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HUMAN:DFFA

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Species (Taxon ID) Homo sapiens (Human). (9606)
Gene Name(s) DFFA (synonyms: DFF1, DFF45)
Protein Name(s) DNA fragmentation factor subunit alpha

DNA fragmentation factor 45 kDa subunit DFF-45 Inhibitor of CAD ICAD

External Links
UniProt O00273
EMBL U91985
AF087573
AF103799
BT006980
AK313317
AL354956
AL354956
CH471130
CH471130
BC000037
BC007112
BC007721
CCDS CCDS118.1
CCDS119.1
RefSeq NP_004392.1
NP_998731.1
UniGene Hs.484782
PDB 1IBX
1IYR
1KOY
PDBsum 1IBX
1IYR
1KOY
DisProt DP00173
ProteinModelPortal O00273
SMR O00273
BioGrid 108040
IntAct O00273
MINT MINT-365527
STRING 9606.ENSP00000366237
iPTMnet O00273
PhosphoSite O00273
BioMuta DFFA
EPD O00273
MaxQB O00273
PaxDb O00273
PeptideAtlas O00273
PRIDE O00273
DNASU 1676
Ensembl ENST00000377036
ENST00000377038
GeneID 1676
KEGG hsa:1676
UCSC uc001arj.4
CTD 1676
GeneCards DFFA
HGNC HGNC:2772
HPA CAB002679
HPA018859
HPA019938
HPA025230
MIM 601882
neXtProt NX_O00273
PharmGKB PA27254
eggNOG ENOG410IU5B
ENOG4111HKY
GeneTree ENSGT00510000048128
HOGENOM HOG000112204
HOVERGEN HBG000683
InParanoid O00273
KO K02310
OMA CLLRRNH
OrthoDB EOG7JQBP8
PhylomeDB O00273
TreeFam TF102021
Reactome R-HSA-211227
SignaLink O00273
ChiTaRS DFFA
EvolutionaryTrace O00273
GeneWiki DFFA
GenomeRNAi 1676
NextBio 6896
PMAP-CutDB Q5T6G5
PRO PR:O00273
Proteomes UP000005640
Bgee O00273
CleanEx HS_DFFA
ExpressionAtlas O00273
Genevisible O00273
GO GO:0005737
GO:0005829
GO:0000790
GO:0005654
GO:0005634
GO:0006309
GO:0006915
GO:0006921
GO:1902511
GO:1900118
GO:0043065
GO:0012501
GO:0070242
Gene3D 1.10.1490.10
InterPro IPR003508
IPR027296
IPR017299
IPR015121
PANTHER PTHR12306:SF16
Pfam PF02017
PF09033
PIRSF PIRSF037865
ProDom PD316494
SMART SM00266
SUPFAM SSF81783
PROSITE PS51135

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

involved_in

GO:0032076

negative regulation of deoxyribonuclease activity

PMID:19944011[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0060703

deoxyribonuclease inhibitor activity

PMID:19944011[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0061077

chaperone-mediated protein folding

PMID:19944011[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0044183

protein folding chaperone

PMID:19944011[1]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:O76075

F

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:22253444[2]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0019904

protein domain specific binding

PMID:11371636[3]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:O76075

F

Seeded From UniProt

complete

involved_in

GO:1900118

negative regulation of execution phase of apoptosis

PMID:9564035[4]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:9108473[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0000790

nuclear chromatin

PMID:19882353[6]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:1900118

negative regulation of execution phase of apoptosis

PMID:21873635[7]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000267119
UniProtKB:O00273

P

Seeded From UniProt

complete

part_of

GO:0005811

lipid droplet

PMID:21873635[7]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:1270845
PANTHER:PTN000959606
UniProtKB:O60543

C

Seeded From UniProt

complete

part_of

GO:0000790

nuclear chromatin

PMID:21873635[7]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000267119
UniProtKB:O00273

C

Seeded From UniProt

complete

involved_in

GO:1902511

negative regulation of apoptotic DNA fragmentation

PMID:15572351[8]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

PMID:15572351[8]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

GO_REF:0000052

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

GO_REF:0000052

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:1902511

negative regulation of apoptotic DNA fragmentation

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:O54786
ensembl:ENSMUSP00000030816

P

Seeded From UniProt

complete

involved_in

GO:0070242

thymocyte apoptotic process

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:O54786
ensembl:ENSMUSP00000030816

P

Seeded From UniProt

complete

involved_in

GO:0043065

positive regulation of apoptotic process

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:O54786
ensembl:ENSMUSP00000030816

P

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:A0A0G2JY18
ensembl:ENSRNOP00000070485

C

Seeded From UniProt

complete

involved_in

GO:0006309

apoptotic DNA fragmentation

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR017299

P

Seeded From UniProt

complete

involved_in

GO:0006915

apoptotic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003508

P

Seeded From UniProt

complete

enables

GO:0060703

deoxyribonuclease inhibitor activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR017299

F

Seeded From UniProt

complete

involved_in

GO:0006309

apoptotic DNA fragmentation

Reactome:R-HSA-140342

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

Reactome:R-HSA-211224
Reactome:R-HSA-211206
Reactome:R-HSA-211191

ECO:0000304

author statement supported by traceable reference used in manual assertion



C

Seeded From UniProt

complete

part_of

GO:0005654

nucleoplasm

Reactome:R-HSA-9029667
Reactome:R-HSA-211207
Reactome:R-HSA-211206
Reactome:R-HSA-211190
Reactome:R-HSA-211186

ECO:0000304

author statement supported by traceable reference used in manual assertion





C

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

involved_in

GO:0006915

apoptotic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0053

P

Seeded From UniProt

complete

edit table

Notes

References

See Help:References for how to manage references in GONUTS.

  1. ↑ 1.0 1.1 1.2 1.3 Park, HH (2009) Fifty C-terminal amino acid residues are necessary for the chaperone activity of DFF45 but not for the inhibition of DFF40. BMB Rep 42 713-8 PubMed GONUTS page
  2. ↑ Iglesias-Guimarais, V et al. (2012) Apoptotic DNA degradation into oligonucleosomal fragments, but not apoptotic nuclear morphology, relies on a cytosolic pool of DFF40/CAD endonuclease. J. Biol. Chem. 287 7766-79 PubMed GONUTS page
  3. ↑ Zhou, P et al. (2001) Solution structure of DFF40 and DFF45 N-terminal domain complex and mutual chaperone activity of DFF40 and DFF45. Proc. Natl. Acad. Sci. U.S.A. 98 6051-5 PubMed GONUTS page
  4. ↑ Inohara, N et al. (1998) CIDE, a novel family of cell death activators with homology to the 45 kDa subunit of the DNA fragmentation factor. EMBO J. 17 2526-33 PubMed GONUTS page
  5. ↑ Liu, X et al. (1997) DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis. Cell 89 175-84 PubMed GONUTS page
  6. ↑ Ninios, YP et al. (2010) Histone H1 subtype preferences of DFF40 and possible nuclear localization of DFF40/45 in normal and trichostatin A-treated NB4 leukemic cells. Apoptosis 15 128-38 PubMed GONUTS page
  7. ↑ 7.0 7.1 7.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  8. ↑ 8.0 8.1 Korn, C et al. (2005) Interaction of DNA fragmentation factor (DFF) with DNA reveals an unprecedented mechanism for nuclease inhibition and suggests that DFF can be activated in a DNA-bound state. J. Biol. Chem. 280 6005-15 PubMed GONUTS page
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