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P63104

- 1433Z_HUMAN

UniProt

P63104 - 1433Z_HUMAN

Protein

14-3-3 protein zeta/delta

Gene

YWHAZ

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (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.5 Publications

    Sites

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

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. protein kinase binding Source: UniProtKB
    5. transcription factor binding Source: UniProtKB

    GO - Biological processi

    1. apoptotic process Source: Reactome
    2. blood coagulation Source: Reactome
    3. gene expression Source: Reactome
    4. histamine secretion by mast cell Source: Ensembl
    5. intrinsic apoptotic signaling pathway Source: Reactome
    6. membrane organization Source: Reactome
    7. mRNA metabolic process Source: Reactome
    8. negative regulation of apoptotic process Source: ProtInc
    9. platelet activation Source: Reactome
    10. positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway Source: Reactome
    11. protein targeting to mitochondrion Source: Ensembl
    12. response to drug Source: Ensembl
    13. RNA metabolic process Source: Reactome
    14. signal transduction Source: ProtInc

    Enzyme and pathway databases

    ReactomeiREACT_147867. Translocation of GLUT4 to the plasma membrane.
    REACT_200731. deactivation of the beta-catenin transactivating complex.
    REACT_23837. Interleukin-3, 5 and GM-CSF signaling.
    REACT_23847. GP1b-IX-V activation signalling.
    REACT_23898. Rap1 signalling.
    REACT_25042. KSRP destabilizes mRNA.
    SignaLinkiP63104.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    14-3-3 protein zeta/delta
    Alternative name(s):
    Protein kinase C inhibitor protein 1
    Short name:
    KCIP-1
    Gene namesi
    Name:YWHAZ
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:12855. YWHAZ.

    Subcellular locationi

    Cytoplasm 1 Publication. Melanosome 1 Publication
    Note: Located to stage I to stage IV melanosomes.

    GO - Cellular componenti

    1. blood microparticle Source: UniProt
    2. cell leading edge Source: Ensembl
    3. cytoplasm Source: ProtInc
    4. cytoplasmic vesicle membrane Source: Reactome
    5. cytosol Source: Reactome
    6. extracellular space Source: UniProt
    7. extracellular vesicular exosome Source: UniProtKB
    8. mast cell granule Source: GOC
    9. melanosome Source: UniProtKB-SubCell
    10. mitochondrion Source: Ensembl
    11. nucleoplasm Source: Reactome
    12. nucleus Source: UniProt
    13. perinuclear region of cytoplasm Source: Ensembl
    14. postsynaptic density Source: Ensembl
    15. protein complex Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi49 – 491K → E: Loss of interaction with NOXA1. 1 Publication
    Mutagenesisi58 – 581S → A: Loss of sphingosine-activated PKA phosphorylation. Promotes homodimerization and heterodimerization with YWHAE. Enhanced transcriptional activity of P53. 2 Publications
    Mutagenesisi58 – 581S → E: Loss of homodimerization. Reduced dimerization with YWHAE. Significantly reduced interaction with P53. No enhancement of P53 transcriptional activity. 2 Publications
    Mutagenesisi184 – 1841S → A: On DNA damage, loss of MAPK8-mediated phosphorylation. Loss of binding ABL1. Attenuates ABL1-mediated apoptosis. No loss of interaction with BAX under stress conditions. Inhibits translocation of BAX to mitochondria. 2 Publications

    Organism-specific databases

    PharmGKBiPA37444.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 24524514-3-3 protein zeta/deltaPRO_0000058627Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine4 Publications
    Modified residuei3 – 31N6-acetyllysine1 Publication
    Modified residuei58 – 581Phosphoserine; by PKA and PKB/AKT14 Publications
    Modified residuei68 – 681N6-acetyllysine1 Publication
    Modified residuei184 – 1841Phosphoserine; by MAPK82 Publications
    Modified residuei207 – 2071Phosphoserine2 Publications
    Modified residuei232 – 2321Phosphothreonine; by CK12 Publications

    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. 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 similarity9 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP63104.
    PaxDbiP63104.
    PRIDEiP63104.

    2D gel databases

    DOSAC-COBS-2DPAGEP63104.
    OGPiP63104.
    UCD-2DPAGEP63104.

    PTM databases

    PhosphoSiteiP63104.

    Expressioni

    Gene expression databases

    ArrayExpressiP63104.
    BgeeiP63104.
    GenevestigatoriP63104.

    Organism-specific databases

    HPAiCAB005065.

    Interactioni

    Subunit structurei

    Interacts with CDK16 and BSPRY By similarity. Interacts with WEE1 (C-terminal). Interacts with SAMSN1 By similarity. Interacts with MLF1 (phosphorylated form); the interaction retains it in the cytoplasm By similarity. Interacts with Thr-phosphorylated ITGB2 By similarity. Interacts with BCL2L11 By similarity. Homodimer. Heterodimerizes with YWHAE. Homo- and hetero-dimerization is inhibited by phosphorylation on Ser-58. Interacts with FOXO4, NOXA1, SSH1 and ARHGEF2. 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. Interacts with GAB2 and TLK2.By similarity18 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-347088,EBI-347088
    AANATQ294953EBI-347088,EBI-446413From a different organism.
    ABL1P005192EBI-347088,EBI-375543
    ACTBP607093EBI-347088,EBI-353944
    ADAM22Q9P0K13EBI-347088,EBI-1567236
    ADAM22Q9P0K1-33EBI-347088,EBI-1567267
    ARAFP103983EBI-347088,EBI-365961
    ARHGEF2Q929742EBI-347088,EBI-302405
    ATP5A1P257053EBI-347088,EBI-351437
    ATP5BP065762EBI-347088,EBI-356231
    BADQ929345EBI-347088,EBI-700771
    BadQ613373EBI-347088,EBI-400328From a different organism.
    BRAFP150563EBI-347088,EBI-365980
    CALM3P621582EBI-347088,EBI-397435
    CBX4O00257-32EBI-347088,EBI-4392727
    CDC25AP303042EBI-347088,EBI-747671
    CDC25BP303054EBI-347088,EBI-1051746
    CDK17Q005372EBI-347088,EBI-624648
    CDK18Q070022EBI-347088,EBI-746238
    CFL1P235283EBI-347088,EBI-352733
    CPS1P313272EBI-347088,EBI-536811
    CSNK1A1P678284EBI-347088,EBI-7540603From a different organism.
    EEF1A1P681042EBI-347088,EBI-352162
    EGFRP005334EBI-347088,EBI-297353
    ENO1P067332EBI-347088,EBI-353877
    FSCN1Q166583EBI-347088,EBI-351076
    GCH1P307934EBI-347088,EBI-958183
    GSK3BP498414EBI-347088,EBI-373586
    Hap1P54256-24EBI-347088,EBI-994554From a different organism.
    HDAC4P565245EBI-347088,EBI-308629
    HDAC5Q9UQL62EBI-347088,EBI-715576
    HDAC7Q8WUI43EBI-347088,EBI-1048378
    HIST1H2AMP0C0S82EBI-347088,EBI-1390628
    HIST1H3DP684313EBI-347088,EBI-79722
    HIST2H4BP628053EBI-347088,EBI-302023
    HNRNPCP079102EBI-347088,EBI-357966
    HSPB1P047922EBI-347088,EBI-352682
    KIF23Q022415EBI-347088,EBI-306852
    LMNAP025452EBI-347088,EBI-351935
    LRRK2Q5S0079EBI-347088,EBI-5323863
    MAP3K5Q996833EBI-347088,EBI-476263
    MAPTP106368EBI-347088,EBI-366182
    MAPTP10636-39EBI-347088,EBI-7145070
    MAPTP291722EBI-347088,EBI-7291149From a different organism.
    MARK2Q7KZI76EBI-347088,EBI-516560
    MARK3P274489EBI-347088,EBI-707595
    NCLP193382EBI-347088,EBI-346967
    NPM1P067482EBI-347088,EBI-78579
    PARD3Q8TEW04EBI-347088,EBI-81968
    PRKCEQ021565EBI-347088,EBI-706254
    PRMT5O147442EBI-347088,EBI-351098
    RAF1P0404912EBI-347088,EBI-365996
    REPS2Q8NFH8-22EBI-347088,EBI-8029141
    RND3P6158711EBI-347088,EBI-1111534
    Rnd3P615883EBI-347088,EBI-6930266From a different organism.
    RPS3P233962EBI-347088,EBI-351193
    SFNP319472EBI-347088,EBI-476295
    SIK1P570594EBI-347088,EBI-1181640
    SIK3Q9Y2K25EBI-347088,EBI-1181460
    SORBS2O948752EBI-347088,EBI-311323
    STK11Q158316EBI-347088,EBI-306838
    STK25O005062EBI-347088,EBI-618295
    TGFBR1P368974EBI-347088,EBI-1027557
    TP53P046372EBI-347088,EBI-366083
    TSC2P498157EBI-347088,EBI-396587
    VCPP550722EBI-347088,EBI-355164
    VIMP086702EBI-347088,EBI-353844
    WEE1P302913EBI-347088,EBI-914695
    YAP1P469373EBI-347088,EBI-1044059
    YWHAEP622585EBI-347088,EBI-356498
    ZAKQ9NYL24EBI-347088,EBI-602273

    Protein-protein interaction databases

    BioGridi113366. 367 interactions.
    DIPiDIP-563N.
    IntActiP63104. 514 interactions.
    MINTiMINT-89071.

    Structurei

    Secondary structure

    1
    245
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 1513
    Helixi19 – 3113
    Helixi38 – 6730
    Turni69 – 713
    Helixi76 – 10328
    Helixi105 – 1084
    Helixi112 – 13120
    Helixi135 – 15925
    Helixi165 – 18016
    Helixi185 – 20016
    Helixi201 – 2055
    Turni208 – 2103
    Helixi211 – 22818

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1IB1X-ray2.70A/B/C/D1-245[»]
    1QJAX-ray2.00A/B1-245[»]
    1QJBX-ray2.00A/B1-245[»]
    2C1JX-ray2.60A/B1-245[»]
    2C1NX-ray2.00A/B1-245[»]
    2O02X-ray1.50A/B1-230[»]
    2WH0X-ray2.25A/B/C/D1-245[»]
    3CU8X-ray2.40A/B1-245[»]
    3NKXX-ray2.40A/B1-245[»]
    3RDHX-ray2.39A/B/C/D1-245[»]
    4BG6X-ray2.30A/B1-245[»]
    4FJ3X-ray1.95A/B1-230[»]
    4HKCX-ray2.20A1-245[»]
    4IHLX-ray2.20A/B1-230[»]
    4N7GX-ray2.25A1-230[»]
    4N7YX-ray2.16A/B1-230[»]
    4N84X-ray2.50A/B1-230[»]
    ProteinModelPortaliP63104.
    SMRiP63104. Positions 1-230.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP63104.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the 14-3-3 family.Curated

    Phylogenomic databases

    eggNOGiCOG5040.
    HOVERGENiHBG050423.
    InParanoidiP63104.
    KOiK16197.
    OrthoDBiEOG7HHWT3.
    PhylomeDBiP63104.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P63104-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « 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
    Isoform 2 (identifier: P63104-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-98: MDKNELVQKA...ELRDICNDVL → MSQPCRKLWRHNYETSSCIEFLK

    Note: No experimental confirmation available.

    Show »
    Length:170
    Mass (Da):19,333
    Checksum:iBE97CE3F0A74C75C
    GO

    Sequence cautioni

    The sequence AAH51814.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence AAH73141.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti22 – 221M → V in AAH68456. (PubMed:15489334)Curated
    Sequence conflicti136 – 1361D → G in BAH12451. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 9898MDKNE…CNDVL → MSQPCRKLWRHNYETSSCIE FLK in isoform 2. 1 PublicationVSP_047505Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M86400 mRNA. Translation: AAA36446.1.
    U28964 mRNA. Translation: AAC52052.1.
    AK289945 mRNA. Translation: BAF82634.1.
    AK296902 mRNA. Translation: BAH12451.1.
    CH471060 Genomic DNA. Translation: EAW91823.1.
    BC003623 mRNA. Translation: AAH03623.3.
    BC051814 mRNA. Translation: AAH51814.1. Different initiation.
    BC063824 mRNA. Translation: AAH63824.2.
    BC068456 mRNA. Translation: AAH68456.2.
    BC072426 mRNA. Translation: AAH72426.2.
    BC073141 mRNA. Translation: AAH73141.1. Different initiation.
    BC083508 mRNA. Translation: AAH83508.2.
    BC099904 mRNA. Translation: AAH99904.1.
    BC101483 mRNA. Translation: AAI01484.1.
    BC108281 mRNA. Translation: AAI08282.1.
    BC111951 mRNA. Translation: AAI11952.1.
    CCDSiCCDS6290.1. [P63104-1]
    PIRiA38246. PSHUAM.
    RefSeqiNP_001129171.1. NM_001135699.1. [P63104-1]
    NP_001129172.1. NM_001135700.1. [P63104-1]
    NP_001129173.1. NM_001135701.1. [P63104-1]
    NP_001129174.1. NM_001135702.1. [P63104-1]
    NP_003397.1. NM_003406.3. [P63104-1]
    NP_663723.1. NM_145690.2. [P63104-1]
    XP_005251118.1. XM_005251061.1. [P63104-1]
    XP_005251119.1. XM_005251062.1. [P63104-1]
    XP_005251120.1. XM_005251063.1. [P63104-1]
    UniGeneiHs.492407.

    Genome annotation databases

    EnsembliENST00000353245; ENSP00000309503; ENSG00000164924. [P63104-1]
    ENST00000395951; ENSP00000379281; ENSG00000164924. [P63104-1]
    ENST00000395953; ENSP00000379283; ENSG00000164924. [P63104-1]
    ENST00000395956; ENSP00000379286; ENSG00000164924. [P63104-1]
    ENST00000395957; ENSP00000379287; ENSG00000164924. [P63104-1]
    ENST00000395958; ENSP00000379288; ENSG00000164924. [P63104-1]
    ENST00000419477; ENSP00000395114; ENSG00000164924. [P63104-1]
    ENST00000457309; ENSP00000398599; ENSG00000164924. [P63104-1]
    ENST00000522542; ENSP00000430072; ENSG00000164924. [P63104-2]
    GeneIDi7534.
    KEGGihsa:7534.
    UCSCiuc003yjv.2. human. [P63104-1]

    Polymorphism databases

    DMDMi52000887.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M86400 mRNA. Translation: AAA36446.1 .
    U28964 mRNA. Translation: AAC52052.1 .
    AK289945 mRNA. Translation: BAF82634.1 .
    AK296902 mRNA. Translation: BAH12451.1 .
    CH471060 Genomic DNA. Translation: EAW91823.1 .
    BC003623 mRNA. Translation: AAH03623.3 .
    BC051814 mRNA. Translation: AAH51814.1 . Different initiation.
    BC063824 mRNA. Translation: AAH63824.2 .
    BC068456 mRNA. Translation: AAH68456.2 .
    BC072426 mRNA. Translation: AAH72426.2 .
    BC073141 mRNA. Translation: AAH73141.1 . Different initiation.
    BC083508 mRNA. Translation: AAH83508.2 .
    BC099904 mRNA. Translation: AAH99904.1 .
    BC101483 mRNA. Translation: AAI01484.1 .
    BC108281 mRNA. Translation: AAI08282.1 .
    BC111951 mRNA. Translation: AAI11952.1 .
    CCDSi CCDS6290.1. [P63104-1 ]
    PIRi A38246. PSHUAM.
    RefSeqi NP_001129171.1. NM_001135699.1. [P63104-1 ]
    NP_001129172.1. NM_001135700.1. [P63104-1 ]
    NP_001129173.1. NM_001135701.1. [P63104-1 ]
    NP_001129174.1. NM_001135702.1. [P63104-1 ]
    NP_003397.1. NM_003406.3. [P63104-1 ]
    NP_663723.1. NM_145690.2. [P63104-1 ]
    XP_005251118.1. XM_005251061.1. [P63104-1 ]
    XP_005251119.1. XM_005251062.1. [P63104-1 ]
    XP_005251120.1. XM_005251063.1. [P63104-1 ]
    UniGenei Hs.492407.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1IB1 X-ray 2.70 A/B/C/D 1-245 [» ]
    1QJA X-ray 2.00 A/B 1-245 [» ]
    1QJB X-ray 2.00 A/B 1-245 [» ]
    2C1J X-ray 2.60 A/B 1-245 [» ]
    2C1N X-ray 2.00 A/B 1-245 [» ]
    2O02 X-ray 1.50 A/B 1-230 [» ]
    2WH0 X-ray 2.25 A/B/C/D 1-245 [» ]
    3CU8 X-ray 2.40 A/B 1-245 [» ]
    3NKX X-ray 2.40 A/B 1-245 [» ]
    3RDH X-ray 2.39 A/B/C/D 1-245 [» ]
    4BG6 X-ray 2.30 A/B 1-245 [» ]
    4FJ3 X-ray 1.95 A/B 1-230 [» ]
    4HKC X-ray 2.20 A 1-245 [» ]
    4IHL X-ray 2.20 A/B 1-230 [» ]
    4N7G X-ray 2.25 A 1-230 [» ]
    4N7Y X-ray 2.16 A/B 1-230 [» ]
    4N84 X-ray 2.50 A/B 1-230 [» ]
    ProteinModelPortali P63104.
    SMRi P63104. Positions 1-230.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113366. 367 interactions.
    DIPi DIP-563N.
    IntActi P63104. 514 interactions.
    MINTi MINT-89071.

    PTM databases

    PhosphoSitei P63104.

    Polymorphism databases

    DMDMi 52000887.

    2D gel databases

    DOSAC-COBS-2DPAGE P63104.
    OGPi P63104.
    UCD-2DPAGE P63104.

    Proteomic databases

    MaxQBi P63104.
    PaxDbi P63104.
    PRIDEi P63104.

    Protocols and materials databases

    DNASUi 7534.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000353245 ; ENSP00000309503 ; ENSG00000164924 . [P63104-1 ]
    ENST00000395951 ; ENSP00000379281 ; ENSG00000164924 . [P63104-1 ]
    ENST00000395953 ; ENSP00000379283 ; ENSG00000164924 . [P63104-1 ]
    ENST00000395956 ; ENSP00000379286 ; ENSG00000164924 . [P63104-1 ]
    ENST00000395957 ; ENSP00000379287 ; ENSG00000164924 . [P63104-1 ]
    ENST00000395958 ; ENSP00000379288 ; ENSG00000164924 . [P63104-1 ]
    ENST00000419477 ; ENSP00000395114 ; ENSG00000164924 . [P63104-1 ]
    ENST00000457309 ; ENSP00000398599 ; ENSG00000164924 . [P63104-1 ]
    ENST00000522542 ; ENSP00000430072 ; ENSG00000164924 . [P63104-2 ]
    GeneIDi 7534.
    KEGGi hsa:7534.
    UCSCi uc003yjv.2. human. [P63104-1 ]

    Organism-specific databases

    CTDi 7534.
    GeneCardsi GC08M101930.
    HGNCi HGNC:12855. YWHAZ.
    HPAi CAB005065.
    MIMi 601288. gene.
    neXtProti NX_P63104.
    PharmGKBi PA37444.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5040.
    HOVERGENi HBG050423.
    InParanoidi P63104.
    KOi K16197.
    OrthoDBi EOG7HHWT3.
    PhylomeDBi P63104.
    TreeFami TF102003.

    Enzyme and pathway databases

    Reactomei REACT_147867. Translocation of GLUT4 to the plasma membrane.
    REACT_200731. deactivation of the beta-catenin transactivating complex.
    REACT_23837. Interleukin-3, 5 and GM-CSF signaling.
    REACT_23847. GP1b-IX-V activation signalling.
    REACT_23898. Rap1 signalling.
    REACT_25042. KSRP destabilizes mRNA.
    SignaLinki P63104.

    Miscellaneous databases

    ChiTaRSi YWHAZ. human.
    EvolutionaryTracei P63104.
    GeneWikii YWHAZ.
    GenomeRNAii 7534.
    NextBioi 29475.
    PROi P63104.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P63104.
    Bgeei P63104.
    Genevestigatori P63104.

    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. "Cloning and expression of a human 14-3-3 protein mediating phospholipolysis. Identification of an arachidonoyl-enzyme intermediate during catalysis."
      Zupan L.A., Steffens D.L., Berry C.A., Landt M.L., Gross R.W.
      J. Biol. Chem. 267:8707-8710(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Placenta.
    2. "Two unique 5' untranslated regions in mRNAs encoding human 14-3-3 zeta: differential expression in hemopoietic cells."
      Seluja G.A., Pietromonaco S.F., Elias L.
      Biochim. Biophys. Acta 1395:281-287(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Bone marrow.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Hippocampus and Tongue.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain, Colon, Eye, Melanoma, PNS, Skin, Testis and Uterus.
    6. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-18.
      Tissue: Platelet.
    7. Bienvenut W.V., Potts A., Barblan J., Claeys D., Quadroni M.
      Submitted (NOV-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 1-9; 12-18; 28-49; 61-68; 86-91; 128-158 AND 213-222, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: B-cell lymphoma and Platelet.
    8. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 92-103; 140-157; 194-212 AND 223-245, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    9. "14-3-3 is phosphorylated by casein kinase I on residue 233. Phosphorylation at this site in vivo regulates Raf/14-3-3 interaction."
      Dubois T., Rommel C., Howell S., Steinhussen U., Soneji Y., Morrice N., Moelling K., Aitken A.
      J. Biol. Chem. 272:28882-28888(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-232, INTERACTION WITH RAF1, FUNCTION.
    10. "Nuclear localization of protein kinase U-alpha is regulated by 14-3-3."
      Zhang S., Xing H., Muslin A.J.
      J. Biol. Chem. 274:24865-24872(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TLK2.
    11. "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.
    12. "Identification of 14-3-3zeta as a protein kinase B/Akt substrate."
      Powell D.W., Rane M.J., Chen Q., Singh S., McLeish K.R.
      J. Biol. Chem. 277:21639-21642(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-58, INTERACTION WITH AKT1.
    13. "The dimeric versus monomeric status of 14-3-3zeta is controlled by phosphorylation of Ser58 at the dimer interface."
      Woodcock J.M., Murphy J., Stomski F.C., Berndt M.C., Lopez A.F.
      J. Biol. Chem. 278:36323-36327(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-58, DIMERIZATION.
    14. "Cellular stabilization of the melatonin rhythm enzyme induced by nonhydrolyzable phosphonate incorporation."
      Zheng W., Zhang Z., Ganguly S., Weller J.L., Klein D.C., Cole P.A.
      Nat. Struct. Biol. 10:1054-1057(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AANAT, FUNCTION.
    15. "JNK promotes Bax translocation to mitochondria through phosphorylation of 14-3-3 proteins."
      Tsuruta F., Sunayama J., Mori Y., Hattori S., Shimizu S., Tsujimoto Y., Yoshioka K., Masuyama N., Gotoh Y.
      EMBO J. 23:1889-1899(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-184, INTERACTION WITH BAX, FUNCTION, MUTAGENESIS OF SER-184.
    16. "A pathway of neuregulin-induced activation of cofilin-phosphatase Slingshot and cofilin in lamellipodia."
      Nagata-Ohashi K., Ohta Y., Goto K., Chiba S., Mori R., Nishita M., Ohashi K., Kousaka K., Iwamatsu A., Niwa R., Uemura T., Mizuno K.
      J. Cell Biol. 165:465-471(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SSH1.
    17. "14-3-3 protein interacts with nuclear localization sequence of forkhead transcription factor FoxO4."
      Obsilova V., Vecer J., Herman P., Pabianova A., Sulc M., Teisinger J., Boura E., Obsil T.
      Biochemistry 44:11608-11617(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MLLT7.
    18. "Interplay between components of a novel LIM kinase-slingshot phosphatase complex regulates cofilin."
      Soosairajah J., Maiti S., Wiggan O., Sarmiere P., Moussi N., Sarcevic B., Sampath R., Bamburg J.R., Bernard O.
      EMBO J. 24:473-486(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SSH1.
    19. "Sphingosine activates protein kinase A type II by a novel cAMP-independent mechanism."
      Ma Y., Pitson S., Hercus T., Murphy J., Lopez A., Woodcock J.
      J. Biol. Chem. 280:26011-26017(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-58, MUTAGENESIS OF SER-58.
    20. "JNK phosphorylation of 14-3-3 proteins regulates nuclear targeting of c-Abl in the apoptotic response to DNA damage."
      Yoshida K., Yamaguchi T., Natsume T., Kufe D., Miki Y.
      Nat. Cell Biol. 7:278-285(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ABL1, IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT SER-184, MUTAGENESIS OF SER-184.
    21. "Melatonin synthesis: 14-3-3-dependent activation and inhibition of arylalkylamine N-acetyltransferase mediated by phosphoserine-205."
      Ganguly S., Weller J.L., Ho A., Chemineau P., Malpaux B., Klein D.C.
      Proc. Natl. Acad. Sci. U.S.A. 102:1222-1227(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AANAT, FUNCTION.
    22. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    23. "Protein kinase A phosphorylates and regulates dimerization of 14-3-3 epsilon."
      Gu Y.-M., Jin Y.-H., Choi J.-K., Baek K.-H., Yeo C.-Y., Lee K.-Y.
      FEBS Lett. 580:305-310(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-58, DIMERIZATION, INTERACTION WITH TP53 AND YWHAE, FUNCTION, MUTAGENESIS OF SER-58.
    24. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Melanoma.
    25. "Regulation of Nox1 activity via PKA-mediated phosphorylation of NoxA1 and 14-3-3 binding."
      Kim J.-S., Diebold B.A., Babior B.M., Knaus U.G., Bokoch G.M.
      J. Biol. Chem. 282:34787-34800(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NOXA1, MUTAGENESIS OF LYS-49.
    26. "p21-activated kinase 1 phosphorylates and regulates 14-3-3 binding to GEF-H1, a microtubule-localized Rho exchange factor."
      Zenke F.T., Krendel M., DerMardirossian C., King C.C., Bohl B.P., Bokoch G.M.
      J. Biol. Chem. 279:18392-18400(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ARHGEF2.
    27. "Phosphorylation-dependent binding of 14-3-3 terminates signalling by the Gab2 docking protein."
      Brummer T., Larance M., Herrera Abreu M.T., Lyons R.J., Timpson P., Emmerich C.H., Fleuren E.D.G., Lehrbach G.M., Schramek D., Guilhaus M., James D.E., Daly R.J.
      EMBO J. 27:2305-2316(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GAB2.
    28. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    29. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    30. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    31. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1; LYS-3 AND LYS-68, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    32. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207 AND THR-232, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    33. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    34. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    35. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    36. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    37. "Structural analysis of 14-3-3 phosphopeptide complexes identifies a dual role for the nuclear export signal of 14-3-3 in ligand binding."
      Rittinger K., Budman J., Xu J., Volinia S., Cantley L.C., Smerdon S.J., Gamblin S.J., Yaffe M.B.
      Mol. Cell 4:153-166(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
    38. "Crystal structure of the 14-3-3zeta:serotonin N-acetyltransferase complex. a role for scaffolding in enzyme regulation."
      Obsil T., Ghirlando R., Klein D.C., Ganguly S., Dyda F.
      Cell 105:257-267(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH AANAT.
    39. Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH HISTONE H3 PHOSPHOPEPTIDE.
    40. "Phosphorylation-independent interaction between 14-3-3 and exoenzyme S: from structure to pathogenesis."
      Ottmann C., Yasmin L., Weyand M., Veesenmeyer J.L., Diaz M.H., Palmer R.H., Francis M.S., Hauser A.R., Wittinghofer A., Hallberg B.
      EMBO J. 26:902-913(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 1-230 IN COMPLEX WITH PSEUDOMONAS AERUGINOSA EXOS.

    Entry informationi

    Entry namei1433Z_HUMAN
    AccessioniPrimary (citable) accession number: P63104
    Secondary accession number(s): A8K1N0
    , B7Z465, P29213, P29312, Q32P43, Q5XJ08, Q6GPI2, Q6IN74, Q6NUR9, Q6P3U9, Q86V33
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 13, 2004
    Last sequence update: September 13, 2004
    Last modified: October 1, 2014
    This is version 131 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

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

    Documents

    1. Human chromosome 8
      Human chromosome 8: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3