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Q61823

- PDCD4_MOUSE

UniProt

Q61823 - PDCD4_MOUSE

Protein

Programmed cell death protein 4

Gene

Pdcd4

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Inhibits translation initiation and cap-dependent translation. May excert its function by hindering the interaction between EIF4A1 and EIF4G. Inhibits the helicase activity of EIF4A. Modulates the activation of JUN kinase. Down-regulates the expression of MAP4K1, thus inhibiting events important in driving invasion, namely, MAPK85 activation and consequent JUN-dependent transcription. May play a role in apoptosis. Tumor suppressor. Inhibits tumor promoter-induced neoplastic transformation. Binds RNA.4 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. RNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. cell aging Source: UniProtKB
    3. negative regulation of JUN kinase activity Source: UniProtKB
    4. negative regulation of transcription, DNA-templated Source: UniProtKB

    Keywords - Biological processi

    Apoptosis

    Keywords - Ligandi

    RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Programmed cell death protein 4
    Alternative name(s):
    Protein MA-3
    Topoisomerase-inhibitor suppressed protein
    Gene namesi
    Name:Pdcd4
    Synonyms:Ma3, Tis
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 19

    Organism-specific databases

    MGIiMGI:107490. Pdcd4.

    Subcellular locationi

    Nucleus. Cytoplasm
    Note: Shuttles between the nucleus and cytoplasm. Predominantly nuclear under normal growth conditions, and when phosphorylated at Ser-457 By similarity. Exported from the nucleus in the absence of serum.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: UniProtKB
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Decreases benign tumor development and malignant progression.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi414 – 4141D → A: Strongly reduced interaction with EIF4A1. 1 Publication
    Mutagenesisi418 – 4181D → A: Strongly reduced interaction with EIF4A1. 1 Publication
    Mutagenesisi457 – 4571S → A or D: No effect on interaction with EIF4A1. 1 Publication

    Keywords - Diseasei

    Tumor suppressor

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 469469Programmed cell death protein 4PRO_0000256520Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei67 – 671Phosphoserine; by PKB and RPS6KB1By similarity
    Modified residuei76 – 761PhosphoserineBy similarity
    Modified residuei78 – 781PhosphoserineBy similarity
    Modified residuei94 – 941PhosphoserineBy similarity
    Modified residuei152 – 1521PhosphotyrosineBy similarity
    Modified residuei457 – 4571Phosphoserine; by PKBBy similarity

    Post-translational modificationi

    Polyubiquitinated, leading to its proteasomal degradation. Rapidly degraded in response to mitogens. Phosphorylation of the phosphodegron promotes interaction with BTRC and proteasomal degradation By similarity.By similarity
    Phosphorylated at Ser-67 by RPS6KB1 in response to mitogens; phosphorylation promotes proteasomal degradation of PDCD4.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ61823.
    PaxDbiQ61823.
    PRIDEiQ61823.

    PTM databases

    PhosphoSiteiQ61823.

    Expressioni

    Tissue specificityi

    Expressed ubiquitously. Highyly expressed in thymus and liver. Moderately expressed in brain, kidney and spleen; weakly in lung and heart. Expression is up- or down-regulated in response to apoptosis inducers. Regulated by many programmed cell death-inducing stimuli.2 Publications

    Gene expression databases

    BgeeiQ61823.
    CleanExiMM_PDCD4.
    GenevestigatoriQ61823.

    Interactioni

    Subunit structurei

    Interacts (via MI domains) with EIF4A1 and EIF4A2 (via N-terminal domain). Heterotrimer with EIF4A1; one molecule of PDCD4 binds two molecules of EIF4A1. Interacts with EIF4G1. May form a complex with EIF4A1 and EIF4G1. The interaction between PDCD4 and EIF4A1 interferes with the interaction between EIF4A1 and EIF4G. When phosphorylated, interacts with BTRC and FBXW11 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Eif4a1P608434EBI-296473,EBI-6665935
    Eif4g2Q624482EBI-296473,EBI-296494

    Protein-protein interaction databases

    BioGridi202070. 1 interaction.
    IntActiQ61823. 4 interactions.
    MINTiMINT-7012023.

    Structurei

    Secondary structure

    1
    469
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi162 – 17817
    Helixi181 – 1899
    Turni190 – 1923
    Helixi195 – 1995
    Helixi200 – 2089
    Helixi213 – 22412
    Turni225 – 2295
    Helixi233 – 24513
    Helixi247 – 2537
    Helixi257 – 27014
    Helixi280 – 2823
    Helixi289 – 30214
    Beta strandi320 – 3223
    Helixi326 – 34116
    Helixi344 – 35411
    Helixi357 – 3593
    Helixi360 – 37314
    Beta strandi374 – 3774
    Helixi378 – 39215
    Helixi398 – 41821
    Helixi422 – 43514
    Helixi441 – 4455

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2HM8NMR-A319-449[»]
    2IOLX-ray2.00A/B320-469[»]
    2IONX-ray1.57A320-467[»]
    2IOSX-ray1.76A320-469[»]
    2KZTNMR-B319-449[»]
    2NSZX-ray1.15A322-450[»]
    3EIQX-ray3.50C120-469[»]
    ProteinModelPortaliQ61823.
    SMRiQ61823. Positions 157-450.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ61823.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini163 – 284122MI 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini326 – 449124MI 2PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi58 – 647Nuclear localization signalSequence Analysis
    Motifi70 – 767PhosphodegronBy similarity
    Motifi448 – 4547Nuclear localization signalSequence Analysis

    Domaini

    Binds EIF4A1 via both MI domains.1 Publication

    Sequence similaritiesi

    Belongs to the PDCD4 family.Curated
    Contains 2 MI domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG249108.
    GeneTreeiENSGT00390000015948.
    HOGENOMiHOG000261612.
    HOVERGENiHBG052841.
    InParanoidiQ61823.
    KOiK16865.
    OMAiLSMSKGG.
    OrthoDBiEOG7X9G6X.
    PhylomeDBiQ61823.
    TreeFamiTF323207.

    Family and domain databases

    Gene3Di1.25.40.180. 2 hits.
    InterProiIPR016024. ARM-type_fold.
    IPR003891. Initiation_fac_eIF4g_MI.
    IPR016021. MIF4-like_typ_1/2/3.
    [Graphical view]
    PfamiPF02847. MA3. 2 hits.
    [Graphical view]
    SMARTiSM00544. MA3. 2 hits.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 2 hits.
    PROSITEiPS51366. MI. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q61823-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDIENEQTLN VNPTDPDNLS DSLFSGDEEN AGTEEIKNEI NGNWISASTI    50
    NEARINAKAK RRLRKNSSRD SGRGDSVSDN GSEAVRSGVA VPTSPKGRLL 100
    DRRSRSGKGR GLPKKGGAGG KGVWGTPGQV YDVEEVDVKD PNYDDDQENC 150
    VYETVVLPLD ETAFEKTLTP IIQEYFEHGD TNEVAEMLRD LNLGEMKSGV 200
    PVLAVSLALE GKASHREMTS KLLSDLCGTV MSTNDVEKSF DKLLKDLPEL 250
    ALDTPRAPQL VGQFIARAVG DGILCNTYID SYKGTVDCVQ ARAALDKATV 300
    LLSMSKGGKR KDSVWGSGGG QQPVNHLVKE IDMLLKEYLL SGDISEAEHC 350
    LKELEVPHFH HELVYEAIVM VLESTGESAF KMILDLLKSL WKSSTITIDQ 400
    MKRGYERIYN EIPDINLDVP HSYSVLERFV EECFQAGIIS KQLRDLCPSR 450
    GRKRFVSEGD GGRLKPESY 469
    Length:469
    Mass (Da):51,702
    Last modified:November 1, 1996 - v1
    Checksum:i6883BCE5011692F1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti232 – 2321S → I in BAA32356. (PubMed:8912629)Curated
    Sequence conflicti232 – 2321S → I in BAA13072. (PubMed:9714845)Curated
    Sequence conflicti369 – 3691V → I in BAA32356. (PubMed:8912629)Curated
    Sequence conflicti369 – 3691V → I in BAA13072. (PubMed:9714845)Curated
    Sequence conflicti414 – 4141D → G in BAE43115. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D50465 mRNA. Translation: BAA09056.1.
    D86344 mRNA. Translation: BAA13072.1.
    AB010139 Genomic DNA. Translation: BAA32356.1.
    DQ479921 Genomic DNA. Translation: ABF51670.1.
    CT010188 mRNA. Translation: CAJ18396.1.
    AK134366 mRNA. Translation: BAE22118.1.
    AK172654 mRNA. Translation: BAE43115.1.
    BC055739 mRNA. Translation: AAH55739.1.
    CCDSiCCDS29903.1.
    PIRiJC4523.
    RefSeqiNP_001161963.1. NM_001168491.1.
    NP_001161964.1. NM_001168492.1.
    NP_035180.2. NM_011050.4.
    XP_006526825.1. XM_006526762.1.
    UniGeneiMm.1605.

    Genome annotation databases

    EnsembliENSMUST00000025931; ENSMUSP00000025931; ENSMUSG00000024975.
    ENSMUST00000074371; ENSMUSP00000073975; ENSMUSG00000024975.
    ENSMUST00000165617; ENSMUSP00000133135; ENSMUSG00000024975.
    GeneIDi18569.
    KEGGimmu:18569.
    UCSCiuc008hxb.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D50465 mRNA. Translation: BAA09056.1 .
    D86344 mRNA. Translation: BAA13072.1 .
    AB010139 Genomic DNA. Translation: BAA32356.1 .
    DQ479921 Genomic DNA. Translation: ABF51670.1 .
    CT010188 mRNA. Translation: CAJ18396.1 .
    AK134366 mRNA. Translation: BAE22118.1 .
    AK172654 mRNA. Translation: BAE43115.1 .
    BC055739 mRNA. Translation: AAH55739.1 .
    CCDSi CCDS29903.1.
    PIRi JC4523.
    RefSeqi NP_001161963.1. NM_001168491.1.
    NP_001161964.1. NM_001168492.1.
    NP_035180.2. NM_011050.4.
    XP_006526825.1. XM_006526762.1.
    UniGenei Mm.1605.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2HM8 NMR - A 319-449 [» ]
    2IOL X-ray 2.00 A/B 320-469 [» ]
    2ION X-ray 1.57 A 320-467 [» ]
    2IOS X-ray 1.76 A 320-469 [» ]
    2KZT NMR - B 319-449 [» ]
    2NSZ X-ray 1.15 A 322-450 [» ]
    3EIQ X-ray 3.50 C 120-469 [» ]
    ProteinModelPortali Q61823.
    SMRi Q61823. Positions 157-450.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202070. 1 interaction.
    IntActi Q61823. 4 interactions.
    MINTi MINT-7012023.

    PTM databases

    PhosphoSitei Q61823.

    Proteomic databases

    MaxQBi Q61823.
    PaxDbi Q61823.
    PRIDEi Q61823.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000025931 ; ENSMUSP00000025931 ; ENSMUSG00000024975 .
    ENSMUST00000074371 ; ENSMUSP00000073975 ; ENSMUSG00000024975 .
    ENSMUST00000165617 ; ENSMUSP00000133135 ; ENSMUSG00000024975 .
    GeneIDi 18569.
    KEGGi mmu:18569.
    UCSCi uc008hxb.2. mouse.

    Organism-specific databases

    CTDi 27250.
    MGIi MGI:107490. Pdcd4.

    Phylogenomic databases

    eggNOGi NOG249108.
    GeneTreei ENSGT00390000015948.
    HOGENOMi HOG000261612.
    HOVERGENi HBG052841.
    InParanoidi Q61823.
    KOi K16865.
    OMAi LSMSKGG.
    OrthoDBi EOG7X9G6X.
    PhylomeDBi Q61823.
    TreeFami TF323207.

    Miscellaneous databases

    ChiTaRSi PDCD4. mouse.
    EvolutionaryTracei Q61823.
    NextBioi 294400.
    PROi Q61823.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q61823.
    CleanExi MM_PDCD4.
    Genevestigatori Q61823.

    Family and domain databases

    Gene3Di 1.25.40.180. 2 hits.
    InterProi IPR016024. ARM-type_fold.
    IPR003891. Initiation_fac_eIF4g_MI.
    IPR016021. MIF4-like_typ_1/2/3.
    [Graphical view ]
    Pfami PF02847. MA3. 2 hits.
    [Graphical view ]
    SMARTi SM00544. MA3. 2 hits.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 2 hits.
    PROSITEi PS51366. MI. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation of a novel mouse gene MA-3 that is induced upon programmed cell death."
      Shibahara K., Asano M., Ishida Y., Aoki T., Koike T., Honjo T.
      Gene 166:297-301(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
      Strain: ICR.
      Tissue: Thymus.
    2. "Molecular cloning of the genes suppressed in RVC lymphoma cells by topoisomerase inhibitors."
      Onishi Y., Kizaki H.
      Biochem. Biophys. Res. Commun. 228:7-13(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Lymphoma.
    3. "Cloning of the TIS gene suppressed by topoisomerase inhibitors."
      Onishi Y., Hashimoto S., Kizaki H.
      Gene 215:453-459(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
    4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: BTBR T+ tf/J.
    5. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J and NOD.
      Tissue: Spleen and Testis.
    6. "Cloning of mouse full open reading frames in Gateway(R) system entry vector (pDONR201)."
      Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J., Wiemann S., Schick M., Korn B.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    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].
      Strain: C57BL/6.
      Tissue: Brain.
    8. "The transformation suppressor Pdcd4 is a novel eukaryotic translation initiation factor 4A binding protein that inhibits translation."
      Yang H.-S., Jansen A.P., Komar A.A., Zheng X., Merrick W.C., Costes S., Lockett S.J., Sonenberg N., Colburn N.H.
      Mol. Cell. Biol. 23:26-37(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH EIF4A1 AND EIF4A2.
    9. "The transformation suppressor protein Pdcd4 shuttles between nucleus and cytoplasm and binds RNA."
      Boehm M., Sawicka K., Siebrasse J.P., Brehmer-Fastnacht A., Peters R., Klempnauer K.-H.
      Oncogene 22:4905-4910(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    10. "Epidermal expression of the translation inhibitor programmed cell death 4 suppresses tumorigenesis."
      Jansen A.P., Camalier C.E., Colburn N.H.
      Cancer Res. 65:6034-6041(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Structural basis for inhibition of translation by the tumor suppressor pdcd4."
      Laronde-Leblanc N., Santhanam A.N., Baker A.R., Wlodawer A., Colburn N.H.
      Mol. Cell. Biol. 27:147-156(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) OF 320-469, FUNCTION, INTERACTION WITH EIF4A AND EIF4G, SUBUNIT, MUTAGENESIS OF ASP-414; ASP-418 AND SER-457.
    12. "Structure of the C-terminal MA-3 domain of the tumour suppressor protein Pdcd4 and characterization of its interaction with eIF4A."
      Waters L.C., Veverka V., Bohm M., Schmedt T., Choong P.T., Muskett F.W., Klempnauer K.H., Carr M.D.
      Oncogene 26:4941-4950(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 319-449, INTERACTION WITH EIF4A1.
    13. "Structural basis for translational inhibition by the tumour suppressor Pdcd4."
      Loh P.G., Yang H.S., Walsh M.A., Wang Q., Wang X., Cheng Z., Liu D., Song H.
      EMBO J. 28:274-285(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 120-469 IN COMPLEX WITH EIF4A1, SUBUNIT, DOMAIN.

    Entry informationi

    Entry nameiPDCD4_MOUSE
    AccessioniPrimary (citable) accession number: Q61823
    Secondary accession number(s): P97296, Q3T9A9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 31, 2006
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 123 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3