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Protein

DNA fragmentation factor subunit beta

Gene

Dffb

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Nuclease that induces DNA fragmentation and chromatin condensation during apoptosis. Degrades naked DNA and induces apoptotic morphology.

Enzyme regulationi

Inhibited by DFFA (DFF45).

GO - Molecular functioni

  • DNA binding Source: MGI
  • enzyme binding Source: MGI
  • nuclease activity Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Nuclease

Keywords - Biological processi

Apoptosis

Enzyme and pathway databases

ReactomeiR-MMU-211227. Activation of DNA fragmentation factor.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA fragmentation factor subunit beta (EC:3.-.-.-)
Alternative name(s):
Caspase-activated deoxyribonuclease
Short name:
CAD
Short name:
Caspase-activated DNase
DNA fragmentation factor 40 kDa subunit
Short name:
DFF-40
Gene namesi
Name:Dffb
Synonyms:Cad
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1196287. Dffb.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 344344DNA fragmentation factor subunit betaPRO_0000144714Add
BLAST

Proteomic databases

EPDiO54788.
MaxQBiO54788.
PaxDbiO54788.
PRIDEiO54788.

PTM databases

PhosphoSiteiO54788.

Expressioni

Gene expression databases

BgeeiO54788.
CleanExiMM_DFFB.
GenevisibleiO54788. MM.

Interactioni

Subunit structurei

Heterodimer of DFFA and DFFB. Interacts with HIST1H1A (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
DFFAO002738EBI-7365197,EBI-727171From a different organism.
DffaO547866EBI-7365197,EBI-1634519

GO - Molecular functioni

Protein-protein interaction databases

BioGridi199222. 3 interactions.
IntActiO54788. 3 interactions.
MINTiMINT-142143.
STRINGi10090.ENSMUSP00000030893.

Structurei

Secondary structure

1
344
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 157Combined sources
Beta strandi16 – 194Combined sources
Beta strandi23 – 286Combined sources
Helixi29 – 3911Combined sources
Beta strandi48 – 514Combined sources
Turni52 – 554Combined sources
Turni60 – 623Combined sources
Beta strandi70 – 756Combined sources
Helixi88 – 947Combined sources
Helixi103 – 1119Combined sources
Helixi116 – 12914Combined sources
Turni138 – 1403Combined sources
Turni142 – 1476Combined sources
Helixi155 – 17521Combined sources
Helixi176 – 1805Combined sources
Turni183 – 1853Combined sources
Helixi186 – 20217Combined sources
Helixi203 – 2108Combined sources
Beta strandi212 – 2143Combined sources
Turni216 – 2183Combined sources
Beta strandi235 – 2373Combined sources
Helixi246 – 2483Combined sources
Helixi250 – 2556Combined sources
Turni256 – 2583Combined sources
Beta strandi259 – 2657Combined sources
Turni267 – 2704Combined sources
Helixi271 – 28111Combined sources
Helixi287 – 2959Combined sources
Turni297 – 2993Combined sources
Beta strandi300 – 3034Combined sources
Helixi305 – 3073Combined sources
Turni319 – 3213Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C9FNMR-A1-87[»]
1F2RNMR-C1-87[»]
1V0DX-ray2.60A1-329[»]
ProteinModelPortaliO54788.
SMRiO54788. Positions 1-328.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO54788.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 8377CIDE-NPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 CIDE-N domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410IFTE. Eukaryota.
ENOG41102TS. LUCA.
GeneTreeiENSGT00390000014490.
HOGENOMiHOG000006502.
HOVERGENiHBG003828.
InParanoidiO54788.
KOiK02311.
OMAiESRFRNK.
OrthoDBiEOG712TW8.
PhylomeDBiO54788.
TreeFamiTF102022.

Family and domain databases

InterProiIPR015311. Apoptosis_DFF40.
IPR003508. CIDE-N_dom.
[Graphical view]
PfamiPF02017. CIDE-N. 1 hit.
PF09230. DFF40. 1 hit.
[Graphical view]
SMARTiSM00266. CAD. 1 hit.
[Graphical view]
PROSITEiPS51135. CIDE_N. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O54788-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCAVLRQPKC VKLRALHSAC KFGVAARSCQ ELLRKGCVRF QLPMPGSRLC
60 70 80 90 100
LYEDGTEVTD DCFPGLPNDA ELLLLTAGET WHGYVSDITR FLSVFNEPHA
110 120 130 140 150
GVIQAARQLL SDEQAPLRQK LLADLLHHVS QNITAETREQ DPSWFEGLES
160 170 180 190 200
RFRNKSGYLR YSCESRIRGY LREVSAYTSM VDEAAQEEYL RVLGSMCQKL
210 220 230 240 250
KSVQYNGSYF DRGAEASSRL CTPEGWFSCQ GPFDLESCLS KHSINPYGNR
260 270 280 290 300
ESRILFSTWN LDHIIEKKRT VVPTLAEAIQ DGREVNWEYF YSLLFTAENL
310 320 330 340
KLVHIACHKK TTHKLECDRS RIYRPQTGSR RKQPARKKRP ARKR
Length:344
Mass (Da):39,449
Last modified:June 1, 1998 - v1
Checksum:iE854B413EA139DE1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB009377 mRNA. Translation: BAA24977.1.
CCDSiCCDS19004.1.
RefSeqiNP_031885.3. NM_007859.4.
UniGeneiMm.388918.

Genome annotation databases

EnsembliENSMUST00000030893; ENSMUSP00000030893; ENSMUSG00000029027.
GeneIDi13368.
KEGGimmu:13368.
UCSCiuc008wav.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB009377 mRNA. Translation: BAA24977.1.
CCDSiCCDS19004.1.
RefSeqiNP_031885.3. NM_007859.4.
UniGeneiMm.388918.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C9FNMR-A1-87[»]
1F2RNMR-C1-87[»]
1V0DX-ray2.60A1-329[»]
ProteinModelPortaliO54788.
SMRiO54788. Positions 1-328.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199222. 3 interactions.
IntActiO54788. 3 interactions.
MINTiMINT-142143.
STRINGi10090.ENSMUSP00000030893.

PTM databases

PhosphoSiteiO54788.

Proteomic databases

EPDiO54788.
MaxQBiO54788.
PaxDbiO54788.
PRIDEiO54788.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030893; ENSMUSP00000030893; ENSMUSG00000029027.
GeneIDi13368.
KEGGimmu:13368.
UCSCiuc008wav.2. mouse.

Organism-specific databases

CTDi1677.
MGIiMGI:1196287. Dffb.

Phylogenomic databases

eggNOGiENOG410IFTE. Eukaryota.
ENOG41102TS. LUCA.
GeneTreeiENSGT00390000014490.
HOGENOMiHOG000006502.
HOVERGENiHBG003828.
InParanoidiO54788.
KOiK02311.
OMAiESRFRNK.
OrthoDBiEOG712TW8.
PhylomeDBiO54788.
TreeFamiTF102022.

Enzyme and pathway databases

ReactomeiR-MMU-211227. Activation of DNA fragmentation factor.

Miscellaneous databases

EvolutionaryTraceiO54788.
NextBioi283710.
PROiO54788.
SOURCEiSearch...

Gene expression databases

BgeeiO54788.
CleanExiMM_DFFB.
GenevisibleiO54788. MM.

Family and domain databases

InterProiIPR015311. Apoptosis_DFF40.
IPR003508. CIDE-N_dom.
[Graphical view]
PfamiPF02017. CIDE-N. 1 hit.
PF09230. DFF40. 1 hit.
[Graphical view]
SMARTiSM00266. CAD. 1 hit.
[Graphical view]
PROSITEiPS51135. CIDE_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD."
    Enari M., Sakahira H., Yokoyama H., Okawa K., Iwamatsu A., Nagata S.
    Nature 391:43-50(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Cleavage of CAD inhibitor in CAD activation and DNA degradation during apoptosis."
    Sakahira H., Enari M., Nagata S.
    Nature 391:96-99(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Spleen.

Entry informationi

Entry nameiDFFB_MOUSE
AccessioniPrimary (citable) accession number: O54788
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: June 1, 1998
Last modified: May 11, 2016
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.