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P63103

- 1433Z_BOVIN

UniProt

P63103 - 1433Z_BOVIN

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Protein
14-3-3 protein zeta/delta
Gene
YWHAZ
Organism
Bos taurus (Bovine)
Status
Reviewed - 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 - Biological processi

  1. protein targeting Source: Ensembl
  2. regulation of cell death Source: Ensembl
Complete GO annotation...

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: Chromosome 14

Subcellular locationi

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

GO - Cellular componenti

  1. extracellular vesicular exosome Source: Ensembl
  2. melanosome Source: UniProtKB-SubCell
  3. mitochondrion Source: Ensembl
  4. 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/delta
PRO_0000058626Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine By similarity
Modified residuei3 – 31N6-acetyllysine By similarity
Modified residuei58 – 581Phosphoserine; by PKA By similarity
Modified residuei68 – 681N6-acetyllysine By similarity
Modified residuei184 – 1841Phosphoserine By similarity
Modified residuei207 – 2071Phosphoserine By similarity
Modified residuei232 – 2321Phosphothreonine; by CK1 By 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.

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 ITGB2.2 Publications

Protein-protein interaction databases

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

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP63103.

Family & Domainsi

Sequence similaritiesi

Belongs to the 14-3-3 family.

Phylogenomic databases

eggNOGiCOG5040.
GeneTreeiENSGT00730000110424.
HOGENOMiHOG000240379.
HOVERGENiHBG050423.
InParanoidiP63103.
KOiK16197.
OMAiRYDDMAG.
OrthoDBiEOG7HHWT3.
TreeFamiTF102003.

Family and domain databases

Gene3Di1.20.190.20. 1 hit.
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

MDKNELVQKA KLAEQAERYD DMAACMKSVT EQGAELSNEE RNLLSVAYKN    50
VVGARRSSWR VVSSIEQKTE GAEKKQQMAR EYREKIETEL RDICNDVLSL 100
LEKFLIPNAS QAESKVFYLK MKGDYYRYLA EVAAGDDKKG IVDQSQQAYQ 150
EAFEISKKEM QPTHPIRLGL ALNFSVFYYE ILNSPEKACS LAKTAFDEAI 200
AELDTLSEES YKDSTLIMQL LRDNLTLWTS DTQGDEAEAG EGGEN 245
Length:245
Mass (Da):27,745
Last modified:September 13, 2004 - v1
Checksum:iD464DF2286BBFE60
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 251C → A AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L07955 mRNA. Translation: AAA30514.1.
BC102382 mRNA. Translation: AAI02383.1.
PIRiA47389.
S65013.
RefSeqiNP_777239.1. NM_174814.2.
XP_005215672.1. XM_005215615.1.
UniGeneiBt.111451.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L07955 mRNA. Translation: AAA30514.1 .
BC102382 mRNA. Translation: AAI02383.1 .
PIRi A47389.
S65013.
RefSeqi NP_777239.1. NM_174814.2.
XP_005215672.1. XM_005215615.1.
UniGenei Bt.111451.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1A37 X-ray 3.60 A/B 1-245 [» ]
1A38 X-ray 3.35 A/B 1-245 [» ]
1A4O X-ray 2.80 A/B/C/D 1-245 [» ]
2V7D X-ray 2.50 A/B/C/D 1-245 [» ]
ProteinModelPortali P63103.
SMRi P63103. Positions 1-230.
ModBasei Search...

Protein-protein interaction databases

BioGridi 160005. 1 interaction.
IntActi P63103. 10 interactions.
MINTi MINT-99823.
STRINGi 9913.ENSBTAP00000000289.

Proteomic databases

PaxDbi P63103.
PRIDEi P63103.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSBTAT00000000289 ; ENSBTAP00000000289 ; ENSBTAG00000000236 .
GeneIDi 287022.
KEGGi bta:287022.

Organism-specific databases

CTDi 7534.

Phylogenomic databases

eggNOGi COG5040.
GeneTreei ENSGT00730000110424.
HOGENOMi HOG000240379.
HOVERGENi HBG050423.
InParanoidi P63103.
KOi K16197.
OMAi RYDDMAG.
OrthoDBi EOG7HHWT3.
TreeFami TF102003.

Miscellaneous databases

EvolutionaryTracei P63103.
NextBioi 20806544.

Family and domain databases

Gene3Di 1.20.190.20. 1 hit.
InterProi IPR000308. 14-3-3.
IPR023409. 14-3-3_CS.
IPR023410. 14-3-3_domain.
[Graphical view ]
PANTHERi PTHR18860. PTHR18860. 1 hit.
Pfami PF00244. 14-3-3. 1 hit.
[Graphical view ]
PIRSFi PIRSF000868. 14-3-3. 1 hit.
PRINTSi PR00305. 1433ZETA.
SMARTi SM00101. 14_3_3. 1 hit.
[Graphical view ]
SUPFAMi SSF48445. SSF48445. 1 hit.
PROSITEi PS00796. 1433_1. 1 hit.
PS00797. 1433_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: May 14, 2014
This is version 94 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

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