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O60671

- RAD1_HUMAN

UniProt

O60671 - RAD1_HUMAN

Protein

Cell cycle checkpoint protein RAD1

Gene

RAD1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 1 (01 Aug 1998)
      Previous versions | rss
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    Functioni

    Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair. The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex. Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER). The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3'-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavage activity on substrates with double, nick, or gap flaps of distinct sequences and lengths; and DNA ligase I (LIG1) on long-patch base excision repair substrates. The 9-1-1 complex is necessary for the recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring during the S phase. Isoform 1 possesses 3'->5' double stranded DNA exonuclease activity.2 Publications

    Catalytic activityi

    Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.

    GO - Molecular functioni

    1. 3'-5' exonuclease activity Source: UniProtKB
    2. damaged DNA binding Source: UniProtKB
    3. exodeoxyribonuclease III activity Source: UniProtKB-EC
    4. protein binding Source: UniProtKB

    GO - Biological processi

    1. cell cycle checkpoint Source: UniProtKB
    2. cellular response to DNA damage stimulus Source: ProtInc
    3. cellular response to ionizing radiation Source: UniProtKB
    4. DNA damage checkpoint Source: UniProtKB
    5. DNA repair Source: ProtInc
    6. DNA replication Source: Reactome
    7. meiotic prophase I Source: ProtInc
    8. nucleic acid phosphodiester bond hydrolysis Source: GOC
    9. substantia nigra development Source: UniProt

    Keywords - Molecular functioni

    Exonuclease, Hydrolase, Nuclease

    Keywords - Biological processi

    DNA damage, DNA repair

    Enzyme and pathway databases

    ReactomeiREACT_6769. Activation of ATR in response to replication stress.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cell cycle checkpoint protein RAD1 (EC:3.1.11.2)
    Short name:
    hRAD1
    Alternative name(s):
    DNA repair exonuclease rad1 homolog
    Rad1-like DNA damage checkpoint protein
    Gene namesi
    Name:RAD1
    Synonyms:REC1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:9806. RAD1.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. intracellular membrane-bounded organelle Source: HPA
    2. nucleoplasm Source: Reactome
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi226 – 2338SLLKPSTK → AAAAAAAA: Abolishes association of the 9-1-1 complex with RAD17. 1 Publication

    Organism-specific databases

    PharmGKBiPA34166.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 282282Cell cycle checkpoint protein RAD1PRO_0000225005Add
    BLAST

    Proteomic databases

    MaxQBiO60671.
    PaxDbiO60671.
    PRIDEiO60671.

    PTM databases

    PhosphoSiteiO60671.

    Expressioni

    Tissue specificityi

    Expressed in testis, uterus, bladder, spleen, ovaries, lung, brain and muscle (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiO60671.
    BgeeiO60671.
    CleanExiHS_RAD1.
    GenevestigatoriO60671.

    Organism-specific databases

    HPAiHPA006692.

    Interactioni

    Subunit structurei

    Component of the toroidal 9-1-1 (RAD9-RAD1-HUS1) complex, composed of RAD9A, RAD1 and HUS1. The 9-1-1 complex associates with LIG1, POLB, FEN1, RAD17, HDAC1, RPA1 and RPA2. The 9-1-1 complex associates with the RAD17-RFC complex. RAD1 interacts with POLB, FEN1, HUS1, HUS1B, RAD9A and RAD9B. Interacts with DNAJC7.13 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HUS1O609214EBI-721835,EBI-1056174
    RAD9AQ996382EBI-721835,EBI-2606224

    Protein-protein interaction databases

    BioGridi111771. 16 interactions.
    DIPiDIP-46061N.
    IntActiO60671. 4 interactions.
    MINTiMINT-1853000.
    STRINGi9606.ENSP00000340879.

    Structurei

    Secondary structure

    1
    282
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi16 – 227
    Helixi25 – 328
    Beta strandi36 – 4510
    Beta strandi48 – 558
    Turni56 – 583
    Beta strandi59 – 668
    Helixi67 – 693
    Beta strandi70 – 789
    Beta strandi80 – 856
    Helixi86 – 938
    Turni94 – 963
    Beta strandi107 – 1126
    Beta strandi114 – 1174
    Beta strandi119 – 1257
    Beta strandi128 – 1347
    Turni149 – 1513
    Beta strandi152 – 1598
    Helixi160 – 1634
    Helixi164 – 1685
    Beta strandi174 – 1818
    Beta strandi183 – 19412
    Beta strandi197 – 2037
    Beta strandi205 – 2073
    Beta strandi208 – 2158
    Beta strandi219 – 2246
    Helixi225 – 2284
    Helixi231 – 2377
    Beta strandi239 – 2468
    Beta strandi247 – 2493
    Beta strandi251 – 2588
    Beta strandi260 – 2623
    Beta strandi264 – 2718

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3A1JX-ray2.50C13-275[»]
    3G65X-ray2.90B1-282[»]
    3GGRX-ray3.20C1-282[»]
    ProteinModelPortaliO60671.
    SMRiO60671. Positions 13-275.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO60671.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the rad1 family.Curated

    Phylogenomic databases

    eggNOGiNOG324428.
    HOGENOMiHOG000008015.
    HOVERGENiHBG053058.
    InParanoidiO60671.
    KOiK02830.
    OMAiCKVSVRT.
    OrthoDBiEOG7N0C4P.
    PhylomeDBiO60671.
    TreeFamiTF101211.

    Family and domain databases

    InterProiIPR003011. Cell_cycle_checkpoint_Rad1.
    IPR003021. Rad1_Rec1_Rad17.
    [Graphical view]
    PANTHERiPTHR10870. PTHR10870. 1 hit.
    PfamiPF02144. Rad1. 1 hit.
    [Graphical view]
    PRINTSiPR01245. RAD1REC1.
    PR01246. RAD1REPAIR.

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O60671-1) [UniParc]FASTAAdd to Basket

    Also known as: Hrad1A

    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

    MPLLTQQIQD EDDQYSLVAS LDNVRNLSTI LKAIHFREHA TCFATKNGIK    50
    VTVENAKCVQ ANAFIQAGIF QEFKVQEESV TFRINLTVLL DCLSIFGSSP 100
    MPGTLTALRM CYQGYGYPLM LFLEEGGVVT VCKINTQEPE ETLDFDFCST 150
    NVINKIILQS EGLREAFSEL DMTSEVLQIT MSPDKPYFRL STFGNAGSSH 200
    LDYPKDSDLM EAFHCNQTQV NRYKISLLKP STKALVLSCK VSIRTDNRGF 250
    LSLQYMIRNE DGQICFVEYY CCPDEEVPES ES 282
    Length:282
    Mass (Da):31,827
    Last modified:August 1, 1998 - v1
    Checksum:i075FBD4CF8A4FDB2
    GO
    Isoform 2 (identifier: O60671-2) [UniParc]FASTAAdd to Basket

    Also known as: Hrad1B

    The sequence of this isoform differs from the canonical sequence as follows:
         67-102: Missing.

    Show »
    Length:246
    Mass (Da):27,828
    Checksum:iE96C130821B8D2D0
    GO
    Isoform 3 (identifier: O60671-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         67-68: AG → GL
         69-282: Missing.

    Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

    Show »
    Length:68
    Mass (Da):7,576
    Checksum:i12B4E5E1CA5B9703
    GO

    Sequence cautioni

    The sequence AAC35550.1 differs from that shown. Reason: Frameshift at position 103.
    The sequence CAA06249.1 differs from that shown. Reason: Frameshift at position 103.
    The sequence AAC35550.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence CAA06249.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti135 – 1351N → T in AAC95466. (PubMed:9828137)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti33 – 331A → G.
    Corresponds to variant rs2308951 [ dbSNP | Ensembl ].
    VAR_051718
    Natural varianti39 – 391H → Q.1 Publication
    Corresponds to variant rs41271673 [ dbSNP | Ensembl ].
    VAR_055376
    Natural varianti104 – 1041T → S.
    Corresponds to variant rs1805328 [ dbSNP | Ensembl ].
    VAR_051719
    Natural varianti114 – 1141G → D.
    Corresponds to variant rs2308957 [ dbSNP | Ensembl ].
    VAR_051720
    Natural varianti281 – 2811E → G.1 Publication
    Corresponds to variant rs1805327 [ dbSNP | Ensembl ].
    VAR_051721

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei67 – 10236Missing in isoform 2. 2 PublicationsVSP_017334Add
    BLAST
    Alternative sequencei67 – 682AG → GL in isoform 3. 1 PublicationVSP_017335
    Alternative sequencei69 – 282214Missing in isoform 3. 1 PublicationVSP_017336Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF074717 mRNA. Translation: AAC98093.1.
    AF073524 mRNA. Translation: AAC95466.1.
    AF030933 mRNA. Translation: AAC95427.1.
    AF076841 mRNA. Translation: AAC95523.1.
    AF090170 mRNA. Translation: AAC95603.1.
    AJ004974 mRNA. Translation: CAA06248.1.
    AJ004975 mRNA. Translation: CAA06249.1. Sequence problems.
    AF011905 mRNA. Translation: AAC27243.1.
    AF058392 mRNA. Translation: AAC14138.1.
    AF084512 mRNA. Translation: AAC35549.1.
    AF084513 mRNA. Translation: AAC35550.1. Sequence problems.
    AK002112 mRNA. Translation: BAG51017.1.
    BT006908 mRNA. Translation: AAP35554.1.
    DQ451401 Genomic DNA. Translation: ABD96829.1.
    CH471119 Genomic DNA. Translation: EAW55904.1.
    BC006837 mRNA. Translation: AAH06837.1.
    BC009804 mRNA. Translation: AAH09804.1.
    BC037857 mRNA. Translation: AAH37857.1.
    AB183821 Genomic DNA. Translation: BAD86789.1.
    AB183822 Genomic DNA. Translation: BAD86790.1.
    CCDSiCCDS3905.1. [O60671-1]
    RefSeqiNP_002844.1. NM_002853.3. [O60671-1]
    UniGeneiHs.38114.

    Genome annotation databases

    EnsembliENST00000325577; ENSP00000313467; ENSG00000113456. [O60671-3]
    ENST00000341754; ENSP00000340879; ENSG00000113456. [O60671-1]
    ENST00000382038; ENSP00000371469; ENSG00000113456. [O60671-1]
    GeneIDi5810.
    KEGGihsa:5810.
    UCSCiuc003jiw.3. human. [O60671-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF074717 mRNA. Translation: AAC98093.1 .
    AF073524 mRNA. Translation: AAC95466.1 .
    AF030933 mRNA. Translation: AAC95427.1 .
    AF076841 mRNA. Translation: AAC95523.1 .
    AF090170 mRNA. Translation: AAC95603.1 .
    AJ004974 mRNA. Translation: CAA06248.1 .
    AJ004975 mRNA. Translation: CAA06249.1 . Sequence problems.
    AF011905 mRNA. Translation: AAC27243.1 .
    AF058392 mRNA. Translation: AAC14138.1 .
    AF084512 mRNA. Translation: AAC35549.1 .
    AF084513 mRNA. Translation: AAC35550.1 . Sequence problems.
    AK002112 mRNA. Translation: BAG51017.1 .
    BT006908 mRNA. Translation: AAP35554.1 .
    DQ451401 Genomic DNA. Translation: ABD96829.1 .
    CH471119 Genomic DNA. Translation: EAW55904.1 .
    BC006837 mRNA. Translation: AAH06837.1 .
    BC009804 mRNA. Translation: AAH09804.1 .
    BC037857 mRNA. Translation: AAH37857.1 .
    AB183821 Genomic DNA. Translation: BAD86789.1 .
    AB183822 Genomic DNA. Translation: BAD86790.1 .
    CCDSi CCDS3905.1. [O60671-1 ]
    RefSeqi NP_002844.1. NM_002853.3. [O60671-1 ]
    UniGenei Hs.38114.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3A1J X-ray 2.50 C 13-275 [» ]
    3G65 X-ray 2.90 B 1-282 [» ]
    3GGR X-ray 3.20 C 1-282 [» ]
    ProteinModelPortali O60671.
    SMRi O60671. Positions 13-275.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111771. 16 interactions.
    DIPi DIP-46061N.
    IntActi O60671. 4 interactions.
    MINTi MINT-1853000.
    STRINGi 9606.ENSP00000340879.

    PTM databases

    PhosphoSitei O60671.

    Proteomic databases

    MaxQBi O60671.
    PaxDbi O60671.
    PRIDEi O60671.

    Protocols and materials databases

    DNASUi 5810.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000325577 ; ENSP00000313467 ; ENSG00000113456 . [O60671-3 ]
    ENST00000341754 ; ENSP00000340879 ; ENSG00000113456 . [O60671-1 ]
    ENST00000382038 ; ENSP00000371469 ; ENSG00000113456 . [O60671-1 ]
    GeneIDi 5810.
    KEGGi hsa:5810.
    UCSCi uc003jiw.3. human. [O60671-1 ]

    Organism-specific databases

    CTDi 5810.
    GeneCardsi GC05M034905.
    HGNCi HGNC:9806. RAD1.
    HPAi HPA006692.
    MIMi 603153. gene.
    neXtProti NX_O60671.
    PharmGKBi PA34166.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG324428.
    HOGENOMi HOG000008015.
    HOVERGENi HBG053058.
    InParanoidi O60671.
    KOi K02830.
    OMAi CKVSVRT.
    OrthoDBi EOG7N0C4P.
    PhylomeDBi O60671.
    TreeFami TF101211.

    Enzyme and pathway databases

    Reactomei REACT_6769. Activation of ATR in response to replication stress.

    Miscellaneous databases

    ChiTaRSi RAD1. human.
    EvolutionaryTracei O60671.
    GeneWikii RAD1_homolog.
    GenomeRNAii 5810.
    NextBioi 22636.
    PROi O60671.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O60671.
    Bgeei O60671.
    CleanExi HS_RAD1.
    Genevestigatori O60671.

    Family and domain databases

    InterProi IPR003011. Cell_cycle_checkpoint_Rad1.
    IPR003021. Rad1_Rec1_Rad17.
    [Graphical view ]
    PANTHERi PTHR10870. PTHR10870. 1 hit.
    Pfami PF02144. Rad1. 1 hit.
    [Graphical view ]
    PRINTSi PR01245. RAD1REC1.
    PR01246. RAD1REPAIR.
    ProtoNeti Search...

    Publicationsi

    1. "Human and mouse homologs of Schizosaccharomyces pombe rad1(+) and Saccharomyces cerevisiae RAD17: linkage to checkpoint control and mammalian meiosis."
      Freire R., Murguia J.R., Tarsounas M., Lowndes N.F., Moens P.B., Jackson S.P.
      Genes Dev. 12:2560-2573(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    2. "A human and mouse homolog of the Schizosaccharomyces pombe rad1+ cell cycle checkpoint control gene."
      Bluyssen H.A.R., van Os R.I., Naus N.C., Jaspers I., Hoeijmakers J.H.J., de Klein A.
      Genomics 54:331-337(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "RAD1, a human structural homolog of the Schizosaccharomyces pombe RAD1 cell cycle checkpoint gene."
      Marathi U.K., Dahlen M., Sunnerhagen P., Romero A.V., Ramagli L.S., Siciliano M.J., Li L., Legerski R.J.
      Genomics 54:344-347(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Cervix carcinoma.
    4. "cDNA cloning and gene mapping of human homologs for Schizosaccharomyces pombe rad17, rad1, and hus1 and cloning of homologs from mouse, Caenorhabditis elegans, and Drosophila melanogaster."
      Dean F.B., Lian L., O'Donnell M.
      Genomics 54:424-436(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
    5. "A human homologue of the Schizosaccharomyces pombe rad1+ checkpoint gene encodes an exonuclease."
      Parker A.E., Van de Weyer I., Laus M.C., Oostveen I., Yon J., Verhasselt P., Luyten W.H.M.L.
      J. Biol. Chem. 273:18332-18339(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION IN EXONUCLEASE ACTIVITY.
    6. "HRAD1 and MRad1 encode mammalian homologues of the fission yeast rad1+ cell cycle checkpoint control gene."
      Udell C.M., Lee S.K., Davey S.
      Nucleic Acids Res. 26:3971-3976(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    7. "Identification and cloning of Hrad1, a human homolog of the Schizosaccharomyces pombe checkpoint protein."
      Hao L., Chang M., Liu J., Chen L.B.
      Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    8. "Mammalian REC1, encoding a 3'-5' exonuclease, is differentially expressed during meiosis."
      Shannon M.E., Naureckiene S., Stubbs L., Holloman W.K., Thelen M.P.
      Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    9. "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] (ISOFORM 1).
      Tissue: Placenta.
    10. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    11. NIEHS SNPs program
      Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLN-39 AND GLY-281.
    12. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    13. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Bone marrow, Placenta and Testis.
    14. "Identification of novel polymorphisms in the RAD1 gene."
      Saegusa K.K., Suga T.K., Imai T.
      Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 104-188 AND 223-282.
    15. "The human G2 checkpoint control protein hRAD9 is a nuclear phosphoprotein that forms complexes with hRAD1 and hHUS1."
      St Onge R.P., Udell C.M., Casselman R., Davey S.
      Mol. Biol. Cell 10:1985-1995(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HUS1 AND RAD9A.
    16. "Physical interaction among human checkpoint control proteins HUS1p, RAD1p, and RAD9p, and implications for the regulation of cell cycle progression."
      Hang H., Lieberman H.B.
      Genomics 65:24-33(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HUS1 AND RAD9A.
    17. "HDAC1, a histone deacetylase, forms a complex with Hus1 and Rad9, two G2/M checkpoint Rad proteins."
      Cai R.L., Yan-Neale Y., Cueto M.A., Xu H., Cohen D.
      J. Biol. Chem. 275:27909-27916(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE 9-1-1 COMPLEX ASSOCIATED WITH HDAC1.
    18. "The human checkpoint protein hRad17 interacts with the PCNA-like proteins hRad1, hHus1, and hRad9."
      Rauen M., Burtelow M.A., Dufault V.M., Karnitz L.M.
      J. Biol. Chem. 275:29767-29771(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE 9-1-1 COMPLEX ASSOCIATED WITH RAD17, MUTAGENESIS OF 226-SER--LYS-233.
    19. "The J domain of Tpr2 regulates its interaction with the proapoptotic and cell-cycle checkpoint protein, Rad9."
      Xiang S.L., Kumano T., Iwasaki S.I., Sun X., Yoshioka K., Yamamoto K.C.
      Biochem. Biophys. Res. Commun. 287:932-940(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DNAJC7.
    20. "Identification and characterization of a paralog of human cell cycle checkpoint gene HUS1."
      Hang H., Zhang Y., Dunbrack R.L. Jr., Wang C., Lieberman H.B.
      Genomics 79:487-492(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HUS1B.
    21. "Expression of mammalian paralogues of HRAD9 and Mrad9 checkpoint control genes in normal and cancerous testicular tissue."
      Hopkins K.M., Wang X., Berlin A., Hang H., Thaker H.M., Lieberman H.B.
      Cancer Res. 63:5291-5298(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAD9B.
    22. "Identification and characterization of RAD9B, a paralog of the RAD9 checkpoint gene."
      Dufault V.M., Oestreich A.J., Vroman B.T., Karnitz L.M.
      Genomics 82:644-651(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAD9B.
    23. "Loading of the human 9-1-1 checkpoint complex onto DNA by the checkpoint clamp loader hRad17-replication factor C complex in vitro."
      Bermudez V.P., Lindsey-Boltz L.A., Cesare A.J., Maniwa Y., Griffith J.D., Hurwitz J., Sancar A.
      Proc. Natl. Acad. Sci. U.S.A. 100:1633-1638(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: ASSOCIATION OF THE 9-1-1 COMPLEX WITH THE RAD17-RFC COMPLEX, ELECTRON MICROSCOPY OF THE 9-1-1 AND RAD17-RFC COMPLEXES BOUND TO DNA.
    24. "The human Rad9/Rad1/Hus1 damage sensor clamp interacts with DNA polymerase beta and increases its DNA substrate utilisation efficiency: implications for DNA repair."
      Toueille M., El-Andaloussi N., Frouin I., Freire R., Funk D., Shevelev I., Friedrich-Heineken E., Villani G., Hottiger M.O., Huebscher U.
      Nucleic Acids Res. 32:3316-3324(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE 9-1-1 COMPLEX ASSOCIATED WITH POLB, INTERACTION WITH POLB.
    25. Cited for: IDENTIFICATION IN THE 9-1-1 COMPLEX ASSOCIATED WITH FEN1.
    26. "The human checkpoint sensor and alternative DNA clamp Rad9-Rad1-Hus1 modulates the activity of DNA ligase I, a component of the long-patch base excision repair machinery."
      Smirnova E., Toueille M., Markkanen E., Huebscher U.
      Biochem. J. 389:13-17(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE 9-1-1 COMPLEX ASSOCIATED WITH LIG1.
    27. "The two DNA clamps Rad9/Rad1/Hus1 complex and proliferating cell nuclear antigen differentially regulate flap endonuclease 1 activity."
      Friedrich-Heineken E., Toueille M., Taennler B., Buerki C., Ferrari E., Hottiger M.O., Huebscher U.
      J. Mol. Biol. 353:980-989(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE 9-1-1 COMPLEX ASSOCIATED WITH FEN1, INTERACTION WITH FEN1.
    28. "Interaction and colocalization of Rad9/Rad1/Hus1 checkpoint complex with replication protein A in human cells."
      Wu X., Shell S.M., Zou Y.
      Oncogene 24:4728-4735(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE 9-1-1 COMPLEX ASSOCIATED WITH RPA1 AND RPA2.
    29. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    30. "A DNA damage response screen identifies RHINO, a 9-1-1 and TopBP1 interacting protein required for ATR signaling."
      Cotta-Ramusino C., McDonald E.R. III, Hurov K., Sowa M.E., Harper J.W., Elledge S.J.
      Science 332:1313-1317(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY.
    31. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiRAD1_HUMAN
    AccessioniPrimary (citable) accession number: O60671
    Secondary accession number(s): O75572
    , O95304, Q1W161, Q5KSM0, Q5KSM1, Q9UEP1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 7, 2006
    Last sequence update: August 1, 1998
    Last modified: October 1, 2014
    This is version 122 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 5
      Human chromosome 5: 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