Reviewed, UniProtKB/Swiss-Prot P43351 (RAD52_HUMAN)

Names and origin

Protein names

Recommended name:
    DNA repair protein RAD52 homolog

Gene names

Name:

RAD52

Organism

Homo sapiens (Human)

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.
Sequence processing	The displayed sequence is not processed.
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.
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 process	DNA damage DNA recombination DNA repair
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	mitotic recombination Ref.1 Traceable author statement. Source: ProtInc reciprocal meiotic recombination Ref.1 Traceable author statement. Source: ProtInc
Cellular component	nucleoplasm Inferred from Experiment. Source: Reactome
Molecular function	DNA 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
WRN	Q14191	4	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

318

1

Phosphothreonine

Natural variations

Natural variant

70

1

R → W

VAR_019218

Natural variant

221

1

Q → E

VAR_019219

Natural variant

287

1

S → N

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

1

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418

Helix Strand Turn

Details...

Helix

33 – 44

12

Turn

49 – 51

3

Beta strand

52 – 56

5

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

198 – 205

8

Sequences

	Sequence		Length	Mass (Da)
	P43351-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 7E1BBCAF0B9CD4AF	FASTA	418	46,169
	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

References

	« Hide 'large scale' referencesShow '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

EMBLGenBankDDBJ

U12134 mRNA. Translation: AAA85793.1.
L33262 mRNA. Translation: AAB05203.1.
U27516 mRNA. Translation: AAA87554.1.
AY527412 Genomic DNA. Translation: AAS00097.1.

PIR

A57518.

RefSeq

NP_602296.2.

UniGene

Hs.410355

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1H2I	X-ray	2.70	A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V	1-209	[»]
1KN0	X-ray	2.85	A/B/C/D/E/F/G/H/I/J/K	1-212	[»]

DisProt

DP00437.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:333N.

IntAct

P43351.

PTM databases

PhosphoSite

P43351.

Polymorphism databases

NIEHS-SNPs

Search...

Genome annotation databases

Ensembl

ENSG00000002016. Homo sapiens. [Contig view]

GeneID

5893.

KEGG

hsa:5893.

Organism-specific databases

H-InvDB

HIX0036706.

HGNC

HGNC:9824. RAD52.

MIM

600392. gene.

PharmGKB

PA34180.

GenAtlas

Search...

GeneCards

Search...

Phylogenomic databases

HOGENOM

P43351.

HOVERGEN

P43351.

Enzyme and pathway databases

Reactome

REACT_216. DNA Repair.

Gene expression databases

ArrayExpress

P43351.

CleanEx

HS_RAD52.

GermOnline

ENSG00000002016. Homo sapiens.

Family and domain databases

InterPro

IPR004585. Rad52.
IPR007232. Rad52_Rad22.
[Graphical view]

PANTHER

PTHR12132. Rad52_Rad22. 1 hit.

Pfam

PF04098. Rad52_Rad22. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00607. rad52. 1 hit.

ProtoNet

Search...

Other Resources

NextBio

22926.

SOURCE

Search...

Entry information

Entry name

RAD52_HUMAN

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)