Annotations for this protein have been verified by the authors of the corresponding papers



DP00173: DNA fragmentation factor subunit alpha [Isoform DFF45]FASTA viewXML view

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



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.

Region 1: 1-116

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.


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:
  1. Circular dichroism (CD) spectroscopy, near-UV (pH: 6; phosphate (buffer) 20 mM; sodium chloride 50 mM)

  2. 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:
  1. 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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