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P43351

- RAD52_HUMAN

UniProt

P43351 - RAD52_HUMAN

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Protein
DNA repair protein RAD52 homolog
Gene
RAD52
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi152 – 15651 Publication

GO - Molecular functioni

  1. DNA binding Source: ProtInc
  2. identical protein binding Source: IntAct
  3. protein binding Source: UniProtKB

GO - Biological processi

  1. DNA recombinase assembly Source: Reactome
  2. DNA recombination Source: UniProtKB
  3. DNA repair Source: Reactome
  4. double-strand break repair Source: Reactome
  5. double-strand break repair via homologous recombination Source: Reactome
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA recombination, DNA repair

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_2141. Assembly of the RAD51-ssDNA nucleoprotein complex.
REACT_408. Presynaptic phase of homologous DNA pairing and strand exchange.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA repair protein RAD52 homolog
Gene namesi
Name:RAD52
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:9824. RAD52.

Subcellular locationi

Nucleus Reviewed prediction

GO - Cellular componenti

  1. nucleoplasm Source: Reactome
  2. nucleus Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi55 – 551R → A: Abolishes ssDNA-binding. 1 Publication
Mutagenesisi65 – 651Y → A: Moderately defective in both ss and dsDNA-binding. 1 Publication
Mutagenesisi152 – 1521K → A: Abolishes ssDNA-binding. 1 Publication
Mutagenesisi153 – 1531R → A: Moderately defective in both ss and dsDNA-binding. 1 Publication
Mutagenesisi156 – 1561R → A: Moderately defective in both ss and dsDNA-binding. 1 Publication

Organism-specific databases

PharmGKBiPA34180.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 418418DNA repair protein RAD52 homolog
PRO_0000173881Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei104 – 1041Phosphotyrosine; by ABL11 Publication
Modified residuei199 – 1991Phosphoserine1 Publication
Modified residuei318 – 3181Phosphothreonine1 Publication
Modified residuei335 – 3351Phosphothreonine1 Publication

Post-translational modificationi

Phosphorylated upon DNA damage by ABL1, and probably by ATM or ATR.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP43351.
PRIDEiP43351.

PTM databases

PhosphoSiteiP43351.

Expressioni

Gene expression databases

ArrayExpressiP43351.
BgeeiP43351.
CleanExiHS_RAD52.
GenevestigatoriP43351.

Interactioni

Subunit structurei

The full-length protein forms heptameric rings. Interacts with ABL1. Interacts with RPA2; the interaction is direct and associates RAD52 with the RPA complex.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-706448,EBI-706448
RAD51Q066093EBI-706448,EBI-297202
RPA3P352442EBI-706448,EBI-621428
WRNQ141919EBI-706448,EBI-368417

Protein-protein interaction databases

BioGridi111830. 39 interactions.
DIPiDIP-333N.
IntActiP43351. 28 interactions.
MINTiMINT-2803258.
STRINGi9606.ENSP00000351284.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni26 – 283
Helixi33 – 4412
Turni49 – 513
Beta strandi52 – 565
Beta strandi58 – 603
Beta strandi62 – 665
Helixi68 – 7912
Turni81 – 833
Beta strandi84 – 11532
Beta strandi120 – 13314
Helixi135 – 15622
Helixi160 – 1623
Helixi165 – 1673
Helixi169 – 1768
Helixi188 – 1903
Helixi198 – 2058

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
DisProtiDP00437.
ProteinModelPortaliP43351.
SMRiP43351. Positions 24-209.

Miscellaneous databases

EvolutionaryTraceiP43351.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni221 – 28060Mediates interaction with RPA2
Add
BLAST

Sequence similaritiesi

Belongs to the RAD52 family.

Phylogenomic databases

eggNOGiCOG5055.
HOGENOMiHOG000237354.
HOVERGENiHBG054676.
InParanoidiP43351.
KOiK10873.
OMAiQARYSSC.
OrthoDBiEOG74XS87.
PhylomeDBiP43351.
TreeFamiTF101221.

Family and domain databases

InterProiIPR004585. DNA_recomb/repair_Rad52.
IPR007232. Rad52_Rad22.
[Graphical view]
PANTHERiPTHR12132. PTHR12132. 1 hit.
PfamiPF04098. Rad52_Rad22. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00607. rad52. 1 hit.

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform alpha (identifier: P43351-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MSGTEEAILG GRDSHPAAGG GSVLCFGQCQ YTAEEYQAIQ KALRQRLGPE    50
YISSRMAGGG QKVCYIEGHR VINLANEMFG YNGWAHSITQ QNVDFVDLNN 100
GKFYVGVCAF VRVQLKDGSY HEDVGYGVSE GLKSKALSLE KARKEAVTDG 150
LKRALRSFGN ALGNCILDKD YLRSLNKLPR QLPLEVDLTK AKRQDLEPSV 200
EEARYNSCRP NMALGHPQLQ QVTSPSRPSH AVIPADQDCS SRSLSSSAVE 250
SEATHQRKLR QKQLQQQFRE RMEKQQVRVS TPSAEKSEAA PPAPPVTHST 300
PVTVSEPLLE KDFLAGVTQE LIKTLEDNSE KWAVTPDAGD GVVKPSSRAD 350
PAQTSDTLAL NNQMVTQNRT PHSVCHQKPQ AKSGSWDLQT YSADQRTTGN 400
WESHRKSQDM KKRKYDPS 418
Length:418
Mass (Da):46,169
Last modified:November 1, 1995 - v1
Checksum:i7E1BBCAF0B9CD4AF
GO
Isoform beta (identifier: P43351-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     157-226: SFGNALGNCI...PQLQQVTSPS → LPLLGVSGRI...SGQRLPEITK
     227-418: Missing.

Note: Unable to interact with isoform alpha, may act as dominant negative.

Show »
Length:226
Mass (Da):24,540
Checksum:i8B0E3FC5773B46FE
GO
Isoform gamma (identifier: P43351-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     117-139: DGSYHEDVGYGVSEGLKSKALSL → VRGWSRPAARKDQWVVGEGWFIS
     140-418: Missing.

Note: Unable to interact with isoform alpha, may act as dominant negative.

Show »
Length:139
Mass (Da):15,350
Checksum:iDFA2F7994CACC1DF
GO
Isoform delta (identifier: P43351-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     94-118: DFVDLNNGKFYVGVCAFVRVQLKDG → GEYALQQWGLLHCPAPAESLLWVRR
     119-418: Missing.

Note: Unable to interact with isoform alpha, may act as dominant negative.

Show »
Length:118
Mass (Da):12,943
Checksum:iC3341B828BE835A5
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti70 – 701R → W.1 Publication
Corresponds to variant rs11571421 [ dbSNP | Ensembl ].
VAR_019218
Natural varianti221 – 2211Q → E.1 Publication
Corresponds to variant rs4987206 [ dbSNP | Ensembl ].
VAR_019219
Natural varianti287 – 2871S → N.1 Publication
Corresponds to variant rs11571463 [ dbSNP | Ensembl ].
VAR_019220

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei94 – 11825DFVDL…QLKDG → GEYALQQWGLLHCPAPAESL LWVRR in isoform delta.
VSP_047749Add
BLAST
Alternative sequencei117 – 13923DGSYH…KALSL → VRGWSRPAARKDQWVVGEGW FIS in isoform gamma.
VSP_047750Add
BLAST
Alternative sequencei119 – 418300Missing in isoform delta.
VSP_047751Add
BLAST
Alternative sequencei140 – 418279Missing in isoform gamma.
VSP_047752Add
BLAST
Alternative sequencei157 – 22670SFGNA…VTSPS → LPLLGVSGRILYSLFSVHSV MCAGGLPTPTASAQTAPSSP CSSAVLRYAQEFWECTWKLY SGQRLPEITK in isoform beta.
VSP_047753Add
BLAST
Alternative sequencei227 – 418192Missing in isoform beta.
VSP_047754Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti100 – 1001N → K in AAA87554. 1 Publication
Sequence conflicti418 – 4181S → SY in AAA87554. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U12134 mRNA. Translation: AAA85793.1.
L33262 mRNA. Translation: AAB05203.1.
U27516 mRNA. Translation: AAA87554.1.
AF125948 mRNA. Translation: AAD24575.1.
AF125949 mRNA. Translation: AAD24576.1.
AF125950 mRNA. Translation: AAD24577.1.
AK292160 mRNA. Translation: BAF84849.1.
AK312026 mRNA. Translation: BAG34963.1.
AY527412 Genomic DNA. Translation: AAS00097.1.
AC004803 Genomic DNA. No translation available.
CH471116 Genomic DNA. Translation: EAW88943.1.
CH471116 Genomic DNA. Translation: EAW88945.1.
CH471116 Genomic DNA. Translation: EAW88946.1.
CH471116 Genomic DNA. Translation: EAW88949.1.
CCDSiCCDS8507.2. [P43351-1]
PIRiA57518.
RefSeqiNP_602296.2. NM_134424.2. [P43351-1]
XP_005253777.1. XM_005253720.2. [P43351-1]
XP_005253778.1. XM_005253721.1. [P43351-1]
XP_005253784.1. XM_005253727.2. [P43351-2]
UniGeneiHs.410355.

Genome annotation databases

EnsembliENST00000358495; ENSP00000351284; ENSG00000002016. [P43351-1]
ENST00000430095; ENSP00000387901; ENSG00000002016. [P43351-1]
ENST00000461568; ENSP00000436008; ENSG00000002016. [P43351-3]
ENST00000468231; ENSP00000434703; ENSG00000002016. [P43351-3]
ENST00000541619; ENSP00000438965; ENSG00000002016. [P43351-4]
ENST00000544742; ENSP00000443254; ENSG00000002016. [P43351-4]
ENST00000545564; ENSP00000440268; ENSG00000002016. [P43351-2]
GeneIDi5893.
KEGGihsa:5893.
UCSCiuc001qis.1. human. [P43351-1]
uc001qix.1. human.

Polymorphism databases

DMDMi1172823.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U12134 mRNA. Translation: AAA85793.1 .
L33262 mRNA. Translation: AAB05203.1 .
U27516 mRNA. Translation: AAA87554.1 .
AF125948 mRNA. Translation: AAD24575.1 .
AF125949 mRNA. Translation: AAD24576.1 .
AF125950 mRNA. Translation: AAD24577.1 .
AK292160 mRNA. Translation: BAF84849.1 .
AK312026 mRNA. Translation: BAG34963.1 .
AY527412 Genomic DNA. Translation: AAS00097.1 .
AC004803 Genomic DNA. No translation available.
CH471116 Genomic DNA. Translation: EAW88943.1 .
CH471116 Genomic DNA. Translation: EAW88945.1 .
CH471116 Genomic DNA. Translation: EAW88946.1 .
CH471116 Genomic DNA. Translation: EAW88949.1 .
CCDSi CCDS8507.2. [P43351-1 ]
PIRi A57518.
RefSeqi NP_602296.2. NM_134424.2. [P43351-1 ]
XP_005253777.1. XM_005253720.2. [P43351-1 ]
XP_005253778.1. XM_005253721.1. [P43351-1 ]
XP_005253784.1. XM_005253727.2. [P43351-2 ]
UniGenei Hs.410355.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
DisProti DP00437.
ProteinModelPortali P43351.
SMRi P43351. Positions 24-209.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111830. 39 interactions.
DIPi DIP-333N.
IntActi P43351. 28 interactions.
MINTi MINT-2803258.
STRINGi 9606.ENSP00000351284.

Chemistry

ChEMBLi CHEMBL2362978.

PTM databases

PhosphoSitei P43351.

Polymorphism databases

DMDMi 1172823.

Proteomic databases

PaxDbi P43351.
PRIDEi P43351.

Protocols and materials databases

DNASUi 5893.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000358495 ; ENSP00000351284 ; ENSG00000002016 . [P43351-1 ]
ENST00000430095 ; ENSP00000387901 ; ENSG00000002016 . [P43351-1 ]
ENST00000461568 ; ENSP00000436008 ; ENSG00000002016 . [P43351-3 ]
ENST00000468231 ; ENSP00000434703 ; ENSG00000002016 . [P43351-3 ]
ENST00000541619 ; ENSP00000438965 ; ENSG00000002016 . [P43351-4 ]
ENST00000544742 ; ENSP00000443254 ; ENSG00000002016 . [P43351-4 ]
ENST00000545564 ; ENSP00000440268 ; ENSG00000002016 . [P43351-2 ]
GeneIDi 5893.
KEGGi hsa:5893.
UCSCi uc001qis.1. human. [P43351-1 ]
uc001qix.1. human.

Organism-specific databases

CTDi 5893.
GeneCardsi GC12M001021.
HGNCi HGNC:9824. RAD52.
MIMi 600392. gene.
neXtProti NX_P43351.
PharmGKBi PA34180.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5055.
HOGENOMi HOG000237354.
HOVERGENi HBG054676.
InParanoidi P43351.
KOi K10873.
OMAi QARYSSC.
OrthoDBi EOG74XS87.
PhylomeDBi P43351.
TreeFami TF101221.

Enzyme and pathway databases

Reactomei REACT_2141. Assembly of the RAD51-ssDNA nucleoprotein complex.
REACT_408. Presynaptic phase of homologous DNA pairing and strand exchange.

Miscellaneous databases

ChiTaRSi RAD52. human.
EvolutionaryTracei P43351.
GeneWikii RAD52.
GenomeRNAii 5893.
NextBioi 22926.
PROi P43351.
SOURCEi Search...

Gene expression databases

ArrayExpressi P43351.
Bgeei P43351.
CleanExi HS_RAD52.
Genevestigatori P43351.

Family and domain databases

InterProi IPR004585. DNA_recomb/repair_Rad52.
IPR007232. Rad52_Rad22.
[Graphical view ]
PANTHERi PTHR12132. PTHR12132. 1 hit.
Pfami PF04098. Rad52_Rad22. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00607. rad52. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] (ISOFORM ALPHA).
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
    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] (ISOFORM ALPHA).
    Tissue: Spleen.
  4. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA; GAMMA AND DELTA), ALTERNATIVE SPLICING.
    Tissue: Testis.
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS GAMMA AND DELTA).
    Tissue: Amygdala and Synovium.
  6. 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.
  7. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "Physical interaction between human RAD52 and RPA is required for homologous recombination in mammalian cells."
    Park M.S., Ludwig D.L., Stigger E., Lee S.H.
    J. Biol. Chem. 271:18996-19000(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN HOMOLOGOUS RECOMBINATION, INTERACTION WITH RPA2, REGION.
  10. "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.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-318, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  12. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Crystal structure of the homologous-pairing domain from the human Rad52 recombinase in the undecameric form."
    Kagawa W., Kurumizaka H., Ishitani R., Fukai S., Nureki O., Shibata T., Yokoyama S.
    Mol. Cell 10:359-371(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 1-212, SUBUNIT, DNA-BINDING REGION, MUTAGENESIS OF ARG-55; TYR-65; LYS-152; ARG-153 AND ARG-156.
  14. "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.

Entry informationi

Entry nameiRAD52_HUMAN
AccessioniPrimary (citable) accession number: P43351
Secondary accession number(s): Q13205
, Q9Y5T7, Q9Y5T8, Q9Y5T9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: September 3, 2014
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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