DP00152: DNA repair protein XRCC4FASTA viewXML view

General information
DisProt:DP00152
Name:DNA repair protein XRCC4
Synonym(s):XRCC4_HUMAN
X-ray repair cross-complementing protein 4
First appeared in release:Release 2.0 (02/14/2005)
UniProt:Q13426
UniGene:Hs.567359
SwissProt: XRCC4_HUMAN
TrEMBL:  
NCBI (GI): 44888352
Source organism:Homo sapiens (Human)
Sequence length:336
Percent disordered:28%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MERKISRIHL VSEPSITHFL QVSWEKTLES GFVITLTDGH SAWTGTVSES EISQEADDMA - 60
MEKGKYVGEL RKALLSGAGP ADVYTFNFSK ESCYFFFEKN LKDVSFRLGS FNLEKVENPA - 120
EVIRELICYC LDTIAENQAK NEHLQKENER LLRDWNDVQG RFEKCVSAKE ALETDLYKRF - 180
ILVLNEKKTK IRSLHNKLLN AAQEREKDIK QEGETAICSE MTADRDPVYD ESTDEESENQ - 240
TDLSGLASAA VSKDDSIISS LDVTDIAPSR KRRQRMQRNL GTEPKMAPQE NQLQEKENSR - 300
PDSSLPETSK KEHISAENMS LETLRNSSPE DLFDEI



Functional narrative    

The DNA repair protein XRCC4 is an important protein in the repair of double strand breaks of DNA. It fixes the damaged DNA by performing nonhomologous end joining (NHEJ). Lack of XRCC4 all but eliminates this function. Although capable of functioning independently, it often interacts with DNA ligase IV and stabilizes the resulting complex. It further stabilizes the assembly of other complexes necessary for NHEJ.

Region 2: 77-80 Region 3: 77-82 Region 6: 179-203 Region 4: 202-213 Region 1: 212-213 Region 5: 204-265

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:212 - 213
Length:2
Region sequence:

EG

Modification type: Engineered
Fragment
PDB: 1IK9:A
Structural/functional type: Relationship to function unknown
Functional classes: Molecular assembly
Functional subclasses: Protein-DNA binding
Detection methods:
  1. X-ray crystallography (pH: 6; 2-(N-morpholino)ethanesulfonic acid 0.1 M; NaCl (buffer) 150 mM; PEG 6000 ((w/v)) 3 %; protein 100 uM; Tris-HCl (pH 8.0) 20 mM; xylitol (precipitant solution (w/v)) 3 %)

References:
  1. Sibanda BL, Critchlow SE, Begun J, Pei XY, Jackson SP, Blundell TL, Pellegrini L. "Crystal structure of an Xrcc4-DNA ligase IV complex." Nat Struct Biol. 2001; 8(12): 1015-9. PubMed: 11702069

Comments:
The experiments were conducted using a fragment of Xrcc4 spanning residues 1 - 213.




Region 2
Type:Disordered
Name: 
Location:77 - 80
Length:4
Region sequence:

GAGP

Modification type: Engineered
Fragment
PDB: 1IK9:A
Structural/functional type: Relationship to function unknown
Functional classes: Unknown
Functional subclasses: Unknown
Detection methods:
  1. X-ray crystallography (pH: 6; 2-(N-morpholino)ethanesulfonic acid 0.1 M; NaCl (buffer) 150 mM; PEG 6000 ((w/v)) 3 %; protein 100 uM; Tris-HCl (pH 8.0) 20 mM; xylitol (precipitant solution (w/v)) 3 %)

References:
  1. Sibanda BL, Critchlow SE, Begun J, Pei XY, Jackson SP, Blundell TL, Pellegrini L. "Crystal structure of an Xrcc4-DNA ligase IV complex." Nat Struct Biol. 2001; 8(12): 1015-9. PubMed: 11702069

Comments:
The experiments were conducted using a fragment of Xrcc4 spanning residues 1 - 213.




Region 3
Type:Disordered
Name: 
Location:77 - 82
Length:6
Region sequence:

GAGPAD

Modification type: Engineered
Fragment
PDB: 1IK9:B
Structural/functional type: Relationship to function unknown
Functional classes: Unknown
Functional subclasses: Unknown
Detection methods:
  1. X-ray crystallography (pH: 6; 2-(N-morpholino)ethanesulfonic acid 0.1 M; NaCl (buffer) 150 mM; PEG 6000 ((w/v)) 3 %; protein 100 uM; Tris-HCl (pH 8.0) 20 mM; xylitol (precipitant solution (w/v)) 3 %)

References:
  1. Sibanda BL, Critchlow SE, Begun J, Pei XY, Jackson SP, Blundell TL, Pellegrini L. "Crystal structure of an Xrcc4-DNA ligase IV complex." Nat Struct Biol. 2001; 8(12): 1015-9. PubMed: 11702069

Comments:
The experiments were conducted using a fragment of Xrcc4 spanning residues 1 - 213.




Region 4
Type:Disordered
Name: 
Location:202 - 213
Length:12
Region sequence:

AQEREKDIKQEG

Modification type: Engineered
Fragment
PDB: 1IK9:B
Structural/functional type: Relationship to function unknown
Functional classes: Molecular assembly
Functional subclasses: Protein-DNA binding
Detection methods:
  1. X-ray crystallography (pH: 6; 2-(N-morpholino)ethanesulfonic acid 0.1 M; NaCl (buffer) 150 mM; PEG 6000 ((w/v)) 3 %; protein 100 uM; Tris-HCl (pH 8.0) 20 mM; xylitol (precipitant solution (w/v)) 3 %)

References:
  1. Sibanda BL, Critchlow SE, Begun J, Pei XY, Jackson SP, Blundell TL, Pellegrini L. "Crystal structure of an Xrcc4-DNA ligase IV complex." Nat Struct Biol. 2001; 8(12): 1015-9. PubMed: 11702069

Comments:
The experiments were conducted using a fragment of Xrcc4 spanning residues 1 - 213.




Region 5
Type:Disordered
Name: 
Location:204 - 265
Length:62
Region sequence:

EREKDIKQEGETAICSEMTADRDPVYDESTDEESENQTDLSGLASAAVSKDDSIISSLDV
TD

Modification type: Fragment
PDB: 1FU1:A
Structural/functional type: Relationship to function unknown
Functional classes: Unknown
Functional subclasses: Unknown
Detection methods:
  1. X-ray crystallography (293 K; pH: 6.5; ammonium sulfate (well solution) 1.2 M; DTT (well solution) 10 mM; magnesium acetate (well solution) 10 mM; protein (per mL) 8 mg; sodium cacodylate (well solution) 100 mM)

References:
  1. Junop MS, Modesti M, Guarne A, Ghirlando R, Gellert M, Yang W. "Crystal structure of the Xrcc4 DNA repair protein and implications for end joining." Embo J. 2000; 19(22): 5962-70. PubMed: 11080143

Comments:
The experiments were conducted using a fragment of Xrcc4 spanning residues 1 - 265.




Region 6
Type:Disordered - Extended
Name: 
Location:179 - 203
Length:25
Region sequence:

RFILVLNEKKTKIRSLHNKLLNAAQ

Modification type: Fragment
PDB: 1FU1:A
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Molecular assembly
Functional subclasses: Protein-DNA binding
Detection methods:
  1. X-ray crystallography (293 K; pH: 6.5; ammonium sulfate (well solution) 1.2 M; DTT (well solution) 10 mM; magnesium acetate (well solution) 10 mM; protein (per mL) 8 mg; sodium cacodylate (well solution) 100 mM)

References:
  1. Junop MS, Modesti M, Guarne A, Ghirlando R, Gellert M, Yang W. "Crystal structure of the Xrcc4 DNA repair protein and implications for end joining." Embo J. 2000; 19(22): 5962-70. PubMed: 11080143

Comments:
This region is disordered in the S subunit.


The experiments were conducted using a fragment of Xrcc4 spanning residues 1 - 213.




References

  1. Hsu HL, Yannone SM, Chen DJ. "Defining interactions between DNA-PK and ligase IV/XRCC4." DNA Repair (Amst). 2002; 1(3): 225-35. PubMed: 12509254

  2. Lee KJ, Jovanovic M, Udayakumar D, Bladen CL, Dynan WS. "Identification of DNA-PKcs phosphorylation sites in XRCC4 and effects of mutations at these sites on DNA end joining in a cell-free system." DNA Repair (Amst). 2004; 3(3): 267-76. PubMed: 15177042

  3. Modesti M, Junop MS, Ghirlando R, van de Rakt M, Gellert M, Yang W, Kanaar R. "Tetramerization and DNA ligase IV interaction of the DNA double-strand break repair protein XRCC4 are mutually exclusive." J Mol Biol. 2003; 334(2): 215-28. PubMed: 14607114


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