| General information | | DisProt: | DP00437 | | Name: | DNA repair protein RAD52 homolog | | Synonym(s): | RAD52_HUMAN
| | First appeared in release: | Release 3.1 (03/31/2006) | | UniProt: | P43351 | | UniGene: | | | SwissProt: | RAD52_HUMAN | | TrEMBL: | | | NCBI (GI): | 1172823 | | Source organism: | Homo sapiens (Human) | | Sequence length: | 418 | | Percent disordered: | 6% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MSGTEEAILG GRDSHPAAGG GSVLCFGQCQ YTAEEYQAIQ KALRQRLGPE YISSRMAGGG - 60
QKVCYIEGHR VINLANEMFG YNGWAHSITQ QNVDFVDLNN GKFYVGVCAF VRVQLKDGSY - 120
HEDVGYGVSE GLKSKALSLE KARKEAVTDG LKRALRSFGN ALGNCILDKD YLRSLNKLPR - 180
QLPLEVDLTK AKRQDLEPSV EEARYNSCRP NMALGHPQLQ QVTSPSRPSH AVIPADQDCS - 240
SRSLSSSAVE SEATHQRKLR QKQLQQQFRE RMEKQQVRVS TPSAEKSEAA PPAPPVTHST - 300
PVTVSEPLLE KDFLAGVTQE LIKTLEDNSE KWAVTPDAGD GVVKPSSRAD PAQTSDTLAL - 360
NNQMVTQNRT PHSVCHQKPQ AKSGSWDLQT YSADQRTTGN WESHRKSQDM KKRKYDPS
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| Functional narrative |
Involved in double-stranded break repair. Plays a central role in genetic recombination and DNA repair by promoting the annealing of complementary single-stranded DNA and by stimulation of the RAD51 recombinase.
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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 - 23 | | Length: | 23 | | Region sequence: |
MSGTEEAILGGRDSHPAAGGGSV | | Modification type: | Fragment
| | PDB: | | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Unknown
| | Functional subclasses: | Protein-DNA binding
| Detection methods:
- X-ray crystallography (ethanol (pH 8, 4-14% (vol/vol)); Tris HCl 100 mM)
| References:
- Singleton MR, Wentzell LM, Liu Y, West SC, Wigley DB. "Structure of the single-strand annealing domain of human RAD52 protein." Proc Natl Acad Sci U S A. 2002; 99(21): 13492-7. PubMed: 12370410
| Comments:
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| References |
- Park MS. "Expression of human RAD52 confers resistance to ionizing radiation in mammalian cells." J Biol Chem. 1995; 270(26): 15467-70. PubMed: 7797537
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| Comments |
The N-terminal region of the protein (residues 1-209) was analyzed in the experiment and was shown to promote in vitro ssDNA annealing as efficiently as the full-size RAD52 (residues 1-418) protein.
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