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O54786

- DFFA_MOUSE

UniProt

O54786 - DFFA_MOUSE

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Protein

DNA fragmentation factor subunit alpha

Gene
Dffa, Icad
Organism
Mus musculus (Mouse)
Status
Reviewed - 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-3 By similarity
Sitei224 – 2252Cleavage; by caspase-3 By similarity

GO - Molecular functioni

  1. protein binding Source: IntAct

GO - Biological processi

  1. apoptotic DNA fragmentation Source: Ensembl
  2. negative regulation of apoptotic DNA fragmentation Source: MGI
  3. negative regulation of execution phase of apoptosis Source: RefGenome
  4. positive regulation of apoptotic process Source: MGI
  5. 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: UniProtKB-SubCell
  2. nuclear chromatin Source: RefGenome
  3. 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-acetylmethionine By 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.
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 – 116
Beta strandi19 – 257
Beta strandi28 – 3811
Helixi39 – 5012
Helixi54 – 563
Beta strandi60 – 667
Beta strandi72 – 798
Beta strandi84 – 885
Beta strandi90 – 923

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F2RNMR-I1-100[»]
ProteinModelPortaliO54786.
SMRiO54786. Positions 1-100, 239-299.

Miscellaneous databases

EvolutionaryTraceiO54786.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 9680CIDE-NAdd
BLAST

Sequence similaritiesi

Contains 1 CIDE-N domain.

Phylogenomic databases

eggNOGiNOG40170.
GeneTreeiENSGT00510000048128.
HOGENOMiHOG000112204.
HOVERGENiHBG000683.
InParanoidiQ8BQC7.
KOiK02310.
OMAiNEKWAYN.
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

MELSRGASAP DPDDVRPLKP CLLRRNHSRD QHGVAASSLE ELRSKACELL    50
AIDKSLTPIT LVLAEDGTIV DDDDYFLCLP SNTKFVALAC NEKWIYNDSD 100
GGTAWVSQES FEADEPDSRA GVKWKNVARQ LKEDLSSIIL LSEEDLQALI 150
DIPCAELAQE LCQSCATVQG LQSTLQQVLD QREEARQSKQ LLELYLQALE 200
KEGNILSNQK ESKAALSEEL DAVDTGVGRE MASEVLLRSQ ILTTLKEKPA 250
PELSLSSQDL ESVSKEDPKA LAVALSWDIR KAETVQQACT TELALRLQQV 300
QSLHSLRNLS ARRSPLPGEP QRPKRAKRDS S 331
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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei262 – 2654SVSK → VGKN in isoform ICAD-S. VSP_001087
Alternative sequencei266 – 33166Missing in isoform ICAD-S. VSP_001088Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti95 – 951I → T in BAA24140. 1 Publication
Sequence conflicti95 – 951I → T in BAA24141. 1 Publication
Sequence conflicti95 – 951I → T in CAQ52098. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS18951.1. [O54786-1 ]
CCDS18952.1. [O54786-2 ]
RefSeqi NP_001020467.1. NM_001025296.2. [O54786-1 ]
UniGenei Mm.41433.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1F2R NMR - I 1-100 [» ]
ProteinModelPortali O54786.
SMRi O54786. Positions 1-100, 239-299.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 199211. 2 interactions.
IntActi O54786. 2 interactions.
MINTi MINT-142152.

PTM databases

PhosphoSitei O54786.

Proteomic databases

MaxQBi O54786.
PaxDbi O54786.
PRIDEi O54786.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000030816 ; ENSMUSP00000030816 ; ENSMUSG00000028974 . [O54786-1 ]
ENSMUST00000103216 ; ENSMUSP00000099505 ; ENSMUSG00000028974 . [O54786-2 ]
GeneIDi 13347.
KEGGi mmu:13347.
UCSCi uc008vvr.1. mouse. [O54786-1 ]

Organism-specific databases

CTDi 1676.
MGIi MGI:1196227. Dffa.

Phylogenomic databases

eggNOGi NOG40170.
GeneTreei ENSGT00510000048128.
HOGENOMi HOG000112204.
HOVERGENi HBG000683.
InParanoidi Q8BQC7.
KOi K02310.
OMAi NEKWAYN.
OrthoDBi EOG7JQBP8.
TreeFami TF102021.

Enzyme and pathway databases

Reactomei REACT_205002. Activation of DNA fragmentation factor.

Miscellaneous databases

EvolutionaryTracei O54786.
NextBioi 283666.
PMAP-CutDB Q8BQC7.
PROi O54786.
SOURCEi Search...

Gene expression databases

Bgeei O54786.
CleanExi MM_DFFA.
Genevestigatori O54786.

Family and domain databases

Gene3Di 1.10.1490.10. 1 hit.
InterProi IPR003508. CIDE-N_dom.
IPR027296. DFF-C_dom.
IPR017299. DNA_fragmentation_factor_asu.
IPR015121. DNA_fragmentation_mid_dom.
[Graphical view ]
Pfami PF02017. CIDE-N. 1 hit.
PF09033. DFF-C. 1 hit.
[Graphical view ]
PIRSFi PIRSF037865. DFF_alpha. 1 hit.
ProDomi PD316494. DNA_fragmentation_C. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00266. CAD. 1 hit.
[Graphical view ]
SUPFAMi SSF81783. SSF81783. 1 hit.
PROSITEi PS51135. CIDE_N. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 122 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

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