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DNA-binding death effector domain-containing protein 2 (DED-containing protein FLAME-3) (FADD-like anti-apoptotic molecule 3)

 DEDD2_HUMAN             Reviewed;         326 AA.
Q8WXF8; Q8NBR2; Q8NES1; Q8TAA8; Q96D35;
10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
20-JUN-2018, entry version 136.
RecName: Full=DNA-binding death effector domain-containing protein 2;
AltName: Full=DED-containing protein FLAME-3;
AltName: Full=FADD-like anti-apoptotic molecule 3;
Name=DEDD2; Synonyms=FLAME3; ORFNames=PSEC0004;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
INTERACTION WITH CASP8.
PubMed=11741985; DOI=10.1074/jbc.M110749200;
Roth W., Stenner-Liewen F., Pawlowski K., Godzik A., Reed J.C.;
"Identification and characterization of DEDD2, a death effector
domain-containing protein.";
J. Biol. Chem. 277:7501-7508(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY,
SUBCELLULAR LOCATION, AND INTERACTION WITH CASP8 AND GTF3C3.
PubMed=11965497; DOI=10.1038/sj.cdd.4401038;
Zhan Y., Hegde R., Srinivasula S.M., Fernandes-Alnemri T.,
Alnemri E.S.;
"Death effector domain-containing proteins DEDD and FLAME-3 form
nuclear complexes with the TFIIIC102 subunit of human transcription
factor IIIC.";
Cell Death Differ. 9:439-447(2002).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=12235123; DOI=10.1083/jcb.200112124;
Lee J.C., Schickling O., Stegh A.H., Oshima R.G., Dinsdale D.,
Cohen G.M., Peter M.E.;
"DEDD regulates degradation of intermediate filaments during
apoptosis.";
J. Cell Biol. 158:1051-1066(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Teratocarcinoma;
PubMed=16303743; DOI=10.1093/dnares/12.2.117;
Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
Isogai T.;
"Signal sequence and keyword trap in silico for selection of full-
length human cDNAs encoding secretion or membrane proteins from oligo-
capped cDNA libraries.";
DNA Res. 12:117-126(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain, and Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
INTERACTION WITH CASP8 AND CASP10.
PubMed=12527898; DOI=10.1038/sj.onc.1206099;
Alcivar A., Hu S., Tang J., Yang X.;
"DEDD and DEDD2 associate with caspase-8/10 and signal cell death.";
Oncogene 22:291-297(2003).
-!- FUNCTION: May play a critical role in death receptor-induced
apoptosis and may target CASP8 and CASP10 to the nucleus. May
regulate 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.
-!- SUBUNIT: Interacts with CASP8, CASP10 and GTF3C3. Homodimerizes
and heterodimerizes with DEDD. {ECO:0000269|PubMed:11741985,
ECO:0000269|PubMed:11965497, ECO:0000269|PubMed:12527898}.
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus
{ECO:0000269|PubMed:11965497}. Note=Nuclear, accumulated in
subnuclear structures resembling nucleoli.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8WXF8-1; Sequence=Displayed;
Name=2;
IsoId=Q8WXF8-2; Sequence=VSP_010312;
-!- TISSUE SPECIFICITY: Expressed in most tissues. High levels were
found in liver, kidney, heart, ovary, spleen, testes, skeletal
muscle and peripheral blood leukocytes. Expression was absent or
low in colon and small intestine. Expression is relatively high in
the tumor cell lines chronic myologenous leukemia K-562 and the
colorectal adenocarcinoma SW480. Expression is moderate in the
cervical carcinoma HeLa, the Burkitt's lymphoma Raji, the lung
carcinoma A-549, and the melanoma G-361. In contrast, two leukemia
cell lines, HL-60 (promyelocytic leukemia) and MOLT-4
(lymphoblastic leukemia), show relatively low levels.
{ECO:0000269|PubMed:11741985, ECO:0000269|PubMed:11965497}.
-!- DOMAIN: Interactions with CASP8 and CASP10 are mediated by the DED
domain.
-!- SEQUENCE CAUTION:
Sequence=AAH13372.2; Type=Frameshift; Positions=186; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF443591; AAL48220.1; -; mRNA.
EMBL; AF457575; AAM10835.1; -; mRNA.
EMBL; AY125488; AAM95240.1; -; mRNA.
EMBL; AK075328; BAC11551.1; -; mRNA.
EMBL; BC013372; AAH13372.2; ALT_FRAME; mRNA.
EMBL; BC027930; AAH27930.1; -; mRNA.
CCDS; CCDS12597.1; -. [Q8WXF8-1]
CCDS; CCDS59391.1; -. [Q8WXF8-2]
RefSeq; NP_001257543.1; NM_001270614.1. [Q8WXF8-1]
RefSeq; NP_001257544.1; NM_001270615.1. [Q8WXF8-2]
RefSeq; NP_579874.1; NM_133328.3. [Q8WXF8-1]
UniGene; Hs.515432; -.
UniGene; Hs.741580; -.
ProteinModelPortal; Q8WXF8; -.
BioGrid; 127838; 13.
IntAct; Q8WXF8; 2.
MINT; Q8WXF8; -.
STRING; 9606.ENSP00000470082; -.
iPTMnet; Q8WXF8; -.
PhosphoSitePlus; Q8WXF8; -.
DMDM; 47116024; -.
PaxDb; Q8WXF8; -.
PeptideAtlas; Q8WXF8; -.
PRIDE; Q8WXF8; -.
ProteomicsDB; 75029; -.
ProteomicsDB; 75030; -. [Q8WXF8-2]
Ensembl; ENST00000336034; ENSP00000336972; ENSG00000160570. [Q8WXF8-2]
Ensembl; ENST00000595337; ENSP00000470082; ENSG00000160570. [Q8WXF8-1]
Ensembl; ENST00000596251; ENSP00000471512; ENSG00000160570. [Q8WXF8-1]
GeneID; 162989; -.
KEGG; hsa:162989; -.
UCSC; uc002osu.3; human. [Q8WXF8-1]
CTD; 162989; -.
EuPathDB; HostDB:ENSG00000160570.13; -.
GeneCards; DEDD2; -.
HGNC; HGNC:24450; DEDD2.
HPA; HPA043419; -.
neXtProt; NX_Q8WXF8; -.
OpenTargets; ENSG00000160570; -.
PharmGKB; PA134912744; -.
eggNOG; ENOG410IGDZ; Eukaryota.
eggNOG; ENOG410XV3E; LUCA.
GeneTree; ENSGT00390000008714; -.
HOGENOM; HOG000049120; -.
HOVERGEN; HBG007220; -.
InParanoid; Q8WXF8; -.
OMA; APCWEED; -.
OrthoDB; EOG091G0DX2; -.
PhylomeDB; Q8WXF8; -.
TreeFam; TF331807; -.
ChiTaRS; DEDD2; human.
GenomeRNAi; 162989; -.
PRO; PR:Q8WXF8; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000160570; -.
CleanEx; HS_DEDD2; -.
ExpressionAtlas; Q8WXF8; baseline and differential.
Genevisible; Q8WXF8; HS.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IBA:GO_Central.
GO; GO:0030159; F:receptor signaling complex scaffold activity; NAS:UniProtKB.
GO; GO:0030262; P:apoptotic nuclear changes; IDA:UniProtKB.
GO; GO:0019725; P:cellular homeostasis; NAS:UniProtKB.
GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IMP:UniProtKB.
GO; GO:0035556; P:intracellular signal transduction; NAS:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; NAS:UniProtKB.
GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IMP:UniProtKB.
GO; GO:0006396; P:RNA processing; NAS:UniProtKB.
GO; GO:0016075; P:rRNA catabolic process; NAS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR011029; DEATH-like_dom_sf.
InterPro; IPR001875; DED_dom.
InterPro; IPR038856; DEDD/DEDD2.
PANTHER; PTHR15205; PTHR15205; 1.
Pfam; PF01335; DED; 1.
SMART; SM00031; DED; 1.
SUPFAM; SSF47986; SSF47986; 1.
PROSITE; PS50168; DED; 1.
1: Evidence at protein level;
Alternative splicing; Apoptosis; Complete proteome; DNA-binding;
Nucleus; Reference proteome; Transcription; Transcription regulation.
CHAIN 1 326 DNA-binding death effector domain-
containing protein 2.
/FTId=PRO_0000191277.
DOMAIN 25 104 DED. {ECO:0000255|PROSITE-
ProRule:PRU00065}.
MOTIF 104 109 Nuclear localization signal.
{ECO:0000255}.
MOTIF 155 173 Bipartite nuclear localization signal.
{ECO:0000255}.
VAR_SEQ 145 149 Missing (in isoform 2).
{ECO:0000303|PubMed:12235123,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_010312.
CONFLICT 27 27 H -> N (in Ref. 2; AAM10835).
{ECO:0000305}.
CONFLICT 56 56 A -> G (in Ref. 2; AAM10835).
{ECO:0000305}.
CONFLICT 79 79 D -> G (in Ref. 4; BAC11551).
{ECO:0000305}.
CONFLICT 207 207 C -> R (in Ref. 2; AAM10835).
{ECO:0000305}.
CONFLICT 230 230 Missing (in Ref. 5; AAH13372).
{ECO:0000305}.
SEQUENCE 326 AA; 36179 MW; 3F7B0B307CC870CD CRC64;
MALSGSTPAP CWEEDECLDY YGMLSLHRMF EVVGGQLTEC ELELLAFLLD EAPGAAGGLA
RARSGLELLL ELERRGQCDE SNLRLLGQLL RVLARHDLLP HLARKRRRPV SPERYSYGTS
SSSKRTEGSC RRRRQSSSSA NSQQGQWETG SPPTKRQRRS RGRPSGGARR RRRGAPAAPQ
QQSEPARPSS EGKVTCDIRL RVRAEYCEHG PALEQGVASR RPQALARQLD VFGQATAVLR
SRDLGSVVCD IKFSELSYLD AFWGDYLSGA LLQALRGVFL TEALREAVGR EAVRLLVSVD
EADYEAGRRR LLLMEEEGGR RPTEAS


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