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P63103

- 1433Z_BOVIN

UniProt

P63103 - 1433Z_BOVIN

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
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 1 (13 Sep 2004)
      Previous versions | rss
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    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

    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

    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 – 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP63103.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the 14-3-3 family.Curated

    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

    Experimental Info

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

    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...
    MobiDBi 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

    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: October 1, 2014
    This is version 95 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