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Protein Page:
PDCD4 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
PDCD4 protein localized to the nucleus in proliferating cells that seems to possess a tumor suppressor activity. Directly interacts with the RNA helicase eIF4A and inhibits protein synthesis by interfering with the assembly of the cap-dependent translation initiation complex. Suppresses carbonic anhydrase type II protein expression in carcinoid cell lines. Since tumor cells require a high bicarbonate flux for their growth, carbonic anhydrase suppression results in growth inhibition. Expression of this gene is modulated by cytokines in natural killer and T cells. The gene product is thought to play a role in apoptosis but the specific role has not yet been determined. Two differentially spliced isoforms have been identified. Note: This description may include information from UniProtKB.
Protein type: Apoptosis
Cellular Component: cytoplasm; nucleolus; cytosol; nucleus
Molecular Function: protein binding; RNA binding
Biological Process: negative regulation of JNK activity; apoptosis; cell aging; negative regulation of transcription, DNA-dependent; negative regulation of cell cycle
Reference #:  Q53EL6 (UniProtKB)
Alt. Names/Synonyms: H731; MGC33046; MGC33047; Neoplastic transformation inhibitor protein; nuclear antigen H731; Nuclear antigen H731-like; PDCD4; programmed cell death 4; programmed cell death 4 (neoplastic transformation inhibitor); Programmed cell death protein 4; Protein 197/15a
Gene Symbols: PDCD4
Molecular weight: 51,735 Da
Basal Isoelectric point: 5.07  Predict pI for various phosphorylation states
CST Pathways:  PI3K/Akt Signaling  |  Translation: eIF4E and p70S6K
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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PDCD4

Protein Structure Not Found.


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Sites Implicated In
cell cycle regulation: S67‑p, S71‑p
cell growth, altered: S67‑p, S71‑p
translation, altered: S67‑p, S71‑p
intracellular localization: S457‑p
molecular association, regulation: S67‑p, S71‑p, S76‑p
protein degradation: S67‑p, S71‑p, S76‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 2 S20-p PADPDNLsDsLFsGD
0 1 S22-p DPDNLsDsLFsGDEE
0 1 S25-p NLsDsLFsGDEENAG
0 2 K58-ub NEARINAkAkRRLRK
0 2 K60-ub ARINAkAkRRLRKNs
4 46 S67-p kRRLRKNssRDsGRG
0 20 S68-p RRLRKNssRDsGRGD
1 28 S71-p RKNssRDsGRGDsVs
2 102 S76-p RDsGRGDsVsDsGsD
0 20 S78-p sGRGDsVsDsGsDAL
0 2 S80-p RGDsVsDsGsDALRs
0 4 S82-p DsVsDsGsDALRsGL
0 2 S87-p sGsDALRsGLtVPts
0 1 T90-p DALRsGLtVPtsPKG
0 23 T93-p RsGLtVPtsPKGRLL
0 68 S94-p sGLtVPtsPKGRLLD
0 1 T126-p GGKGVWGtPGQVyDV
0 2 Y131-p WGtPGQVyDVEEVDV
0 1 Y143-p VDVKDPNyDDDQENC
0 14 Y152-p DDQENCVyETVVLPL
0 3 K166-ub LDERAFEkTLTPIIQ
0 2 K212-ub VSLALEGkASHREMT
0 2 K242-ub DVEKSFDkLLkDLPE
0 5 K245-ub KSFDkLLkDLPELAL
0 8 K283-ub NTYIDSYkGTVDCVQ
0 1 K297 QARAALDKAtVLLsM
0 1 T299-p RAALDKAtVLLsMSK
0 1 S303-p DKAtVLLsMSKGGKR
0 1 K306 tVLLsMSKGGKRKDs
0 9 S313-p KGGKRKDsVWGsGGG
0 4 S317-p RKDsVWGsGGGQQsV
0 1 S323-p GsGGGQQsVNHLVKE
0 1 Y405-p VDQMKRGyERIYNEI
0 1 S440-p CFQAGIIsKQLRDLC
5 70 S457-p RGRKRFVsEGDGGRL
0 2 S468-p GGRLKPEsY______
  mouse

 
S20 PTDPDNLSDSLFSGD
S22 DPDNLSDSLFSGDEE
S25 NLSDSLFSGDEENAG
K58 NEARINAKAKRRLRK
K60 ARINAKAKRRLRKNs
S67-p KRRLRKNssRDsGRG
S68-p RRLRKNssRDsGRGD
S71-p RKNssRDsGRGDsVs
S76-p RDsGRGDsVsDNGsE
S78-p sGRGDsVsDNGsEAV
N80 RGDsVsDNGsEAVRS
S82-p DsVsDNGsEAVRSGV
S87 NGsEAVRSGVAVPts
A90 EAVRSGVAVPtsPKG
T93-p RSGVAVPtsPKGRLL
S94-p SGVAVPtsPKGRLLD
T126 GGKGVWGTPGQVYDV
Y131 WGTPGQVYDVEEVDV
Y143 VDVKDPNYDDDQENC
Y152-p DDQENCVyETVVLPL
K166 LDETAFEKTLTPIIQ
K212 VSLALEGKASHREMT
K242-ub DVEKSFDkLLkDLPE
K245-ub KSFDkLLkDLPELAL
K283 NTYIDSYKGTVDCVQ
K297-ub QARAALDkATVLLSM
T299 RAALDkATVLLSMSk
S303 DkATVLLSMSkGGKR
K306-ub TVLLSMSkGGKRKDs
S313-p kGGKRKDsVWGSGGG
S317 RKDsVWGSGGGQQPV
P323 GSGGGQQPVNHLVKE
Y405 IDQMKRGYERIYNEI
S440 CFQAGIISKQLRDLC
S457-p RGRKRFVsEGDGGRL
S468 GGRLKPESY______
  rat

 
S20 PTDPDNLSDSLFSGD
S22 DPDNLSDSLFSGDEE
S25 NLSDSLFSGDEENAG
K58 NEARINAKAKRRLRK
K60 ARINAKAKRRLRKNs
S67-p KRRLRKNsSRDSGRG
S68 RRLRKNsSRDSGRGD
S71 RKNsSRDSGRGDSVS
S76 RDSGRGDSVSDNGSE
S78 SGRGDSVSDNGSEAV
N80 RGDSVSDNGSEAVRS
S82 DSVSDNGSEAVRSGV
S87 NGSEAVRSGVAVPts
A90 EAVRSGVAVPtsPKG
T93-p RSGVAVPtsPKGRLL
S94-p SGVAVPtsPKGRLLD
T126 GGKGVWGTPGQVYDV
Y131 WGTPGQVYDVEEVDV
Y143 VDVKDPNYDDDQENC
Y152 DDQENCVYETVVLPL
K166 LDETAFEKTLTPIIQ
K212 VSLALEGKASHREMT
K242 DVEKSFDKLLKDLPE
K245 KSFDKLLKDLPELAL
K283 NTYIDSYKGTVDCVQ
K297 QARAALDKATVLLSM
T299 RAALDKATVLLSMSK
S303 DKATVLLSMSKGGKR
K306 TVLLSMSKGGKRKDS
S313 KGGKRKDSVWGSGGG
S317 RKDSVWGSGGGQQPV
P323 GSGGGQQPVNHLVKE
Y405 IDQMKRGYERIYNEI
S440 CFQAGIISKQLRDLC
S457-p RGRKRFVsEGDGGRL
S468 GGRLKPESY______
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