DFFA_HUMAN
ID DFFA_HUMAN Reviewed; 331 AA.
AC O00273; Q5T6G5; Q5T6G6; Q96I97; Q9Y6C6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 215.
DE RecName: Full=DNA fragmentation factor subunit alpha;
DE AltName: Full=DNA fragmentation factor 45 kDa subunit;
DE Short=DFF-45;
DE AltName: Full=Inhibitor of CAD;
DE Short=ICAD;
GN Name=DFFA; Synonyms=DFF1, DFF45; ORFNames=H13;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DFF45), AND PROTEIN SEQUENCE OF
RP 171-181; 190-201; 214-218 AND 230-242.
RX PubMed=9108473; DOI=10.1016/s0092-8674(00)80197-x;
RA Liu X., Zou H., Slaughter C., Wang X.;
RT "DFF, a heterodimeric protein that functions downstream of caspase-3 to
RT trigger DNA fragmentation during apoptosis.";
RL Cell 89:175-184(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DFF35).
RX PubMed=10409614; DOI=10.1074/jbc.274.30.20759;
RA Gu J.J., Dong R.P., Zhang C., McLaughlin D.F., Wu M.X., Schlossman S.F.;
RT "Functional interaction of DFF35 and DFF45 with caspase-activated DNA
RT fragmentation nuclease DFF40.";
RL J. Biol. Chem. 274:20759-20762(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DFF35).
RX PubMed=10497265; DOI=10.1093/nar/27.20.4008;
RA Oh J.J., Grosshans D.R., Wong S.G., Slamon D.J.;
RT "Identification of differentially expressed genes associated with HER-2/neu
RT overexpression in human breast cancer cells.";
RL Nucleic Acids Res. 27:4008-4017(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM DFF45).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM DFF45).
RC TISSUE=Mammary gland;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM DFF45).
RC TISSUE=Eye, Kidney, and Skeletal muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PROTEIN SEQUENCE OF 1-16; 171-182; 190-201; 214-246; 249-269 AND 297-307,
RP ACETYLATION AT MET-1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V.;
RL Submitted (JAN-2010) to UniProtKB.
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-243 AND SER-315, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [21]
RP STRUCTURE BY NMR OF 11-100, AND SUBUNIT.
RX PubMed=11371636; DOI=10.1073/pnas.111145098;
RA Zhou P., Lugovskoy A.A., McCarty J.S., Li P., Wagner G.;
RT "Solution structure of DFF40 and DFF45 N-terminal domain complex and mutual
RT chaperone activity of DFF40 and DFF45.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:6051-6055(2001).
CC -!- FUNCTION: Inhibitor of the caspase-activated DNase (DFF40).
CC -!- SUBUNIT: Heterodimer of DFFA and DFFB. {ECO:0000269|PubMed:11371636}.
CC -!- INTERACTION:
CC O00273; O76075: DFFB; NbExp=5; IntAct=EBI-727171, EBI-1053821;
CC O00273; P04792: HSPB1; NbExp=2; IntAct=EBI-727171, EBI-352682;
CC O00273; O54788: Dffb; Xeno; NbExp=8; IntAct=EBI-727171, EBI-7365197;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=DFF45;
CC IsoId=O00273-1; Sequence=Displayed;
CC Name=DFF35;
CC IsoId=O00273-2; Sequence=VSP_001085, VSP_001086;
CC -!- PTM: Caspase-3 cleaves DFF45 at 2 sites to generate an active factor.
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DR EMBL; U91985; AAC51249.1; -; mRNA.
DR EMBL; AF087573; AAD32953.1; -; mRNA.
DR EMBL; AF103799; AAF02419.1; -; mRNA.
DR EMBL; BT006980; AAP35626.1; -; mRNA.
DR EMBL; AK313317; BAG36122.1; -; mRNA.
DR EMBL; AL354956; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471130; EAW71656.1; -; Genomic_DNA.
DR EMBL; CH471130; EAW71657.1; -; Genomic_DNA.
DR EMBL; BC000037; AAH00037.1; -; mRNA.
DR EMBL; BC007112; AAH07112.1; -; mRNA.
DR EMBL; BC007721; AAH07721.1; -; mRNA.
DR CCDS; CCDS118.1; -. [O00273-1]
DR CCDS; CCDS119.1; -. [O00273-2]
DR RefSeq; NP_004392.1; NM_004401.2. [O00273-1]
DR RefSeq; NP_998731.1; NM_213566.1. [O00273-2]
DR PDB; 1IBX; NMR; -; B=11-100.
DR PDB; 1IYR; NMR; -; A=225-331.
DR PDB; 1KOY; NMR; -; A=239-300.
DR PDBsum; 1IBX; -.
DR PDBsum; 1IYR; -.
DR PDBsum; 1KOY; -.
DR AlphaFoldDB; O00273; -.
DR BMRB; O00273; -.
DR SMR; O00273; -.
DR BioGRID; 108040; 50.
DR ComplexPortal; CPX-2498; DNA fragmentation factor complex.
DR IntAct; O00273; 14.
DR MINT; O00273; -.
DR STRING; 9606.ENSP00000366237; -.
DR GlyGen; O00273; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O00273; -.
DR PhosphoSitePlus; O00273; -.
DR BioMuta; DFFA; -.
DR EPD; O00273; -.
DR jPOST; O00273; -.
DR MassIVE; O00273; -.
DR MaxQB; O00273; -.
DR PaxDb; O00273; -.
DR PeptideAtlas; O00273; -.
DR PRIDE; O00273; -.
DR ProteomicsDB; 47820; -. [O00273-1]
DR ProteomicsDB; 47821; -. [O00273-2]
DR Antibodypedia; 3633; 854 antibodies from 46 providers.
DR DNASU; 1676; -.
DR Ensembl; ENST00000377036.2; ENSP00000366235.2; ENSG00000160049.12. [O00273-2]
DR Ensembl; ENST00000377038.8; ENSP00000366237.3; ENSG00000160049.12. [O00273-1]
DR GeneID; 1676; -.
DR KEGG; hsa:1676; -.
DR MANE-Select; ENST00000377038.8; ENSP00000366237.3; NM_004401.3; NP_004392.1.
DR UCSC; uc001arj.4; human. [O00273-1]
DR CTD; 1676; -.
DR DisGeNET; 1676; -.
DR GeneCards; DFFA; -.
DR HGNC; HGNC:2772; DFFA.
DR HPA; ENSG00000160049; Low tissue specificity.
DR MIM; 601882; gene.
DR neXtProt; NX_O00273; -.
DR OpenTargets; ENSG00000160049; -.
DR PharmGKB; PA27254; -.
DR VEuPathDB; HostDB:ENSG00000160049; -.
DR eggNOG; ENOG502RQ19; Eukaryota.
DR GeneTree; ENSGT00390000018596; -.
DR HOGENOM; CLU_086234_0_0_1; -.
DR InParanoid; O00273; -.
DR OMA; WMARESV; -.
DR OrthoDB; 1564672at2759; -.
DR PhylomeDB; O00273; -.
DR TreeFam; TF102021; -.
DR PathwayCommons; O00273; -.
DR Reactome; R-HSA-140342; Apoptosis induced DNA fragmentation.
DR SignaLink; O00273; -.
DR SIGNOR; O00273; -.
DR BioGRID-ORCS; 1676; 14 hits in 1084 CRISPR screens.
DR ChiTaRS; DFFA; human.
DR EvolutionaryTrace; O00273; -.
DR GeneWiki; DFFA; -.
DR GenomeRNAi; 1676; -.
DR Pharos; O00273; Tbio.
DR PRO; PR:O00273; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O00273; protein.
DR Bgee; ENSG00000160049; Expressed in medial globus pallidus and 204 other tissues.
DR ExpressionAtlas; O00273; baseline and differential.
DR Genevisible; O00273; HS.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0032991; C:protein-containing complex; IDA:CAFA.
DR GO; GO:0060703; F:deoxyribonuclease inhibitor activity; IMP:CAFA.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0044183; F:protein folding chaperone; IPI:CAFA.
DR GO; GO:0006309; P:apoptotic DNA fragmentation; IEA:InterPro.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IMP:CAFA.
DR GO; GO:1902511; P:negative regulation of apoptotic DNA fragmentation; IDA:ComplexPortal.
DR GO; GO:0032076; P:negative regulation of deoxyribonuclease activity; IMP:CAFA.
DR GO; GO:1900118; P:negative regulation of execution phase of apoptosis; IDA:BHF-UCL.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0070242; P:thymocyte apoptotic process; IEA:Ensembl.
DR DisProt; DP00173; -.
DR InterPro; IPR003508; CIDE-N_dom.
DR InterPro; IPR027296; DFF-C.
DR InterPro; IPR017299; DFF45.
DR InterPro; IPR015121; DNA_fragmentation_mid_dom.
DR PANTHER; PTHR12306:SF16; PTHR12306:SF16; 1.
DR Pfam; PF02017; CIDE-N; 1.
DR Pfam; PF09033; DFF-C; 1.
DR PIRSF; PIRSF037865; DFF_alpha; 1.
DR SMART; SM00266; CAD; 1.
DR SUPFAM; SSF81783; SSF81783; 1.
DR PROSITE; PS51135; CIDE_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Apoptosis; Cytoplasm;
KW Direct protein sequencing; Phosphoprotein; Reference proteome.
FT CHAIN 1..331
FT /note="DNA fragmentation factor subunit alpha"
FT /id="PRO_0000144716"
FT DOMAIN 17..96
FT /note="CIDE-N"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00447"
FT REGION 305..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 117..118
FT /note="Cleavage; by caspase-3"
FT SITE 224..225
FT /note="Cleavage; by caspase-3"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|Ref.9, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 243
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 262..268
FT /note="LVTKEDP -> VGGNQGH (in isoform DFF35)"
FT /evidence="ECO:0000303|PubMed:10409614,
FT ECO:0000303|PubMed:10497265"
FT /id="VSP_001085"
FT VAR_SEQ 269..331
FT /note="Missing (in isoform DFF35)"
FT /evidence="ECO:0000303|PubMed:10409614,
FT ECO:0000303|PubMed:10497265"
FT /id="VSP_001086"
FT CONFLICT 291
FT /note="R -> W (in Ref. 8; AAH07721)"
FT /evidence="ECO:0000305"
FT HELIX 39..50
FT /evidence="ECO:0007829|PDB:1IBX"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:1IBX"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:1IBX"
FT HELIX 73..78
FT /evidence="ECO:0007829|PDB:1IBX"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:1IBX"
FT HELIX 239..246
FT /evidence="ECO:0007829|PDB:1IYR"
FT TURN 251..254
FT /evidence="ECO:0007829|PDB:1IYR"
FT HELIX 257..264
FT /evidence="ECO:0007829|PDB:1IYR"
FT HELIX 268..274
FT /evidence="ECO:0007829|PDB:1IYR"
FT HELIX 279..297
FT /evidence="ECO:0007829|PDB:1IYR"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:1IYR"
SQ SEQUENCE 331 AA; 36522 MW; 8656FE45DB003DF3 CRC64;
MEVTGDAGVP ESGEIRTLKP CLLRRNYSRE QHGVAASCLE DLRSKACDIL AIDKSLTPVT
LVLAEDGTIV DDDDYFLCLP SNTKFVALAS NEKWAYNNSD GGTAWISQES FDVDETDSGA
GLKWKNVARQ LKEDLSSIIL LSEEDLQMLV DAPCSDLAQE LRQSCATVQR LQHTLQQVLD
QREEVRQSKQ LLQLYLQALE KEGSLLSKQE ESKAAFGEEV DAVDTGISRE TSSDVALASH
ILTALREKQA PELSLSSQDL ELVTKEDPKA LAVALNWDIK KTETVQEACE RELALRLQQT
QSLHSLRSIS ASKASPPGDL QNPKRARQDP T
