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Reviewed, UniProtKB/Swiss-Prot P43351 (RAD52_HUMAN)

Last modified November 25, 2008. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    DNA repair protein RAD52 homolog
Gene names
Name: RAD52
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length418 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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.

Subunit structure

Forms a undecameric ring.

Subcellular location

NucleusPotential.

Post-translational modification

Phosphorylated upon DNA damage, probably by ATM or ATR.

Sequence similarities

Belongs to the RAD52 family.

Ontologies

Keywords

   Biological processDNA damage
DNA recombination
DNA repair
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   PTMPhosphoprotein
   Technical term3D-structure

Gene Ontology (GO)

   Biological processmitotic recombination Ref.1

Traceable author statement. Source: ProtInc

reciprocal meiotic recombination Ref.1

Traceable author statement. Source: ProtInc

   Cellular componentnucleoplasm

Inferred from Experiment. Source: Reactome

   Molecular functionDNA binding Ref.1

Traceable author statement. Source: ProtInc

protein binding

Inferred from physical interaction. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

WRNQ141914EBI-706448,EBI-368417

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 418418DNA repair protein RAD52 homolog
PRO_0000173881

Amino acid modifications

Modified residue3181Phosphothreonine

Natural variations

Natural variant701R → W
VAR_019218
Natural variant2211Q → E
VAR_019219
Natural variant2871S → N
VAR_019220

Experimental info

Sequence conflict1001N → K in AAA87554. Ref.3
Sequence conflict4181S → SY in AAA87554. Ref.3

Secondary structure

......................... 418
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P43351-1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 7E1BBCAF0B9CD4AF

FASTA41846,169
        10         20         30         40         50         60 
MSGTEEAILG GRDSHPAAGG GSVLCFGQCQ YTAEEYQAIQ KALRQRLGPE YISSRMAGGG 

        70         80         90        100        110        120 
QKVCYIEGHR VINLANEMFG YNGWAHSITQ QNVDFVDLNN GKFYVGVCAF VRVQLKDGSY 

       130        140        150        160        170        180 
HEDVGYGVSE GLKSKALSLE KARKEAVTDG LKRALRSFGN ALGNCILDKD YLRSLNKLPR 

       190        200        210        220        230        240 
QLPLEVDLTK AKRQDLEPSV EEARYNSCRP NMALGHPQLQ QVTSPSRPSH AVIPADQDCS 

       250        260        270        280        290        300 
SRSLSSSAVE SEATHQRKLR QKQLQQQFRE RMEKQQVRVS TPSAEKSEAA PPAPPVTHST 

       310        320        330        340        350        360 
PVTVSEPLLE KDFLAGVTQE LIKTLEDNSE KWAVTPDAGD GVVKPSSRAD PAQTSDTLAL 

       370        380        390        400        410 
NNQMVTQNRT PHSVCHQKPQ AKSGSWDLQT YSADQRTTGN WESHRKSQDM KKRKYDPS 

« Hide

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: 7774919] [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: 7526206] [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: 7797537] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Spleen.
[4]"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu)."
Livingston R.J., Rieder M.J., Chung M.-W., Ritchie T.K., Olson A.N., Nguyen C.P., Nguyen D.A., Poel C.L., Robertson P.D., Schackwitz W.S., Sherwood J.K., Sherwood A.M., Leithauser B.J., Nickerson D.A.
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS TRP-70; GLU-221 AND ASN-287.
[5]"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: 17525332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-318, MASS SPECTROMETRY.
[6]"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: 12370410] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 24-209.
+Additional computationally mapped references.

Cross-references

Sequence databases

U12134 mRNA. Translation: AAA85793.1.
L33262 mRNA. Translation: AAB05203.1.
U27516 mRNA. Translation: AAA87554.1.
AY527412 Genomic DNA. Translation: AAS00097.1.
PIRA57518.
RefSeqNP_602296.2.
UniGeneHs.410355

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1H2IX-ray2.70A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V1-209[»]
1KN0X-ray2.85A/B/C/D/E/F/G/H/I/J/K1-212[»]
DisProtDP00437.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:333N.
IntActP43351.

PTM databases

PhosphoSiteP43351.

Polymorphism databases

NIEHS-SNPsSearch...

Genome annotation databases

EnsemblENSG00000002016. Homo sapiens. [Contig view]
GeneID5893.
KEGGhsa:5893.

Organism-specific databases

H-InvDBHIX0036706.
HGNCHGNC:9824. RAD52.
MIM600392. gene.
PharmGKBPA34180.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOGENOMP43351.
HOVERGENP43351.

Enzyme and pathway databases

ReactomeREACT_216. DNA Repair.

Gene expression databases

ArrayExpressP43351.
CleanExHS_RAD52.
GermOnlineENSG00000002016. Homo sapiens.

Family and domain databases

InterProIPR004585. Rad52.
IPR007232. Rad52_Rad22.
[Graphical view]
PANTHERPTHR12132. Rad52_Rad22. 1 hit.
PfamPF04098. Rad52_Rad22. 1 hit.
[Graphical view]
TIGRFAMsTIGR00607. rad52. 1 hit.
ProtoNetSearch...

Other Resources

NextBio22926.
SOURCESearch...

Entry information

Entry nameRAD52_HUMAN
AccessionPrimary (citable) accession number: P43351
Secondary accession number(s): Q13205
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 25, 2008
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents