input: P29312
primary accession: P29312
SwissProt id: 143Z_HUMAN
acc from id: P29312
organelle: (null)
isCurated: 1
aaSize: 245
molWeight: 27745
createDate: 1992-12-01
seqDate: 1992-12-01
annDate: 2003-09-15
description: 14-3-3 protein zeta/delta (Protein kinase C inhibitor protein-1) (KCIP-1) (Factor activating exoenzyme S) (FAS).
taxon: 9606
first scientific name: Homo sapiens
first common name: Human
taxon from sci: 9606
taxon from common: 9606
all scientific names: Homo sapiens, Bos taurus,
gene(s): YWHAZ,
 any YWHAZ: P29312, P35215, P29361, Q86V33, Q8BWN0,
 Human YWHAZ: P29312, Q86V33,
keyword(s): Brain, Neurone, Phosphorylation, Acetylation, Multigene family, , 3D-structure,
Human Brain (10): P31946 P42655 Q04917 P35214...
all Brain (93): P29358 P31946 Q9CQV8 P35213...
all Neurone (152): P29358 P31946 Q9CQV8 P35213...
all Phosphorylation (8643): P29358 P31946 Q9CQV8 P35213...
all Acetylation (1635): P29358 P31946 Q9CQV8 P35213...
all Multigene family (9969): P19084 P15455 P15456 O23878...
all  (159069): P29358 P31946 Q9CQV8 P35213...
all 3D-structure (5446): P29312 P01892 P18485 P37821...
All comments:
 ACTIVATES TYROSINE AND TRYPTOPHAN HYDROXYLASES IN THE PRESENCE OF CA(2+)/CALMODULIN-DEPENDENT PROTEIN KINASE II, AND STRONGLY ACTIVATES PROTEIN KINASE C. IS PROBABLY A MULTIFUNCTIONAL REGULATOR OF THE CELL SIGNALING PROCESSES MEDIATED BY BOTH KINASES. ACTIVATES THE ADP-RIBOSYLTRANSFERASE (EXOS) ACTIVITY OF BACTERIAL ORIGIN.
 Homodimer.
 Cytoplasmic.
 14-3-3 proteins are localized in neurons, and are axonally transported to the nerve terminals. They may be also present, at lower levels, in various other eukaryotic tissues.
 ISOFORM DELTA DIFFERS FROM ISOFORM ZETA IN BEING PHOSPHORYLATED (BY SIMILARITY).
 Belongs to the 14-3-3 family.
 WAS ORIGINALLY (REF.1) THOUGHT TO HAVE PHOSPHOLIPASE A2 ACTIVITY.
SUBCELLULAR LOCATION comments:
 Cytoplasmic.
TISSUE SPECIFICITY comments:
 14-3-3 proteins are localized in neurons, and are axonally transported to the nerve terminals. They may be also present, at lower levels, in various other eukaryotic tissues.
SIMILARITY comments:
 Belongs to the 14-3-3 family.
FUNCTION comments:
 ACTIVATES TYROSINE AND TRYPTOPHAN HYDROXYLASES IN THE PRESENCE OF CA(2+)/CALMODULIN-DEPENDENT PROTEIN KINASE II, AND STRONGLY ACTIVATES PROTEIN KINASE C. IS PROBABLY A MULTIFUNCTIONAL REGULATOR OF THE CELL SIGNALING PROCESSES MEDIATED BY BOTH KINASES. ACTIVATES THE ADP-RIBOSYLTRANSFERASE (EXOS) ACTIVITY OF BACTERIAL ORIGIN.
SUBUNIT comments:
 Homodimer.
PTM comments:
 ISOFORM DELTA DIFFERS FROM ISOFORM ZETA IN BEING PHOSPHORYLATED (BY SIMILARITY).
CAUTION comments:
 WAS ORIGINALLY (REF.1) THOUGHT TO HAVE PHOSPHOLIPASE A2 ACTIVITY.
GenBank/EMBL: M86400, U28964, BC003623, L07955,
acc from M86400: P29312
PDB: 1A37, 1A38, 1A4O, 1QJA, 1QJB, 1IB1,
All features:
MOD_RES	0	1	ACETYLATION (BY SIMILARITY)
MOD_RES	183	184	PHOSPHORYLATION (BY SIMILARITY)
CONFLICT	24	25	C -> A (IN REF. 4)
HELIX	2	16	n/a
TURN	16	17	n/a
HELIX	18	31	n/a
TURN	31	32	n/a
HELIX	37	68	n/a
TURN	68	71	n/a
HELIX	72	103	n/a
TURN	103	104	n/a
HELIX	104	108	n/a
HELIX	111	131	n/a
TURN	131	132	n/a
HELIX	137	159	n/a
TURN	161	163	n/a
HELIX	164	180	n/a
TURN	180	181	n/a
HELIX	184	201	n/a
HELIX	202	205	n/a
TURN	207	210	n/a
HELIX	210	229	n/a
title: Cloning and expression of a human 14-3-3 protein mediating phospholipolysis. Identification of an arachidonoyl-enzyme intermediate during catalysis.
authors: Zupan L.A.,  Steffens D.L.,  Berry C.A.,  Landt M.L.,  Gross R.W., 
location: J. Biol. Chem. 267:8707-8710(1992).
pubMed: 1577711
title: Two unique 5' untranslated regions in mRNAs encoding human 14-3-3 zeta: differential expression in hemopoietic cells.
authors: Seluja G.A.,  Pietromonaco S.F.,  Elias L., 
location: Biochim. Biophys. Acta 1395:281-287(1998).
pubMed: 9512661
title: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.
authors: Strausberg R.L.,  Feingold E.A.,  Grouse L.H.,  Derge J.G.,  Klausner R.D.,  Collins F.S.,  Wagner L.,  Shenmen C.M.,  Schuler G.D.,  Altschul S.F.,  Zeeberg B.,  Buetow K.H.,  Schaefer C.F.,  Bhat N.K.,  Hopkins R.F.,  Jordan H.,  Moore T.,  Max S.I.,  Wang J.,  Hsieh F.,  Diatchenko L.,  Marusina K.,  Farmer A.A.,  Rubin G.M.,  Hong L.,  Stapleton M.,  Soares M.B.,  Bonaldo M.F.,  Casavant T.L.,  Scheetz T.E.,  Brownstein M.J.,  Usdin T.B.,  Toshiyuki S.,  Carninci P.,  Prange C.,  Raha S.S.,  Loquellano N.A.,  Peters G.J.,  Abramson R.D.,  Mullahy S.J.,  Bosak S.A.,  McEwan P.J.,  McKernan K.J.,  Malek J.A.,  Gunaratne P.H.,  Richards S.,  Worley K.C.,  Hale S.,  Garcia A.M.,  Gay L.J.,  Hulyk S.W.,  Villalon D.K.,  Muzny D.M.,  Sodergren E.J.,  Lu X.,  Gibbs R.A.,  Fahey J.,  Helton E.,  Ketteman M.,  Madan A.,  Rodrigues S.,  Sanchez A.,  Whiting M.,  Madan A.,  Young A.C.,  Shevchenko Y.,  Bouffard G.G.,  Blakesley R.W.,  Touchman J.W.,  Green E.D.,  Dickson M.C.,  Rodriguez A.C.,  Grimwood J.,  Schmutz J.,  Myers R.M.,  Butterfield Y.S.N.,  Krzywinski M.I.,  Skalska U.,  Smailus D.E.,  Schnerch A.,  Schein J.E.,  Jones S.J.M.,  Marra M.A., 
location: Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
pubMed: 12477932
title: The eukaryotic host factor that activates exoenzyme S of Pseudomonas aeruginosa is a member of the 14-3-3 protein family.
authors: Fu H.,  Coburn J.,  Collier R.J., 
location: Proc. Natl. Acad. Sci. U.S.A. 90:2320-2324(1993).
pubMed: 8460141
title: Activation of protein kinase C by the 14-3-3 proteins homologous with Exo1 protein that stimulates calcium-dependent exocytosis.
authors: Isobe T.,  Hiyane Y.,  Ichimura T.,  Okuyama T.,  Takahashi N.,  Nakajo S.,  Nakaya K., 
location: FEBS Lett. 308:121-124(1992).
pubMed: 1499718
title: Crystal structure of the zeta isoform of the 14-3-3 protein.
authors: Liu D.,  Blenkowska J.,  Petosa C.,  Collier R.J.,  Fu H.,  Liddington R., 
location: Nature 376:191-194(1995).
pubMed: 7603574
title: Structural analysis of 14-3-3 phosphopeptide complexes identifies a dual role for the nuclear export signal of 14-3-3 in ligand binding.
authors: Rittinger K.,  Budman J.,  Xu J.,  Volinia S.,  Cantley L.C.,  Smerdon S.J.,  Gamblin S.J.,  Yaffe M.B., 
location: Mol. Cell 4:153-166(1999).
pubMed: 10488331
other accs associated with last reference:
	  (1): P29312
