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Q9NX09

- DDIT4_HUMAN

UniProt

Q9NX09 - DDIT4_HUMAN

Protein

DNA damage-inducible transcript 4 protein

Gene

DDIT4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Regulates cell growth, proliferation and survival via inhibition of the activity of the mammalian target of rapamycin complex 1 (mTORC1). Inhibition of mTORC1 is mediated by a pathway that involves DDIT4/REDD1, AKT1, the TSC1-TSC2 complex and the GTPase RHEB. Plays an important role in responses to cellular energy levels and cellular stress, including responses to hypoxia and DNA damage. Regulates p53/TP53-mediated apoptosis in response to DNA damage via its effect on mTORC1 activity. Its role in the response to hypoxia depends on the cell type; it mediates mTORC1 inhibition in fibroblasts and thymocytes, but not in hepatocytes By similarity. Required for mTORC1-mediated defense against viral protein synthesis and virus replication By similarity. Inhibits neuronal differentiation and neurite outgrowth mediated by NGF via its effect on mTORC1 activity. Required for normal neuron migration during embryonic brain development. Plays a role in neuronal cell death.By similarity8 Publications

    GO - Biological processi

    1. brain development Source: UniProtKB
    2. cell proliferation Source: UniProtKB
    3. defense response to virus Source: UniProtKB-KW
    4. intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: UniProtKB
    5. negative regulation of glycolytic process Source: Ensembl
    6. negative regulation of intracellular signal transduction Source: UniProtKB
    7. negative regulation of peptidyl-serine phosphorylation Source: UniProtKB
    8. negative regulation of peptidyl-threonine phosphorylation Source: UniProtKB
    9. negative regulation of TOR signaling Source: UniProtKB
    10. neuron differentiation Source: UniProtKB
    11. neuron migration Source: UniProtKB
    12. neurotrophin TRK receptor signaling pathway Source: UniProtKB
    13. positive regulation of neuron death Source: UniProtKB
    14. protein complex disassembly Source: Ensembl
    15. reactive oxygen species metabolic process Source: Ensembl
    16. response to hypoxia Source: UniProtKB

    Keywords - Biological processi

    Antiviral defense, Apoptosis

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA damage-inducible transcript 4 protein
    Alternative name(s):
    HIF-1 responsive protein RTP801
    Protein regulated in development and DNA damage response 1
    Short name:
    REDD-1
    Gene namesi
    Name:DDIT4
    Synonyms:REDD1, RTP801
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:24944. DDIT4.

    Subcellular locationi

    Mitochondrion By similarity. Cytoplasmcytosol 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: UniProtKB-SubCell
    3. intracellular Source: LIFEdb
    4. mitochondrion Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi19 – 191S → A: Strongly inhibits proteasomal degradation. 1 Publication
    Mutagenesisi23 – 231T → A: Strongly inhibits proteasomal degradation. Strongly inhibits proteasomal degradation; when associated with A-25. 1 Publication
    Mutagenesisi25 – 251T → A: Strongly inhibits proteasomal degradation; when associated with A-23. 1 Publication
    Mutagenesisi103 – 1031S → L or W: No effect on inhibition of mTORC1. 1 Publication
    Mutagenesisi133 – 1331R → A: No effect on inhibition of mTORC1. 1 Publication
    Mutagenesisi137 – 1371S → A or D: No effect on inhibition of mTORC1. 1 Publication
    Mutagenesisi139 – 1391P → A: Abolishes inhibition of mTORC1. 1 Publication
    Mutagenesisi140 – 1401C → S: Mildly reduces inhibition of mTORC1. 1 Publication
    Mutagenesisi219 – 2191K → A: Reduces inhibition of mTORC1. Abolishes inhibition of mTORC1; when associated with A-222. 1 Publication
    Mutagenesisi221 – 2211L → A: Reduces inhibition of mTORC1. 1 Publication
    Mutagenesisi222 – 2221Y → A: Reduces inhibition of mTORC1. Abolishes inhibition of mTORC1; when associated with A-219. 1 Publication

    Organism-specific databases

    PharmGKBiPA134977994.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 232232DNA damage-inducible transcript 4 proteinPRO_0000307197Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei19 – 191Phosphoserine1 Publication
    Modified residuei23 – 231Phosphothreonine1 Publication
    Modified residuei25 – 251Phosphothreonine1 Publication
    Modified residuei121 – 1211Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylated by GSK3B; this promotes proteasomal degradation.1 Publication
    Polyubiquitinated by a DCX (DDB1-CUL4A-RBX1) E3 ubiquitin-protein ligase complex with BTRC as substrate-recognition component, leading to its proteasomal degradation.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9NX09.
    PaxDbiQ9NX09.
    PRIDEiQ9NX09.

    PTM databases

    PhosphoSiteiQ9NX09.

    Expressioni

    Tissue specificityi

    Broadly expressed, with lowest levels in brain, skeletal muscle and intestine. Up-regulated in substantia nigra neurons from Parkinson disease patients (at protein level).4 Publications

    Inductioni

    Up-regulated in fibroblasts upon ionizing radiation, via a TP53-dependent pathway. Up-regulated by TP63 in primary keratinocytes, and down-regulated during keratinocyte differentiation. Up-regulated upon DNA alkylation. Up-regulated by amyloid beta-peptide and retinoic acid. Up-regulated by hypoxia, via a PI3K and HIF1A-dependent but TP53/TP63-independent mechanism (at protein level).7 Publications

    Gene expression databases

    BgeeiQ9NX09.
    CleanExiHS_DDIT4.
    GenevestigatoriQ9NX09.

    Organism-specific databases

    HPAiHPA034508.

    Interactioni

    Subunit structurei

    Monomer. Interacts with BTRC. Identified in a complex with CUL4A, DDB1 and BTRC. Interacts with TXNIP; this inhibits the proteasomal degradation of DDIT4.3 Publications

    Protein-protein interaction databases

    BioGridi120028. 8 interactions.
    IntActiQ9NX09. 10 interactions.
    MINTiMINT-1405734.
    STRINGi9606.ENSP00000307305.

    Structurei

    Secondary structure

    1
    232
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi90 – 10415
    Beta strandi107 – 1126
    Helixi121 – 13515
    Helixi141 – 1444
    Beta strandi145 – 1539
    Beta strandi156 – 16510
    Beta strandi173 – 1808
    Beta strandi214 – 2207

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3LQ9X-ray2.00A/B89-226[»]
    ProteinModelPortaliQ9NX09.
    SMRiQ9NX09. Positions 89-222.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NX09.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the DDIT4 family.Curated

    Phylogenomic databases

    eggNOGiNOG78982.
    HOGENOMiHOG000082523.
    HOVERGENiHBG104439.
    InParanoidiQ9NX09.
    KOiK08270.
    OMAiDEHLCAS.
    OrthoDBiEOG7P2XTF.
    PhylomeDBiQ9NX09.
    TreeFamiTF105007.

    Family and domain databases

    InterProiIPR012918. RTP801-like.
    [Graphical view]
    PANTHERiPTHR12478. PTHR12478. 1 hit.
    PfamiPF07809. RTP801_C. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9NX09-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPSLWDRFSS SSTSSSPSSL PRTPTPDRPP RSAWGSATRE EGFDRSTSLE    50
    SSDCESLDSS NSGFGPEEDT AYLDGVSLPD FELLSDPEDE HLCANLMQLL 100
    QESLAQARLG SRRPARLLMP SQLVSQVGKE LLRLAYSEPC GLRGALLDVC 150
    VEQGKSCHSV GQLALDPSLV PTFQLTLVLR LDSRLWPKIQ GLFSSANSPF 200
    LPGFSQSLTL STGFRVIKKK LYSSEQLLIE EC 232
    Length:232
    Mass (Da):25,371
    Last modified:October 1, 2000 - v1
    Checksum:i774E941EBDD08198
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti228 – 2281L → P in CAB66603. (PubMed:11230166)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY090097 mRNA. Translation: AAM10442.1.
    AF335324 mRNA. Translation: AAL38424.1.
    AL136668 mRNA. Translation: CAB66603.1.
    AK000507 mRNA. Translation: BAA91214.1.
    AL683820 Genomic DNA. Translation: CAH73863.1.
    CH471083 Genomic DNA. Translation: EAW54452.1.
    BC000708 mRNA. Translation: AAH00708.1.
    BC007714 mRNA. Translation: AAH07714.1.
    BC015236 mRNA. Translation: AAH15236.1.
    CCDSiCCDS7315.1.
    RefSeqiNP_061931.1. NM_019058.2.
    UniGeneiHs.744875.

    Genome annotation databases

    EnsembliENST00000307365; ENSP00000307305; ENSG00000168209.
    GeneIDi54541.
    KEGGihsa:54541.
    UCSCiuc001jsx.1. human.

    Polymorphism databases

    DMDMi74753036.

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY090097 mRNA. Translation: AAM10442.1 .
    AF335324 mRNA. Translation: AAL38424.1 .
    AL136668 mRNA. Translation: CAB66603.1 .
    AK000507 mRNA. Translation: BAA91214.1 .
    AL683820 Genomic DNA. Translation: CAH73863.1 .
    CH471083 Genomic DNA. Translation: EAW54452.1 .
    BC000708 mRNA. Translation: AAH00708.1 .
    BC007714 mRNA. Translation: AAH07714.1 .
    BC015236 mRNA. Translation: AAH15236.1 .
    CCDSi CCDS7315.1.
    RefSeqi NP_061931.1. NM_019058.2.
    UniGenei Hs.744875.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3LQ9 X-ray 2.00 A/B 89-226 [» ]
    ProteinModelPortali Q9NX09.
    SMRi Q9NX09. Positions 89-222.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120028. 8 interactions.
    IntActi Q9NX09. 10 interactions.
    MINTi MINT-1405734.
    STRINGi 9606.ENSP00000307305.

    PTM databases

    PhosphoSitei Q9NX09.

    Polymorphism databases

    DMDMi 74753036.

    Proteomic databases

    MaxQBi Q9NX09.
    PaxDbi Q9NX09.
    PRIDEi Q9NX09.

    Protocols and materials databases

    DNASUi 54541.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000307365 ; ENSP00000307305 ; ENSG00000168209 .
    GeneIDi 54541.
    KEGGi hsa:54541.
    UCSCi uc001jsx.1. human.

    Organism-specific databases

    CTDi 54541.
    GeneCardsi GC10P074033.
    HGNCi HGNC:24944. DDIT4.
    HPAi HPA034508.
    MIMi 607729. gene.
    neXtProti NX_Q9NX09.
    PharmGKBi PA134977994.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG78982.
    HOGENOMi HOG000082523.
    HOVERGENi HBG104439.
    InParanoidi Q9NX09.
    KOi K08270.
    OMAi DEHLCAS.
    OrthoDBi EOG7P2XTF.
    PhylomeDBi Q9NX09.
    TreeFami TF105007.

    Miscellaneous databases

    ChiTaRSi DDIT4. human.
    EvolutionaryTracei Q9NX09.
    GeneWikii DDIT4.
    GenomeRNAii 54541.
    NextBioi 56981.
    PROi Q9NX09.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9NX09.
    CleanExi HS_DDIT4.
    Genevestigatori Q9NX09.

    Family and domain databases

    InterProi IPR012918. RTP801-like.
    [Graphical view ]
    PANTHERi PTHR12478. PTHR12478. 1 hit.
    Pfami PF07809. RTP801_C. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "REDD1, a developmentally regulated transcriptional target of p63 and p53, links p63 to regulation of reactive oxygen species."
      Ellisen L.W., Ramsayer K.D., Johannessen C.M., Yang A., Beppu H., Minda K., Oliner J.D., McKeon F., Haber D.A.
      Mol. Cell 10:995-1005(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION BY DNA DAMAGE, SUBCELLULAR LOCATION.
      Tissue: Fetal brain.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    4. "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].
    5. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: Kidney and Uterus.
    8. "Identification of amyloid beta-peptide responsive genes by cDNA microarray technology: involvement of RTP801 in amyloid beta-peptide toxicity."
      Kim J.-R., Lee S.-R., Chung H.J., Kim S., Baek S.-H., Kim J.H., Kim Y.-S.
      Exp. Mol. Med. 35:403-411(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    9. "Regulation of mTOR function in response to hypoxia by REDD1 and the TSC1/TSC2 tumor suppressor complex."
      Brugarolas J., Lei K., Hurley R.L., Manning B.D., Reiling J.H., Hafen E., Witters L.A., Ellisen L.W., Kaelin W.G. Jr.
      Genes Dev. 18:2893-2904(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Induction of a cell stress response gene RTP801 by DNA damaging agent methyl methanesulfonate through CCAAT/enhancer binding protein."
      Lin L., Qian Y., Shi X., Chen Y.
      Biochemistry 44:3909-3914(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    11. "The stress-inducted proteins RTP801 and RTP801L are negative regulators of the mammalian target of rapamycin pathway."
      Corradetti M.N., Inoki K., Guan K.-L.
      J. Biol. Chem. 280:9769-9772(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "Regulation of mTOR and cell growth in response to energy stress by REDD1."
      Sofer A., Lei K., Johannessen C.M., Ellisen L.W.
      Mol. Cell. Biol. 25:5834-5845(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "REDD1 integrates hypoxia-mediated survival signaling downstream of phosphatidylinositol 3-kinase."
      Schwarzer R., Tondera D., Arnold W., Giese K., Klippel A., Kaufmann J.
      Oncogene 24:1138-1149(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    14. "RTP801 is elevated in Parkinson brain substantia nigral neurons and mediates death in cellular models of Parkinson's disease by a mechanism involving mammalian target of rapamycin inactivation."
      Malagelada C., Ryu E.J., Biswas S.C., Jackson-Lewis V., Greene L.A.
      J. Neurosci. 26:9996-10005(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    15. "RTP801 is a novel retinoic acid-responsive gene associated with myeloid differentiation."
      Gery S., Park D.J., Vuong P.T., Virk R.K., Muller C.I., Hofmann W.-K., Koeffler H.P.
      Exp. Hematol. 35:572-578(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION.
    16. "REDD1, an inhibitor of mTOR signalling, is regulated by the CUL4A-DDB1 ubiquitin ligase."
      Katiyar S., Liu E., Knutzen C.A., Lang E.S., Lombardo C.R., Sankar S., Toth J.I., Petroski M.D., Ronai Z., Chiang G.G.
      EMBO Rep. 10:866-872(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, UBIQUITINATION, INTERACTION WITH BTRC, IDENTIFICATION IN A COMPLEX WITH CUL4A; DDB1 AND BTRC, IDENTIFICATION BY MASS SPECTROMETRY, PARTIAL PROTEIN SEQUENCE, MUTAGENESIS OF SER-19; THR-23 AND THR-25, PHOSPHORYLATION AT SER-19; THR-23; THR-25 AND SER-121.
    17. "TXNIP potentiates Redd1-induced mTOR suppression through stabilization of Redd1."
      Jin H.O., Seo S.K., Kim Y.S., Woo S.H., Lee K.H., Yi J.Y., Lee S.J., Choe T.B., Lee J.H., An S., Hong S.I., Park I.C.
      Oncogene 30:3792-3801(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TXNIP, FUNCTION.
    18. "Structural analysis and functional implications of the negative mTORC1 regulator REDD1."
      Vega-Rubin-de-Celis S., Abdallah Z., Kinch L., Grishin N.V., Brugarolas J., Zhang X.
      Biochemistry 49:2491-2501(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 89-226, FUNCTION, SUBUNIT, INDUCTION, MUTAGENESIS OF SER-103; ARG-133; SER-137; PRO-139; CYS-140; LYS-219; LEU-221 AND TYR-222.

    Entry informationi

    Entry nameiDDIT4_HUMAN
    AccessioniPrimary (citable) accession number: Q9NX09
    Secondary accession number(s): Q9H0S3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 23, 2007
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 105 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 10
      Human chromosome 10: 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