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
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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.
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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: | 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:
- 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:
- 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.
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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:
- 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:
- 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.
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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:
- 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:
- 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.
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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:
- 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:
- 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.
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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:
- 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:
- 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.
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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:
- 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:
- 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.
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References |
- 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
- 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
- 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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