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Protein

14-3-3 protein zeta/delta

Gene

YWHAZ

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei56 – 561Interaction with phosphoserine on interacting protein
Sitei127 – 1271Interaction with phosphoserine on interacting protein

GO - Molecular functioni

  1. poly(A) RNA binding Source: Ensembl
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_271382. GP1b-IX-V activation signalling.
REACT_284336. Translocation of GLUT4 to the plasma membrane.
REACT_286999. Interleukin-3, 5 and GM-CSF signaling.
REACT_295837. deactivation of the beta-catenin transactivating complex.
REACT_305658. Activation of BAD and translocation to mitochondria.
REACT_306445. KSRP destabilizes mRNA.
REACT_348169. Rap1 signalling.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:YWHAZ
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136 Componenti: Chromosome 14

Subcellular locationi

  1. Cytoplasm
  2. Melanosome

  3. Note: Located to stage I to stage IV melanosomes.By similarity

GO - Cellular componenti

  1. blood microparticle Source: Ensembl
  2. extracellular vesicular exosome Source: Ensembl
  3. focal adhesion Source: Ensembl
  4. melanosome Source: UniProtKB-SubCell
  5. nucleus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 24524514-3-3 protein zeta/deltaPRO_0000058626Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei3 – 31N6-acetyllysineBy similarity
Modified residuei58 – 581Phosphoserine; by PKABy similarity
Modified residuei68 – 681N6-acetyllysineBy similarity
Modified residuei184 – 1841PhosphoserineBy similarity
Modified residuei207 – 2071PhosphoserineBy similarity
Modified residuei232 – 2321Phosphothreonine; by CK1By similarity

Post-translational modificationi

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).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP63103.
PRIDEiP63103.

Interactioni

Subunit structurei

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.By similarity2 Publications

Protein-protein interaction databases

BioGridi160005. 1 interaction.
IntActiP63103. 10 interactions.
MINTiMINT-99823.
STRINGi9913.ENSBTAP00000000289.

Structurei

Secondary structure

1
245
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1513Combined sources
Helixi19 – 3012Combined sources
Turni31 – 333Combined sources
Helixi38 – 6730Combined sources
Helixi74 – 10330Combined sources
Turni104 – 1074Combined sources
Helixi112 – 1154Combined sources
Helixi117 – 13115Combined sources
Helixi137 – 15620Combined sources
Turni157 – 1593Combined sources
Helixi165 – 18016Combined sources
Helixi185 – 20117Combined sources
Turni202 – 2054Combined sources
Turni208 – 2103Combined sources
Helixi211 – 22616Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP63103.
SMRiP63103. Positions 1-230.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP63103.

Family & Domainsi

Sequence similaritiesi

Belongs to the 14-3-3 family.Curated

Phylogenomic databases

eggNOGiCOG5040.
GeneTreeiENSGT00760000119116.
HOGENOMiHOG000240379.
HOVERGENiHBG050423.
InParanoidiP63103.
KOiK16197.
OMAiRYDDMAG.
OrthoDBiEOG7HHWT3.
TreeFamiTF102003.

Family and domain databases

InterProiIPR000308. 14-3-3.
IPR023409. 14-3-3_CS.
IPR023410. 14-3-3_domain.
[Graphical view]
PANTHERiPTHR18860. PTHR18860. 1 hit.
PfamiPF00244. 14-3-3. 1 hit.
[Graphical view]
PIRSFiPIRSF000868. 14-3-3. 1 hit.
PRINTSiPR00305. 1433ZETA.
SMARTiSM00101. 14_3_3. 1 hit.
[Graphical view]
SUPFAMiSSF48445. SSF48445. 1 hit.
PROSITEiPS00796. 1433_1. 1 hit.
PS00797. 1433_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P63103-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDKNELVQKA KLAEQAERYD DMAACMKSVT EQGAELSNEE RNLLSVAYKN
60 70 80 90 100
VVGARRSSWR VVSSIEQKTE GAEKKQQMAR EYREKIETEL RDICNDVLSL
110 120 130 140 150
LEKFLIPNAS QAESKVFYLK MKGDYYRYLA EVAAGDDKKG IVDQSQQAYQ
160 170 180 190 200
EAFEISKKEM QPTHPIRLGL ALNFSVFYYE ILNSPEKACS LAKTAFDEAI
210 220 230 240
AELDTLSEES YKDSTLIMQL LRDNLTLWTS DTQGDEAEAG EGGEN
Length:245
Mass (Da):27,745
Last modified:September 13, 2004 - v1
Checksum:iD464DF2286BBFE60
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 251C → A AA sequence (PubMed:1499718).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07955 mRNA. Translation: AAA30514.1.
BC102382 mRNA. Translation: AAI02383.1.
PIRiA47389.
S65013.
RefSeqiNP_777239.1. NM_174814.2.
UniGeneiBt.111451.

Genome annotation databases

EnsembliENSBTAT00000000289; ENSBTAP00000000289; ENSBTAG00000000236.
GeneIDi287022.
KEGGibta:287022.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07955 mRNA. Translation: AAA30514.1.
BC102382 mRNA. Translation: AAI02383.1.
PIRiA47389.
S65013.
RefSeqiNP_777239.1. NM_174814.2.
UniGeneiBt.111451.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP63103.
SMRiP63103. Positions 1-230.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi160005. 1 interaction.
IntActiP63103. 10 interactions.
MINTiMINT-99823.
STRINGi9913.ENSBTAP00000000289.

Proteomic databases

PaxDbiP63103.
PRIDEiP63103.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000000289; ENSBTAP00000000289; ENSBTAG00000000236.
GeneIDi287022.
KEGGibta:287022.

Organism-specific databases

CTDi7534.

Phylogenomic databases

eggNOGiCOG5040.
GeneTreeiENSGT00760000119116.
HOGENOMiHOG000240379.
HOVERGENiHBG050423.
InParanoidiP63103.
KOiK16197.
OMAiRYDDMAG.
OrthoDBiEOG7HHWT3.
TreeFamiTF102003.

Enzyme and pathway databases

ReactomeiREACT_271382. GP1b-IX-V activation signalling.
REACT_284336. Translocation of GLUT4 to the plasma membrane.
REACT_286999. Interleukin-3, 5 and GM-CSF signaling.
REACT_295837. deactivation of the beta-catenin transactivating complex.
REACT_305658. Activation of BAD and translocation to mitochondria.
REACT_306445. KSRP destabilizes mRNA.
REACT_348169. Rap1 signalling.

Miscellaneous databases

EvolutionaryTraceiP63103.
NextBioi20806544.
PROiP63103.

Family and domain databases

InterProiIPR000308. 14-3-3.
IPR023409. 14-3-3_CS.
IPR023410. 14-3-3_domain.
[Graphical view]
PANTHERiPTHR18860. PTHR18860. 1 hit.
PfamiPF00244. 14-3-3. 1 hit.
[Graphical view]
PIRSFiPIRSF000868. 14-3-3. 1 hit.
PRINTSiPR00305. 1433ZETA.
SMARTiSM00101. 14_3_3. 1 hit.
[Graphical view]
SUPFAMiSSF48445. SSF48445. 1 hit.
PROSITEiPS00796. 1433_1. 1 hit.
PS00797. 1433_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry namei1433Z_BOVIN
AccessioniPrimary (citable) accession number: P63103
Secondary accession number(s): P29213, P29312, Q3ZCF9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: September 13, 2004
Last modified: April 29, 2015
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.