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P61981

- 1433G_HUMAN

UniProt

P61981 - 1433G_HUMAN

Protein

14-3-3 protein gamma

Gene

YWHAG

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 2 (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.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. insulin-like growth factor receptor binding Source: UniProtKB
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. protein kinase C binding Source: UniProtKB
    5. protein kinase C inhibitor activity Source: UniProtKB

    GO - Biological processi

    1. apoptotic process Source: Reactome
    2. cellular response to insulin stimulus Source: Ensembl
    3. G2/M transition of mitotic cell cycle Source: Reactome
    4. intrinsic apoptotic signaling pathway Source: Reactome
    5. membrane organization Source: Reactome
    6. mitotic cell cycle Source: Reactome
    7. negative regulation of protein kinase activity Source: UniProtKB
    8. negative regulation of protein serine/threonine kinase activity Source: GOC
    9. positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway Source: Reactome
    10. protein targeting Source: Ensembl
    11. regulation of neuron differentiation Source: UniProtKB
    12. regulation of signal transduction Source: UniProtKB
    13. regulation of synaptic plasticity Source: UniProtKB

    Enzyme and pathway databases

    ReactomeiREACT_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.
    SignaLinkiP61981.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    14-3-3 protein gamma
    Alternative name(s):
    Protein kinase C inhibitor protein 1
    Short name:
    KCIP-1
    Cleaved into the following chain:
    Gene namesi
    Name:YWHAG
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:12852. YWHAG.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasmic vesicle membrane Source: Reactome
    2. cytosol Source: Reactome
    3. extracellular vesicular exosome Source: UniProtKB
    4. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA37441.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 24724714-3-3 protein gammaPRO_0000367907Add
    BLAST
    Initiator methioninei1 – 11Removed; alternate5 Publications
    Chaini2 – 24724614-3-3 protein gamma, N-terminally processedPRO_0000058606Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine; in 14-3-3 protein gamma; alternate; partial1 Publication
    Modified residuei2 – 21N-acetylvaline; in 14-3-3 protein gamma, N-terminally processed; partial4 Publications
    Modified residuei2 – 21N-acetylvaline; partial4 Publications
    Modified residuei145 – 1451Phosphothreonine2 Publications

    Post-translational modificationi

    Phosphorylated by various PKC isozymes.2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP61981.
    PaxDbiP61981.
    PeptideAtlasiP61981.
    PRIDEiP61981.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00220642.

    PTM databases

    PhosphoSiteiP61981.

    Expressioni

    Tissue specificityi

    Highly expressed in brain, skeletal muscle, and heart.1 Publication

    Gene expression databases

    ArrayExpressiP61981.
    BgeeiP61981.
    CleanExiHS_YWHAG.
    GenevestigatoriP61981.

    Organism-specific databases

    HPAiCAB013274.
    CAB018389.
    HPA026918.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with SAMSN1 By similarity. Interacts with RAF1, SSH1 and CRTC2/TORC2. Interacts with ABL1 (phosphorylated form); the interaction retains it in the cytoplasm. Interacts with GAB2. Interacts with MDM4 (phosphorylated); negatively regulates MDM4 activity toward TP53. Interacts with PKA-phosphorylated AANAT and SIRT2.By similarity9 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CHEK1O147577EBI-359832,EBI-974488
    CSNK1A1P678283EBI-359832,EBI-7540603From a different organism.
    HDAC4P565243EBI-359832,EBI-308629
    KANK1Q14678-23EBI-359832,EBI-6173812
    LRRK2Q5S0074EBI-359832,EBI-5323863
    MARK2Q7KZI72EBI-359832,EBI-516560
    MARK3P274482EBI-359832,EBI-707595
    MDM4O151517EBI-359832,EBI-398437
    Rnd3P615882EBI-359832,EBI-6930266From a different organism.
    TP53P046375EBI-359832,EBI-366083
    YWHAEP622584EBI-359832,EBI-356498

    Protein-protein interaction databases

    BioGridi113364. 252 interactions.
    IntActiP61981. 103 interactions.
    MINTiMINT-248956.
    STRINGi9606.ENSP00000306330.

    Structurei

    Secondary structure

    1
    247
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 1613
    Helixi20 – 3112
    Helixi39 – 7032
    Helixi79 – 10628
    Helixi108 – 1114
    Helixi117 – 13721
    Helixi140 – 16425
    Helixi170 – 18516
    Helixi190 – 20617
    Helixi207 – 2104
    Turni213 – 2153
    Helixi216 – 23318

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2B05X-ray2.55A/B/C/D/E/F2-247[»]
    3UZDX-ray1.86A1-247[»]
    4E2EX-ray2.25A1-247[»]
    4J6SX-ray3.08A/B/C/D1-247[»]
    4O46X-ray2.90A/B/C/D/E/F1-247[»]
    ProteinModelPortaliP61981.
    SMRiP61981. Positions 1-235.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP61981.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the 14-3-3 family.Curated

    Phylogenomic databases

    eggNOGiCOG5040.
    HOGENOMiHOG000240379.
    HOVERGENiHBG050423.
    InParanoidiP61981.
    KOiK16198.
    OMAiCSETQHE.
    OrthoDBiEOG7HHWT3.
    PhylomeDBiP61981.
    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.

    P61981-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVDREQLVQK ARLAEQAERY DDMAAAMKNV TELNEPLSNE ERNLLSVAYK    50
    NVVGARRSSW RVISSIEQKT SADGNEKKIE MVRAYREKIE KELEAVCQDV 100
    LSLLDNYLIK NCSETQYESK VFYLKMKGDY YRYLAEVATG EKRATVVESS 150
    EKAYSEAHEI SKEHMQPTHP IRLGLALNYS VFYYEIQNAP EQACHLAKTA 200
    FDDAIAELDT LNEDSYKDST LIMQLLRDNL TLWTSDQQDD DGGEGNN 247
    Length:247
    Mass (Da):28,303
    Last modified:January 23, 2007 - v2
    Checksum:iB0D16C6DE1F4455D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti4 – 41R → P in AAD48408. (PubMed:10433554)Curated
    Sequence conflicti19 – 191R → G in AAD48408. (PubMed:10433554)Curated
    Sequence conflicti78 – 781Missing in AAD48408. (PubMed:10433554)Curated
    Sequence conflicti89 – 891I → V in AAD48408. (PubMed:10433554)Curated
    Sequence conflicti104 – 1041L → V in AAD48408. (PubMed:10433554)Curated
    Sequence conflicti109 – 1091I → Y in AAD48408. (PubMed:10433554)Curated
    Sequence conflicti119 – 1224SKVF → RKDL in AAD48408. (PubMed:10433554)Curated
    Sequence conflicti144 – 1452AT → GD in AAD48408. (PubMed:10433554)Curated
    Sequence conflicti157 – 1582AH → R in AAD48408. (PubMed:10433554)Curated
    Sequence conflicti200 – 2023AFD → EFE in AAD48408. (PubMed:10433554)Curated
    Sequence conflicti214 – 2141D → E in AAD48408. (PubMed:10433554)Curated
    Sequence conflicti240 – 2401D → DH in AAD48408. (PubMed:10433554)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF142498 mRNA. Translation: AAD48408.1.
    AB024334 mRNA. Translation: BAA85184.1.
    CR541904 mRNA. Translation: CAG46702.1.
    CR541925 mRNA. Translation: CAG46723.1.
    AC006388 Genomic DNA. No translation available.
    BC020963 mRNA. Translation: AAH20963.1.
    CCDSiCCDS5584.1.
    RefSeqiNP_036611.2. NM_012479.3.
    UniGeneiHs.744840.

    Genome annotation databases

    EnsembliENST00000307630; ENSP00000306330; ENSG00000170027.
    GeneIDi7532.
    KEGGihsa:7532.
    UCSCiuc011kgj.1. human.

    Polymorphism databases

    DMDMi48428721.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF142498 mRNA. Translation: AAD48408.1 .
    AB024334 mRNA. Translation: BAA85184.1 .
    CR541904 mRNA. Translation: CAG46702.1 .
    CR541925 mRNA. Translation: CAG46723.1 .
    AC006388 Genomic DNA. No translation available.
    BC020963 mRNA. Translation: AAH20963.1 .
    CCDSi CCDS5584.1.
    RefSeqi NP_036611.2. NM_012479.3.
    UniGenei Hs.744840.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2B05 X-ray 2.55 A/B/C/D/E/F 2-247 [» ]
    3UZD X-ray 1.86 A 1-247 [» ]
    4E2E X-ray 2.25 A 1-247 [» ]
    4J6S X-ray 3.08 A/B/C/D 1-247 [» ]
    4O46 X-ray 2.90 A/B/C/D/E/F 1-247 [» ]
    ProteinModelPortali P61981.
    SMRi P61981. Positions 1-235.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113364. 252 interactions.
    IntActi P61981. 103 interactions.
    MINTi MINT-248956.
    STRINGi 9606.ENSP00000306330.

    Chemistry

    BindingDBi P61981.
    ChEMBLi CHEMBL1293296.

    PTM databases

    PhosphoSitei P61981.

    Polymorphism databases

    DMDMi 48428721.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00220642.

    Proteomic databases

    MaxQBi P61981.
    PaxDbi P61981.
    PeptideAtlasi P61981.
    PRIDEi P61981.

    Protocols and materials databases

    DNASUi 7532.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000307630 ; ENSP00000306330 ; ENSG00000170027 .
    GeneIDi 7532.
    KEGGi hsa:7532.
    UCSCi uc011kgj.1. human.

    Organism-specific databases

    CTDi 7532.
    GeneCardsi GC07M075956.
    HGNCi HGNC:12852. YWHAG.
    HPAi CAB013274.
    CAB018389.
    HPA026918.
    MIMi 605356. gene.
    neXtProti NX_P61981.
    PharmGKBi PA37441.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5040.
    HOGENOMi HOG000240379.
    HOVERGENi HBG050423.
    InParanoidi P61981.
    KOi K16198.
    OMAi CSETQHE.
    OrthoDBi EOG7HHWT3.
    PhylomeDBi P61981.
    TreeFami TF102003.

    Enzyme and pathway databases

    Reactomei 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.
    SignaLinki P61981.

    Miscellaneous databases

    ChiTaRSi YWHAG. human.
    EvolutionaryTracei P61981.
    GeneWikii YWHAG.
    GenomeRNAii 7532.
    NextBioi 29467.
    PROi P61981.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P61981.
    Bgeei P61981.
    CleanExi HS_YWHAG.
    Genevestigatori P61981.

    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. "14-3-3gamma interacts with and is phosphorylated by multiple protein kinase C isoforms in PDGF-stimulated human vascular smooth muscle cells."
      Autieri M.V., Carbone C.J.
      DNA Cell Biol. 18:555-564(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION, INTERACTION WITH RAF1.
      Tissue: Vascular smooth muscle.
    2. "Cloning, expression, and chromosomal mapping of the human 14-3-3gamma gene (YWHAG) to 7q11.23."
      Horie M., Suzuki M., Takahashi E., Tanigami A.
      Genomics 60:241-243(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
      Tissue: Fetal brain.
    3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      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: Endometrial tumor.
    6. Bienvenut W.V., Boldt K., von Kriegsheim A.F., Zebisch A., Kolch W.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 1-10; 13-56; 62-69; 133-172 AND 199-227, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT MET-1 AND VAL-2, PHOSPHORYLATION AT THR-145, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Colon carcinoma and Hepatoma.
    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 2-12.
      Tissue: Platelet.
    8. Bienvenut W.V., Claeys D.
      Submitted (NOV-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-10; 13-19; 29-42; 62-69; 133-143 AND 218-227, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT VAL-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Platelet.
    9. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 92-110; 199-217 AND 228-247, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    10. "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.
    11. Cited for: CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT VAL-2, IDENTIFICATION BY MASS SPECTROMETRY.
    12. "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.
    13. "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.
    14. "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.
    15. "14-3-3gamma binds to MDMX that is phosphorylated by UV-activated Chk1, resulting in p53 activation."
      Jin Y., Dai M.S., Lu S.Z., Xu Y., Luo Z., Zhao Y., Lu H.
      EMBO J. 25:1207-1218(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TP53 ACTIVATION, INTERACTION WITH MDM4.
    16. "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.
    17. "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.
    18. "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 VAL-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "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.
    20. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS), IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH PHOSPHOSERINE MOTIFS, SUBUNIT.

    Entry informationi

    Entry namei1433G_HUMAN
    AccessioniPrimary (citable) accession number: P61981
    Secondary accession number(s): O70457
    , P35214, Q6FH52, Q9UDP2, Q9UN99
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2004
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 124 of the entry and version 2 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 7
      Human chromosome 7: 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