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   05-JUL-2004 (Rel. 44, Last annotation update)
DE   14-3-3 protein tau (14-3-3 protein theta) (14-3-3 protein T-cell) (HS1
DE   protein).
GN   Name=YWHAQ;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   SEQUENCE FROM N.A.
RC   TISSUE=T-cell;
RX   MEDLINE=91198149; PubMed=2015305;
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; PubMed=8515476;
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   SEQUENCE FROM N.A.
RC   TISSUE=Skin;
RX   MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899;
RA   Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA   Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA   Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA   Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA   Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA   Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA   Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA   Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA   Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA   Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA   Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA   Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA   Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA   Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA   Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA   Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA   Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT   "Generation and initial analysis of more than 15,000 full-length human
RT   and mouse cDNA sequences.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN   [4]
RP   SEQUENCE OF 1-18.
RC   TISSUE=Platelet;
RX   MEDLINE=22608298; PubMed=12665801; DOI=10.1038/nbt810;
RA   Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA   Thomas G.R., Vandekerckhove J.;
RT   "Exploring proteomes and analyzing protein processing by mass
RT   spectrometric identification of sorted N-terminal peptides.";
RL   Nat. Biotechnol. 21:566-569(2003).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX   MEDLINE=95327195; PubMed=7603573;
RA   Xiao B., Smerdon S.J., Jones D.H., Dodson G.G., Soneji Y., Aitken A.,
RA   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   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   EMBL; BC056867; AAH56867.1; -.
DR   PIR; S15076; S15076.
DR   HSSP; P93343; 1O9E.
DR   IntAct; P27348; -.
DR   OGP; P27348; -.
DR   Genew; HGNC:12854; YWHAQ.
DR   GO; GO:0005515; F:protein binding; TAS.
DR   InterPro; IPR000308; 14-3-3.
DR   Pfam; PF00244; 14-3-3; 1.
DR   PRINTS; PR00305; 1433ZETA.
DR   ProDom; PD000600; 14-3-3; 1.
DR   PROSITE; PS00796; 1433_1; 1.
DR   PROSITE; PS00797; 1433_2; 1.
KW   Direct protein sequencing; Multigene family; Phosphorylation.
SQ   SEQUENCE   245 AA;  27764 MW;  175534325E9E37C4 CRC64;
     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
//