P43351 (RAD52_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA repair protein RAD52 homolog

Gene names

Name:

RAD52

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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 recombination Traceable author statement Ref.1. Source: ProtInc reciprocal meiotic recombination Traceable 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

1

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418

Helix Strand Turn

Details...

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

	Sequence		Length	Mass (Da)
	P43351 [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] [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

NIEHS-SNPs

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

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.

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

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	May 1, 2013
This is version 116 of the entry and version 1 of the sequence. [Complete 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.