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Q53EL6 (PDCD4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Programmed cell death protein 4
Alternative name(s):
Neoplastic transformation inhibitor protein
Nuclear antigen H731-like
Protein 197/15a
Gene names
Name:PDCD4
Synonyms:H731
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length469 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.10 Ref.13 Ref.15 Ref.22 Ref.23 Ref.24

Subunit structure

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. Ref.15 Ref.22 Ref.23 Ref.24

Subcellular location

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. Ref.7 Ref.10

Tissue specificity

Up-regulated in proliferative cells. Highly expressed in epithelial cells of the mammary gland. Reduced expression in lung cancer and colon carcinoma. Ref.7 Ref.8 Ref.13

Induction

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

Domain

Binds EIF4A1 via both MI domains. Ref.22 Ref.24

Post-translational modification

Polyubiquitinated, leading to its proteasomal degradation. Rapidly degraded in response to mitogens. Phosphorylation of the phosphodegron promotes interaction with BTRC and proteasomal degradation.

Phosphorylated at Ser-67 by RPS6KB1 in response to mitogens; phosphorylation promotes proteasomal degradation of PDCD4. Ref.10 Ref.15

Sequence similarities

Belongs to the PDCD4 family.

Contains 2 MI domains.

Sequence caution

The sequence AAB42218.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence AAH15036.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q53EL6-1)

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.
Isoform 2 (identifier: Q53EL6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: MDVENEQILNVNPAD → MTKY
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 469469Programmed cell death protein 4
PRO_0000256519

Regions

Domain163 – 284122MI 1
Domain326 – 449124MI 2
Motif58 – 647Nuclear localization signal Potential
Motif70 – 767Phosphodegron
Motif241 – 25010Nuclear localization signal Potential

Amino acid modifications

Modified residue11N-acetylmethionine Ref.18
Modified residue671Phosphoserine; by PKB and RPS6KB1 Ref.10 Ref.15
Modified residue761Phosphoserine Ref.16 Ref.18
Modified residue781Phosphoserine Ref.16 Ref.18
Modified residue801Phosphoserine Ref.16
Modified residue941Phosphoserine Ref.16 Ref.18
Modified residue1521Phosphotyrosine Ref.11
Modified residue4571Phosphoserine; by PKB Ref.9 Ref.10 Ref.12 Ref.14 Ref.18 Ref.20

Natural variations

Alternative sequence1 – 1515MDVEN…VNPAD → MTKY in isoform 2.
VSP_045622
Natural variant361I → V. Ref.1 Ref.2 Ref.3 Ref.4 Ref.6 Ref.18
Corresponds to variant rs7081726 [ dbSNP | Ensembl ].
VAR_028901
Natural variant481S → Y. Ref.6
Corresponds to variant rs11548765 [ dbSNP | Ensembl ].
VAR_028902
Natural variant1201G → R in a breast cancer sample; somatic mutation. Ref.25
VAR_036375

Experimental info

Mutagenesis671S → A: Loss of phosphorylation site. Reduces interaction with BTRC. Abolishes phosphorylation by PKB; when associated with A-457. Ref.10 Ref.15
Mutagenesis711S → A: Strongly reduced interaction with BTRC. Strongly reduced ubiquitination. Ref.15
Mutagenesis761S → A: Strongly reduced interaction with BTRC. Strongly reduced ubiquitination. Ref.15
Mutagenesis1741E → A: Reduced inhibition of EIF4A1 helicase activity. Ref.23
Mutagenesis2101E → A: Reduced inhibition of EIF4A1 helicase activity. Strongly reduced inhibition of translation. Ref.23
Mutagenesis2491E → A: Reduced interaction with EIF4A1. Ref.23
Mutagenesis2521L → A: Strongly reduced interaction with EIF4A1. Reduced inhibition of EIF4A1 helicase activity. Strongly reduced inhibition of translation. Ref.23
Mutagenesis2531D → A: Strongly reduced interaction with EIF4A1. Strongly reduced inhibition of translation. Reduced inhibition of EIF4A1 helicase activity. Ref.23 Ref.24
Mutagenesis2551P → A: Reduced inhibition of EIF4A1 helicase activity. Strongly reduced inhibition of translation. Ref.23
Mutagenesis3331M → A: No effect on inhibition of EIF4A1 and on inhibition of translation; when associated with A-340. Ref.24
Mutagenesis3371E → A: No effect on inhibition of EIF4A1 and on inhibition of translation. Ref.24
Mutagenesis3401L → A: No effect on inhibition of EIF4A1 and on inhibition of translation; when associated with A-333. Ref.24
Mutagenesis3581H → A: Strongly reduced interaction with EIF4A1. Ref.23
Mutagenesis3591F → A: Strongly reduced inhibition of EIF4A1. Strongly reduced inhibition of translation. Ref.24
Mutagenesis3611H → A: Strongly reduced inhibition of EIF4A1. Strongly reduced inhibition of translation. Ref.24
Mutagenesis4141D → A: Strongly reduced interaction with EIF4A1. Strongly reduced inhibition of translation. Ref.23
Mutagenesis4181D → A: Reduced interaction with EIF4A1. Strongly reduced inhibition of translation. Ref.23
Mutagenesis4201P → A: Strongly reduced interaction with EIF4A1. Strongly reduced inhibition of translation. Ref.23
Mutagenesis4571S → A: Loss of phosphorylation site, and loss of nuclear accumulation. Abolishes phosphorylation by PKB; when associated with A-67. Ref.10
Sequence conflict791D → E in AAB42218. Ref.1
Sequence conflict1021R → G in AAB67706. Ref.2
Sequence conflict1301V → G in AAB67706. Ref.2
Sequence conflict2201S → T in AAB42218. Ref.1
Sequence conflict2221L → F in AAB67706. Ref.2
Sequence conflict3091K → R in BAG37701. Ref.3
Sequence conflict3141V → A in BAG37701. Ref.3
Sequence conflict4401S → W in AAB67706. Ref.2

Secondary structure

..................................... 469
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 11, 2011. Version 2.
Checksum: 2CAE1D2055491177

FASTA46951,735
        10         20         30         40         50         60 
MDVENEQILN VNPADPDNLS DSLFSGDEEN AGTEEIKNEI NGNWISASSI NEARINAKAK 

        70         80         90        100        110        120 
RRLRKNSSRD SGRGDSVSDS GSDALRSGLT VPTSPKGRLL DRRSRSGKGR GLPKKGGAGG 

       130        140        150        160        170        180 
KGVWGTPGQV YDVEEVDVKD PNYDDDQENC VYETVVLPLD ERAFEKTLTP IIQEYFEHGD 

       190        200        210        220        230        240 
TNEVAEMLRD LNLGEMKSGV PVLAVSLALE GKASHREMTS KLLSDLCGTV MSTTDVEKSF 

       250        260        270        280        290        300 
DKLLKDLPEL ALDTPRAPQL VGQFIARAVG DGILCNTYID SYKGTVDCVQ ARAALDKATV 

       310        320        330        340        350        360 
LLSMSKGGKR KDSVWGSGGG QQSVNHLVKE IDMLLKEYLL SGDISEAEHC LKELEVPHFH 

       370        380        390        400        410        420 
HELVYEAIIM VLESTGESTF KMILDLLKSL WKSSTITVDQ MKRGYERIYN EIPDINLDVP 

       430        440        450        460 
HSYSVLERFV EECFQAGIIS KQLRDLCPSR GRKRFVSEGD GGRLKPESY 

« Hide

Isoform 2 [UniParc].

Checksum: E887AA311F3EB4D4
Show »

FASTA45850,576

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"Crystal structure of the eIF4A-PDCD4 complex."
Chang J.H., Cho Y.H., Sohn S.Y., Choi J.M., Kim A., Kim Y.C., Jang S.K., Cho Y.
Proc. Natl. Acad. Sci. U.S.A. 106:3148-3153(2009) [PubMed] [Europe PMC] [Abstract]
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]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-120.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRJC5193.
RefSeqNP_055271.2. NM_014456.4.
NP_663314.1. NM_145341.3.
UniGeneHs.711490.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2GGFNMR-A327-450[»]
2KZTNMR-A157-318[»]
2RG8X-ray1.80A/B157-320[»]
2ZU6X-ray2.80B/E163-469[»]
3EIJX-ray2.80A/B157-469[»]
ProteinModelPortalQ53EL6.
SMRQ53EL6. Positions 157-450.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118098. 29 interactions.
DIPDIP-29756N.
IntActQ53EL6. 10 interactions.
STRING9606.ENSP00000280154.

Chemistry

BindingDBQ53EL6.
ChEMBLCHEMBL1781868.

PTM databases

PhosphoSiteQ53EL6.

Polymorphism databases

DMDM317373317.

Proteomic databases

PaxDbQ53EL6.
PRIDEQ53EL6.

Protocols and materials databases

DNASU27250.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000280154; ENSP00000280154; ENSG00000150593. [Q53EL6-1]
ENST00000393104; ENSP00000376816; ENSG00000150593. [Q53EL6-2]
GeneID27250.
KEGGhsa:27250.
UCSCuc001kzh.3. human. [Q53EL6-1]

Organism-specific databases

CTD27250.
GeneCardsGC10P112618.
H-InvDBHIX0009201.
HGNCHGNC:8763. PDCD4.
HPACAB037024.
HPA001032.
HPA027214.
MIM608610. gene.
neXtProtNX_Q53EL6.
PharmGKBPA33113.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG249108.
HOGENOMHOG000261612.
HOVERGENHBG052841.
InParanoidQ53EL6.
KOK16865.
OMALSMSKGG.
OrthoDBEOG7X9G6X.
PhylomeDBQ53EL6.
TreeFamTF323207.

Gene expression databases

ArrayExpressQ53EL6.
BgeeQ53EL6.
CleanExHS_PDCD4.
GenevestigatorQ53EL6.

Family and domain databases

Gene3D1.25.40.180. 2 hits.
InterProIPR016024. ARM-type_fold.
IPR003891. Initiation_fac_eIF4g_MI.
IPR016021. MIF4-like_typ_1/2/3.
[Graphical view]
PfamPF02847. MA3. 2 hits.
[Graphical view]
SMARTSM00544. MA3. 2 hits.
[Graphical view]
SUPFAMSSF48371. SSF48371. 2 hits.
PROSITEPS51366. MI. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPDCD4. human.
EvolutionaryTraceQ53EL6.
GeneWikiPDCD4.
GenomeRNAi27250.
NextBio50179.
PROQ53EL6.
SOURCESearch...

Entry information

Entry namePDCD4_HUMAN
AccessionPrimary (citable) accession number: Q53EL6
Secondary accession number(s): B2RCV4 expand/collapse secondary AC list , B5ME91, O15501, Q5VZS6, Q6PJI5, Q8TAR5, Q99834
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: January 11, 2011
Last modified: April 16, 2014
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM