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O75618 (DEDD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Death effector domain-containing protein
Alternative name(s):
DEDPro1
Death effector domain-containing testicular molecule
FLDED-1
Gene names
Name:DEDD
Synonyms:DEDPRO1, DEFT
ORF Names:KE05
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length318 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

A scaffold protein that directs CASP3 to certain substrates and facilitates their ordered degradation during apoptosis. May also play a role in mediating CASP3 cleavage of KRT18. Regulates degradation of intermediate filaments during apoptosis. May play a role in the general transcription machinery in the nucleus and might be an important regulator of the activity of GTF3C3. Inhibits DNA transcription in vitro By similarity. Ref.10

Subunit structure

Interacts with CASP8, CASP10, KRT8, KRT18, CASP3 and FADD. Homodimerizes and heterodimerizes with DEDD2. Ref.10 Ref.11 Ref.12

Subcellular location

Cytoplasm. Nucleusnucleolus By similarity. Note: Translocated to the nucleus during CD95-mediated apoptosis where it is localized in the nucleoli By similarity. Following apoptosis induction, the mono and/or diubiquitination form increases and forms filamentous structures that colocalize with KRT8 and KRT18 intermediate filament network in simple epithelial cells.

Tissue specificity

Widely expressed with highest levels in testis. Ref.2

Post-translational modification

Exists predominantly in a mono- or diubiquitinated form.

Sequence similarities

Contains 1 DED (death effector) domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

APLP2Q064813EBI-1043164,EBI-79306

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O75618-1)

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.
Isoform 2 (identifier: O75618-2)

The sequence of this isoform differs from the canonical sequence as follows:
     194-194: D → GEEIQGFQRWSRLEGEYKELLGHWAVYAIQY
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 318318Death effector domain-containing protein
PRO_0000191274

Regions

Domain25 – 10379DED

Natural variations

Alternative sequence1941D → GEEIQGFQRWSRLEGEYKEL LGHWAVYAIQY in isoform 2.
VSP_003846

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: FF9D5FF9B61F6BB6

FASTA31836,794
        10         20         30         40         50         60 
MAGLKRRASQ VWPEEHGEQE HGLYSLHRMF DIVGTHLTHR DVRVLSFLFV DVIDDHERGL 

        70         80         90        100        110        120 
IRNGRDFLLA LERQGRCDES NFRQVLQLLR IITRHDLLPY VTLKRRRAVC PDLVDKYLEE 

       130        140        150        160        170        180 
TSIRYVTPRA LSDPEPRPPQ PSKTVPPHYP VVCCPTSGPQ MCSKRPARGR ATLGSQRKRR 

       190        200        210        220        230        240 
KSVTPDPKEK QTCDIRLRVR AEYCQHETAL QGNVFSNKQD PLERQFERFN QANTILKSRD 

       250        260        270        280        290        300 
LGSIICDIKF SELTYLDAFW RDYINGSLLE ALKGVFITDS LKQAVGHEAI KLLVNVDEED 

       310 
YELGRQKLLR NLMLQALP 

« Hide

Isoform 2 [UniParc].

Checksum: 7E40585470706387
Show »

FASTA34840,418

References

« Hide 'large scale' references
[1]"DEDD, a novel death effector domain-containing protein, targeted to the nucleolus."
Stegh A.H., Schickling O., Ehret A., Scaffidi C., Peterhaensel C., Hofmann T.G., Grummt I., Krammer P.H., Peter M.E.
EMBO J. 17:5974-5986(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"DEFT, a novel death effector domain-containing molecule predominantly expressed in testicular germ cells."
Leo C.P., Hsu S.Y., McGee E.A., Salanova M., Hsueh A.J.W.
Endocrinology 139:4839-4848(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
Tissue: Testis.
[3]"FLDED-1, a novel molecule with a DED-like domain."
Pan G.
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]"DEDPRO1, a novel DED-containing protein."
Thome M., Tschopp J.
Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[5]"A novel gene from human dendritic cell."
Zhao Z., Huang X., Li N., Zhu X., Cao X.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Dendritic cell.
[6]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[7]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Bone marrow and Placenta.
[10]"DEDD regulates degradation of intermediate filaments during apoptosis."
Lee J.C., Schickling O., Stegh A.H., Oshima R.G., Dinsdale D., Cohen G.M., Peter M.E.
J. Cell Biol. 158:1051-1066(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH KRT8; KRT18 AND CASP3.
[11]"Death effector domain-containing proteins DEDD and FLAME-3 form nuclear complexes with the TFIIIC102 subunit of human transcription factor IIIC."
Zhan Y., Hegde R., Srinivasula S.M., Fernandes-Alnemri T., Alnemri E.S.
Cell Death Differ. 9:439-447(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GTF3C3.
[12]"DEDD and DEDD2 associate with caspase-8/10 and signal cell death."
Alcivar A., Hu S., Tang J., Yang X.
Oncogene 22:291-297(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CASP8 AND CASP10.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF083236 mRNA. Translation: AAC33105.1.
AF100341 mRNA. Translation: AAD16414.1.
AF043733 mRNA. Translation: AAC80280.1.
AJ010973 mRNA. Translation: CAA09445.1.
AF064605 mRNA. Translation: AAC17110.3.
CR536556 mRNA. Translation: CAG38793.1.
AL591806 Genomic DNA. Translation: CAI15381.1.
CH471121 Genomic DNA. Translation: EAW52648.1.
CH471121 Genomic DNA. Translation: EAW52650.1.
CH471121 Genomic DNA. Translation: EAW52651.1.
CH471121 Genomic DNA. Translation: EAW52652.1.
CH471121 Genomic DNA. Translation: EAW52653.1.
BC016724 mRNA. Translation: AAH16724.1.
BC013910 mRNA. Translation: AAH13910.1.
RefSeqNP_001034800.1. NM_001039711.1.
NP_001034801.1. NM_001039712.1.
NP_127491.1. NM_032998.2.
UniGeneHs.744092.

3D structure databases

ProteinModelPortalO75618.
SMRO75618. Positions 29-101.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114627. 20 interactions.
IntActO75618. 15 interactions.
MINTMINT-201863.
STRING9606.ENSP00000356985.

PTM databases

PhosphoSiteO75618.

Proteomic databases

PaxDbO75618.
PRIDEO75618.

Protocols and materials databases

DNASU9191.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000368006; ENSP00000356985; ENSG00000158796. [O75618-1]
ENST00000458050; ENSP00000414821; ENSG00000158796. [O75618-1]
ENST00000490843; ENSP00000476946; ENSG00000158796. [O75618-1]
ENST00000545495; ENSP00000445835; ENSG00000158796. [O75618-1]
GeneID9191.
KEGGhsa:9191.
UCSCuc001fxz.3. human. [O75618-1]

Organism-specific databases

CTD9191.
GeneCardsGC01M161090.
HGNCHGNC:2755. DEDD.
HPAHPA055853.
MIM606841. gene.
neXtProtNX_O75618.
PharmGKBPA27236.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG40331.
HOGENOMHOG000049120.
HOVERGENHBG007220.
OrthoDBEOG7BCNBW.
PhylomeDBO75618.
TreeFamTF331807.

Gene expression databases

ArrayExpressO75618.
BgeeO75618.
CleanExHS_DEDD.
GenevestigatorO75618.

Family and domain databases

Gene3D1.10.533.10. 1 hit.
InterProIPR011029. DEATH-like_dom.
IPR001875. DED.
[Graphical view]
PfamPF01335. DED. 1 hit.
[Graphical view]
SMARTSM00031. DED. 1 hit.
[Graphical view]
SUPFAMSSF47986. SSF47986. 1 hit.
PROSITEPS50168. DED. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiDEDD.
GenomeRNAi9191.
NextBio34461.
PROO75618.
SOURCESearch...

Entry information

Entry nameDEDD_HUMAN
AccessionPrimary (citable) accession number: O75618
Secondary accession number(s): D3DVF5, O60737
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: November 1, 1998
Last modified: March 19, 2014
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM