P43351 (RAD52_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 116.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: DNA repair protein RAD52 homolog | ||
| Gene names |
| ||
| Organism | Homo sapiens (Human) [Reference proteome] | ||
| Taxonomic identifier | 9606 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo![]() |
Protein attributes
| Sequence length | 418 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| 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. Ref.5 |
| Subunit structure | Forms a undecameric ring. Interacts with ABL1. Ref.5 |
| Subcellular location | Nucleus Potential. |
| Post-translational modification | Phosphorylated upon DNA damage by ABL1, and probably by ATM or ATR. Ref.5 |
| Sequence similarities | Belongs to the RAD52 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | DNA damage DNA recombination DNA repair |
| Cellular component | Nucleus |
| Coding sequence diversity | Polymorphism |
| PTM | Phosphoprotein |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | DNA recombinase assembly Traceable author statement. Source: Reactome mitotic recombinationTraceable author statement Ref.1. Source: ProtInc reciprocal meiotic recombinationTraceable author statement Ref.1. Source: ProtInc |
| Cellular_component | nucleoplasm Traceable author statement. Source: Reactome |
| Molecular_function | DNA binding Traceable author statement Ref.1. Source: ProtInc |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| RAD51 | Q06609 | 3 | EBI-706448,EBI-297202 | |
| RPA3 | P35244 | 2 | EBI-706448,EBI-621428 | |
| WRN | Q14191 | 9 | EBI-706448,EBI-368417 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 418 | 418 | DNA repair protein RAD52 homolog | PRO_0000173881 | |||||||||||||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||||||||||||||
| Modified residue | 104 | 1 | Phosphotyrosine; by ABL1 Ref.5 | ||||||||||||||||||||||||||||||||||||
| Modified residue | 199 | 1 | Phosphoserine Ref.7 | ||||||||||||||||||||||||||||||||||||
| Modified residue | 318 | 1 | Phosphothreonine Ref.6 | ||||||||||||||||||||||||||||||||||||
| Modified residue | 335 | 1 | Phosphothreonine Ref.7 | ||||||||||||||||||||||||||||||||||||
Natural variations | |||||||||||||||||||||||||||||||||||||||
| Natural variant | 70 | 1 | R → W. Ref.4 Corresponds to variant rs11571421 [ dbSNP | Ensembl ]. | VAR_019218 | |||||||||||||||||||||||||||||||||||
| Natural variant | 221 | 1 | Q → E. Ref.4 Corresponds to variant rs4987206 [ dbSNP | Ensembl ]. | VAR_019219 | |||||||||||||||||||||||||||||||||||
| Natural variant | 287 | 1 | S → N. Ref.4 Corresponds to variant rs11571463 [ dbSNP | Ensembl ]. | VAR_019220 | |||||||||||||||||||||||||||||||||||
Experimental info | |||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 100 | 1 | N → K in AAA87554. Ref.3 | ||||||||||||||||||||||||||||||||||||
| Sequence conflict | 418 | 1 | S → SY in AAA87554. Ref.3 | ||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||
| Turn | 26 – 28 | 3 | |||||||||||||||||||||||||||||||||||||
| Helix | 33 – 44 | 12 | |||||||||||||||||||||||||||||||||||||
| Turn | 49 – 51 | 3 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 52 – 56 | 5 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 58 – 60 | 3 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 62 – 66 | 5 | |||||||||||||||||||||||||||||||||||||
| Helix | 68 – 79 | 12 | |||||||||||||||||||||||||||||||||||||
| Turn | 81 – 83 | 3 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 84 – 115 | 32 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 120 – 133 | 14 | |||||||||||||||||||||||||||||||||||||
| Helix | 135 – 156 | 22 | |||||||||||||||||||||||||||||||||||||
| Helix | 160 – 162 | 3 | |||||||||||||||||||||||||||||||||||||
| Helix | 165 – 167 | 3 | |||||||||||||||||||||||||||||||||||||
| Helix | 169 – 176 | 8 | |||||||||||||||||||||||||||||||||||||
| Helix | 188 – 190 | 3 | |||||||||||||||||||||||||||||||||||||
| Helix | 198 – 205 | 8 | |||||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "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 J.M., Chen D.J. Genomics 25:199-206(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [2] | "Cloning of human and mouse genes homologous to RAD52, a yeast gene involved in DNA repair and recombination." Muris D.F., Bezzubova O., Buerstedde J.-M., Vreeken K., Balajee A.S., Osgood C.J., Troelstra C., Hoeijmakers J.H., Ostermann K., Schmidt H., Natarajan A.T., Eeken J.C.J., Lohman P.H.M., Pastink A. Mutat. Res. 315:295-305(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Testis. |
| [3] | "Expression of human RAD52 confers resistance to ionizing radiation in mammalian cells." Park M.S. J. Biol. Chem. 270:15467-15470(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Spleen. |
| [4] | NIEHS SNPs program Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS TRP-70; GLU-221 AND ASN-287. |
| [5] | "Regulation of ionizing radiation-induced Rad52 nuclear foci formation by c-Abl-mediated phosphorylation." Kitao H., Yuan Z.M. J. Biol. Chem. 277:48944-48948(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH ABL1, PHOSPHORYLATION AT TYR-104. |
| [6] | "ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-318, MASS SPECTROMETRY. Tissue: Embryonic kidney. |
| [7] | "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199 AND THR-335, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [8] | "Structure of the single-strand annealing domain of human RAD52 protein." Singleton M.R., Wentzell L.M., Liu Y., West S.C., Wigley D.B. Proc. Natl. Acad. Sci. U.S.A. 99:13492-13497(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 24-209. |
| + | Additional computationally mapped references. |
Web resources
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | U12134 mRNA. Translation: AAA85793.1. L33262 mRNA. Translation: AAB05203.1. U27516 mRNA. Translation: AAA87554.1. AY527412 Genomic DNA. Translation: AAS00097.1. | ||||||||||||||||||
| IPI | IPI00301078. | ||||||||||||||||||
| PIR | A57518. | ||||||||||||||||||
| RefSeq | NP_602296.2. NM_134424.2. | ||||||||||||||||||
| UniGene | Hs.410355. | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
| PDBe RCSB PDB PDBj |
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| DisProt | DP00437. | ||||||||||||||||||
| ProteinModelPortal | P43351. | ||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||
| DIP | DIP-333N. | ||||||||||||||||||
| IntAct | P43351. 28 interactions. | ||||||||||||||||||
| MINT | MINT-2803258. | ||||||||||||||||||
| STRING | 9606.ENSP00000351284. | ||||||||||||||||||
PTM databases | |||||||||||||||||||
| PhosphoSite | P43351. | ||||||||||||||||||
Polymorphism databases | |||||||||||||||||||
| DMDM | 1172823. | ||||||||||||||||||
Proteomic databases | |||||||||||||||||||
| PaxDb | P43351. | ||||||||||||||||||
| PRIDE | P43351. | ||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||
| DNASU | 5893. | ||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||
Genome annotation databases | |||||||||||||||||||
| Ensembl | ENST00000358495; ENSP00000351284; ENSG00000002016. ENST00000430095; ENSP00000387901; ENSG00000002016. | ||||||||||||||||||
| GeneID | 5893. | ||||||||||||||||||
| KEGG | hsa:5893. | ||||||||||||||||||
| UCSC | uc001qis.1. human. | ||||||||||||||||||
Organism-specific databases | |||||||||||||||||||
| CTD | 5893. | ||||||||||||||||||
| GeneCards | GC12M001021. | ||||||||||||||||||
| HGNC | HGNC:9824. RAD52. | ||||||||||||||||||
| MIM | 600392. gene. | ||||||||||||||||||
| neXtProt | NX_P43351. | ||||||||||||||||||
| PharmGKB | PA34180. | ||||||||||||||||||
| GenAtlas | Search... | ||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||
| eggNOG | COG5055. | ||||||||||||||||||
| HOGENOM | HOG000237354. | ||||||||||||||||||
| HOVERGEN | HBG054676. | ||||||||||||||||||
| InParanoid | P43351. | ||||||||||||||||||
| KO | K10873. | ||||||||||||||||||
| OMA | RKSQDMK. | ||||||||||||||||||
| OrthoDB | EOG451DR1. | ||||||||||||||||||
| PhylomeDB | P43351. | ||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||
| Reactome | REACT_216. DNA Repair. | ||||||||||||||||||
Gene expression databases | |||||||||||||||||||
| ArrayExpress | P43351. | ||||||||||||||||||
| Bgee | P43351. | ||||||||||||||||||
| CleanEx | HS_RAD52. | ||||||||||||||||||
| Genevestigator | P43351. | ||||||||||||||||||
| GermOnline | ENSG00000002016. Homo sapiens. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| InterPro | IPR004585. DNA_recomb/repair_Rad52. IPR007232. Rad52_Rad22. [Graphical view] | ||||||||||||||||||
| PANTHER | PTHR12132. PTHR12132. 1 hit. | ||||||||||||||||||
| Pfam | PF04098. Rad52_Rad22. 1 hit. [Graphical view] | ||||||||||||||||||
| TIGRFAMs | TIGR00607. rad52. 1 hit. | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Other | |||||||||||||||||||
| ChiTaRS | RAD52. human. | ||||||||||||||||||
| EvolutionaryTrace | P43351. | ||||||||||||||||||
| GenomeRNAi | 5893. | ||||||||||||||||||
| NextBio | 22926. | ||||||||||||||||||
| SOURCE | Search... | ||||||||||||||||||
Entry information
| Entry name | RAD52_HUMAN | ||||||||
| Accession | Primary (citable) accession number: P43351 Secondary accession number(s): Q13205 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | ||||||||
Relevant documents
| Human chromosome 12 Human chromosome 12: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
