General information | DisProt: | DP00173 | Name: | DNA fragmentation factor subunit alpha [Isoform DFF45] | Synonym(s): | DFFA_HUMAN
DNA fragmentation factor 45 kDa subunit
DFF-45
Inhibitor of CAD
ICAD
| First appeared in release: | Release 2.0 (02/14/2005) | UniProt: | O00273-1 | UniGene: | Hs.484782 | SwissProt: | DFFA_HUMAN | TrEMBL: | | NCBI (GI): | 2810997 | Source organism: | Homo sapiens (Human) | Sequence length: | 331 | Percent disordered: | 35% | Homologues: | |
Native sequence |
10 20 30 40 50 60 | | | | | | MEVTGDAGVP ESGEIRTLKP CLLRRNYSRE QHGVAASCLE DLRSKACDIL AIDKSLTPVT - 60 LVLAEDGTIV DDDDYFLCLP SNTKFVALAS NEKWAYNNSD GGTAWISQES FDVDETDSGA - 120 GLKWKNVARQ LKEDLSSIIL LSEEDLQMLV DAPCSDLAQE LRQSCATVQR LQHTLQQVLD - 180 QREEVRQSKQ LLQLYLQALE KEGSLLSKQE ESKAAFGEEV DAVDTGISRE TSSDVALASH - 240 ILTALREKQA PELSLSSQDL ELVTKEDPKA LAVALNWDIK KTETVQEACE RELALRLQQT - 300 QSLHSLRSIS ASKASPPGDL QNPKRARQDP T
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Functional narrative |
Located in the cytoplasm and a member of the CIDE family of proteins, malfunctions or mutations in DNA defragmentation factor alpha subunit (DFF45) are associated with various forms of cancer and other degenerative disorders. DFF45 forms a heterodimeric complex with DFF40 and thus inhibits DFF45 activity. DFF45 is cut into 3 fragments by capases and released from DFF40, thus activating DFF40 for apoptosis-related DNA fragmentation. The N-terminal domain fragment of DFF45, (amino acids 1-116), is fully capable of hindering the nuclease activity of DFF40. In addition, high levels of DFF45 increase the threshold for downstream signaling in apoptosis.
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Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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Region 1 | Type: | Disordered | Name: | | Location: | 1 - 116 | Length: | 116 | Region sequence: |
MEVTGDAGVPESGEIRTLKPCLLRRNYSREQHGVAASCLEDLRSKACDILAIDKSLTPVT LVLAEDGTIVDDDDYFLCLPSNTKFVALASNEKWAYNNSDGGTAWISQESFDVDET | Modification type: | Fragment
| PDB: | | Structural/functional type: | Function arises via a disorder to order transition | Functional classes: | Molecular assembly
| Functional subclasses: | Protein-protein binding
| Detection methods:
- Circular dichroism (CD) spectroscopy, near-UV (pH: 6; phosphate (buffer) 20 mM; sodium chloride 50 mM)
- Nuclear magnetic resonance (NMR) (296 K; pH: 6; DTT 5 mM; phosphate (buffer) 20 mM; sodium chloride (in D2O ( 1 vol/vol)) 50 mM; sodium chloride (in water (9 vol/vol)) 50 mM)
| References:
- Zhou P, Lugovskoy AA, McCarty JS, 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. 2001; 98(11): 6051-6055. PubMed: 11371636
| Comments:This fragment is disordered in solution and becomes ordered when it interacts with DFF40.
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