Q61823 · PDCD4_MOUSE
- ProteinProgrammed cell death protein 4
- GenePdcd4
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids469 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended nameProgrammed cell death protein 4
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ61823
- Secondary accessions
Proteomes
Organism-specific databases
Phenotypes & Variants
Involvement in disease
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 414 | Strongly reduced interaction with EIF4A1. | ||||
Sequence: D → A | ||||||
Mutagenesis | 418 | Strongly reduced interaction with EIF4A1. | ||||
Sequence: D → A | ||||||
Mutagenesis | 457 | No effect on interaction with EIF4A1. | ||||
Sequence: S → A or D |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 8 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
PTM/Processing
Features
Showing features for modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 1 | N-acetylmethionine | ||||
Sequence: M | ||||||
Chain | PRO_0000256520 | 1-469 | Programmed cell death protein 4 | |||
Sequence: MDIENEQTLNVNPTDPDNLSDSLFSGDEENAGTEEIKNEINGNWISASTINEARINAKAKRRLRKNSSRDSGRGDSVSDNGSEAVRSGVAVPTSPKGRLLDRRSRSGKGRGLPKKGGAGGKGVWGTPGQVYDVEEVDVKDPNYDDDQENCVYETVVLPLDETAFEKTLTPIIQEYFEHGDTNEVAEMLRDLNLGEMKSGVPVLAVSLALEGKASHREMTSKLLSDLCGTVMSTNDVEKSFDKLLKDLPELALDTPRAPQLVGQFIARAVGDGILCNTYIDSYKGTVDCVQARAALDKATVLLSMSKGGKRKDSVWGSGGGQQPVNHLVKEIDMLLKEYLLSGDISEAEHCLKELEVPHFHHELVYEAIVMVLESTGESAFKMILDLLKSLWKSSTITIDQMKRGYERIYNEIPDINLDVPHSYSVLERFVEECFQAGIISKQLRDLCPSRGRKRFVSEGDGGRLKPESY | ||||||
Modified residue | 25 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 67 | Phosphoserine; by PKB and RPS6KB1 | ||||
Sequence: S | ||||||
Modified residue | 68 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 71 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 76 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 78 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 94 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 152 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 313 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 317 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 457 | Phosphoserine; by PKB | ||||
Sequence: S |
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 (By similarity).
Phosphorylated at Ser-67 by RPS6KB1 in response to mitogens; phosphorylation promotes proteasomal degradation of PDCD4.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed ubiquitously. Highyly expressed in thymus and liver. Moderately expressed in brain, kidney and spleen; weakly in lung and heart. Expression is up- or down-regulated in response to apoptosis inducers. Regulated by many programmed cell death-inducing stimuli.
Gene expression databases
Interaction
Subunit
Interacts (via MI domains) with EIF4A1 and EIF4A2 (via N-terminal domain). Heterotrimer with EIF4A1; one molecule of PDCD4 binds two molecules of EIF4A1. Interacts with EIF4G1. May form a complex with EIF4A1 and EIF4G1. The interaction between PDCD4 and EIF4A1 interferes with the interaction between EIF4A1 and EIF4G. When phosphorylated, interacts with BTRC and FBXW11 (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q61823 | Eif4a1 P60843 | 4 | EBI-296473, EBI-6665935 | |
BINARY | Q61823 | Eif4g2 Q62448 | 2 | EBI-296473, EBI-296494 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region, motif, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-27 | Polar residues | ||||
Sequence: MDIENEQTLNVNPTDPDNLSDSLFSGD | ||||||
Region | 1-37 | Disordered | ||||
Sequence: MDIENEQTLNVNPTDPDNLSDSLFSGDEENAGTEEIK | ||||||
Motif | 58-64 | Nuclear localization signal | ||||
Sequence: KAKRRLR | ||||||
Region | 58-128 | Disordered | ||||
Sequence: KAKRRLRKNSSRDSGRGDSVSDNGSEAVRSGVAVPTSPKGRLLDRRSRSGKGRGLPKKGGAGGKGVWGTPG | ||||||
Motif | 70-76 | Phosphodegron | ||||
Sequence: DSGRGDS | ||||||
Domain | 163-284 | MI 1 | ||||
Sequence: AFEKTLTPIIQEYFEHGDTNEVAEMLRDLNLGEMKSGVPVLAVSLALEGKASHREMTSKLLSDLCGTVMSTNDVEKSFDKLLKDLPELALDTPRAPQLVGQFIARAVGDGILCNTYIDSYKG | ||||||
Domain | 326-449 | MI 2 | ||||
Sequence: HLVKEIDMLLKEYLLSGDISEAEHCLKELEVPHFHHELVYEAIVMVLESTGESAFKMILDLLKSLWKSSTITIDQMKRGYERIYNEIPDINLDVPHSYSVLERFVEECFQAGIISKQLRDLCPS | ||||||
Motif | 448-454 | Nuclear localization signal | ||||
Sequence: PSRGRKR |
Domain
Binds EIF4A1 via both MI domains.
Sequence similarities
Belongs to the PDCD4 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length469
- Mass (Da)51,702
- Last updated1996-11-01 v1
- Checksum6883BCE5011692F1
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A494BA05 | A0A494BA05_MOUSE | Pdcd4 | 319 |
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-27 | Polar residues | ||||
Sequence: MDIENEQTLNVNPTDPDNLSDSLFSGD | ||||||
Sequence conflict | 232 | in Ref. 2; BAA32356 and 3; BAA13072 | ||||
Sequence: S → I | ||||||
Sequence conflict | 369 | in Ref. 2; BAA32356 and 3; BAA13072 | ||||
Sequence: V → I | ||||||
Sequence conflict | 414 | in Ref. 5; BAE43115 | ||||
Sequence: D → G |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D50465 EMBL· GenBank· DDBJ | BAA09056.1 EMBL· GenBank· DDBJ | mRNA | ||
D86344 EMBL· GenBank· DDBJ | BAA13072.1 EMBL· GenBank· DDBJ | mRNA | ||
AB010139 EMBL· GenBank· DDBJ | BAA32356.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DQ479921 EMBL· GenBank· DDBJ | ABF51670.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CT010188 EMBL· GenBank· DDBJ | CAJ18396.1 EMBL· GenBank· DDBJ | mRNA | ||
AK134366 EMBL· GenBank· DDBJ | BAE22118.1 EMBL· GenBank· DDBJ | mRNA | ||
AK172654 EMBL· GenBank· DDBJ | BAE43115.1 EMBL· GenBank· DDBJ | mRNA | ||
BC055739 EMBL· GenBank· DDBJ | AAH55739.1 EMBL· GenBank· DDBJ | mRNA |