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Protein

DNA fragmentation factor subunit alpha

Gene

Dffa

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

Functioni

Inhibitor of the caspase-activated DNase (DFF40).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei117 – 1182Cleavage; by caspase-3By similarity
Sitei224 – 2252Cleavage; by caspase-3By similarity

GO - Biological processi

  1. negative regulation of apoptotic DNA fragmentation Source: MGI
  2. negative regulation of execution phase of apoptosis Source: MGI
  3. positive regulation of apoptotic process Source: MGI
  4. thymocyte apoptotic process Source: MGI
Complete GO annotation...

Keywords - Biological processi

Apoptosis

Enzyme and pathway databases

ReactomeiREACT_205002. Activation of DNA fragmentation factor.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA fragmentation factor subunit alpha
Alternative name(s):
DNA fragmentation factor 45 kDa subunit
Short name:
DFF-45
Inhibitor of CAD
Short name:
ICAD
Gene namesi
Name:Dffa
Synonyms:Icad
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:1196227. Dffa.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. cytosol Source: MGI
  3. nuclear chromatin Source: MGI
  4. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 331331DNA fragmentation factor subunit alphaPRO_0000144717Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity

Post-translational modificationi

Caspase-3 cleaves DFF45 at 2 sites to generate an active factor.By similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiO54786.
PaxDbiO54786.
PRIDEiO54786.

PTM databases

PhosphoSiteiO54786.

Miscellaneous databases

PMAP-CutDBQ8BQC7.

Expressioni

Gene expression databases

BgeeiO54786.
CleanExiMM_DFFA.
ExpressionAtlasiO54786. baseline.
GenevestigatoriO54786.

Interactioni

Subunit structurei

Heterodimer of DFFA and DFFB.

Binary interactionsi

WithEntry#Exp.IntActNotes
DffbO547886EBI-1634519,EBI-7365197

Protein-protein interaction databases

BioGridi199211. 2 interactions.
IntActiO54786. 2 interactions.
MINTiMINT-142152.

Structurei

Secondary structure

1
331
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 116Combined sources
Beta strandi19 – 257Combined sources
Beta strandi28 – 3811Combined sources
Helixi39 – 5012Combined sources
Helixi54 – 563Combined sources
Beta strandi60 – 667Combined sources
Beta strandi72 – 798Combined sources
Beta strandi84 – 885Combined sources
Beta strandi90 – 923Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F2RNMR-I1-100[»]
ProteinModelPortaliO54786.
SMRiO54786. Positions 1-100, 239-299.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO54786.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 9680CIDE-NPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 CIDE-N domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG40170.
GeneTreeiENSGT00510000048128.
HOGENOMiHOG000112204.
HOVERGENiHBG000683.
InParanoidiO54786.
KOiK02310.
OMAiCLLRRNH.
OrthoDBiEOG7JQBP8.
TreeFamiTF102021.

Family and domain databases

Gene3Di1.10.1490.10. 1 hit.
InterProiIPR003508. CIDE-N_dom.
IPR027296. DFF-C_dom.
IPR017299. DNA_fragmentation_factor_asu.
IPR015121. DNA_fragmentation_mid_dom.
[Graphical view]
PfamiPF02017. CIDE-N. 1 hit.
PF09033. DFF-C. 1 hit.
[Graphical view]
PIRSFiPIRSF037865. DFF_alpha. 1 hit.
ProDomiPD316494. DNA_fragmentation_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00266. CAD. 1 hit.
[Graphical view]
SUPFAMiSSF81783. SSF81783. 1 hit.
PROSITEiPS51135. CIDE_N. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform ICAD-L (identifier: O54786-1) [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
MELSRGASAP DPDDVRPLKP CLLRRNHSRD QHGVAASSLE ELRSKACELL
60 70 80 90 100
AIDKSLTPIT LVLAEDGTIV DDDDYFLCLP SNTKFVALAC NEKWIYNDSD
110 120 130 140 150
GGTAWVSQES FEADEPDSRA GVKWKNVARQ LKEDLSSIIL LSEEDLQALI
160 170 180 190 200
DIPCAELAQE LCQSCATVQG LQSTLQQVLD QREEARQSKQ LLELYLQALE
210 220 230 240 250
KEGNILSNQK ESKAALSEEL DAVDTGVGRE MASEVLLRSQ ILTTLKEKPA
260 270 280 290 300
PELSLSSQDL ESVSKEDPKA LAVALSWDIR KAETVQQACT TELALRLQQV
310 320 330
QSLHSLRNLS ARRSPLPGEP QRPKRAKRDS S
Length:331
Mass (Da):36,572
Last modified:July 27, 2011 - v2
Checksum:i4EA9314DD470040F
GO
Isoform ICAD-S (identifier: O54786-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     262-265: SVSK → VGKN
     266-331: Missing.

Show »
Length:265
Mass (Da):29,183
Checksum:i588DCABE1E987912
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti95 – 951I → T in BAA24140. (PubMed:9422506)Curated
Sequence conflicti95 – 951I → T in BAA24141. (PubMed:9422513)Curated
Sequence conflicti95 – 951I → T in CAQ52098. (PubMed:19468303)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei262 – 2654SVSK → VGKN in isoform ICAD-S. CuratedVSP_001087
Alternative sequencei266 – 33166Missing in isoform ICAD-S. CuratedVSP_001088Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB009375 mRNA. Translation: BAA24140.1.
AB009376 mRNA. Translation: BAA24141.1.
AK051011 mRNA. Translation: BAC34496.1.
AL611967 Genomic DNA. Translation: CAM13988.1.
CU210839 Genomic DNA. Translation: CAQ52098.1.
CCDSiCCDS18951.1. [O54786-1]
CCDS18952.1. [O54786-2]
RefSeqiNP_001020467.1. NM_001025296.2. [O54786-1]
UniGeneiMm.41433.

Genome annotation databases

EnsembliENSMUST00000030816; ENSMUSP00000030816; ENSMUSG00000028974. [O54786-1]
ENSMUST00000103216; ENSMUSP00000099505; ENSMUSG00000028974. [O54786-2]
GeneIDi13347.
KEGGimmu:13347.
UCSCiuc008vvr.1. mouse. [O54786-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB009375 mRNA. Translation: BAA24140.1.
AB009376 mRNA. Translation: BAA24141.1.
AK051011 mRNA. Translation: BAC34496.1.
AL611967 Genomic DNA. Translation: CAM13988.1.
CU210839 Genomic DNA. Translation: CAQ52098.1.
CCDSiCCDS18951.1. [O54786-1]
CCDS18952.1. [O54786-2]
RefSeqiNP_001020467.1. NM_001025296.2. [O54786-1]
UniGeneiMm.41433.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F2RNMR-I1-100[»]
ProteinModelPortaliO54786.
SMRiO54786. Positions 1-100, 239-299.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199211. 2 interactions.
IntActiO54786. 2 interactions.
MINTiMINT-142152.

PTM databases

PhosphoSiteiO54786.

Proteomic databases

MaxQBiO54786.
PaxDbiO54786.
PRIDEiO54786.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030816; ENSMUSP00000030816; ENSMUSG00000028974. [O54786-1]
ENSMUST00000103216; ENSMUSP00000099505; ENSMUSG00000028974. [O54786-2]
GeneIDi13347.
KEGGimmu:13347.
UCSCiuc008vvr.1. mouse. [O54786-1]

Organism-specific databases

CTDi1676.
MGIiMGI:1196227. Dffa.

Phylogenomic databases

eggNOGiNOG40170.
GeneTreeiENSGT00510000048128.
HOGENOMiHOG000112204.
HOVERGENiHBG000683.
InParanoidiO54786.
KOiK02310.
OMAiCLLRRNH.
OrthoDBiEOG7JQBP8.
TreeFamiTF102021.

Enzyme and pathway databases

ReactomeiREACT_205002. Activation of DNA fragmentation factor.

Miscellaneous databases

ChiTaRSiDffa. mouse.
EvolutionaryTraceiO54786.
NextBioi283666.
PMAP-CutDBQ8BQC7.
PROiO54786.
SOURCEiSearch...

Gene expression databases

BgeeiO54786.
CleanExiMM_DFFA.
ExpressionAtlasiO54786. baseline.
GenevestigatoriO54786.

Family and domain databases

Gene3Di1.10.1490.10. 1 hit.
InterProiIPR003508. CIDE-N_dom.
IPR027296. DFF-C_dom.
IPR017299. DNA_fragmentation_factor_asu.
IPR015121. DNA_fragmentation_mid_dom.
[Graphical view]
PfamiPF02017. CIDE-N. 1 hit.
PF09033. DFF-C. 1 hit.
[Graphical view]
PIRSFiPIRSF037865. DFF_alpha. 1 hit.
ProDomiPD316494. DNA_fragmentation_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00266. CAD. 1 hit.
[Graphical view]
SUPFAMiSSF81783. SSF81783. 1 hit.
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: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.

Entry informationi

Entry nameiDFFA_MOUSE
AccessioniPrimary (citable) accession number: O54786
Secondary accession number(s): B2KFX0, O54787, Q8BQC7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: July 27, 2011
Last modified: February 4, 2015
This is version 127 of the entry and version 2 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

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.