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PDCD4 (human)

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; nucleus; cytosol 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®

Select Structure to View Below PDCD4 2GGF - A=320-450 (human) 2KZT - A=157-318 (human) 2RG8 - A/B=157-320 (human) 2ZU6 - E/B=163-469 (human) 3EIJ - A/B=157-469 (human) 2HM8 - A=319-449 (mouse) 2IOL - A/B=320-469 (mouse) 2ION - A=320-469 (mouse) 2IOS - A=320-469 (mouse) 2KZT - B=319-449 (mouse) 2NSZ - A=320-469 (mouse) 3EIQ - C=120-469 (mouse)

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB 2GGF 2KZT 2RG8 2ZU6 3EIJ  |  Phospho3D  |  DISEASE  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene

	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

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	1		S20-p	PADPDNLsDSLFsGD
0	1		S25-p	NLsDSLFsGDEENAG
0	2		K58-u	NEARINAkAkRRLRK
0	2		K60-u	ARINAkAkRRLRKNs
2	40		S67-p	kRRLRKNssRDsGRG
0	13		S68-p	RRLRKNssRDsGRGD
1	19		S71-p	RKNssRDsGRGDsVs
1	84		S76-p	RDsGRGDsVsDsGsD
0	16		S78-p	sGRGDsVsDsGsDAL
0	2		S80-p	RGDsVsDsGsDALRs
0	4		S82-p	DsVsDsGsDALRsGL
0	2		S87-p	sGsDALRsGLTVPts
0	21		T93-p	RsGLTVPtsPKGRLL
0	64		S94-p	sGLTVPtsPKGRLLD
0	1		T126-p	GGKGVWGtPGQVyDV
0	2		Y131-p	WGtPGQVyDVEEVDV
0	2		Y143-p	VDVKDPNyDDDQENC
0	16		Y152-p	DDQENCVyETVVLPL
0	3		K166-u	LDERAFEkTLTPIIQ
0	2		K212-u	VSLALEGkASHREMT
0	2		K242-u	DVEKSFDkLLkDLPE
0	5		K245-u	KSFDkLLkDLPELAL
0	8		K283-u	NTYIDSYkGTVDCVQ
0	1		K297	QARAALDKATVLLSM
0	1		K306	TVLLSMSKGGKRKDs
0	5		S313-p	KGGKRKDsVWGsGGG
0	1		S317-p	RKDsVWGsGGGQQSV
0	1		Y405-p	VDQMKRGyERIYNEI
0	1		S440-p	CFQAGIIsKQLRDLC
3	61		S457-p	RGRKRFVsEGDGGRL

	mouse
S20	PTDPDNLSDSLFSGD
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
T93-p	RSGVAVPtsPKGRLL
S94-p	SGVAVPtsPKGRLLD
T126	GGKGVWGTPGQVYDV
Y131	WGTPGQVYDVEEVDV
Y143	VDVKDPNYDDDQENC
Y152-p	DDQENCVyETVVLPL
K166	LDETAFEKTLTPIIQ
K212	VSLALEGKASHREMT
K242-u	DVEKSFDkLLkDLPE
K245-u	KSFDkLLkDLPELAL
K283	NTYIDSYKGTVDCVQ
K297-u	QARAALDkATVLLSM
K306-u	TVLLSMSkGGKRKDs
S313-p	kGGKRKDsVWGSGGG
S317	RKDsVWGSGGGQQPV
Y405	IDQMKRGYERIYNEI
S440	CFQAGIISKQLRDLC
S457-p	RGRKRFVsEGDGGRL

	rat
S20	PTDPDNLSDSLFSGD
S25	NLSDSLFSGDEENAG
K58	NEARINAKAKRRLRK
K60	ARINAKAKRRLRKNS
S67	KRRLRKNSSRDSGRG
S68	RRLRKNSSRDSGRGD
S71	RKNSSRDSGRGDSVS
S76	RDSGRGDSVSDNGSE
S78	SGRGDSVSDNGSEAV
N80	RGDSVSDNGSEAVRS
S82	DSVSDNGSEAVRSGV
S87	NGSEAVRSGVAVPts
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
K306	TVLLSMSKGGKRKDS
S313	KGGKRKDSVWGSGGG
S317	RKDSVWGSGGGQQPV
Y405	IDQMKRGYERIYNEI
S440	CFQAGIISKQLRDLC
S457-p	RGRKRFVsEGDGGRL

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