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)

P31947

- 1433S_HUMAN

UniProt

P31947 - 1433S_HUMAN

Protein

14-3-3 protein sigma

Gene

SFN

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 155 (01 Oct 2014)
      Sequence version 1 (01 Jul 1993)
      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. When bound to KRT17, regulates protein synthesis and epithelial cell growth by stimulating Akt/mTOR pathway. May also regulate MDM2 autoubiquitination and degradation and thereby activate p53/TP53.1 Publication
    p53-regulated inhibitor of G2/M progression.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei56 – 561Interaction with phosphoserine on interacting protein
    Sitei129 – 1291Interaction with phosphoserine on interacting protein

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. protein kinase C inhibitor activity Source: ProtInc

    GO - Biological processi

    1. apoptotic process Source: Reactome
    2. establishment of skin barrier Source: UniProtKB
    3. intrinsic apoptotic signaling pathway Source: Reactome
    4. intrinsic apoptotic signaling pathway in response to DNA damage Source: HGNC
    5. keratinocyte differentiation Source: Ensembl
    6. keratinocyte proliferation Source: Ensembl
    7. membrane organization Source: Reactome
    8. negative regulation of cell proliferation Source: Ensembl
    9. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: HGNC
    10. negative regulation of protein kinase activity Source: ProtInc
    11. negative regulation of protein serine/threonine kinase activity Source: GOC
    12. positive regulation of cell growth Source: Ensembl
    13. positive regulation of epidermal cell differentiation Source: UniProtKB
    14. positive regulation of protein export from nucleus Source: Ensembl
    15. positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway Source: Reactome
    16. regulation of cyclin-dependent protein serine/threonine kinase activity Source: Ensembl
    17. regulation of epidermal cell division Source: UniProtKB
    18. release of cytochrome c from mitochondria Source: HGNC
    19. signal transduction Source: ProtInc

    Enzyme and pathway databases

    ReactomeiREACT_147867. Translocation of GLUT4 to the plasma membrane.
    SignaLinkiP31947.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    14-3-3 protein sigma
    Alternative name(s):
    Epithelial cell marker protein 1
    Stratifin
    Gene namesi
    Name:SFN
    Synonyms:HME1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:10773. SFN.

    Subcellular locationi

    Cytoplasm. Nucleus By similarity. Secreted
    Note: May be secreted by a non-classical secretory pathway.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytoplasmic vesicle membrane Source: Reactome
    3. cytosol Source: Reactome
    4. extracellular space Source: ProtInc
    5. extracellular vesicular exosome Source: UniProt
    6. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA177.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 24824814-3-3 protein sigmaPRO_0000058643Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei5 – 51Phosphoserine1 Publication
    Modified residuei248 – 2481Phosphoserine4 Publications

    Post-translational modificationi

    Ubiquitinated. Ubiquitination by RFFL induces proteasomal degradation and indirectly regulates p53/TP53 activation.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP31947.
    PaxDbiP31947.
    PeptideAtlasiP31947.
    PRIDEiP31947.

    2D gel databases

    OGPiP31947.
    SWISS-2DPAGEP31947.

    PTM databases

    PhosphoSiteiP31947.

    Expressioni

    Tissue specificityi

    Present mainly in tissues enriched in stratified squamous keratinizing epithelium.

    Gene expression databases

    BgeeiP31947.
    CleanExiHS_SFN.
    GenevestigatoriP31947.

    Organism-specific databases

    HPAiCAB006268.
    CAB040552.
    HPA011105.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with KRT17 and SAMSN1 By similarity. Found in a complex with XPO7, EIF4A1, ARHGAP1, VPS26A, VPS29, VPS35 and SFN. Interacts with GAB2. Interacts with SRPK2. Interacts with COPS6. Interacts with RFWD2; this interaction leads to proteasomal degradation.By similarity6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ABL1P005192EBI-476295,EBI-375543
    AJUBAQ96IF12EBI-476295,EBI-949782
    BADQ929344EBI-476295,EBI-700771
    COPS6Q7L5N17EBI-476295,EBI-486838
    ERRFI1Q9UJM33EBI-476295,EBI-2941912
    GPRIN2O602692EBI-476295,EBI-740397
    HDAC4P565244EBI-476295,EBI-308629
    HDAC5Q9UQL63EBI-476295,EBI-715576
    HDAC7Q8WUI43EBI-476295,EBI-1048378
    HNRNPDQ14103-47EBI-476295,EBI-432545
    MARK3P274482EBI-476295,EBI-707595
    PLK4O004442EBI-476295,EBI-746202
    RAF1P040492EBI-476295,EBI-365996
    REPS2Q8NFH8-22EBI-476295,EBI-8029141
    RFWD2Q8NHY26EBI-476295,EBI-1176214
    TP53P046374EBI-476295,EBI-366083
    YWHAZP631042EBI-476295,EBI-347088

    Protein-protein interaction databases

    BioGridi109072. 138 interactions.
    DIPiDIP-29861N.
    IntActiP31947. 150 interactions.
    MINTiMINT-108060.
    STRINGi9606.ENSP00000340989.

    Structurei

    Secondary structure

    1
    248
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 1513
    Helixi19 – 3113
    Helixi38 – 6932
    Helixi80 – 10425
    Helixi107 – 1104
    Helixi114 – 13421
    Beta strandi137 – 1393
    Helixi140 – 16122
    Helixi167 – 18216
    Helixi187 – 20418
    Helixi205 – 2073
    Helixi210 – 23021

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1YWTX-ray2.40A/B1-248[»]
    1YZ5X-ray2.80A/B1-248[»]
    3IQJX-ray1.15A1-231[»]
    3IQUX-ray1.05A1-231[»]
    3IQVX-ray1.20A1-231[»]
    3LW1X-ray1.28A1-248[»]
    3MHRX-ray1.15A1-231[»]
    3O8IX-ray2.00A1-231[»]
    3P1NX-ray1.40A1-231[»]
    3P1OX-ray1.90A1-231[»]
    3P1PX-ray1.95A1-231[»]
    3P1QX-ray1.70A1-231[»]
    3P1RX-ray1.70A1-231[»]
    3P1SX-ray1.65A1-231[»]
    3SMKX-ray2.10A1-231[»]
    3SMLX-ray1.90A1-231[»]
    3SMMX-ray2.00A1-231[»]
    3SMNX-ray2.00A1-231[»]
    3SMOX-ray1.80A1-231[»]
    3SPRX-ray1.99A1-231[»]
    3T0LX-ray1.60A1-231[»]
    3T0MX-ray1.62A1-231[»]
    3U9XX-ray1.80A1-231[»]
    3UX0X-ray1.75A1-231[»]
    4DATX-ray1.40A1-231[»]
    4DAUX-ray2.00A1-231[»]
    4DHMX-ray1.70A1-231[»]
    4DHNX-ray1.80A1-231[»]
    4DHOX-ray1.70A1-231[»]
    4DHPX-ray1.75A1-231[»]
    4DHQX-ray1.75A1-231[»]
    4DHRX-ray1.40A1-231[»]
    4DHSX-ray1.74A1-231[»]
    4DHTX-ray1.80A1-231[»]
    4DHUX-ray1.67A1-231[»]
    4FL5X-ray1.90A/B1-231[»]
    4FR3X-ray1.90A1-231[»]
    4HQWX-ray2.35A1-231[»]
    4HRUX-ray3.15A1-231[»]
    4IEAX-ray1.70A1-231[»]
    4JC3X-ray2.05A1-231[»]
    4JDDX-ray2.10A1-231[»]
    ProteinModelPortaliP31947.
    SMRiP31947. Positions 1-231.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP31947.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the 14-3-3 family.Curated

    Phylogenomic databases

    eggNOGiCOG5040.
    HOGENOMiHOG000240379.
    HOVERGENiHBG050423.
    InParanoidiP31947.
    KOiK06644.
    OMAiEQKGNEE.
    OrthoDBiEOG7HHWT3.
    PhylomeDBiP31947.
    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: P31947-1) [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

    MERASLIQKA KLAEQAERYE DMAAFMKGAV EKGEELSCEE RNLLSVAYKN    50
    VVGGQRAAWR VLSSIEQKSN EEGSEEKGPE VREYREKVET ELQGVCDTVL 100
    GLLDSHLIKE AGDAESRVFY LKMKGDYYRY LAEVATGDDK KRIIDSARSA 150
    YQEAMDISKK EMPPTNPIRL GLALNFSVFH YEIANSPEEA ISLAKTTFDE 200
    AMADLHTLSE DSYKDSTLIM QLLRDNLTLW TADNAGEEGG EAPQEPQS 248
    Length:248
    Mass (Da):27,774
    Last modified:July 1, 1993 - v1
    Checksum:i7F4B44E3AA59ECE6
    GO
    Isoform 2 (identifier: P31947-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         85-116: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:216
    Mass (Da):24,336
    Checksum:i14CBC2F26014D926
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti77 – 771K → M in CAG46703. 1 PublicationCurated
    Sequence conflicti120 – 1201Y → H in AAA59546. (PubMed:8515476)Curated
    Sequence conflicti242 – 2421A → V in AAA59546. (PubMed:8515476)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti155 – 1551M → I.
    Corresponds to variant rs11542705 [ dbSNP | Ensembl ].
    VAR_048095

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei85 – 11632Missing in isoform 2. 1 PublicationVSP_021768Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M93010 mRNA. Translation: AAA59546.1.
    X57348 mRNA. Translation: CAA40623.1.
    AF029081 Genomic DNA. Translation: AAC52029.1.
    AF029082 mRNA. Translation: AAC52030.1.
    CR541905 mRNA. Translation: CAG46703.1.
    CR541926 mRNA. Translation: CAG46724.1.
    AL034380 Genomic DNA. Translation: CAB92118.1.
    BC000329 mRNA. Translation: AAH00329.1.
    BC000995 mRNA. Translation: AAH00995.1.
    BC001550 mRNA. Translation: AAH01550.1.
    BC002995 mRNA. Translation: AAH02995.1.
    BC023552 mRNA. Translation: AAH23552.1.
    CCDSiCCDS288.1. [P31947-1]
    PIRiS34753.
    S38956.
    RefSeqiNP_006133.1. NM_006142.3. [P31947-1]
    UniGeneiHs.523718.

    Genome annotation databases

    EnsembliENST00000339276; ENSP00000340989; ENSG00000175793. [P31947-1]
    GeneIDi2810.
    KEGGihsa:2810.
    UCSCiuc001bnc.1. human. [P31947-1]

    Polymorphism databases

    DMDMi398953.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M93010 mRNA. Translation: AAA59546.1 .
    X57348 mRNA. Translation: CAA40623.1 .
    AF029081 Genomic DNA. Translation: AAC52029.1 .
    AF029082 mRNA. Translation: AAC52030.1 .
    CR541905 mRNA. Translation: CAG46703.1 .
    CR541926 mRNA. Translation: CAG46724.1 .
    AL034380 Genomic DNA. Translation: CAB92118.1 .
    BC000329 mRNA. Translation: AAH00329.1 .
    BC000995 mRNA. Translation: AAH00995.1 .
    BC001550 mRNA. Translation: AAH01550.1 .
    BC002995 mRNA. Translation: AAH02995.1 .
    BC023552 mRNA. Translation: AAH23552.1 .
    CCDSi CCDS288.1. [P31947-1 ]
    PIRi S34753.
    S38956.
    RefSeqi NP_006133.1. NM_006142.3. [P31947-1 ]
    UniGenei Hs.523718.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1YWT X-ray 2.40 A/B 1-248 [» ]
    1YZ5 X-ray 2.80 A/B 1-248 [» ]
    3IQJ X-ray 1.15 A 1-231 [» ]
    3IQU X-ray 1.05 A 1-231 [» ]
    3IQV X-ray 1.20 A 1-231 [» ]
    3LW1 X-ray 1.28 A 1-248 [» ]
    3MHR X-ray 1.15 A 1-231 [» ]
    3O8I X-ray 2.00 A 1-231 [» ]
    3P1N X-ray 1.40 A 1-231 [» ]
    3P1O X-ray 1.90 A 1-231 [» ]
    3P1P X-ray 1.95 A 1-231 [» ]
    3P1Q X-ray 1.70 A 1-231 [» ]
    3P1R X-ray 1.70 A 1-231 [» ]
    3P1S X-ray 1.65 A 1-231 [» ]
    3SMK X-ray 2.10 A 1-231 [» ]
    3SML X-ray 1.90 A 1-231 [» ]
    3SMM X-ray 2.00 A 1-231 [» ]
    3SMN X-ray 2.00 A 1-231 [» ]
    3SMO X-ray 1.80 A 1-231 [» ]
    3SPR X-ray 1.99 A 1-231 [» ]
    3T0L X-ray 1.60 A 1-231 [» ]
    3T0M X-ray 1.62 A 1-231 [» ]
    3U9X X-ray 1.80 A 1-231 [» ]
    3UX0 X-ray 1.75 A 1-231 [» ]
    4DAT X-ray 1.40 A 1-231 [» ]
    4DAU X-ray 2.00 A 1-231 [» ]
    4DHM X-ray 1.70 A 1-231 [» ]
    4DHN X-ray 1.80 A 1-231 [» ]
    4DHO X-ray 1.70 A 1-231 [» ]
    4DHP X-ray 1.75 A 1-231 [» ]
    4DHQ X-ray 1.75 A 1-231 [» ]
    4DHR X-ray 1.40 A 1-231 [» ]
    4DHS X-ray 1.74 A 1-231 [» ]
    4DHT X-ray 1.80 A 1-231 [» ]
    4DHU X-ray 1.67 A 1-231 [» ]
    4FL5 X-ray 1.90 A/B 1-231 [» ]
    4FR3 X-ray 1.90 A 1-231 [» ]
    4HQW X-ray 2.35 A 1-231 [» ]
    4HRU X-ray 3.15 A 1-231 [» ]
    4IEA X-ray 1.70 A 1-231 [» ]
    4JC3 X-ray 2.05 A 1-231 [» ]
    4JDD X-ray 2.10 A 1-231 [» ]
    ProteinModelPortali P31947.
    SMRi P31947. Positions 1-231.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109072. 138 interactions.
    DIPi DIP-29861N.
    IntActi P31947. 150 interactions.
    MINTi MINT-108060.
    STRINGi 9606.ENSP00000340989.

    Chemistry

    BindingDBi P31947.
    ChEMBLi CHEMBL1909482.

    PTM databases

    PhosphoSitei P31947.

    Polymorphism databases

    DMDMi 398953.

    2D gel databases

    OGPi P31947.
    SWISS-2DPAGE P31947.

    Proteomic databases

    MaxQBi P31947.
    PaxDbi P31947.
    PeptideAtlasi P31947.
    PRIDEi P31947.

    Protocols and materials databases

    DNASUi 2810.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000339276 ; ENSP00000340989 ; ENSG00000175793 . [P31947-1 ]
    GeneIDi 2810.
    KEGGi hsa:2810.
    UCSCi uc001bnc.1. human. [P31947-1 ]

    Organism-specific databases

    CTDi 2810.
    GeneCardsi GC01P027189.
    HGNCi HGNC:10773. SFN.
    HPAi CAB006268.
    CAB040552.
    HPA011105.
    MIMi 601290. gene.
    neXtProti NX_P31947.
    PharmGKBi PA177.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5040.
    HOGENOMi HOG000240379.
    HOVERGENi HBG050423.
    InParanoidi P31947.
    KOi K06644.
    OMAi EQKGNEE.
    OrthoDBi EOG7HHWT3.
    PhylomeDBi P31947.
    TreeFami TF102003.

    Enzyme and pathway databases

    Reactomei REACT_147867. Translocation of GLUT4 to the plasma membrane.
    SignaLinki P31947.

    Miscellaneous databases

    EvolutionaryTracei P31947.
    GeneWikii Stratifin.
    GenomeRNAii 2810.
    NextBioi 11071.
    PROi P31947.
    SOURCEi Search...

    Gene expression databases

    Bgeei P31947.
    CleanExi HS_SFN.
    Genevestigatori P31947.

    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. "Complementary DNA cloning of a novel epithelial cell marker protein, HME1, that may be down-regulated in neoplastic mammary cells."
      Prasad G.L., Valverius E.M., McDuffie E., Cooper H.L.
      Cell Growth Differ. 3:507-513(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Epithelium.
    2. "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] (ISOFORM 1), PROTEIN SEQUENCE OF 19-25; 42-49; 118-122; 130-139; 149-159; 161-181; 196-199; 225-229 AND 231-239.
      Tissue: Keratinocyte.
    3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
    4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    5. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORMS 1 AND 2).
      Tissue: Cervix, Lung and Placenta.
    7. "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes."
      Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.
      Electrophoresis 13:960-969(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 42-49 AND 118-122.
      Tissue: Keratinocyte.
    8. "Exportin 7 defines a novel general nuclear export pathway."
      Mingot J.-M., Bohnsack M.T., Jaekle U., Goerlich D.
      EMBO J. 23:3227-3236(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH XPO7; ARHGAP1; EIF4A1; VPS26A; VPS29 AND VPS35.
    9. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "CARPs enhance p53 turnover by degrading 14-3-3sigma and stabilizing MDM2."
      Yang W., Dicker D.T., Chen J., El-Deiry W.S.
      Cell Cycle 7:670-682(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MDM2 UBIQUITINATION, UBIQUITINATION BY RFFL.
    11. "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.
    12. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "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.
    15. "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-5 AND SER-248, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "COP9 signalosome subunit 6 stabilizes COP1, which functions as an E3 ubiquitin ligase for 14-3-3sigma."
      Choi H.H., Gully C., Su C.H., Velazquez-Torres G., Chou P.C., Tseng C., Zhao R., Phan L., Shaiken T., Chen J., Yeung S.C., Lee M.H.
      Oncogene 30:4791-4801(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH COPS6 AND RFWD2.
    18. "A structural basis for 14-3-3sigma functional specificity."
      Wilker E.W., Grant R.A., Artim S.C., Yaffe M.B.
      J. Biol. Chem. 280:18891-18898(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH PHOSPHOSERINE PEPTIDE.
    19. "Identification and structural characterization of two 14-3-3 binding sites in the human peptidylarginine deiminase type VI."
      Rose R., Rose M., Ottmann C.
      J. Struct. Biol. 180:65-72(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 1-231 IN COMPLEX WITH PADI6 PHOSPHOPEPTIDES.

    Entry informationi

    Entry namei1433S_HUMAN
    AccessioniPrimary (citable) accession number: P31947
    Secondary accession number(s): Q6FH30, Q6FH51, Q96DH0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: July 1, 1993
    Last modified: October 1, 2014
    This is version 155 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 1
      Human chromosome 1: 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