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P62258

- 1433E_HUMAN

UniProt

P62258 - 1433E_HUMAN

Protein

14-3-3 protein epsilon

Gene

YWHAE

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 1 (05 Jul 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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei57 – 571Interaction with phosphoserine on interacting protein
    Sitei130 – 1301Interaction with phosphoserine on interacting protein

    GO - Molecular functioni

    1. enzyme binding Source: UniProtKB
    2. histone deacetylase binding Source: BHF-UCL
    3. ion channel binding Source: BHF-UCL
    4. MHC class II protein complex binding Source: UniProt
    5. phosphoprotein binding Source: BHF-UCL
    6. phosphoserine binding Source: BHF-UCL
    7. poly(A) RNA binding Source: UniProtKB
    8. potassium channel regulator activity Source: BHF-UCL
    9. protein binding Source: UniProtKB
    10. protein heterodimerization activity Source: BHF-UCL

    GO - Biological processi

    1. apoptotic process Source: Reactome
    2. apoptotic signaling pathway Source: Reactome
    3. cerebral cortex development Source: Ensembl
    4. G2/M transition of mitotic cell cycle Source: Reactome
    5. hippocampus development Source: Ensembl
    6. hippo signaling Source: Reactome
    7. intracellular signal transduction Source: ProtInc
    8. intrinsic apoptotic signaling pathway Source: Reactome
    9. membrane organization Source: Reactome
    10. membrane repolarization during cardiac muscle cell action potential Source: BHF-UCL
    11. mitotic cell cycle Source: Reactome
    12. negative regulation of peptidyl-serine dephosphorylation Source: BHF-UCL
    13. neuron migration Source: Ensembl
    14. neurotrophin TRK receptor signaling pathway Source: Reactome
    15. positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway Source: Reactome
    16. protein targeting Source: Ensembl
    17. regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: Reactome
    18. regulation of heart rate by cardiac conduction Source: BHF-UCL
    19. regulation of heart rate by hormone Source: BHF-UCL
    20. regulation of membrane repolarization Source: BHF-UCL
    21. regulation of potassium ion transmembrane transporter activity Source: BHF-UCL
    22. substantia nigra development Source: UniProt
    23. viral process Source: UniProtKB-KW

    Keywords - Biological processi

    Host-virus interaction

    Enzyme and pathway databases

    ReactomeiREACT_118607. Signaling by Hippo.
    REACT_13526. NADE modulates death signalling.
    REACT_147867. Translocation of GLUT4 to the plasma membrane.
    REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
    REACT_15364. Loss of Nlp from mitotic centrosomes.
    REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
    REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
    REACT_200744. HSF1 activation.
    REACT_200780. Regulation of HSF1-mediated heat shock response.
    SignaLinkiP62258.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    14-3-3 protein epsilon
    Short name:
    14-3-3E
    Gene namesi
    Name:YWHAE
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:12851. YWHAE.

    Subcellular locationi

    Cytoplasm By similarity. Melanosome 2 Publications
    Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV.

    GO - Cellular componenti

    1. cytoplasmic vesicle membrane Source: Reactome
    2. cytosol Source: Reactome
    3. extracellular vesicular exosome Source: UniProtKB
    4. kinesin complex Source: Ensembl
    5. melanosome Source: UniProtKB-SubCell
    6. membrane Source: UniProtKB
    7. mitochondrion Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    Orphaneti217385. 17p13.3 microduplication syndrome.
    261257. Distal 17p13.3 microdeletion syndrome.
    531. Miller-Dieker syndrome.
    PharmGKBiPA37440.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 25525514-3-3 protein epsilonPRO_0000058618Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine2 Publications
    Modified residuei50 – 501N6-acetyllysine1 Publication
    Modified residuei69 – 691N6-acetyllysine1 Publication
    Modified residuei118 – 1181N6-acetyllysine1 Publication
    Modified residuei123 – 1231N6-acetyllysine1 Publication
    Modified residuei210 – 2101Phosphoserine2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP62258.
    PaxDbiP62258.
    PeptideAtlasiP62258.
    PRIDEiP62258.

    2D gel databases

    OGPiP42655.
    UCD-2DPAGEP62258.

    PTM databases

    PhosphoSiteiP62258.

    Miscellaneous databases

    PMAP-CutDBP62258.

    Expressioni

    Gene expression databases

    ArrayExpressiP62258.
    BgeeiP62258.
    CleanExiHS_YWHAE.
    GenevestigatoriP62258.

    Organism-specific databases

    HPAiCAB016200.
    CAB021109.
    CAB047350.
    HPA008445.

    Interactioni

    Subunit structurei

    Homodimer. Heterodimerizes with YWHAZ. Interacts with NDEL1, ARHGEF28 and TIAM2 By similarity. Interacts with HCV core protein. Interacts with ABL1 (phosphorylated form); the interaction retains it in the cytoplasm. Weakly interacts with CDKN1B. Interacts with GAB2. Interacts with phosphorylated GRB10. Interacts with PKA-phosphorylated AANAT. Interacts with the phosphorylated (by AKT1) form of SRPK2.By similarity9 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    O929725EBI-356498,EBI-9213553From a different organism.
    APAF1O147272EBI-356498,EBI-446492
    CBX4O00257-32EBI-356498,EBI-4392727
    CDK14O949213EBI-356498,EBI-1043945
    FBXO4Q9UKT55EBI-356498,EBI-960409
    HDAC4P565244EBI-356498,EBI-308629
    KANK1Q14678-23EBI-356498,EBI-6173812
    LRRK2Q5S0076EBI-356498,EBI-5323863
    MAP3K3Q997593EBI-356498,EBI-307281
    MDM4O151513EBI-356498,EBI-398437
    MLF1P583403EBI-356498,EBI-721328
    Prdx6O352442EBI-356498,EBI-915490From a different organism.
    Rnd3P615882EBI-356498,EBI-6930266From a different organism.
    STACQ994692EBI-356498,EBI-2652799
    WWTR1Q9GZV53EBI-356498,EBI-747743
    YWHABP319463EBI-356498,EBI-359815
    YWHAGP619814EBI-356498,EBI-359832
    YWHAZP631045EBI-356498,EBI-347088

    Protein-protein interaction databases

    BioGridi113363. 305 interactions.
    DIPiDIP-36676N.
    IntActiP62258. 149 interactions.
    MINTiMINT-4998623.
    STRINGi9606.ENSP00000264335.

    Structurei

    Secondary structure

    1
    255
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 1714
    Helixi20 – 3112
    Helixi39 – 7335
    Helixi76 – 10631
    Helixi108 – 1114
    Helixi115 – 13521
    Helixi138 – 16225
    Helixi168 – 18316
    Helixi188 – 20417
    Helixi205 – 2084
    Turni211 – 2133
    Helixi214 – 23118

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2BR9X-ray1.75A1-233[»]
    3UALX-ray1.80A1-232[»]
    3UBWX-ray1.90A1-234[»]
    ProteinModelPortaliP62258.
    SMRiP62258. Positions 3-232.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP62258.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the 14-3-3 family.Curated

    Phylogenomic databases

    eggNOGiCOG5040.
    HOVERGENiHBG050423.
    InParanoidiP62258.
    KOiK06630.
    OMAiMQESDKP.
    OrthoDBiEOG7HHWT3.
    PhylomeDBiP62258.
    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: P62258-1) [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

    MDDREDLVYQ AKLAEQAERY DEMVESMKKV AGMDVELTVE ERNLLSVAYK    50
    NVIGARRASW RIISSIEQKE ENKGGEDKLK MIREYRQMVE TELKLICCDI 100
    LDVLDKHLIP AANTGESKVF YYKMKGDYHR YLAEFATGND RKEAAENSLV 150
    AYKAASDIAM TELPPTHPIR LGLALNFSVF YYEILNSPDR ACRLAKAAFD 200
    DAIAELDTLS EESYKDSTLI MQLLRDNLTL WTSDMQGDGE EQNKEALQDV 250
    EDENQ 255
    Length:255
    Mass (Da):29,174
    Last modified:July 5, 2004 - v1
    Checksum:i07817CCBD1F75B26
    GO
    Isoform SV (identifier: P62258-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-22: Missing.

    Note: Unable to dimerize with YWHAZ.

    Show »
    Length:233
    Mass (Da):26,504
    Checksum:i20302F1E0AB73C8A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti106 – 1072KH → NY AA sequence (PubMed:2026444)Curated
    Sequence conflicti143 – 1431E → F AA sequence (PubMed:2026444)Curated
    Sequence conflicti148 – 1481S → T AA sequence (PubMed:2026444)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2222Missing in isoform SV. 2 PublicationsVSP_040621Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U20972 mRNA. Translation: AAC50175.1.
    U54778 mRNA. Translation: AAC50710.1.
    U43399 mRNA. Translation: AAC50625.1.
    U43430 mRNA. Translation: AAD00026.1.
    U28936 mRNA. Translation: AAA75301.1.
    AB017103 Genomic DNA. Translation: BAA32538.1.
    AY883089 mRNA. Translation: AAX68683.1.
    AK128785 mRNA. Translation: BAG54733.1.
    AK295260 mRNA. Translation: BAG58249.1.
    AK316185 mRNA. Translation: BAH14556.1.
    BT007161 mRNA. Translation: AAP35825.1.
    CH471108 Genomic DNA. Translation: EAW90628.1.
    CH471108 Genomic DNA. Translation: EAW90629.1.
    BC000179 mRNA. Translation: AAH00179.1.
    BC001440 mRNA. Translation: AAH01440.1.
    CCDSiCCDS11001.1. [P62258-1]
    PIRiA61235.
    I38947.
    RefSeqiNP_006752.1. NM_006761.4. [P62258-1]
    UniGeneiHs.513851.

    Genome annotation databases

    EnsembliENST00000264335; ENSP00000264335; ENSG00000108953. [P62258-1]
    ENST00000571732; ENSP00000461762; ENSG00000108953. [P62258-2]
    GeneIDi7531.
    KEGGihsa:7531.
    UCSCiuc002fsj.3. human. [P62258-1]

    Polymorphism databases

    DMDMi51702210.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U20972 mRNA. Translation: AAC50175.1 .
    U54778 mRNA. Translation: AAC50710.1 .
    U43399 mRNA. Translation: AAC50625.1 .
    U43430 mRNA. Translation: AAD00026.1 .
    U28936 mRNA. Translation: AAA75301.1 .
    AB017103 Genomic DNA. Translation: BAA32538.1 .
    AY883089 mRNA. Translation: AAX68683.1 .
    AK128785 mRNA. Translation: BAG54733.1 .
    AK295260 mRNA. Translation: BAG58249.1 .
    AK316185 mRNA. Translation: BAH14556.1 .
    BT007161 mRNA. Translation: AAP35825.1 .
    CH471108 Genomic DNA. Translation: EAW90628.1 .
    CH471108 Genomic DNA. Translation: EAW90629.1 .
    BC000179 mRNA. Translation: AAH00179.1 .
    BC001440 mRNA. Translation: AAH01440.1 .
    CCDSi CCDS11001.1. [P62258-1 ]
    PIRi A61235.
    I38947.
    RefSeqi NP_006752.1. NM_006761.4. [P62258-1 ]
    UniGenei Hs.513851.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2BR9 X-ray 1.75 A 1-233 [» ]
    3UAL X-ray 1.80 A 1-232 [» ]
    3UBW X-ray 1.90 A 1-234 [» ]
    ProteinModelPortali P62258.
    SMRi P62258. Positions 3-232.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113363. 305 interactions.
    DIPi DIP-36676N.
    IntActi P62258. 149 interactions.
    MINTi MINT-4998623.
    STRINGi 9606.ENSP00000264335.

    PTM databases

    PhosphoSitei P62258.

    Polymorphism databases

    DMDMi 51702210.

    2D gel databases

    OGPi P42655.
    UCD-2DPAGE P62258.

    Proteomic databases

    MaxQBi P62258.
    PaxDbi P62258.
    PeptideAtlasi P62258.
    PRIDEi P62258.

    Protocols and materials databases

    DNASUi 7531.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000264335 ; ENSP00000264335 ; ENSG00000108953 . [P62258-1 ]
    ENST00000571732 ; ENSP00000461762 ; ENSG00000108953 . [P62258-2 ]
    GeneIDi 7531.
    KEGGi hsa:7531.
    UCSCi uc002fsj.3. human. [P62258-1 ]

    Organism-specific databases

    CTDi 7531.
    GeneCardsi GC17M001148.
    H-InvDB HIX0013751.
    HIX0030006.
    HGNCi HGNC:12851. YWHAE.
    HPAi CAB016200.
    CAB021109.
    CAB047350.
    HPA008445.
    MIMi 605066. gene.
    neXtProti NX_P62258.
    Orphaneti 217385. 17p13.3 microduplication syndrome.
    261257. Distal 17p13.3 microdeletion syndrome.
    531. Miller-Dieker syndrome.
    PharmGKBi PA37440.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5040.
    HOVERGENi HBG050423.
    InParanoidi P62258.
    KOi K06630.
    OMAi MQESDKP.
    OrthoDBi EOG7HHWT3.
    PhylomeDBi P62258.
    TreeFami TF102003.

    Enzyme and pathway databases

    Reactomei REACT_118607. Signaling by Hippo.
    REACT_13526. NADE modulates death signalling.
    REACT_147867. Translocation of GLUT4 to the plasma membrane.
    REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
    REACT_15364. Loss of Nlp from mitotic centrosomes.
    REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
    REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
    REACT_200744. HSF1 activation.
    REACT_200780. Regulation of HSF1-mediated heat shock response.
    SignaLinki P62258.

    Miscellaneous databases

    ChiTaRSi YWHAE. human.
    EvolutionaryTracei P62258.
    GeneWikii YWHAE.
    GenomeRNAii 7531.
    NextBioi 29461.
    PMAP-CutDB P62258.
    PROi P62258.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P62258.
    Bgeei P62258.
    CleanExi HS_YWHAE.
    Genevestigatori P62258.

    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. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "14-3-3 epsilon has no homology to LIS1 and lies telomeric to it on chromosome 17p13.3 outside the Miller-Dieker syndrome chromosome region."
      Chong S.S., Tanigami A., Roschke A.V., Ledbetter D.H.
      Genome Res. 6:735-741(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Liver.
    3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. "Functional identification of a novel 14-3-3 epsilon splicing variant suggests dimerization is not necessary for 14-3-3 epsilon to inhibit UV-induced apoptosis."
      Han D., Ye G., Liu T., Chen C., Yang X., Wan B., Pan Y., Yu L.
      Biochem. Biophys. Res. Commun. 396:401-406(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SV), ALTERNATIVE SPLICING.
      Tissue: Brain.
    5. "Sequence determination of human epsilon 14-3-3 protein."
      Luk S.C.W., Lee C.Y., Waye M.M.Y.
      Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Heart.
    6. "14-3-3 epsilon genomic sequence."
      Tanigami A., Chong S.S., Ledbetter D.H.
      Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    7. "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 SV).
      Tissue: Caudate nucleus, Heart and Subthalamic nucleus.
    8. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "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: Placenta.
    11. "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 1-19.
      Tissue: Platelet.
    12. Bienvenut W.V.
      Submitted (MAY-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 1-19; 30-50 AND 131-170, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: B-cell lymphoma.
    13. "Isolation and partial characterization of the structures of fibroblast activating factor-related proteins from U937 cells."
      Demeter J., Medzihradszky D., Kha H., Goetzl E.J., Turck C.W.
      Immunology 72:350-354(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 103-108; 120-123; 131-141 AND 143-153.
      Tissue: Histiocytic lymphoma.
    14. Lubec G., Afjehi-Sadat L.
      Submitted (MAR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 131-141 AND 154-190, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain and Cajal-Retzius cell.
    15. "Hepatitis C virus core protein interacts with 14-3-3 protein and activates the kinase Raf-1."
      Aoki H., Hayashi J., Moriyama M., Arakawa Y., Hino O.
      J. Virol. 74:1736-1741(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HCV CORE PROTEIN.
    16. "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.
    17. "Akt-dependent phosphorylation of p27Kip1 promotes binding to 14-3-3 and cytoplasmic localization."
      Fujita N., Sato S., Katayama K., Tsuruo T.
      J. Biol. Chem. 277:28706-28713(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CDKN1B, SUBCELLULAR LOCATION.
    18. "Phosphorylation of grb10 regulates its interaction with 14-3-3."
      Urschel S., Bassermann F., Bai R.Y., Munch S., Peschel C., Duyster J.
      J. Biol. Chem. 280:16987-16993(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GRB10.
    19. "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.
    20. "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: INTERACTION WITH YWHAZ.
    21. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Melanoma.
    22. "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.
    23. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
      Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
      Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    24. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "Interaction of Akt-phosphorylated SRPK2 with 14-3-3 mediates cell cycle and cell death in neurons."
      Jang S.W., Liu X., Fu H., Rees H., Yepes M., Levey A., Ye K.
      J. Biol. Chem. 284:24512-24525(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SRPK2.
    26. "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 LYS-50; LYS-69; LYS-118 AND LYS-123, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. "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-210, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    28. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    29. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    30. Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 1-233, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH PHOSPHOSERINE MOTIFS, SUBUNIT.

    Entry informationi

    Entry namei1433E_HUMAN
    AccessioniPrimary (citable) accession number: P62258
    Secondary accession number(s): B3KY71
    , D3DTH5, P29360, P42655, Q4VJB6, Q53XZ5, Q63631, Q7M4R4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 5, 2004
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 126 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 17
      Human chromosome 17: 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