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Protein

Programmed cell death protein 4

Gene

Pdcd4

Organism
Rattus norvegicus (Rat)
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 similarity1 Publication

GO - Molecular functioni

GO - Biological processi

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):
Death up-regulated gene protein
Gene namesi
Name:Pdcd4
Synonyms:Dug
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi620816. Pdcd4.

Subcellular locationi

  • Nucleus By similarity
  • Cytoplasm By similarity

  • Note: Shuttles between the nucleus and cytoplasm. Predominantly nuclear under normal growth conditions, and when phosphorylated at Ser-457 (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 469469Programmed cell death protein 4PRO_0000256522Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei25 – 251PhosphoserineCombined sources
Modified residuei67 – 671Phosphoserine; by PKB and RPS6KB1By similarity
Modified residuei68 – 681PhosphoserineBy similarity
Modified residuei71 – 711PhosphoserineBy similarity
Modified residuei76 – 761PhosphoserineCombined sources
Modified residuei78 – 781PhosphoserineBy similarity
Modified residuei94 – 941PhosphoserineBy similarity
Modified residuei152 – 1521PhosphotyrosineBy similarity
Modified residuei313 – 3131PhosphoserineBy similarity
Modified residuei317 – 3171PhosphoserineBy similarity
Modified residuei457 – 4571PhosphoserineCombined sources

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

PaxDbiQ9JID1.
PRIDEiQ9JID1.

PTM databases

PhosphoSiteiQ9JID1.

Expressioni

Inductioni

Up-regulated by apoptotic inducers.1 Publication

Gene expression databases

ExpressionAtlasiQ9JID1. baseline and differential.
GenevisibleiQ9JID1. RN.

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 similarity).By similarity

Protein-protein interaction databases

IntActiQ9JID1. 1 interaction.
STRINGi10116.ENSRNOP00000020155.

Structurei

3D structure databases

ProteinModelPortaliQ9JID1.
SMRiQ9JID1. Positions 157-305, 319-449.
ModBaseiSearch...
MobiDBiSearch...

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.

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0403. Eukaryota.
ENOG410XQZZ. LUCA.
GeneTreeiENSGT00390000015948.
HOGENOMiHOG000261612.
HOVERGENiHBG052841.
InParanoidiQ9JID1.
KOiK16865.
OMAiDGYKGTV.
OrthoDBiEOG7X9G6X.
PhylomeDBiQ9JID1.
TreeFamiTF323207.

Family and domain databases

Gene3Di1.25.40.180. 2 hits.
InterProiIPR016024. ARM-type_fold.
IPR003891. Initiation_fac_eIF4g_MI.
IPR016021. MIF4-like.
[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: Q9JID1-1) [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 VNPTDPDNLS DSLFSGDEEN AGTEEIKNEI NGNWISASTI
60 70 80 90 100
NEARINAKAK RRLRKNSSRD SGRGDSVSDN GSEAVRSGVA VPTSPKGRLL
110 120 130 140 150
DRRSRSGKGR GLPKKGGAGG KGVWGTPGQV YDVEEVDVKD PNYDDDQENC
160 170 180 190 200
VYETVVLPLD ETAFEKTLTP IIQEYFEHGD TNEVAEMLRD LNLGEMKSGV
210 220 230 240 250
PVLAVSLALE GKASHREMTS KLLSDLCGTV MSTNDVEKSF DKLLKDLPEL
260 270 280 290 300
ALDTPRAPQL VGQFIARAVG DGILCNTYID SYKGTVDCVQ ARAALDKATV
310 320 330 340 350
LLSMSKGGKR KDSVWGSGGG QQPVNHLVKE IDMLLKEYLL SGDMSEAEHC
360 370 380 390 400
LKELEVPHFH HELVYEAIVM VLESTGESAF KMMLDLLKSL WKSSTITIDQ
410 420 430 440 450
MKRGYERIYN EIPDINLDVP HSYSVLERFV EECFQAGIIS KQLRDLCPSR
460
GRKRFVSEGD GGRLKPESY
Length:469
Mass (Da):51,736
Last modified:October 1, 2002 - v2
Checksum:i16D712EA267F9EEC
GO
Isoform 2 (identifier: Q9JID1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     367-403: Missing.

Show »
Length:432
Mass (Da):47,551
Checksum:i800052C62E66E429
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei367 – 40337Missing in isoform 2. 1 PublicationVSP_021356Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF239739 mRNA. Translation: AAF73961.2.
RefSeqiNP_071601.2. NM_022265.2. [Q9JID1-1]
XP_006231675.1. XM_006231613.2. [Q9JID1-1]
XP_006231676.1. XM_006231614.2. [Q9JID1-1]
XP_006231677.1. XM_006231615.2. [Q9JID1-1]
XP_006231678.1. XM_006231616.2. [Q9JID1-1]
UniGeneiRn.122017.

Genome annotation databases

EnsembliENSRNOT00000020155; ENSRNOP00000020155; ENSRNOG00000014779. [Q9JID1-1]
GeneIDi64031.
KEGGirno:64031.
UCSCiRGD:620816. rat. [Q9JID1-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF239739 mRNA. Translation: AAF73961.2.
RefSeqiNP_071601.2. NM_022265.2. [Q9JID1-1]
XP_006231675.1. XM_006231613.2. [Q9JID1-1]
XP_006231676.1. XM_006231614.2. [Q9JID1-1]
XP_006231677.1. XM_006231615.2. [Q9JID1-1]
XP_006231678.1. XM_006231616.2. [Q9JID1-1]
UniGeneiRn.122017.

3D structure databases

ProteinModelPortaliQ9JID1.
SMRiQ9JID1. Positions 157-305, 319-449.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9JID1. 1 interaction.
STRINGi10116.ENSRNOP00000020155.

PTM databases

PhosphoSiteiQ9JID1.

Proteomic databases

PaxDbiQ9JID1.
PRIDEiQ9JID1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000020155; ENSRNOP00000020155; ENSRNOG00000014779. [Q9JID1-1]
GeneIDi64031.
KEGGirno:64031.
UCSCiRGD:620816. rat. [Q9JID1-1]

Organism-specific databases

CTDi27250.
RGDi620816. Pdcd4.

Phylogenomic databases

eggNOGiKOG0403. Eukaryota.
ENOG410XQZZ. LUCA.
GeneTreeiENSGT00390000015948.
HOGENOMiHOG000261612.
HOVERGENiHBG052841.
InParanoidiQ9JID1.
KOiK16865.
OMAiDGYKGTV.
OrthoDBiEOG7X9G6X.
PhylomeDBiQ9JID1.
TreeFamiTF323207.

Miscellaneous databases

NextBioi612654.
PROiQ9JID1.

Gene expression databases

ExpressionAtlasiQ9JID1. baseline and differential.
GenevisibleiQ9JID1. RN.

Family and domain databases

Gene3Di1.25.40.180. 2 hits.
InterProiIPR016024. ARM-type_fold.
IPR003891. Initiation_fac_eIF4g_MI.
IPR016021. MIF4-like.
[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. "DUG is a novel homologue of translation initiation factor 4G that binds eIF4A."
    Goeke A., Goeke R., Knolle A., Trusheim H., Schmidt H., Wilmen A., Carmody R., Goeke B., Chen Y.H.
    Biochem. Biophys. Res. Commun. 297:78-82(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, INTERACTION WITH EIF4A1, INDUCTION, ALTERNATIVE SPLICING.
  2. "Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites."
    Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.
    Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  3. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-76 AND SER-457, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPDCD4_RAT
AccessioniPrimary (citable) accession number: Q9JID1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: October 1, 2002
Last modified: May 11, 2016
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

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.