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P43351

- RAD52_HUMAN

UniProt

P43351 - RAD52_HUMAN

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
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    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 – 1565

    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

    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 Curated

    GO - Cellular componenti

    1. nucleoplasm Source: Reactome
    2. nucleus Source: ProtInc

    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 homologPRO_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.3 Publications

    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

    1
    418
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP43351.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni221 – 28060Mediates interaction with RPA2Add
    BLAST

    Sequence similaritiesi

    Belongs to the RAD52 family.Curated

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti100 – 1001N → K in AAA87554. (PubMed:7797537)Curated
    Sequence conflicti418 – 4181S → SY in AAA87554. (PubMed:7797537)Curated

    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. 2 PublicationsVSP_047749Add
    BLAST
    Alternative sequencei117 – 13923DGSYH…KALSL → VRGWSRPAARKDQWVVGEGW FIS in isoform gamma. 2 PublicationsVSP_047750Add
    BLAST
    Alternative sequencei119 – 418300Missing in isoform delta. 2 PublicationsVSP_047751Add
    BLAST
    Alternative sequencei140 – 418279Missing in isoform gamma. 2 PublicationsVSP_047752Add
    BLAST
    Alternative sequencei157 – 22670SFGNA…VTSPS → LPLLGVSGRILYSLFSVHSV MCAGGLPTPTASAQTAPSSP CSSAVLRYAQEFWECTWKLY SGQRLPEITK in isoform beta. 1 PublicationVSP_047753Add
    BLAST
    Alternative sequencei227 – 418192Missing in isoform beta. 1 PublicationVSP_047754Add
    BLAST

    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

    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: October 1, 2014
    This is version 131 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