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Protein

Programmed cell death protein 4

Gene

PDCD4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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. 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
Complete GO annotation...

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. nucleoplasm Source: HPA
  4. nucleus Source: UniProtKB
Complete GO annotation...

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 RPS6KB13 Publications
Modified residuei68 – 681Phosphoserine1 Publication
Modified residuei71 – 711Phosphoserine1 Publication
Modified residuei76 – 761Phosphoserine3 Publications
Modified residuei78 – 781Phosphoserine3 Publications
Modified residuei80 – 801Phosphoserine1 Publication
Modified residuei94 – 941Phosphoserine2 Publications
Modified residuei152 – 1521Phosphotyrosine1 Publication
Modified residuei313 – 3131Phosphoserine1 Publication
Modified residuei317 – 3171Phosphoserine1 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

BgeeiQ53EL6.
CleanExiHS_PDCD4.
ExpressionAtlasiQ53EL6. baseline and differential.
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
EIF4A1P608422EBI-935824,EBI-73449
PSEN2P498103EBI-935824,EBI-2010251
RELAQ042066EBI-935824,EBI-73886
RPS13P622772EBI-935824,EBI-351850

Protein-protein interaction databases

BioGridi118098. 31 interactions.
DIPiDIP-29756N.
IntActiQ53EL6. 14 interactions.
STRINGi9606.ENSP00000280154.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000015948.
HOGENOMiHOG000261612.
HOVERGENiHBG052841.
InParanoidiQ53EL6.
KOiK16865.
OMAiDGYKGTV.
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. AlignAdd to basket

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

        10         20         30         40         50
MDVENEQILN VNPADPDNLS DSLFSGDEEN AGTEEIKNEI NGNWISASSI
60 70 80 90 100
NEARINAKAK RRLRKNSSRD SGRGDSVSDS GSDALRSGLT VPTSPKGRLL
110 120 130 140 150
DRRSRSGKGR GLPKKGGAGG KGVWGTPGQV YDVEEVDVKD PNYDDDQENC
160 170 180 190 200
VYETVVLPLD ERAFEKTLTP IIQEYFEHGD TNEVAEMLRD LNLGEMKSGV
210 220 230 240 250
PVLAVSLALE GKASHREMTS KLLSDLCGTV MSTTDVEKSF DKLLKDLPEL
260 270 280 290 300
ALDTPRAPQL VGQFIARAVG DGILCNTYID SYKGTVDCVQ ARAALDKATV
310 320 330 340 350
LLSMSKGGKR KDSVWGSGGG QQSVNHLVKE IDMLLKEYLL SGDISEAEHC
360 370 380 390 400
LKELEVPHFH HELVYEAIIM VLESTGESTF KMILDLLKSL WKSSTITVDQ
410 420 430 440 450
MKRGYERIYN EIPDINLDVP HSYSVLERFV EECFQAGIIS KQLRDLCPSR
460
GRKRFVSEGD GGRLKPESY
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 AAB42218.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence AAH15036.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti79 – 791D → E in AAB42218 (Ref. 1) Curated
Sequence conflicti102 – 1021R → G in AAB67706 (PubMed:9759869).Curated
Sequence conflicti130 – 1301V → G in AAB67706 (PubMed:9759869).Curated
Sequence conflicti220 – 2201S → T in AAB42218 (Ref. 1) Curated
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi118098. 31 interactions.
DIPiDIP-29756N.
IntActiQ53EL6. 14 interactions.
STRINGi9606.ENSP00000280154.

Chemistry

BindingDBiQ53EL6.
ChEMBLiCHEMBL1781868.

PTM databases

PhosphoSiteiQ53EL6.

Polymorphism databases

DMDMi317373317.

Proteomic databases

MaxQBiQ53EL6.
PaxDbiQ53EL6.
PRIDEiQ53EL6.

Protocols and materials databases

DNASUi27250.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi27250.
GeneCardsiGC10P112618.
H-InvDBHIX0009201.
HGNCiHGNC:8763. PDCD4.
HPAiCAB037024.
HPA001032.
HPA027214.
MIMi608610. gene.
neXtProtiNX_Q53EL6.
PharmGKBiPA33113.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG249108.
GeneTreeiENSGT00390000015948.
HOGENOMiHOG000261612.
HOVERGENiHBG052841.
InParanoidiQ53EL6.
KOiK16865.
OMAiDGYKGTV.
OrthoDBiEOG7X9G6X.
PhylomeDBiQ53EL6.
TreeFamiTF323207.

Miscellaneous databases

ChiTaRSiPDCD4. human.
EvolutionaryTraceiQ53EL6.
GeneWikiiPDCD4.
GenomeRNAii27250.
NextBioi50179.
PROiQ53EL6.
SOURCEiSearch...

Gene expression databases

BgeeiQ53EL6.
CleanExiHS_PDCD4.
ExpressionAtlasiQ53EL6. baseline and differential.
GenevestigatoriQ53EL6.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67; SER-68; SER-71; SER-76; SER-78; SER-313 AND SER-317, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  22. "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.
  23. "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.
  24. "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.
  25. 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.
  26. 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: March 4, 2015
This is version 100 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.