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P63103 (1433Z_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
14-3-3 protein zeta/delta
Alternative name(s):
Factor activating exoenzyme S
Short name=FAS
Protein kinase C inhibitor protein 1
Short name=KCIP-1
Gene names
Name:YWHAZ
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length245 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Activates the ADP-ribosyltransferase (exoS) activity of bacterial origin. Ref.4

Subunit structure

Homodimer. Heterodimerizes with YWHAE By similarity. Homo- and hetero-dimerization is inhibited by phosphorylation on Ser-58 By similarity. Interacts with FOXO4, NOXA1, SSH1 ARHGEF2, CDK16 and BSPRY. Interacts with WEE1 (C-terminal). Interacts with MLF1 (phosphorylated form); the interaction retains it in the cytoplasm. Interacts with BAX; the interaction occurs in the cytoplasm. Under stress conditions, MAPK8-mediated phosphorylation releases BAX to mitochondria. 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 By similarity. Interacts with AKT1; the interaction phosphorylates YWHAZ and modulates dimerization By similarity. Interacts with GAB2. Interacts with BCL2L11, SAMSN1 and TLK2 By similarity. Interacts with phosphorylated RAF1; the interaction is inhibited when YWHAZ is phosphorylated on Thr-232. Interacts with Thr-phosphorylated ITGB2. Ref.6 Ref.7

Subcellular location

Cytoplasm. Melanosome. Note: Located to stage I to stage IV melanosomes By similarity.

Post-translational modification

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.

Sequence similarities

Belongs to the 14-3-3 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 24524514-3-3 protein zeta/delta
PRO_0000058626

Sites

Site561Interaction with phosphoserine on interacting protein
Site1271Interaction with phosphoserine on interacting protein

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue31N6-acetyllysine By similarity
Modified residue581Phosphoserine; by PKA By similarity
Modified residue681N6-acetyllysine By similarity
Modified residue1841Phosphoserine By similarity
Modified residue2071Phosphoserine By similarity
Modified residue2321Phosphothreonine; by CK1 By similarity

Experimental info

Sequence conflict251C → A AA sequence Ref.1

Secondary structure

.......................... 245
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P63103 [UniParc].

Last modified September 13, 2004. Version 1.
Checksum: D464DF2286BBFE60

FASTA24527,745
        10         20         30         40         50         60 
MDKNELVQKA KLAEQAERYD DMAACMKSVT EQGAELSNEE RNLLSVAYKN VVGARRSSWR 

        70         80         90        100        110        120 
VVSSIEQKTE GAEKKQQMAR EYREKIETEL RDICNDVLSL LEKFLIPNAS QAESKVFYLK 

       130        140        150        160        170        180 
MKGDYYRYLA EVAAGDDKKG IVDQSQQAYQ EAFEISKKEM QPTHPIRLGL ALNFSVFYYE 

       190        200        210        220        230        240 
ILNSPEKACS LAKTAFDEAI AELDTLSEES YKDSTLIMQL LRDNLTLWTS DTQGDEAEAG 


EGGEN 

« Hide

References

« Hide 'large scale' references
[1]"Activation of protein kinase C by the 14-3-3 proteins homologous with Exo1 protein that stimulates calcium-dependent exocytosis."
Isobe T., Hiyane Y., Ichimura T., Okuyama T., Takahashi N., Nakajo S., Nakaya K.
FEBS Lett. 308:121-124(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Brain.
[2]"The eukaryotic host factor that activates exoenzyme S of Pseudomonas aeruginosa is a member of the 14-3-3 protein family."
Fu H., Coburn J., Collier R.J.
Proc. Natl. Acad. Sci. U.S.A. 90:2320-2324(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 104-115; 140-157 AND 194-212.
Tissue: Brain.
[3]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Crossbred X Angus.
Tissue: Ileum.
[4]"Activation of protein kinase C by purified bovine brain 14-3-3: comparison with tyrosine hydroxylase activation."
Tanji M., Horwitz R., Rosenfeld G., Waymire J.C.
J. Neurochem. 63:1908-1916(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"Crystal structure of the zeta isoform of the 14-3-3 protein."
Liu D., Blenkowska J., Petosa C., Collier R.J., Fu H., Liddington R.
Nature 376:191-194(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[6]"14-3-3zeta binds a phosphorylated Raf peptide and an unphosphorylated peptide via its conserved amphipathic groove."
Petosa C., Masters S.C., Bankston L.A., Pohl J., Wang B., Fu H., Liddington R.C.
J. Biol. Chem. 273:16305-16310(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS) IN COMPLEX WITH PHOSPHORYLATED RAF1, INTERACTION WITH PHOSPHOSERINE PEPTIDE, SUBUNIT.
[7]"Beta2 integrin phosphorylation on Thr758 acts as a molecular switch to regulate 14-3-3 and filamin binding."
Takala H., Nurminen E., Nurmi S.M., Aatonen M., Strandin T., Takatalo M., Kiema T., Gahmberg C.G., Ylaenne J., Fagerholm S.C.
Blood 112:1853-1862(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH PHOSPHORYLATED ITGB2, INTERACTION WITH PHOSPHORYLATED ITGB2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L07955 mRNA. Translation: AAA30514.1.
BC102382 mRNA. Translation: AAI02383.1.
PIRA47389.
S65013.
RefSeqNP_777239.1. NM_174814.2.
XP_005215672.1. XM_005215615.1.
UniGeneBt.111451.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A37X-ray3.60A/B1-245[»]
1A38X-ray3.35A/B1-245[»]
1A4OX-ray2.80A/B/C/D1-245[»]
2V7DX-ray2.50A/B/C/D1-245[»]
ProteinModelPortalP63103.
SMRP63103. Positions 1-230.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid160005. 1 interaction.
IntActP63103. 10 interactions.
MINTMINT-99823.
STRING9913.ENSBTAP00000000289.

Proteomic databases

PaxDbP63103.
PRIDEP63103.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000000289; ENSBTAP00000000289; ENSBTAG00000000236.
GeneID287022.
KEGGbta:287022.

Organism-specific databases

CTD7534.

Phylogenomic databases

eggNOGCOG5040.
GeneTreeENSGT00730000110424.
HOGENOMHOG000240379.
HOVERGENHBG050423.
InParanoidP63103.
KOK16197.
OMARYDDMAG.
OrthoDBEOG7HHWT3.
TreeFamTF102003.

Family and domain databases

Gene3D1.20.190.20. 1 hit.
InterProIPR000308. 14-3-3.
IPR023409. 14-3-3_CS.
IPR023410. 14-3-3_domain.
[Graphical view]
PANTHERPTHR18860. PTHR18860. 1 hit.
PfamPF00244. 14-3-3. 1 hit.
[Graphical view]
PIRSFPIRSF000868. 14-3-3. 1 hit.
PRINTSPR00305. 1433ZETA.
SMARTSM00101. 14_3_3. 1 hit.
[Graphical view]
SUPFAMSSF48445. SSF48445. 1 hit.
PROSITEPS00796. 1433_1. 1 hit.
PS00797. 1433_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP63103.
NextBio20806544.

Entry information

Entry name1433Z_BOVIN
AccessionPrimary (citable) accession number: P63103
Secondary accession number(s): P29213, P29312, Q3ZCF9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: September 13, 2004
Last modified: February 19, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references