVATES TYROSINE AND TRYPTOPHAN HYDROXYLASES IN THE CC PRESENCE OF CA(2+)/CALMODULIN-DEPENDENT PROTEIN KINASE II, AND CC STRONGLY ACTIVATES PROTEIN KINASE C. IS PROBABLY A MULTIFUNCTIONAL CC REGULATOR OF THE CELL SIGNALING PROCESSES MEDIATED BY BOTH CC KINASES. CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- TISSUE SPECIFICITY: 14-3-3 PROTEINS ARE LOCALIZED IN NEURONS, AND CC ARE AXONALLY TRANSPORTED TO THE NERVE TERMINALS. THEY MAY BE ALSO CC PRESENT, AT LOWER LEVELS, IN VARIOUS OTHER EUKARYOTIC TISSUES. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X56468; CAA39840.1; -. DR EMBL; X57347; CAA40622.1; -. DR PIR; S15076; S15076. DR PIR; S29342; S29342. DR PIR; S34754; S34754. DR PFAM; PF00244; 14-3-3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Brain; Neurone; Phosphorylation; Multigene family. SQ SEQUENCE 245 AA; 27764 MW; EBED446B CRC32; MEKTELIQKA KLAEQAERYD DMATCMKAVT EQGAELSNEE RNLLSVAYKN VVGGRRSAWR VISSIEQKTD TSDKKLQLIK DYREKVESEL RSICTTVLEL LDKYLIANAT NPESKVFYLK MKGDYFRYLA EVACGDDRKQ TIDNSQGAYQ EAFDISKKEM QPTHPIRLGL ALNFSVFYYE ILNNPELACT LAKTAFDEAI AELDTLNEDS YKDSTLIMQL LRDNLTLWTS DSAGEECDAA EGAEN //