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Q53EL6

- PDCD4_HUMAN

UniProt

Q53EL6 - PDCD4_HUMAN

Protein

Programmed cell death protein 4

Gene

PDCD4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 2 (11 Jan 2011)
      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 By similarity.By similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. apoptotic process Source: UniProtKB
    2. cell aging Source: UniProtKB
    3. negative regulation of cell cycle Source: UniProtKB
    4. negative regulation of JUN kinase activity Source: UniProtKB
    5. 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):
    Neoplastic transformation inhibitor protein
    Nuclear antigen H731-like
    Protein 197/15a
    Gene namesi
    Name:PDCD4
    Synonyms:H731
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:8763. PDCD4.

    Subcellular locationi

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

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi67 – 671S → A: Loss of phosphorylation site. Reduces interaction with BTRC. Abolishes phosphorylation by PKB; when associated with A-457. 2 Publications
    Mutagenesisi71 – 711S → A: Strongly reduced interaction with BTRC. Strongly reduced ubiquitination. 1 Publication
    Mutagenesisi76 – 761S → A: Strongly reduced interaction with BTRC. Strongly reduced ubiquitination. 1 Publication
    Mutagenesisi174 – 1741E → A: Reduced inhibition of EIF4A1 helicase activity. 1 Publication
    Mutagenesisi210 – 2101E → A: Reduced inhibition of EIF4A1 helicase activity. Strongly reduced inhibition of translation. 1 Publication
    Mutagenesisi249 – 2491E → A: Reduced interaction with EIF4A1. 1 Publication
    Mutagenesisi252 – 2521L → A: Strongly reduced interaction with EIF4A1. Reduced inhibition of EIF4A1 helicase activity. Strongly reduced inhibition of translation. 1 Publication
    Mutagenesisi253 – 2531D → A: Strongly reduced interaction with EIF4A1. Strongly reduced inhibition of translation. Reduced inhibition of EIF4A1 helicase activity. 2 Publications
    Mutagenesisi255 – 2551P → A: Reduced inhibition of EIF4A1 helicase activity. Strongly reduced inhibition of translation. 1 Publication
    Mutagenesisi333 – 3331M → A: No effect on inhibition of EIF4A1 and on inhibition of translation; when associated with A-340. 1 Publication
    Mutagenesisi337 – 3371E → A: No effect on inhibition of EIF4A1 and on inhibition of translation. 1 Publication
    Mutagenesisi340 – 3401L → A: No effect on inhibition of EIF4A1 and on inhibition of translation; when associated with A-333. 1 Publication
    Mutagenesisi358 – 3581H → A: Strongly reduced interaction with EIF4A1. 1 Publication
    Mutagenesisi359 – 3591F → A: Strongly reduced inhibition of EIF4A1. Strongly reduced inhibition of translation. 1 Publication
    Mutagenesisi361 – 3611H → A: Strongly reduced inhibition of EIF4A1. Strongly reduced inhibition of translation. 1 Publication
    Mutagenesisi414 – 4141D → A: Strongly reduced interaction with EIF4A1. Strongly reduced inhibition of translation. 1 Publication
    Mutagenesisi418 – 4181D → A: Reduced interaction with EIF4A1. Strongly reduced inhibition of translation. 1 Publication
    Mutagenesisi420 – 4201P → A: Strongly reduced interaction with EIF4A1. Strongly reduced inhibition of translation. 1 Publication
    Mutagenesisi457 – 4571S → A: Loss of phosphorylation site, and loss of nuclear accumulation. Abolishes phosphorylation by PKB; when associated with A-67. 1 Publication

    Keywords - Diseasei

    Tumor suppressor

    Organism-specific databases

    PharmGKBiPA33113.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 469469Programmed cell death protein 4PRO_0000256519Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei67 – 671Phosphoserine; by PKB and RPS6KB12 Publications
    Modified residuei76 – 761Phosphoserine2 Publications
    Modified residuei78 – 781Phosphoserine2 Publications
    Modified residuei80 – 801Phosphoserine1 Publication
    Modified residuei94 – 941Phosphoserine2 Publications
    Modified residuei152 – 1521Phosphotyrosine1 Publication
    Modified residuei457 – 4571Phosphoserine; by PKB6 Publications

    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.1 Publication
    Phosphorylated at Ser-67 by RPS6KB1 in response to mitogens; phosphorylation promotes proteasomal degradation of PDCD4.2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ53EL6.
    PaxDbiQ53EL6.
    PRIDEiQ53EL6.

    PTM databases

    PhosphoSiteiQ53EL6.

    Expressioni

    Tissue specificityi

    Up-regulated in proliferative cells. Highly expressed in epithelial cells of the mammary gland. Reduced expression in lung cancer and colon carcinoma.3 Publications

    Inductioni

    IL2/interleukin-2 stimulation inhibits expression, while IL12/interleukin-12 increases expression.1 Publication

    Gene expression databases

    ArrayExpressiQ53EL6.
    BgeeiQ53EL6.
    CleanExiHS_PDCD4.
    GenevestigatoriQ53EL6.

    Organism-specific databases

    HPAiCAB037024.
    HPA001032.
    HPA027214.

    Interactioni

    Subunit structurei

    Interacts (via MI domains) with EIF4A2 By similarity. Interacts (via MI domains) with EIF4A1 (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 similarity4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    APOEP026493EBI-935824,EBI-1222467
    PSEN2P498103EBI-935824,EBI-2010251
    RPS13P622772EBI-935824,EBI-351850

    Protein-protein interaction databases

    BioGridi118098. 29 interactions.
    DIPiDIP-29756N.
    IntActiQ53EL6. 12 interactions.
    STRINGi9606.ENSP00000280154.

    Structurei

    Secondary structure

    1
    469
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi161 – 17818
    Helixi181 – 19111
    Helixi195 – 1984
    Helixi199 – 20911
    Helixi213 – 22614
    Turni227 – 2293
    Helixi233 – 25321
    Helixi257 – 27014
    Helixi278 – 2814
    Turni282 – 2843
    Helixi289 – 30315
    Beta strandi308 – 3136
    Helixi324 – 34118
    Helixi344 – 35411
    Helixi357 – 3593
    Helixi360 – 37213
    Helixi378 – 39316
    Helixi398 – 41821
    Helixi422 – 43514
    Helixi441 – 4455

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2GGFNMR-A327-450[»]
    2KZTNMR-A157-318[»]
    2RG8X-ray1.80A/B157-320[»]
    2ZU6X-ray2.80B/E163-469[»]
    3EIJX-ray2.80A/B157-469[»]
    ProteinModelPortaliQ53EL6.
    SMRiQ53EL6. Positions 157-450.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ53EL6.

    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 – 767Phosphodegron
    Motifi241 – 25010Nuclear localization signalSequence Analysis

    Domaini

    Binds EIF4A1 via both MI domains.2 Publications

    Sequence similaritiesi

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

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG249108.
    HOGENOMiHOG000261612.
    HOVERGENiHBG052841.
    InParanoidiQ53EL6.
    KOiK16865.
    OMAiLSMSKGG.
    OrthoDBiEOG7X9G6X.
    PhylomeDBiQ53EL6.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q53EL6-1) [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

    MDVENEQILN VNPADPDNLS DSLFSGDEEN AGTEEIKNEI NGNWISASSI    50
    NEARINAKAK RRLRKNSSRD SGRGDSVSDS GSDALRSGLT VPTSPKGRLL 100
    DRRSRSGKGR GLPKKGGAGG KGVWGTPGQV YDVEEVDVKD PNYDDDQENC 150
    VYETVVLPLD ERAFEKTLTP IIQEYFEHGD TNEVAEMLRD LNLGEMKSGV 200
    PVLAVSLALE GKASHREMTS KLLSDLCGTV MSTTDVEKSF DKLLKDLPEL 250
    ALDTPRAPQL VGQFIARAVG DGILCNTYID SYKGTVDCVQ ARAALDKATV 300
    LLSMSKGGKR KDSVWGSGGG QQSVNHLVKE IDMLLKEYLL SGDISEAEHC 350
    LKELEVPHFH HELVYEAIIM VLESTGESTF KMILDLLKSL WKSSTITVDQ 400
    MKRGYERIYN EIPDINLDVP HSYSVLERFV EECFQAGIIS KQLRDLCPSR 450
    GRKRFVSEGD GGRLKPESY 469
    Length:469
    Mass (Da):51,735
    Last modified:January 11, 2011 - v2
    Checksum:i2CAE1D2055491177
    GO
    Isoform 2 (identifier: Q53EL6-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-15: MDVENEQILNVNPAD → MTKY

    Note: No experimental confirmation available.

    Show »
    Length:458
    Mass (Da):50,576
    Checksum:iE887AA311F3EB4D4
    GO

    Sequence cautioni

    The sequence AAH15036.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence AAB42218.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti79 – 791D → E in AAB42218. 1 PublicationCurated
    Sequence conflicti102 – 1021R → G in AAB67706. (PubMed:9759869)Curated
    Sequence conflicti130 – 1301V → G in AAB67706. (PubMed:9759869)Curated
    Sequence conflicti220 – 2201S → T in AAB42218. 1 PublicationCurated
    Sequence conflicti222 – 2221L → F in AAB67706. (PubMed:9759869)Curated
    Sequence conflicti309 – 3091K → R in BAG37701. (PubMed:14702039)Curated
    Sequence conflicti314 – 3141V → A in BAG37701. (PubMed:14702039)Curated
    Sequence conflicti440 – 4401S → W in AAB67706. (PubMed:9759869)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti36 – 361I → V.6 Publications
    Corresponds to variant rs7081726 [ dbSNP | Ensembl ].
    VAR_028901
    Natural varianti48 – 481S → Y.1 Publication
    Corresponds to variant rs11548765 [ dbSNP | Ensembl ].
    VAR_028902
    Natural varianti120 – 1201G → R in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036375

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1515MDVEN…VNPAD → MTKY in isoform 2. 1 PublicationVSP_045622Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U83908 Genomic DNA. Translation: AAB42218.1. Sequence problems.
    U96628 mRNA. Translation: AAB67706.1.
    AK315295 mRNA. Translation: BAG37701.1.
    AK223623 mRNA. Translation: BAD97343.1.
    AL158163, AL136368 Genomic DNA. Translation: CAH72815.1.
    AL136368, AL158163 Genomic DNA. Translation: CAI40095.1.
    BC015036 mRNA. Translation: AAH15036.1. Sequence problems.
    BC026104 mRNA. Translation: AAH26104.1.
    BC031049 mRNA. Translation: AAH31049.1.
    CCDSiCCDS44478.1. [Q53EL6-2]
    CCDS7567.1. [Q53EL6-1]
    PIRiJC5193.
    RefSeqiNP_055271.2. NM_014456.4. [Q53EL6-1]
    NP_663314.1. NM_145341.3. [Q53EL6-2]
    UniGeneiHs.711490.

    Genome annotation databases

    EnsembliENST00000280154; ENSP00000280154; ENSG00000150593. [Q53EL6-1]
    ENST00000393104; ENSP00000376816; ENSG00000150593. [Q53EL6-2]
    GeneIDi27250.
    KEGGihsa:27250.
    UCSCiuc001kzh.3. human. [Q53EL6-1]

    Polymorphism databases

    DMDMi317373317.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U83908 Genomic DNA. Translation: AAB42218.1 . Sequence problems.
    U96628 mRNA. Translation: AAB67706.1 .
    AK315295 mRNA. Translation: BAG37701.1 .
    AK223623 mRNA. Translation: BAD97343.1 .
    AL158163 , AL136368 Genomic DNA. Translation: CAH72815.1 .
    AL136368 , AL158163 Genomic DNA. Translation: CAI40095.1 .
    BC015036 mRNA. Translation: AAH15036.1 . Sequence problems.
    BC026104 mRNA. Translation: AAH26104.1 .
    BC031049 mRNA. Translation: AAH31049.1 .
    CCDSi CCDS44478.1. [Q53EL6-2 ]
    CCDS7567.1. [Q53EL6-1 ]
    PIRi JC5193.
    RefSeqi NP_055271.2. NM_014456.4. [Q53EL6-1 ]
    NP_663314.1. NM_145341.3. [Q53EL6-2 ]
    UniGenei Hs.711490.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2GGF NMR - A 327-450 [» ]
    2KZT NMR - A 157-318 [» ]
    2RG8 X-ray 1.80 A/B 157-320 [» ]
    2ZU6 X-ray 2.80 B/E 163-469 [» ]
    3EIJ X-ray 2.80 A/B 157-469 [» ]
    ProteinModelPortali Q53EL6.
    SMRi Q53EL6. Positions 157-450.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118098. 29 interactions.
    DIPi DIP-29756N.
    IntActi Q53EL6. 12 interactions.
    STRINGi 9606.ENSP00000280154.

    Chemistry

    BindingDBi Q53EL6.
    ChEMBLi CHEMBL1781868.

    PTM databases

    PhosphoSitei Q53EL6.

    Polymorphism databases

    DMDMi 317373317.

    Proteomic databases

    MaxQBi Q53EL6.
    PaxDbi Q53EL6.
    PRIDEi Q53EL6.

    Protocols and materials databases

    DNASUi 27250.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000280154 ; ENSP00000280154 ; ENSG00000150593 . [Q53EL6-1 ]
    ENST00000393104 ; ENSP00000376816 ; ENSG00000150593 . [Q53EL6-2 ]
    GeneIDi 27250.
    KEGGi hsa:27250.
    UCSCi uc001kzh.3. human. [Q53EL6-1 ]

    Organism-specific databases

    CTDi 27250.
    GeneCardsi GC10P112618.
    H-InvDB HIX0009201.
    HGNCi HGNC:8763. PDCD4.
    HPAi CAB037024.
    HPA001032.
    HPA027214.
    MIMi 608610. gene.
    neXtProti NX_Q53EL6.
    PharmGKBi PA33113.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG249108.
    HOGENOMi HOG000261612.
    HOVERGENi HBG052841.
    InParanoidi Q53EL6.
    KOi K16865.
    OMAi LSMSKGG.
    OrthoDBi EOG7X9G6X.
    PhylomeDBi Q53EL6.
    TreeFami TF323207.

    Miscellaneous databases

    ChiTaRSi PDCD4. human.
    EvolutionaryTracei Q53EL6.
    GeneWikii PDCD4.
    GenomeRNAii 27250.
    NextBioi 50179.
    PROi Q53EL6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q53EL6.
    Bgeei Q53EL6.
    CleanExi HS_PDCD4.
    Genevestigatori Q53EL6.

    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 gene from a human cell line with Pr-28 MAb which recognizes a nuclear antigen involved in the cell cycle."
      Matsuhashi S., Yoshinaga H., Yatsuki H., Tsugita A., Hori K.
      Res. Commun. Biochem. Cell Mol. Biol. 1:109-120(1997)
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-36.
      Tissue: Glial tumor.
    2. "Differential transcriptional regulation of CD161 and a novel gene, 197/15a, by IL-2, IL-15, and IL-12 in NK and T cells."
      Azzoni L., Zatsepina O., Abebe B., Bennett I.M., Kanakaraj P., Perussia B.
      J. Immunol. 161:3493-3500(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION, VARIANT VAL-36.
      Tissue: Blood.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT VAL-36.
    4. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT VAL-36.
      Tissue: Spleen.
    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. "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] (ISOFORM 1), VARIANTS VAL-36 AND TYR-48.
      Tissue: Brain and Skin.
    7. "Novel human PDCD4 (H731) gene expressed in proliferative cells is expressed in the small duct epithelial cells of the breast as revealed by an anti-H731 antibody."
      Yoshinaga H., Matsuhashi S., Fujiyama C., Masaki Z.
      Pathol. Int. 49:1067-1077(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    8. "Loss of PDCD4 expression in human lung cancer correlates with tumour progression and prognosis."
      Chen Y., Knosel T., Kristiansen G., Pietas A., Garber M.E., Matsuhashi S., Ozaki I., Petersen I.
      J. Pathol. 200:640-646(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    9. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
      Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
      Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-457, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    10. "Akt phosphorylates and regulates Pdcd4 tumor suppressor protein."
      Palamarchuk A., Efanov A., Maximov V., Aqeilan R.I., Croce C.M., Pekarsky Y.
      Cancer Res. 65:11282-11286(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-67 AND SER-457 BY PKB, FUNCTION, MUTAGENESIS OF SER-67 AND SER-457, SUBCELLULAR LOCATION.
    11. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-152, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-457, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Tumorigenesis suppressor Pdcd4 down-regulates mitogen-activated protein kinase kinase kinase kinase 1 expression to suppress colon carcinoma cell invasion."
      Yang H.-S., Matthews C.P., Clair T., Wang Q., Baker A.R., Li C.-C., Tan T.-H., Colburn N.H.
      Mol. Cell. Biol. 26:1297-1306(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    14. "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-457, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "S6K1- and betaTRCP-mediated degradation of PDCD4 promotes protein translation and cell growth."
      Dorrello N.V., Peschiaroli A., Guardavaccaro D., Colburn N.H., Sherman N.E., Pagano M.
      Science 314:467-471(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT SER-67 BY RPS6KB1, PHOSPHODEGRON MOTIF, INTERACTION WITH BTRC AND FBXW11, UBIQUITINATION, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF SER-67; SER-71 AND SER-76.
    16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76; SER-78; SER-80 AND SER-94, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76; SER-78; SER-94 AND SER-457, VARIANT [LARGE SCALE ANALYSIS] VAL-36, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-457, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "Solution structure of the MA3 domain of human programmed cell death 4."
      RIKEN structural genomics initiative (RSGI)
      Submitted (APR-2007) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 320-450.
    22. "PDCD4 inhibits translation initiation by binding to eIF4A using both its MA3 domains."
      Suzuki C., Garces R.G., Edmonds K.A., Hiller S., Hyberts S.G., Marintchev A., Wagner G.
      Proc. Natl. Acad. Sci. U.S.A. 105:3274-3279(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 157-320, FUNCTION, DOMAIN, INTERACTION WITH EIF4A, SUBUNIT.
    23. "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 (2.8 ANGSTROMS) OF 157-469, FUNCTION, INTERACTION WITH EIF4A1 AND EIF4G, SUBUNIT, MUTAGENESIS OF GLU-174; GLU-210; GLU-249; LEU-252; ASP-253; PRO-255; HIS-358; ASP-414; ASP-418 AND PRO-420.
    24. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 163-469 IN COMPLEX WITH EIF4A1, FUNCTION, SUBUNIT, DOMAIN, MUTAGENESIS OF ASP-253; MET-333; GLU-337; LEU-340; PHE-359 AND HIS-361.
    25. Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-120.

    Entry informationi

    Entry nameiPDCD4_HUMAN
    AccessioniPrimary (citable) accession number: Q53EL6
    Secondary accession number(s): B2RCV4
    , B5ME91, O15501, Q5VZS6, Q6PJI5, Q8TAR5, Q99834
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 31, 2006
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 95 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, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: 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