Q53EL6 (PDCD4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Programmed cell death protein 4

Alternative name(s):
Neoplastic transformation inhibitor protein
Nuclear antigen H731-like
Protein 197/15a

Gene names

Name:	PDCD4
Synonyms:	H731

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	469 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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 By similarity. Ref.8 Ref.11 Ref.13 Ref.22 Ref.23 Ref.24
Subunit structure	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. Ref.13 Ref.22 Ref.23 Ref.24
Subcellular location	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. Ref.6 Ref.8
Tissue specificity	Up-regulated in proliferative cells. Highly expressed in epithelial cells of the mammary gland. Reduced expression in lung cancer and colon carcinoma. Ref.6 Ref.7 Ref.11
Induction	IL2/interleukin-2 stimulation inhibits expression, while IL12/interleukin-12 increases expression. Ref.2
Domain	Binds EIF4A1 via both MI domains. Ref.22 Ref.24
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. Phosphorylated at Ser-67 by RPS6KB1 in response to mitogens; phosphorylation promotes proteasomal degradation of PDCD4. Ref.8 Ref.9 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19
Sequence similarities	Belongs to the PDCD4 family. Contains 2 MI domains.
Sequence caution	The sequence AAB42218.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence AAH15036.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
Biological process	Apoptosis
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
Disease	Tumor suppressor
Domain	Repeat
Ligand	RNA-binding
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	apoptotic process Non-traceable author statement. Source: UniProtKB cell aging Inferred from direct assay. Source: UniProtKB negative regulation of JUN kinase activity Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of cell cycle Non-traceable author statement. Source: UniProtKB negative regulation of transcription, DNA-dependent Inferred from direct assay Ref.8. Source: UniProtKB
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB nucleus Inferred from mutant phenotype Ref.8. Source: UniProtKB
Molecular function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction Ref.8. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
APOE	P02649	3	EBI-935824,EBI-1222467
PSEN2	P49810	3	EBI-935824,EBI-2010251
RPS13	P62277	2	EBI-935824,EBI-351850

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 469

469

Programmed cell death protein 4

PRO_0000256519

Regions

Domain

163 – 284

122

MI 1

Domain

326 – 449

124

MI 2

Motif

58 – 64

7

Nuclear localization signal Potential

Motif

70 – 76

7

Phosphodegron

Motif

241 – 250

10

Nuclear localization signal Potential

Amino acid modifications

Modified residue

67

1

Phosphoserine; by PKB and RPS6KB1 Ref.8 Ref.13

Modified residue

76

1

Phosphoserine Ref.10 Ref.15 Ref.17

Modified residue

78

1

Phosphoserine Ref.17 Ref.18

Modified residue

80

1

Phosphoserine Ref.17

Modified residue

93

1

Phosphothreonine Ref.12 Ref.16

Modified residue

94

1

Phosphoserine Ref.16 Ref.17 Ref.18 Ref.19

Modified residue

152

1

Phosphotyrosine Ref.9

Modified residue

457

1

Phosphoserine; by PKB Ref.8 Ref.10 Ref.12 Ref.14 Ref.16 Ref.17

Natural variations

Natural variant

36

1

I → V. Ref.1 Ref.2 Ref.3 Ref.5
Corresponds to variant rs7081726 [ dbSNP | Ensembl ].

VAR_028901

Natural variant

48

1

S → Y. Ref.5
Corresponds to variant rs11548765 [ dbSNP | Ensembl ].

VAR_028902

Natural variant

120

1

G → R in a breast cancer sample; somatic mutation. Ref.25

VAR_036375

Experimental info

Mutagenesis

67

1

S → A: Loss of phosphorylation site. Reduces interaction with BTRC. Abolishes phosphorylation by PKB; when associated with A-457. Ref.8 Ref.13

Mutagenesis

71

1

S → A: Strongly reduced interaction with BTRC. Strongly reduced ubiquitination. Ref.13

Mutagenesis

76

1

S → A: Strongly reduced interaction with BTRC. Strongly reduced ubiquitination. Ref.13

Mutagenesis

174

1

E → A: Reduced inhibition of EIF4A1 helicase activity. Ref.23

Mutagenesis

210

1

E → A: Reduced inhibition of EIF4A1 helicase activity. Strongly reduced inhibition of translation. Ref.23

Mutagenesis

249

1

E → A: Reduced interaction with EIF4A1. Ref.23

Mutagenesis

252

1

L → A: Strongly reduced interaction with EIF4A1. Reduced inhibition of EIF4A1 helicase activity. Strongly reduced inhibition of translation. Ref.23

Mutagenesis

253

1

D → A: Strongly reduced interaction with EIF4A1. Strongly reduced inhibition of translation. Reduced inhibition of EIF4A1 helicase activity. Ref.23 Ref.24

Mutagenesis

255

1

P → A: Reduced inhibition of EIF4A1 helicase activity. Strongly reduced inhibition of translation. Ref.23

Mutagenesis

333

1

M → A: No effect on inhibition of EIF4A1 and on inhibition of translation; when associated with A-340. Ref.24

Mutagenesis

337

1

E → A: No effect on inhibition of EIF4A1 and on inhibition of translation. Ref.24

Mutagenesis

340

1

L → A: No effect on inhibition of EIF4A1 and on inhibition of translation; when associated with A-333. Ref.24

Mutagenesis

358

1

H → A: Strongly reduced interaction with EIF4A1. Ref.23

Mutagenesis

359

1

F → A: Strongly reduced inhibition of EIF4A1. Strongly reduced inhibition of translation. Ref.24

Mutagenesis

361

1

H → A: Strongly reduced inhibition of EIF4A1. Strongly reduced inhibition of translation. Ref.24

Mutagenesis

414

1

D → A: Strongly reduced interaction with EIF4A1. Strongly reduced inhibition of translation. Ref.23

Mutagenesis

418

1

D → A: Reduced interaction with EIF4A1. Strongly reduced inhibition of translation. Ref.23

Mutagenesis

420

1

P → A: Strongly reduced interaction with EIF4A1. Strongly reduced inhibition of translation. Ref.23

Mutagenesis

457

1

S → A: Loss of phosphorylation site, and loss of nuclear accumulation. Abolishes phosphorylation by PKB; when associated with A-67. Ref.8

Sequence conflict

79

1

D → E in AAB42218. Ref.1

Sequence conflict

102

1

R → G in AAB67706. Ref.2

Sequence conflict

130

1

V → G in AAB67706. Ref.2

Sequence conflict

220

1

S → T in AAB42218. Ref.1

Sequence conflict

222

1

L → F in AAB67706. Ref.2

Sequence conflict

440

1

S → W in AAB67706. Ref.2

Secondary structure

1

.

.

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.

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.

.

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.

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.

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469

Helix Strand Turn

Details...

Helix

161 – 178

18

Helix

181 – 191

11

Helix

195 – 198

4

Helix

199 – 209

11

Helix

213 – 226

14

Turn

227 – 229

3

Helix

233 – 253

21

Helix

257 – 270

14

Helix

278 – 281

4

Turn

282 – 284

3

Helix

289 – 303

15

Helix

328 – 341

14

Helix

344 – 353

10

Helix

357 – 359

3

Helix

360 – 373

14

Helix

377 – 392

16

Helix

398 – 418

21

Helix

422 – 436

15

Helix

441 – 446

6

Sequences

	Sequence		Length	Mass (Da)
	Q53EL6 [UniParc]. Last modified January 11, 2011. Version 2. Checksum: 2CAE1D2055491177	FASTA	469	51,735
	10 20 30 40 50 60 MDVENEQILN VNPADPDNLS DSLFSGDEEN AGTEEIKNEI NGNWISASSI NEARINAKAK 70 80 90 100 110 120 RRLRKNSSRD SGRGDSVSDS GSDALRSGLT VPTSPKGRLL DRRSRSGKGR GLPKKGGAGG 130 140 150 160 170 180 KGVWGTPGQV YDVEEVDVKD PNYDDDQENC VYETVVLPLD ERAFEKTLTP IIQEYFEHGD 190 200 210 220 230 240 TNEVAEMLRD LNLGEMKSGV PVLAVSLALE GKASHREMTS KLLSDLCGTV MSTTDVEKSF 250 260 270 280 290 300 DKLLKDLPEL ALDTPRAPQL VGQFIARAVG DGILCNTYID SYKGTVDCVQ ARAALDKATV 310 320 330 340 350 360 LLSMSKGGKR KDSVWGSGGG QQSVNHLVKE IDMLLKEYLL SGDISEAEHC LKELEVPHFH 370 380 390 400 410 420 HELVYEAIIM VLESTGESTF KMILDLLKSL WKSSTITVDQ MKRGYERIYN EIPDINLDVP 430 440 450 460 HSYSVLERFV EECFQAGIIS KQLRDLCPSR GRKRFVSEGD GGRLKPESY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 9759869] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, VARIANT VAL-36. Tissue: Blood.
[3]	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], VARIANT VAL-36. Tissue: Spleen.
[4]	"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: 15164054] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS VAL-36 AND TYR-48. Tissue: Brain and Skin.
[6]	"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: 10632927] [Abstract] Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[7]	"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: 12898601] [Abstract] Cited for: TISSUE SPECIFICITY.
[8]	"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: 16357133] [Abstract] Cited for: PHOSPHORYLATION AT SER-67 AND SER-457 BY PKB, FUNCTION, MUTAGENESIS OF SER-67 AND SER-457, SUBCELLULAR LOCATION.
[9]	"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: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-152, MASS SPECTROMETRY.
[10]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76 AND SER-457, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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: 16449643] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY.
[12]	"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: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-93 AND SER-457, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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: 17053147] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION AT SER-67 BY RPS6KB1, PHOSPHODEGRON MOTIF, INTERACTION WITH BTRC AND FBXW11, UBIQUITINATION, MASS SPECTROMETRY, MUTAGENESIS OF SER-67; SER-71 AND SER-76.
[14]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-457, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[15]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-93; SER-94 AND SER-457, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76; SER-78; SER-80; SER-94 AND SER-457, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78 AND SER-94, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[19]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[20]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]	"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.
[22]	"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: 18296639] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 157-320, FUNCTION, DOMAIN, INTERACTION WITH EIF4A, SUBUNIT.
[23]	"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: 19153607] [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.
[24]	"Crystal structure of the eIF4A-PDCD4 complex." Chang J.H., Cho Y.H., Sohn S.Y., Choi J.M., Kim A., Kim Y.C., Jang S.K., Cho Y. Proc. Natl. Acad. Sci. U.S.A. 106:3148-3153(2009) [PubMed: 19204291] [Abstract] 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.
[25]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-120.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U83908 Genomic DNA. Translation: AAB42218.1. Sequence problems.
U96628 mRNA. Translation: AAB67706.1.
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.

IPI

IPI00290110.

PIR

JC5193.

RefSeq

NP_055271.2. NM_014456.4.

UniGene

Hs.711490.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2GGF	NMR	-	A	327-450	[»]
2KZT	NMR	-	A	157-318	[»]
2RG8	X-ray	1.80	A/B	157-320	[»]
2ZU6	X-ray	2.80	B/E	163-469	[»]
3EIJ	X-ray	2.80	A/B	157-469	[»]

ProteinModelPortal

Q53EL6.

SMR

Q53EL6. Positions 157-450.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29756N.

IntAct

Q53EL6. 8 interactions.

STRING

Q53EL6.

PTM databases

PhosphoSite

Q53EL6.

Polymorphism databases

DMDM

74725796.

Proteomic databases

PRIDE

Q53EL6.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000280154; ENSP00000280154; ENSG00000150593.

GeneID

27250.

KEGG

hsa:27250.

UCSC

uc001kzh.1. human.

Organism-specific databases

CTD

27250.

GeneCards

GC10P112618.

H-InvDB

HIX0009201.

HGNC

HGNC:8763. PDCD4.

HPA

HPA001032.
HPA027214.

MIM

608610. gene.

neXtProt

NX_Q53EL6.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG10989.

GeneTree

ENSGT00390000015948.

HOGENOM

HBG714347.

HOVERGEN

HBG052841.

InParanoid

Q53EL6.

OMA

MSKGGKR.

OrthoDB

EOG4GMTX3.

PhylomeDB

Q53EL6.

Gene expression databases

ArrayExpress

Q53EL6.

Bgee

Q53EL6.

CleanEx

HS_PDCD4.

Genevestigator

Q53EL6.

GermOnline

ENSG00000150593. Homo sapiens.

Family and domain databases

InterPro

IPR016024. ARM-type_fold.
IPR003891. Initiation_fac_eIF4g_MI.
[Graphical view]

Pfam

PF02847. MA3. 2 hits.
[Graphical view]

SMART

SM00544. MA3. 2 hits.
[Graphical view]

SUPFAM

SSF48371. ARM-type_fold. 2 hits.

PROSITE

PS51366. MI. 2 hits.
[Graphical view]

ProtoNet

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Other

NextBio

50179.

SOURCE

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Entry information

Entry name

PDCD4_HUMAN

Accession

Primary (citable) accession number: Q53EL6
Secondary accession number(s): O15501 , Q5VZS6, Q6PJI5, Q8TAR5, Q99834

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	January 11, 2011
Last modified:	January 25, 2012
This is version 71 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.