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Protein

Death effector domain-containing protein

Gene

DEDD

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Molecular functioni

  1. DNA binding Source: UniProtKB

GO - Biological processi

  1. decidualization Source: Ensembl
  2. extrinsic apoptotic signaling pathway via death domain receptors Source: ProtInc
  3. negative regulation of protein catabolic process Source: Ensembl
  4. negative regulation of transcription of nuclear large rRNA transcript from RNA polymerase I promoter Source: Ensembl
  5. regulation of apoptotic process Source: InterPro
  6. spermatogenesis Source: ProtInc
  7. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Apoptosis, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Death effector domain-containing protein
Alternative name(s):
DEDPro1
Death effector domain-containing testicular molecule
FLDED-1
Gene namesi
Name:DEDD
Synonyms:DEDPRO1, DEFT
ORF Names:KE05
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:2755. DEDD.

Subcellular locationi

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.By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleolus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27236.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 318318Death effector domain-containing proteinPRO_0000191274Add
BLAST

Post-translational modificationi

Exists predominantly in a mono- or diubiquitinated form.

Keywords - PTMi

Ubl conjugation

Proteomic databases

MaxQBiO75618.
PaxDbiO75618.
PRIDEiO75618.

PTM databases

PhosphoSiteiO75618.

Expressioni

Tissue specificityi

Widely expressed with highest levels in testis.1 Publication

Gene expression databases

BgeeiO75618.
CleanExiHS_DEDD.
ExpressionAtlasiO75618. baseline and differential.
GenevestigatoriO75618.

Organism-specific databases

HPAiHPA055853.

Interactioni

Subunit structurei

Interacts with CASP8, CASP10, KRT8, KRT18, CASP3 and FADD. Homodimerizes and heterodimerizes with DEDD2.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
APLP2Q064813EBI-1043164,EBI-79306

Protein-protein interaction databases

BioGridi114627. 20 interactions.
DIPiDIP-41944N.
IntActiO75618. 15 interactions.
MINTiMINT-201863.
STRINGi9606.ENSP00000356985.

Structurei

3D structure databases

ProteinModelPortaliO75618.
SMRiO75618. Positions 29-101.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 10379DEDPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 DED (death effector) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG40331.
GeneTreeiENSGT00390000008714.
HOGENOMiHOG000049120.
HOVERGENiHBG007220.
InParanoidiO75618.
OrthoDBiEOG7BCNBW.
PhylomeDBiO75618.
TreeFamiTF331807.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
InterProiIPR011029. DEATH-like_dom.
IPR001875. DED.
[Graphical view]
PfamiPF01335. DED. 1 hit.
[Graphical view]
SMARTiSM00031. DED. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
PROSITEiPS50168. DED. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O75618-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MAGLKRRASQ VWPEEHGEQE HGLYSLHRMF DIVGTHLTHR DVRVLSFLFV
60 70 80 90 100
DVIDDHERGL IRNGRDFLLA LERQGRCDES NFRQVLQLLR IITRHDLLPY
110 120 130 140 150
VTLKRRRAVC PDLVDKYLEE TSIRYVTPRA LSDPEPRPPQ PSKTVPPHYP
160 170 180 190 200
VVCCPTSGPQ MCSKRPARGR ATLGSQRKRR KSVTPDPKEK QTCDIRLRVR
210 220 230 240 250
AEYCQHETAL QGNVFSNKQD PLERQFERFN QANTILKSRD LGSIICDIKF
260 270 280 290 300
SELTYLDAFW RDYINGSLLE ALKGVFITDS LKQAVGHEAI KLLVNVDEED
310
YELGRQKLLR NLMLQALP
Length:318
Mass (Da):36,794
Last modified:November 1, 1998 - v1
Checksum:iFF9D5FF9B61F6BB6
GO
Isoform 2 (identifier: O75618-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     194-194: D → GEEIQGFQRWSRLEGEYKELLGHWAVYAIQY

Note: No experimental confirmation available.

Show »
Length:348
Mass (Da):40,418
Checksum:i7E40585470706387
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei194 – 1941D → GEEIQGFQRWSRLEGEYKEL LGHWAVYAIQY in isoform 2. 1 PublicationVSP_003846

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS1219.1. [O75618-1]
RefSeqiNP_001034800.1. NM_001039711.1. [O75618-1]
NP_001034801.1. NM_001039712.1. [O75618-1]
NP_127491.1. NM_032998.2. [O75618-1]
UniGeneiHs.744092.

Genome annotation databases

EnsembliENST00000368006; ENSP00000356985; ENSG00000158796. [O75618-1]
ENST00000458050; ENSP00000414821; ENSG00000158796. [O75618-1]
ENST00000490843; ENSP00000476946; ENSG00000158796. [O75618-1]
ENST00000545495; ENSP00000445835; ENSG00000158796. [O75618-1]
GeneIDi9191.
KEGGihsa:9191.
UCSCiuc001fxz.3. human. [O75618-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS1219.1. [O75618-1]
RefSeqiNP_001034800.1. NM_001039711.1. [O75618-1]
NP_001034801.1. NM_001039712.1. [O75618-1]
NP_127491.1. NM_032998.2. [O75618-1]
UniGeneiHs.744092.

3D structure databases

ProteinModelPortaliO75618.
SMRiO75618. Positions 29-101.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114627. 20 interactions.
DIPiDIP-41944N.
IntActiO75618. 15 interactions.
MINTiMINT-201863.
STRINGi9606.ENSP00000356985.

PTM databases

PhosphoSiteiO75618.

Proteomic databases

MaxQBiO75618.
PaxDbiO75618.
PRIDEiO75618.

Protocols and materials databases

DNASUi9191.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000368006; ENSP00000356985; ENSG00000158796. [O75618-1]
ENST00000458050; ENSP00000414821; ENSG00000158796. [O75618-1]
ENST00000490843; ENSP00000476946; ENSG00000158796. [O75618-1]
ENST00000545495; ENSP00000445835; ENSG00000158796. [O75618-1]
GeneIDi9191.
KEGGihsa:9191.
UCSCiuc001fxz.3. human. [O75618-1]

Organism-specific databases

CTDi9191.
GeneCardsiGC01M161090.
HGNCiHGNC:2755. DEDD.
HPAiHPA055853.
MIMi606841. gene.
neXtProtiNX_O75618.
PharmGKBiPA27236.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG40331.
GeneTreeiENSGT00390000008714.
HOGENOMiHOG000049120.
HOVERGENiHBG007220.
InParanoidiO75618.
OrthoDBiEOG7BCNBW.
PhylomeDBiO75618.
TreeFamiTF331807.

Miscellaneous databases

GeneWikiiDEDD.
GenomeRNAii9191.
NextBioi34461.
PROiO75618.
SOURCEiSearch...

Gene expression databases

BgeeiO75618.
CleanExiHS_DEDD.
ExpressionAtlasiO75618. baseline and differential.
GenevestigatoriO75618.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
InterProiIPR011029. DEATH-like_dom.
IPR001875. DED.
[Graphical view]
PfamiPF01335. DED. 1 hit.
[Graphical view]
SMARTiSM00031. DED. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
PROSITEiPS50168. DED. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiDEDD_HUMAN
AccessioniPrimary (citable) accession number: O75618
Secondary accession number(s): D3DVF5, O60737
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: November 1, 1998
Last modified: January 7, 2015
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.