Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P31946

- 1433B_HUMAN

UniProt

P31946 - 1433B_HUMAN

Protein

14-3-3 protein beta/alpha

Gene

YWHAB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 168 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. Negative regulator of osteogenesis. Blocks the nuclear translocation of the phosphorylated form (by AKT1) of SRPK2 and antagonizes its stimulatory effect on cyclin D1 expression resulting in blockage of neuronal apoptosis elicited by SRPK2.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei58 – 581Interaction with phosphoserine on interacting proteinBy similarity
    Sitei129 – 1291Interaction with phosphoserine on interacting proteinBy similarity

    GO - Molecular functioni

    1. enzyme binding Source: BHF-UCL
    2. histone deacetylase binding Source: BHF-UCL
    3. phosphoprotein binding Source: BHF-UCL
    4. phosphoserine binding Source: BHF-UCL
    5. protein binding Source: UniProtKB
    6. protein domain specific binding Source: UniProtKB
    7. transcription corepressor activity Source: Ensembl

    GO - Biological processi

    1. activation of MAPKK activity Source: Reactome
    2. apoptotic process Source: Reactome
    3. axon guidance Source: Reactome
    4. cytoplasmic sequestering of protein Source: BHF-UCL
    5. epidermal growth factor receptor signaling pathway Source: Reactome
    6. Fc-epsilon receptor signaling pathway Source: Reactome
    7. fibroblast growth factor receptor signaling pathway Source: Reactome
    8. gene expression Source: Reactome
    9. hippo signaling Source: Reactome
    10. innate immune response Source: Reactome
    11. insulin receptor signaling pathway Source: Reactome
    12. intrinsic apoptotic signaling pathway Source: Reactome
    13. MAPK cascade Source: Reactome
    14. membrane organization Source: Reactome
    15. mRNA metabolic process Source: Reactome
    16. negative regulation of protein dephosphorylation Source: BHF-UCL
    17. negative regulation of transcription, DNA-templated Source: Ensembl
    18. neurotrophin TRK receptor signaling pathway Source: Reactome
    19. positive regulation of catalytic activity Source: BHF-UCL
    20. positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway Source: Reactome
    21. protein heterooligomerization Source: Ensembl
    22. protein targeting Source: Ensembl
    23. Ras protein signal transduction Source: Reactome
    24. RNA metabolic process Source: Reactome
    25. small GTPase mediated signal transduction Source: Reactome

    Enzyme and pathway databases

    ReactomeiREACT_118607. Signaling by Hippo.
    REACT_12002. ARMS-mediated activation.
    REACT_12076. Frs2-mediated activation.
    REACT_147867. Translocation of GLUT4 to the plasma membrane.
    REACT_2077. RAF activation.
    REACT_23898. Rap1 signalling.
    REACT_24915. Butyrate Response Factor 1 (BRF1) destabilizes mRNA.
    REACT_25064. Tristetraprolin (TTP) destabilizes mRNA.
    REACT_614. RAF phosphorylates MEK.
    REACT_962. MEK activation.
    SignaLinkiP31946.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    14-3-3 protein beta/alpha
    Alternative name(s):
    Protein 1054
    Protein kinase C inhibitor protein 1
    Short name:
    KCIP-1
    Cleaved into the following chain:
    Gene namesi
    Name:YWHAB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:12849. YWHAB.

    Subcellular locationi

    Cytoplasm 1 Publication. Melanosome 1 Publication
    Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytoplasmic vesicle membrane Source: Reactome
    3. cytosol Source: Reactome
    4. extracellular vesicular exosome Source: UniProtKB
    5. melanosome Source: UniProtKB-SubCell
    6. membrane Source: UniProtKB
    7. nucleus Source: Ensembl
    8. perinuclear region of cytoplasm Source: UniProtKB
    9. transcriptional repressor complex Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA37438.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 24624614-3-3 protein beta/alphaPRO_0000367900Add
    BLAST
    Initiator methioninei1 – 11Removed; alternate1 Publication
    Chaini2 – 24624514-3-3 protein beta/alpha, N-terminally processedPRO_0000000003Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine; in 14-3-3 protein beta/alpha; alternate2 Publications
    Modified residuei2 – 21N-acetylthreonine; in 14-3-3 protein beta/alpha, N-terminally processed2 Publications
    Modified residuei60 – 601PhosphoserineBy similarity
    Modified residuei70 – 701N6-acetyllysine1 Publication
    Modified residuei84 – 841Nitrated tyrosineBy similarity
    Modified residuei106 – 1061Nitrated tyrosineBy similarity
    Modified residuei117 – 1171N6-acetyllysine1 Publication
    Modified residuei186 – 1861PhosphoserineBy similarity

    Post-translational modificationi

    The alpha, brain-specific form differs from the beta form in being phosphorylated. Phosphorylated on Ser-60 by protein kinase C delta type catalytic subunit in a sphingosine-dependent fashion.By similarity
    Isoform Short contains a N-acetylmethionine at position 1.By similarity

    Keywords - PTMi

    Acetylation, Nitration, Phosphoprotein

    Proteomic databases

    MaxQBiP31946.
    PaxDbiP31946.
    PRIDEiP31946.

    2D gel databases

    OGPiP31946.
    REPRODUCTION-2DPAGEIPI00216318.

    PTM databases

    PhosphoSiteiP31946.

    Expressioni

    Gene expression databases

    ArrayExpressiP31946.
    BgeeiP31946.
    CleanExiHS_YWHAB.
    GenevestigatoriP31946.

    Organism-specific databases

    HPAiCAB003759.
    HPA007925.
    HPA011212.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with SAMSN1 and PRKCE By similarity. Interacts with SSH1 and TORC2/CRTC2. Interacts with ABL1; the interaction results in cytoplasmic location of ABL1 and inhibition of cABL-mediated apoptosis. Interacts with ROR2 (dimer); the interaction results in phosphorylation of YWHAB on tyrosine residues. Interacts with GAB2 and YAP1 (phosphorylated form). Interacts with the phosphorylated (by AKT1) form of SRPK2. Interacts with PKA-phosphorylated AANAT. Interacts with MYO1C and SIRT2.By similarity10 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Q763533EBI-359815,EBI-6248077From a different organism.
    ADAM22Q9P0K1-32EBI-359815,EBI-1567267
    BRAFP150563EBI-359815,EBI-365980
    CBLP226813EBI-359815,EBI-518228
    CBX4O002572EBI-359815,EBI-722425
    CDC25AP303048EBI-359815,EBI-747671
    CDC25BP303054EBI-359815,EBI-1051746
    CDK14O949215EBI-359815,EBI-1043945
    CSNK1A1P678283EBI-359815,EBI-7540603From a different organism.
    DACT1Q9NYF04EBI-359815,EBI-3951744
    DYRK1AQ13627-23EBI-359815,EBI-1053621
    GAB2Q9UQC24EBI-359815,EBI-975200
    GEMP550403EBI-359815,EBI-744104
    GemP550413EBI-359815,EBI-7082069From a different organism.
    HDAC4P565243EBI-359815,EBI-308629
    let-756Q111842EBI-359815,EBI-3843983From a different organism.
    LRRK2Q5S0075EBI-359815,EBI-5323863
    MAP3K3Q997592EBI-359815,EBI-307281
    MAP3K5Q996833EBI-359815,EBI-476263
    MARK2Q7KZI73EBI-359815,EBI-516560
    MARK3P274484EBI-359815,EBI-707595
    RAF1P0404917EBI-359815,EBI-365996
    RMDN3Q96TC75EBI-359815,EBI-1056589
    RND3P615872EBI-359815,EBI-1111534
    Rnd3P615885EBI-359815,EBI-6930266From a different organism.
    SRPK2P783622EBI-359815,EBI-593303
    SSH1Q8WYL53EBI-359815,EBI-1222387
    Synpo2Q91YE83EBI-359815,EBI-7623057From a different organism.
    TSC2P498154EBI-359815,EBI-396587
    YAP1P469375EBI-359815,EBI-1044059
    YWHAEP622583EBI-359815,EBI-356498
    Zfp36P228935EBI-359815,EBI-647803From a different organism.

    Protein-protein interaction databases

    BioGridi113361. 298 interactions.
    DIPiDIP-743N.
    IntActiP31946. 240 interactions.
    MINTiMINT-99570.
    STRINGi9606.ENSP00000300161.

    Structurei

    Secondary structure

    1
    246
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi5 – 1713
    Helixi21 – 3313
    Helixi40 – 6930
    Helixi75 – 10531
    Helixi107 – 1104
    Helixi114 – 13320
    Helixi139 – 16123
    Helixi167 – 18216
    Helixi187 – 20216
    Helixi203 – 2075
    Turni210 – 2123
    Helixi213 – 23220

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2BQ0X-ray2.50A/B2-239[»]
    2C23X-ray2.65A2-239[»]
    4DNKX-ray2.20A/B1-246[»]
    ProteinModelPortaliP31946.
    SMRiP31946. Positions 1-234.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP31946.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the 14-3-3 family.Curated

    Phylogenomic databases

    eggNOGiCOG5040.
    HOGENOMiHOG000240379.
    HOVERGENiHBG050423.
    InParanoidiP31946.
    KOiK16197.
    OMAiMGREYRE.
    OrthoDBiEOG7HHWT3.
    PhylomeDBiP31946.
    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.

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

    This entry describes 2 isoformsi produced by alternative initiation. Align

    Isoform Long (identifier: P31946-1) [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

    MTMDKSELVQ KAKLAEQAER YDDMAAAMKA VTEQGHELSN EERNLLSVAY    50
    KNVVGARRSS WRVISSIEQK TERNEKKQQM GKEYREKIEA ELQDICNDVL 100
    ELLDKYLIPN ATQPESKVFY LKMKGDYFRY LSEVASGDNK QTTVSNSQQA 150
    YQEAFEISKK EMQPTHPIRL GLALNFSVFY YEILNSPEKA CSLAKTAFDE 200
    AIAELDTLNE ESYKDSTLIM QLLRDNLTLW TSENQGDEGD AGEGEN 246
    Length:246
    Mass (Da):28,082
    Last modified:January 23, 2007 - v3
    Checksum:i6BE1A9BF97468017
    GO
    Isoform Short (identifier: P31946-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-2: Missing.

    Note: Contains a N-acetylmethionine at position 1.By similarity

    Show »
    Length:244
    Mass (Da):27,850
    Checksum:iCE0A59BF8C33FE2F
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti99 – 991V → I Found in a renal cell carcinoma sample; somatic mutation. 1 Publication
    VAR_064762

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 22Missing in isoform Short. CuratedVSP_018632

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X57346 mRNA. Translation: CAA40621.1.
    AK292717 mRNA. Translation: BAF85406.1.
    AL008725 Genomic DNA. Translation: CAA15497.1.
    CH471077 Genomic DNA. Translation: EAW75893.1.
    CH471077 Genomic DNA. Translation: EAW75894.1.
    CH471077 Genomic DNA. Translation: EAW75896.1.
    BC001359 mRNA. Translation: AAH01359.1.
    CCDSiCCDS13339.1. [P31946-1]
    PIRiS34755.
    RefSeqiNP_003395.1. NM_003404.4. [P31946-1]
    NP_647539.1. NM_139323.3. [P31946-1]
    UniGeneiHs.643544.

    Genome annotation databases

    EnsembliENST00000353703; ENSP00000300161; ENSG00000166913. [P31946-1]
    ENST00000372839; ENSP00000361930; ENSG00000166913. [P31946-1]
    GeneIDi7529.
    KEGGihsa:7529.
    UCSCiuc002xmt.3. human. [P31946-1]

    Polymorphism databases

    DMDMi1345590.

    Keywords - Coding sequence diversityi

    Alternative initiation, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X57346 mRNA. Translation: CAA40621.1 .
    AK292717 mRNA. Translation: BAF85406.1 .
    AL008725 Genomic DNA. Translation: CAA15497.1 .
    CH471077 Genomic DNA. Translation: EAW75893.1 .
    CH471077 Genomic DNA. Translation: EAW75894.1 .
    CH471077 Genomic DNA. Translation: EAW75896.1 .
    BC001359 mRNA. Translation: AAH01359.1 .
    CCDSi CCDS13339.1. [P31946-1 ]
    PIRi S34755.
    RefSeqi NP_003395.1. NM_003404.4. [P31946-1 ]
    NP_647539.1. NM_139323.3. [P31946-1 ]
    UniGenei Hs.643544.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2BQ0 X-ray 2.50 A/B 2-239 [» ]
    2C23 X-ray 2.65 A 2-239 [» ]
    4DNK X-ray 2.20 A/B 1-246 [» ]
    ProteinModelPortali P31946.
    SMRi P31946. Positions 1-234.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113361. 298 interactions.
    DIPi DIP-743N.
    IntActi P31946. 240 interactions.
    MINTi MINT-99570.
    STRINGi 9606.ENSP00000300161.

    PTM databases

    PhosphoSitei P31946.

    Polymorphism databases

    DMDMi 1345590.

    2D gel databases

    OGPi P31946.
    REPRODUCTION-2DPAGE IPI00216318.

    Proteomic databases

    MaxQBi P31946.
    PaxDbi P31946.
    PRIDEi P31946.

    Protocols and materials databases

    DNASUi 7529.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000353703 ; ENSP00000300161 ; ENSG00000166913 . [P31946-1 ]
    ENST00000372839 ; ENSP00000361930 ; ENSG00000166913 . [P31946-1 ]
    GeneIDi 7529.
    KEGGi hsa:7529.
    UCSCi uc002xmt.3. human. [P31946-1 ]

    Organism-specific databases

    CTDi 7529.
    GeneCardsi GC20P043515.
    HGNCi HGNC:12849. YWHAB.
    HPAi CAB003759.
    HPA007925.
    HPA011212.
    MIMi 601289. gene.
    neXtProti NX_P31946.
    PharmGKBi PA37438.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5040.
    HOGENOMi HOG000240379.
    HOVERGENi HBG050423.
    InParanoidi P31946.
    KOi K16197.
    OMAi MGREYRE.
    OrthoDBi EOG7HHWT3.
    PhylomeDBi P31946.
    TreeFami TF102003.

    Enzyme and pathway databases

    Reactomei REACT_118607. Signaling by Hippo.
    REACT_12002. ARMS-mediated activation.
    REACT_12076. Frs2-mediated activation.
    REACT_147867. Translocation of GLUT4 to the plasma membrane.
    REACT_2077. RAF activation.
    REACT_23898. Rap1 signalling.
    REACT_24915. Butyrate Response Factor 1 (BRF1) destabilizes mRNA.
    REACT_25064. Tristetraprolin (TTP) destabilizes mRNA.
    REACT_614. RAF phosphorylates MEK.
    REACT_962. MEK activation.
    SignaLinki P31946.

    Miscellaneous databases

    ChiTaRSi YWHAB. human.
    EvolutionaryTracei P31946.
    GeneWikii YWHAB.
    GenomeRNAii 7529.
    NextBioi 29453.
    PROi P31946.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P31946.
    Bgeei P31946.
    CleanExi HS_YWHAB.
    Genevestigatori P31946.

    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. "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].
      Tissue: Keratinocyte.
    2. "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] (ISOFORM LONG).
      Tissue: Thymus.
    3. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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].
      Tissue: Skin.
    6. Bienvenut W.V., Zebisch A., Kolch W.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 1-11; 14-57; 63-70; 106-117; 130-169 AND 215-246, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT MET-1 AND THR-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Colon carcinoma.
    7. "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 3-20.
      Tissue: Platelet.
    8. "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.
    9. "The CREB coactivator TORC2 functions as a calcium- and cAMP-sensitive coincidence detector."
      Screaton R.A., Conkright M.D., Katoh Y., Best J.L., Canettieri G., Jeffries S., Guzman E., Niessen S., Yates J.R. III, Takemori H., Okamoto M., Montminy M.
      Cell 119:61-74(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CRTC2.
    10. "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.
    11. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Melanoma.
    12. "Inactivation of YAP oncoprotein by the Hippo pathway is involved in cell contact inhibition and tissue growth control."
      Zhao B., Wei X., Li W., Udan R.S., Yang Q., Kim J., Xie J., Ikenoue T., Yu J., Li L., Zheng P., Ye K., Chinnaiyan A., Halder G., Lai Z.C., Guan K.L.
      Genes Dev. 21:2747-2761(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH YAP1.
    13. "Homodimerization of Ror2 tyrosine kinase receptor induces 14-3-3(beta) phosphorylation and promotes osteoblast differentiation and bone formation."
      Liu Y., Ross J.F., Bodine P.V.N., Billiard J.
      Mol. Endocrinol. 21:3050-3061(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ROR2, FUNCTION, PHOSPHORYLATION, DIMERIZATION, IDENTIFICATION BY MASS SPECTROMETRY.
    14. "Sirt2 interacts with 14-3-3 beta/gamma and down-regulates the activity of p53."
      Jin Y.H., Kim Y.J., Kim D.W., Baek K.H., Kang B.Y., Yeo C.Y., Lee K.Y.
      Biochem. Biophys. Res. Commun. 368:690-695(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SIRT2.
    15. "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.
    16. "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: FUNCTION, INTERACTION WITH SRPK2.
    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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    18. "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-70 AND LYS-117, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "Crystal structure of human myosin 1c - the motor in GLUT4 exocytosis: implications for Ca(2+)-regulation and 14-3-3 binding."
      Stefan Munnich M.H., Manstein D.J.
      J. Mol. Biol. 426:2070-2081(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MYO1C.
    22. Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-239, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH PHOSPHOSERINE MOTIFS, SUBUNIT.
    23. Cited for: VARIANT ILE-99.

    Entry informationi

    Entry namei1433B_HUMAN
    AccessioniPrimary (citable) accession number: P31946
    Secondary accession number(s): A8K9K2, E1P616
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 168 of the entry and version 3 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 20
      Human chromosome 20: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3