P29361 (1433Z_SHEEP) Reviewed, UniProtKB/Swiss-Prot
Last modified April 3, 2013. Version 86. History...
Names and origin
|Protein names||Recommended name:|
14-3-3 protein zeta/delta
Protein kinase C inhibitor protein 1
|Organism||Ovis aries (Sheep)|
|Taxonomic identifier||9940 [NCBI]|
|Taxonomic lineage||Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Caprinae › Ovis|
|Sequence length||245 AA.|
|Protein existence||Evidence at protein level|
General annotation (Comments)
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.
Homodimer. Heterodimerizes with YWHAE By similarity. Homo- and hetero-dimerization is inhibited by phosphorylation on Ser-58 By similarity. Interacts with FOXO4, NOXA1, SSH1 and ARHGEF2. Interacts with CDK16 and with WEE1 (C-terminal). Interacts with MLF1 (phosphorylated form); the interaction retains it in the cytoplasm. Interacts with BSPRY. Interacts with Thr-phosphorylated ITGB2. Interacts with Pseudomonas aeruginosa exoS (unphosphorylated form). Interacts with BAX; the interaction occurs in the cytoplasm. Under stress conditions, MAPK8-mediated phosphorylation releases BAX to mitochondria. Interacts with phosphorylated RAF1; the interaction is inhibited when YWHAZ is phosphorylated on Thr-232. Interacts with TP53; the interaction enhances p53 transcriptional activity. The Ser-58 phosphorylated form inhibits this interaction and p53 transcriptional activity. Interacts with ABL1 (phosphorylated form); the interaction retains ABL1 in the cytoplasm. Interacts with PKA-phosphorylated AANAT; the interaction modulates AANAT enzymatic activity by increasing affinity for arylalkylamines and acetyl-CoA and protecting the enzyme from dephosphorylation and proteasomal degradation. It may also prevent thiol-dependent inactivation. Interacts with AKT1; the interaction phosphorylates YWHAZ and modulates dimerization By similarity. Interacts with GAB2 and SAMSN1 By similarity. Interacts with BCL2L11. Binds to TLK2 By similarity. Ref.5
Highly expressed in brain (at protein level).
The delta, brain-specific form differs from the zeta form in being phosphorylated By similarity. Phosphorylation on Ser-184 by MAPK8; promotes dissociation of BAX and translocation of BAX to mitochondria. Phosphorylation on Thr-232; inhibits binding of RAF1 By similarity. Phosphorylated on Ser-58 by PKA and protein kinase C delta type catalytic subunit in a sphingosine-dependent fashion. Phosphorylation on Ser-58 by PKA; disrupts homodimerization and heterodimerization with YHAE and TP53 By similarity. Ref.3
Belongs to the 14-3-3 family.
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Chain||1 – 245||245||14-3-3 protein zeta/delta||PRO_0000058631|
|Site||56||1||Interaction with phosphoserine on interacting protein By similarity|
|Site||127||1||Interaction with phosphoserine on interacting protein By similarity|
Amino acid modifications
|Modified residue||1||1||N-acetylmethionine Ref.1|
|Modified residue||3||1||N6-acetyllysine By similarity|
|Modified residue||58||1||Phosphoserine; by PKA By similarity|
|Modified residue||68||1||N6-acetyllysine By similarity|
|Modified residue||184||1||Phosphoserine Ref.3|
|Modified residue||207||1||Phosphoserine By similarity|
|Modified residue||232||1||Phosphothreonine; by CK1 By similarity|
|||"Multiple isoforms of a protein kinase C inhibitor (KCIP-1/14-3-3) from sheep brain. Amino acid sequence of phosphorylated forms."|
Toker A., Sellers L.A., Amess B., Patel Y., Harris A., Aitken A.
Eur. J. Biochem. 206:453-461(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
|||"Protein kinase C inhibitor proteins. Purification from sheep brain and sequence similarity to lipocortins and 14-3-3 protein."|
Toker A., Ellis C.A., Sellers L.A., Aitken A.
Eur. J. Biochem. 191:421-429(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-22 AND 122-137.
|||"14-3-3 alpha and delta are the phosphorylated forms of raf-activating 14-3-3 beta and zeta. In vivo stoichiometric phosphorylation in brain at a Ser-Pro-Glu-Lys motif."|
Aitken A., Howell S., Jones D., Madrazo J., Patel Y.
J. Biol. Chem. 270:5706-5709(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-184.
|||"Electrospray mass spectroscopy analysis with online trapping of posttranslationally modified mammalian and avian brain 14-3-3 isoforms."|
Aitken A., Patel Y., Martin H., Jones D., Robinson K., Madrazo J., Howell S.
J. Protein Chem. 13:463-465(1994)
Cited for: POST-TRANSLATIONAL MODIFICATIONS.
|||"Role of a pineal cAMP-operated arylalkylamine N-acetyltransferase/14-3-3-binding switch in melatonin synthesis."|
Ganguly S., Gastel J.A., Weller J.L., Schwartz C., Jaffe H., Namboodiri M.A., Coon S.L., Hickman A.B., Rollag M., Obsil T., Beauverger P., Ferry G., Boutin J.A., Klein D.C.
Proc. Natl. Acad. Sci. U.S.A. 98:8083-8088(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AANAT.
3D structure databases
|SMR||P29361. Positions 1-232. |
Protocols and materials databases
Family and domain databases
|Gene3D||126.96.36.199. 1 hit. |
|InterPro||IPR000308. 14-3-3. |
|PANTHER||PTHR18860. PTHR18860. 1 hit. |
|Pfam||PF00244. 14-3-3. 1 hit. |
|PIRSF||PIRSF000868. 14-3-3. 1 hit. |
|PRINTS||PR00305. 1433ZETA. |
|SMART||SM00101. 14_3_3. 1 hit. |
|SUPFAM||SSF48445. 14-3-3. 1 hit. |
|PROSITE||PS00796. 1433_1. 1 hit. |
PS00797. 1433_2. 1 hit.
|Accession||Primary (citable) accession number: P29361|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Chordata Protein Annotation Program|
Index of protein domains and families