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UniProtKB/Swiss-Prot entry O00273


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name DFFA_HUMAN
Primary accession number O00273
Secondary accession numbers Q96I97 Q9Y6C6
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on July 1, 1997 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 100)
Name and origin of the protein
Protein name DNA fragmentation factor subunit alpha
Synonyms DNA fragmentation factor 45 kDa subunit
DFF-45
Inhibitor of CAD
ICAD
Gene name
Name: DFFA
Synonyms: DFF1, DFF45
ORFNames: H13
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DFF45), AND PROTEIN SEQUENCE OF 171-181; 190-201; 214-218 AND 230-242.
DOI=10.1016/S0092-8674(00)80197-X; PubMed=9108473 [NCBI, ExPASy, EBI, Israel, Japan]
Liu X., Zou H., Slaughter C., Wang X.;
"DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis.";
Cell 89:175-184(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DFF35).
DOI=10.1074/jbc.274.30.20759; PubMed=10409614 [NCBI, ExPASy, EBI, Israel, Japan]
Gu J.J., Dong R.P., Zhang C., McLaughlin D.F., Wu M.X., Schlossman S.F.;
"Functional interaction of DFF35 and DFF45 with caspase-activated DNA fragmentation nuclease DFF40.";
J. Biol. Chem. 274:20759-20762(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DFF35).
DOI=10.1093/nar/27.20.4008; PubMed=10497265 [NCBI, ExPASy, EBI, Israel, Japan]
Oh J.J., Grosshans D.R., Wong S.G., Slamon D.J.;
"Identification of differentially expressed genes associated with HER-2/neu overexpression in human breast cancer cells.";
Nucleic Acids Res. 27:4008-4017(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM DFF45).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM DFF45).
TISSUE=Eye, Kidney, and Skeletal muscle;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1038/nbt1240; PubMed=16964243 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1021/pr070152u; PubMed=17924679 [NCBI, ExPASy, EBI, Israel, Japan]
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257, AND MASS SPECTROMETRY.
DOI=10.1126/science.1140321; PubMed=17525332 [NCBI, ExPASy, EBI, Israel, Japan]
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.";
Science 316:1160-1166(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310 AND SER-315, AND MASS SPECTROMETRY.
DOI=10.2116/analsci.24.161; PubMed=18187866 [NCBI, ExPASy, EBI, Israel, Japan]
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Anal. Sci. 24:161-166(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[11]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[12]
STRUCTURE BY NMR OF 11-100.
DOI=10.1073/pnas.111145098; PubMed=11371636 [NCBI, ExPASy, EBI, Israel, Japan]
Zhou P., Lugovskoy A.A., McCarty J.S., Li P., Wagner G.;
"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. 98:6051-6055(2001).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U91985; AAC51249.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF087573; AAD32953.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF103799; AAF02419.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT006980; AAP35626.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC000037; AAH00037.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC007112; AAH07112.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC007721; AAH07721.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00010882; -.
IPI00604566; -.
RefSeq NP_004392.1; -.
NP_998731.1; -.
UniGene Hs.149983
3D structure databases
PDB
1IBX; NMR; -; B=11-100.[ExPASy / RCSB / EBI]
1IYR; NMR; -; A=225-331.[ExPASy / RCSB / EBI]
1KOY; NMR; -; A=239-300.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1IBX; -.
1IYR; -.
1KOY; -.
SMR O00273; 12-100.
DisProt DP00173; -.
ModBase O00273.
Protein-protein interaction databases
IntAct O00273; 19.
PTM databases
PhosphoSite O00273; -.
Enzyme and pathway databases
Pathway_Interaction_DB caspase_pathway; Caspase cascade in apoptosis.
faspathway; FAS signaling pathway (CD95).
hivnefpathway; HIV-1 Nef: Negative effector of Fas and TNF-alpha.
Reactome REACT_578; Apoptosis.
Organism-specific databases
GeneCards GC01M010454; -.
H-InvDB HIX0000115; -.
HGNC HGNC:2772; DFFA.
GenAtlas DFFA.
HPA CAB002679; -.
MIM 601882; gene. [NCBI / EBI]
PharmGKB PA27254; -.
Gene expression databases
ArrayExpress O00273; -.
Bgee O00273; -.
CleanEx HS_DFFA; -.
GermOnline ENSG00000160049; Homo sapiens.
Ontologies
GO
GO:0005829; Cellular component: cytosol (traceable author statement from ProtInc).
GO:0005654; Cellular component: nucleoplasm (inferred from experiment from Reactome).
GO:0004537; Molecular function: caspase-activated deoxyribonuclease activity (traceable author statement from ProtInc).
GO:0042802; Molecular function: identical protein binding (inferred from physical interaction from IntAct).
GO:0006309; Biological process: DNA fragmentation involved in apoptosis (inferred from direct assay from MGI).
GO:0007242; Biological process: intracellular signaling cascade (traceable author statement from ProtInc).
GO:0043066; Biological process: negative regulation of apoptosis (inferred from direct assay from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR003508; CAD.
IPR015121; DNA_fragmentation_C.
IPR017299; DNA_fragmentation_factor_asu.
Graphical view of domain structure.
Pfam PF02017; CIDE-N; 1.
PF09033; DFF-C; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF037865; DFF_alpha; 1.
SMART SM00266; CAD; 1.
SMART graphical view of domain structure.
PROSITE PS51135; CIDE_N; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PeptideAtlas O00273; -.
PRIDE O00273; -.
Genome annotation databases
Ensembl ENSG00000160049; Homo sapiens. [Contig view]
GeneID 1676; -.
KEGG hsa:1676; -.
Phylogenomic databases
HOGENOM O00273; -.
HOVERGEN O00273; -.
OMA O00273; DGGTAWI.
Other
NextBio 6896; -.
PMAP-CutDB O00273; -.
SOURCE DFFA; Homo sapiens.
ProtoNet O00273.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Apoptosis; Cytoplasm; Direct protein sequencing; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   331  331     DNA fragmentation factor subunit alpha. PRO_0000144716
DOMAIN   17    96  80     CIDE-N. 
SITE   117   118  2     Cleavage; by caspase-3. 
SITE   224   225  2     Cleavage; by caspase-3. 
MOD_RES   257   257        Phosphoserine. 
MOD_RES   310   310        Phosphoserine. 
MOD_RES   315   315        Phosphoserine. 
VAR_SEQ   262   268        LVTKEDP -> VGGNQGH (in isoform DFF35). VSP_001085
VAR_SEQ   269   331        Missing (in isoform DFF35). VSP_001086
CONFLICT   291   291        R -> W (in Ref. 5; AAH07721). 
HELIX   239   246  8      
TURN   251   254  4      
HELIX   257   264  8      
HELIX   268   274  7      
HELIX   279   297  19      
HELIX   298   300  3      
Sequence information
Length: 331 AA [This is the length of the unprocessed precursor] Molecular weight: 36522 Da [This is the MW of the unprocessed precursor] CRC64: 8656FE45DB003DF3 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MEVTGDAGVP ESGEIRTLKP CLLRRNYSRE QHGVAASCLE DLRSKACDIL AIDKSLTPVT 

        70         80         90        100        110        120 
LVLAEDGTIV DDDDYFLCLP SNTKFVALAS NEKWAYNNSD GGTAWISQES FDVDETDSGA 

       130        140        150        160        170        180 
GLKWKNVARQ LKEDLSSIIL LSEEDLQMLV DAPCSDLAQE LRQSCATVQR LQHTLQQVLD 

       190        200        210        220        230        240 
QREEVRQSKQ LLQLYLQALE KEGSLLSKQE ESKAAFGEEV DAVDTGISRE TSSDVALASH 

       250        260        270        280        290        300 
ILTALREKQA PELSLSSQDL ELVTKEDPKA LAVALNWDIK KTETVQEACE RELALRLQQT 

       310        320        330 
QSLHSLRSIS ASKASPPGDL QNPKRARQDP T 

O00273 in FASTA format

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