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Q04917

- 1433F_HUMAN

UniProt

Q04917 - 1433F_HUMAN

Protein

14-3-3 protein eta

Gene

YWHAH

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 163 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      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. Negatively regulates the kinase activity of PDPK1.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei57 – 571Interaction with phosphoserine on interacting protein
    Sitei132 – 1321Interaction with phosphoserine on interacting protein

    GO - Molecular functioni

    1. enzyme binding Source: BHF-UCL
    2. glucocorticoid receptor binding Source: UniProtKB
    3. insulin-like growth factor receptor binding Source: UniProtKB
    4. ion channel binding Source: BHF-UCL
    5. protein binding Source: UniProtKB
    6. protein domain specific binding Source: UniProtKB
    7. protein heterodimerization activity Source: BHF-UCL
    8. sodium channel regulator activity Source: BHF-UCL

    GO - Biological processi

    1. apoptotic process Source: Reactome
    2. glucocorticoid catabolic process Source: UniProtKB
    3. glucocorticoid receptor signaling pathway Source: UniProtKB
    4. intracellular protein transport Source: UniProtKB
    5. intrinsic apoptotic signaling pathway Source: Reactome
    6. membrane depolarization during action potential Source: BHF-UCL
    7. membrane organization Source: Reactome
    8. negative regulation of dendrite morphogenesis Source: UniProtKB
    9. positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway Source: Reactome
    10. positive regulation of transcription, DNA-templated Source: UniProtKB
    11. regulation of neuron differentiation Source: UniProtKB
    12. regulation of sodium ion transmembrane transporter activity Source: BHF-UCL
    13. regulation of sodium ion transport Source: BHF-UCL
    14. regulation of synaptic plasticity Source: UniProtKB
    15. substantia nigra development Source: UniProt

    Enzyme and pathway databases

    ReactomeiREACT_147867. Translocation of GLUT4 to the plasma membrane.
    SignaLinkiQ04917.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    14-3-3 protein eta
    Alternative name(s):
    Protein AS1
    Gene namesi
    Name:YWHAH
    Synonyms:YWHA1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:12853. YWHAH.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytoplasmic vesicle membrane Source: Reactome
    3. cytosol Source: Reactome
    4. extracellular vesicular exosome Source: UniProtKB
    5. intercalated disc Source: BHF-UCL
    6. plasma membrane Source: BHF-UCL

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA37442.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 24624514-3-3 protein etaPRO_0000058623Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylglycine1 Publication
    Modified residuei25 – 251Phosphoserine1 Publication
    Modified residuei59 – 591PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated on Ser-59 by protein kinase C delta type catalytic subunit in a sphingosine-dependent fashion.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ04917.
    PaxDbiQ04917.
    PeptideAtlasiQ04917.
    PRIDEiQ04917.

    PTM databases

    PhosphoSiteiQ04917.

    Expressioni

    Tissue specificityi

    Expressed mainly in the brain and present in other tissues albeit at lower levels.

    Gene expression databases

    ArrayExpressiQ04917.
    BgeeiQ04917.
    CleanExiHS_YWHAH.
    GenevestigatoriQ04917.

    Organism-specific databases

    HPAiCAB025918.

    Interactioni

    Subunit structurei

    Homodimer By similarity. Interacts with many nuclear hormone receptors and cofactors including AR, ESR1, ESR2, MC2R, NR3C1, NRIP1, PPARBP and THRA. Interacts with ABL1 (phosphorylated form); the interaction retains it in the cytoplasm. Interacts with ARHGEF28 and CDK16 By similarity. Weakly interacts with CDKN1B. Interacts with GAB2. Interacts with KCNK18 in a phosphorylation-dependent manner. Interacts with SAMSN1 By similarity. Interacts with the 'Ser-241' phosphorylated form of PDPK1.By similarity6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AKT1S1Q96B363EBI-306940,EBI-720593
    CAMKK1Q8N5S95EBI-306940,EBI-6424030
    CDC25BP303053EBI-306940,EBI-1051746
    CDK14O949213EBI-306940,EBI-1043945
    CSNK1A1P678288EBI-306940,EBI-7540603From a different organism.
    GREM1O605655EBI-306940,EBI-944395
    HDAC4P565243EBI-306940,EBI-308629
    KANK1Q14678-23EBI-306940,EBI-6173812
    LRRK2Q5S0073EBI-306940,EBI-5323863
    MARK2Q7KZI78EBI-306940,EBI-516560
    MARK3P274484EBI-306940,EBI-707595
    MARK4Q96L346EBI-306940,EBI-302319
    PARD3Q8TEW06EBI-306940,EBI-81968
    PARD6AQ9NPB62EBI-306940,EBI-81876
    PARD6BQ9BYG52EBI-306940,EBI-295391
    PARD6GQ9BYG42EBI-306940,EBI-295417
    PRKCIP417433EBI-306940,EBI-286199
    RAF1P040493EBI-306940,EBI-365996
    Rnd3P615882EBI-306940,EBI-6930266From a different organism.

    Protein-protein interaction databases

    BioGridi113365. 119 interactions.
    DIPiDIP-27566N.
    IntActiQ04917. 146 interactions.
    MINTiMINT-124456.
    STRINGi9606.ENSP00000248975.

    Structurei

    Secondary structure

    1
    246
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 1613
    Helixi20 – 3112
    Helixi39 – 7335
    Helixi76 – 10631
    Turni107 – 1115
    Helixi117 – 13721
    Helixi140 – 16425
    Helixi170 – 18516
    Helixi190 – 20617
    Helixi207 – 2104
    Turni213 – 2153
    Helixi216 – 23419

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2C63X-ray2.15A/B/C/D2-246[»]
    2C74X-ray2.70A/B2-246[»]
    ProteinModelPortaliQ04917.
    SMRiQ04917. Positions 3-235.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ04917.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the 14-3-3 family.Curated

    Phylogenomic databases

    eggNOGiCOG5040.
    HOGENOMiHOG000240379.
    HOVERGENiHBG050423.
    InParanoidiQ04917.
    KOiK16198.
    OMAiESSEAAY.
    OrthoDBiEOG7HHWT3.
    PhylomeDBiQ04917.
    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q04917-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGDREQLLQR ARLAEQAERY DDMASAMKAV TELNEPLSNE DRNLLSVAYK    50
    NVVGARRSSW RVISSIEQKT MADGNEKKLE KVKAYREKIE KELETVCNDV 100
    LSLLDKFLIK NCNDFQYESK VFYLKMKGDY YRYLAEVASG EKKNSVVEAS 150
    EAAYKEAFEI SKEQMQPTHP IRLGLALNFS VFYYEIQNAP EQACLLAKQA 200
    FDDAIAELDT LNEDSYKDST LIMQLLRDNL TLWTSDQQDE EAGEGN 246
    Length:246
    Mass (Da):28,219
    Last modified:January 23, 2007 - v4
    Checksum:iD70FBC100C45D6E5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti144 – 1441N → T in CAA40620. (PubMed:8515476)Curated
    Sequence conflicti157 – 1571A → G in AAA35483. (PubMed:8218406)Curated
    Sequence conflicti237 – 2371Q → L in AAA35483. (PubMed:8218406)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L20422 mRNA. Translation: AAA35483.1.
    X80536 Genomic DNA. Translation: CAA56676.1.
    X78138 mRNA. Translation: CAA55017.1.
    X57345 mRNA. Translation: CAA40620.1.
    D78577 Genomic DNA. Translation: BAA11418.1.
    S80794 mRNA. Translation: AAB36036.1.
    CR456612 mRNA. Translation: CAG30498.1.
    Z82248 Genomic DNA. Translation: CAB05112.1.
    BC003047 mRNA. Translation: AAH03047.1.
    CCDSiCCDS13901.1.
    PIRiS34756.
    S38509.
    S38532.
    RefSeqiNP_003396.1. NM_003405.3.
    UniGeneiHs.226755.

    Genome annotation databases

    EnsembliENST00000248975; ENSP00000248975; ENSG00000128245.
    GeneIDi7533.
    KEGGihsa:7533.
    UCSCiuc003alz.3. human.

    Polymorphism databases

    DMDMi1345593.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L20422 mRNA. Translation: AAA35483.1 .
    X80536 Genomic DNA. Translation: CAA56676.1 .
    X78138 mRNA. Translation: CAA55017.1 .
    X57345 mRNA. Translation: CAA40620.1 .
    D78577 Genomic DNA. Translation: BAA11418.1 .
    S80794 mRNA. Translation: AAB36036.1 .
    CR456612 mRNA. Translation: CAG30498.1 .
    Z82248 Genomic DNA. Translation: CAB05112.1 .
    BC003047 mRNA. Translation: AAH03047.1 .
    CCDSi CCDS13901.1.
    PIRi S34756.
    S38509.
    S38532.
    RefSeqi NP_003396.1. NM_003405.3.
    UniGenei Hs.226755.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2C63 X-ray 2.15 A/B/C/D 2-246 [» ]
    2C74 X-ray 2.70 A/B 2-246 [» ]
    ProteinModelPortali Q04917.
    SMRi Q04917. Positions 3-235.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113365. 119 interactions.
    DIPi DIP-27566N.
    IntActi Q04917. 146 interactions.
    MINTi MINT-124456.
    STRINGi 9606.ENSP00000248975.

    PTM databases

    PhosphoSitei Q04917.

    Polymorphism databases

    DMDMi 1345593.

    Proteomic databases

    MaxQBi Q04917.
    PaxDbi Q04917.
    PeptideAtlasi Q04917.
    PRIDEi Q04917.

    Protocols and materials databases

    DNASUi 7533.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000248975 ; ENSP00000248975 ; ENSG00000128245 .
    GeneIDi 7533.
    KEGGi hsa:7533.
    UCSCi uc003alz.3. human.

    Organism-specific databases

    CTDi 7533.
    GeneCardsi GC22P032340.
    HGNCi HGNC:12853. YWHAH.
    HPAi CAB025918.
    MIMi 113508. gene.
    neXtProti NX_Q04917.
    PharmGKBi PA37442.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5040.
    HOGENOMi HOG000240379.
    HOVERGENi HBG050423.
    InParanoidi Q04917.
    KOi K16198.
    OMAi ESSEAAY.
    OrthoDBi EOG7HHWT3.
    PhylomeDBi Q04917.
    TreeFami TF102003.

    Enzyme and pathway databases

    Reactomei REACT_147867. Translocation of GLUT4 to the plasma membrane.
    SignaLinki Q04917.

    Miscellaneous databases

    ChiTaRSi YWHAH. human.
    EvolutionaryTracei Q04917.
    GeneWikii YWHAH.
    GenomeRNAii 7533.
    NextBioi 29471.
    PROi Q04917.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q04917.
    Bgeei Q04917.
    CleanExi HS_YWHAH.
    Genevestigatori Q04917.

    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. "The human and bovine 14-3-3 eta protein mRNAs are highly conserved in both their translated and untranslated regions."
      Swanson K.D., Dhar M.S., Joshi J.G.
      Biochim. Biophys. Acta 1216:145-148(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    2. "cDNA cloning and chromosome assignment of the gene for human brain 14-3-3 protein eta chain."
      Ichimura-Ohshima Y., Morii K., Ichimura T., Araki K., Takahashi Y., Isobe T., Minoshima S., Fukuyama R., Shimizu N., Kuwano R.
      J. Neurosci. Res. 31:600-605(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Brain.
    3. Leffers H., Tommerup N., Celis J.E.
      Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "The effect on methamphetamine on the mRNA level for 14.3.3 eta chain in the human cultured cells."
      Muratake T., Hayashi S., Ichimura Y., Morii K., Kuwano R., Ichikawa T., Kumanishi T., Isobe T., Watanabe M., Kondo H.
      Mol. Neurobiol. 11:223-230(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    5. "Structural organization and chromosomal assignment of the human 14-3-3 eta chain gene (YWHAH)."
      Muratake T., Hayashi S., Ichikawa T., Kumanishi T., Ichimura Y., Kuwano R., Isobe T., Wang Y., Minoshima S., Shimizu N., Takahashi Y.
      Genomics 36:63-69(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    7. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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].
      Tissue: Lymph.
    9. "Molecular cloning and expression of the transformation sensitive epithelial marker stratifin. A member of a protein family that has been involved in the protein kinase C signalling pathway."
      Leffers H., Madsen P., Rasmussen H.H., Honore B., Andersen A.H., Walbum E., Vandekerckhove J., Celis J.E.
      J. Mol. Biol. 231:982-998(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 27-225.
      Tissue: Keratinocyte.
    10. "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 2-10.
      Tissue: Platelet.
    11. Bienvenut W.V.
      Submitted (AUG-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-10; 29-50; 62-69; 126-132; 144-155; 163-172 AND 218-227, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT GLY-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Platelet.
    12. "Regulation of glucocorticoid receptor activity by 14-3-3-dependent intracellular relocalization of the corepressor RIP140."
      Zilliacus J., Holter E., Wakui H., Tazawa H., Treuter E., Gustafsson J.-A.
      Mol. Endocrinol. 15:501-511(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AR; ESR1; ESR2; MC2R; NRIP1; NR3C1; PPARBP AND THRA.
    13. "Regulation of kinase activity of 3-phosphoinositide-dependent protein kinase-1 by binding to 14-3-3."
      Sato S., Fujita N., Tsuruo T.
      J. Biol. Chem. 277:39360-39367(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PDPK1.
    14. "Phosphorylation of p27Kip1 at threonine 198 by p90 ribosomal protein S6 kinases promotes its binding to 14-3-3 and cytoplasmic localization."
      Fujita N., Sato S., Tsuruo T.
      J. Biol. Chem. 278:49254-49260(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CDKN1B.
    15. "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.
    16. "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.
    17. "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-25, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS), IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH PHOSPHOSERINE MOTIFS, SUBUNIT.

    Entry informationi

    Entry namei1433F_HUMAN
    AccessioniPrimary (citable) accession number: Q04917
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 163 of the entry and version 4 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 22
      Human chromosome 22: 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