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RAD52

Protein FULL name:

RAD52 homolog isoform alpha [Homo sapiens].


RAD52 (Homo sapiens) is product of expression of RAD52 gene.


RAD52 is involved in:

HRR in Homo sapiens

Keywords:



FUNCTION: 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.

SUBUNIT: Forms a undecameric ring.

INTERACTION: Q14191:WRN; NbExp=4; IntAct=EBI-706448, EBI-368417;

SUBCELLULAR LOCATION: Nucleus (Potential).

PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.

SIMILARITY: Belongs to the RAD52 family.

WEB RESOURCE: Name=NIEHS-SNPs; [LINK]


NCBI GenPept GI number(s): 20143952
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot P43351 P43351
PFAM: - P43351 (Link - using uniprot id)
InterPro: - P43351 (Link - using uniprot id)
CATH: - -
SCOP: - -
PDB: - -


Protein sequence:
MSGTEEAILGGRDSHPAAGGGSVLCFGQCQYTAEEYQAIQKALRQRLGPE
YISSRMAGGGQKVCYIEGHRVINLANEMFGYNGWAHSITQQNVDFVDLNN
GKFYVGVCAFVRVQLKDGSYHEDVGYGVSEGLKSKALSLEKARKEAVTDG
LKRALRSFGNALGNCILDKDYLRSLNKLPRQLPLEVDLTKAKRQDLEPSV
EEARYNSCRPNMALGHPQLQQVTSPSRPSHAVIPADQDCSSRSLSSSAVE
SEATHQRKLRQKQLQQQFRERMEKQQVRVSTPSAEKSEAAPPAPPVTHST
PVTVSEPLLEKDFLAGVTQELIKTLEDNSEKWAVTPDAGDGVVKPSSRAD
PAQTSDTLALNNQMVTQNRTPHSVCHQKPQAKSGSWDLQTYSADQRTTGN
WESHRKSQDMKKRKYDPSY

RAD52 (Homo sapiens) is able to recognize following damages:
References:

Title Authors Journal
Cloning of human and mouse genes homologous to RAD52, a yeast gene involved in DNA repair and recombination. Muris DF, Bezzubova O, Buerstedde JM, Vreeken K, Balajee AS, Osgood CJ, Troelstra C, Hoeijmakers JH, Ostermann K, Schmidt H, et al. Mutat Res Nov. 1, 1994
The human and mouse homologs of the yeast RAD52 gene: cDNA cloning, sequence analysis, assignment to human chromosome 12p12.2-p13, and mRNA expression in mouse tissues. Shen Z, Denison K, Lobb R, Gatewood JM, Chen DJ Genomics Feb. 1, 1995
Expression of human RAD52 confers resistance to ionizing radiation in mammalian cells. Park MS J Biol Chem June 1, 1995
Structure of the single-strand annealing domain of human RAD52 protein. Singleton MR, Wentzell LM, Liu Y, West SC, Wigley DB Proc Natl Acad Sci U S A Oct. 15, 2002
ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ Science May 25, 2007
Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M Mol Cell Aug. 8, 2008


Last modification of this entry: Oct. 21, 2010.

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