O75618 (DEDD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	318 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Nucleus › nucleolus 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.

Ontologies

Keywords
Biological process	Apoptosis Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Ligand	DNA-binding
Molecular function	Repressor
PTM	Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	decidualization Inferred from electronic annotation. Source: Compara extrinsic apoptotic signaling pathway via death domain receptors Traceable author statement Ref.1. Source: ProtInc induction of apoptosis Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of protein catabolic process Inferred from electronic annotation. Source: Compara negative regulation of transcription, DNA-dependent Inferred from sequence or structural similarity. Source: UniProtKB spermatogenesis Traceable author statement Ref.2. Source: ProtInc transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB nucleolus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	DNA binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
APLP2	Q06481	3	EBI-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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 318	318	Death effector domain-containing protein		PRO_0000191274
Regions
	Domain	25 – 103	79	DED
Natural variations
	Alternative sequence	194	1	D → GEEIQGFQRWSRLEGEYKEL LGHWAVYAIQY in isoform 2.		VSP_003846

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: FF9D5FF9B61F6BB6	FASTA	318	36,794
	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
	Isoform 2 [UniParc]. Checksum: 7E40585470706387	FASTA	348	40,418
	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 QTCGEEIQGF QRWSRLEGEY KELLGHWAVY AIQYIRLRVR AEYCQHETAL 250 260 270 280 290 300 QGNVFSNKQD PLERQFERFN QANTILKSRD LGSIICDIKF SELTYLDAFW RDYINGSLLE 310 320 330 340 ALKGVFITDS LKQAVGHEAI KLLVNVDEED YELGRQKLLR NLMLQALP

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
IPI	IPI00004539. IPI00216748.
RefSeq	NP_001034800.1. NM_001039711.1. NP_001034801.1. NM_001039712.1. NP_127491.1. NM_032998.2.
UniGene	Hs.744092.
3D structure databases
ProteinModelPortal	O75618.
SMR	O75618. Positions 29-101.
ModBase	Search...
Protein-protein interaction databases
IntAct	O75618. 14 interactions.
MINT	MINT-201863.
STRING	9606.ENSP00000356985.
PTM databases
PhosphoSite	O75618.
Proteomic databases
PaxDb	O75618.
PRIDE	O75618.
Protocols and materials databases
DNASU	9191.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000368006; ENSP00000356985; ENSG00000158796. ENST00000458050; ENSP00000414821; ENSG00000158796. ENST00000541906; ENSP00000442587; ENSG00000158796. ENST00000545495; ENSP00000445835; ENSG00000158796.
GeneID	9191.
KEGG	hsa:9191.
UCSC	uc001fxz.3. human.
Organism-specific databases
CTD	9191.
GeneCards	GC01M161090.
HGNC	HGNC:2755. DEDD.
MIM	606841. gene.
neXtProt	NX_O75618.
PharmGKB	PA27236.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG40331.
HOGENOM	HOG000049120.
HOVERGEN	HBG007220.
OrthoDB	EOG466VM6.
PhylomeDB	O75618.
Gene expression databases
ArrayExpress	O75618.
Bgee	O75618.
CleanEx	HS_DEDD.
Genevestigator	O75618.
GermOnline	ENSG00000158796. Homo sapiens.
Family and domain databases
Gene3D	1.10.533.10. 1 hit.
InterPro	IPR011029. DEATH-like_dom. IPR001875. DED. [Graphical view]
Pfam	PF01335. DED. 1 hit. [Graphical view]
SMART	SM00031. DED. 1 hit. [Graphical view]
SUPFAM	SSF47986. DEATH_like. 1 hit.
PROSITE	PS50168. DED. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	9191.
NextBio	34461.
SOURCE	Search...

Entry information

Entry name

DEDD_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 111 of the entry and version 1 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.