Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O75943

- RAD17_HUMAN

UniProt

O75943 - RAD17_HUMAN

Protein

Cell cycle checkpoint protein RAD17

Gene

RAD17

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 2 (29 Mar 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Essential for sustained cell growth, maintenance of chromosomal stability, and ATR-dependent checkpoint activation upon DNA damage. Has a weak ATPase activity required for binding to chromatin. Participates in the recruitment of the RAD1-RAD9-HUS1 complex and RHNO1 onto chromatin, and in CHEK1 activation. May also serve as a sensor of DNA replication progression, and may be involved in homologous recombination.11 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi137 – 1448ATPSequence Analysis

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. nucleoside-triphosphatase activity Source: InterPro
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. cellular response to DNA damage stimulus Source: UniProtKB
    2. DNA damage checkpoint Source: UniProtKB
    3. DNA repair Source: ProtInc
    4. DNA replication Source: Reactome
    5. DNA replication checkpoint Source: ProtInc
    6. mitotic cell cycle checkpoint Source: UniProtKB
    7. negative regulation of DNA replication Source: UniProtKB
    8. regulation of phosphorylation Source: UniProtKB

    Keywords - Biological processi

    Cell cycle, DNA damage

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_6769. Activation of ATR in response to replication stress.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cell cycle checkpoint protein RAD17
    Short name:
    hRad17
    Alternative name(s):
    RF-C/activator 1 homolog
    Gene namesi
    Name:RAD17
    Synonyms:R24L
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:9807. RAD17.

    Subcellular locationi

    Nucleus 4 Publications
    Note: Phosphorylated form redistributes to discrete nuclear foci upon DNA damage.

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi143 – 1431K → E: Impairs phosphorylation on S-656. Abolishes interaction with the RAD1-RAD9-HUS1 complex; does not affect interaction with RFC3. 3 Publications
    Mutagenesisi143 – 1431K → G: Impairs phosphorylation. Impairs interaction with DNA and the RAD1-RAD9-HUS1 complex; does not affect interaction with RFC3. 3 Publications
    Mutagenesisi191 – 1911S → A: No effect on phosphorylation by ATR. 1 Publication
    Mutagenesisi646 – 6461S → A: Reduces by 50% phosphorylation by ATR, and abolishes interaction with RAD1. Abolishes phosphorylation by ATR and checkpoint activation without affecting interaction with RFC3, RFC4, ATM or ATR; when associated with A-656. 4 Publications
    Mutagenesisi646 – 6461S → D: Abolishes interaction with RAD1; when associated with D-656. 4 Publications
    Mutagenesisi656 – 6561S → A: Reduces by 50% phosphorylation by ATR, and abolishes interaction with RAD1. Abolishes phosphorylation by ATR and checkpoint activation without affecting interaction with RFC3, RFC4, ATM or ATR; when associated with A-646. 4 Publications
    Mutagenesisi656 – 6561S → D: Abolishes interaction with RAD1; when associated with D-646. 4 Publications

    Organism-specific databases

    PharmGKBiPA34167.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 681681Cell cycle checkpoint protein RAD17PRO_0000209948Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei55 – 551PhosphothreonineBy similarity
    Modified residuei646 – 6461Phosphoserine; by ATR and ATM5 Publications
    Modified residuei656 – 6561Phosphoserine; by ATR and ATM4 Publications

    Post-translational modificationi

    Phosphorylated. Phosphorylation on Ser-646 and Ser-656 is cell cycle-regulated, enhanced by genotoxic stress, and required for activation of checkpoint signaling. Phosphorylation is mediated by ATR upon UV or replication arrest, whereas it may be mediated both by ATR and ATM upon ionizing radiation. Phosphorylation on both sites is required for interaction with RAD1 but dispensable for interaction with RFC3 or RFC4.5 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO75943.
    PaxDbiO75943.
    PRIDEiO75943.

    PTM databases

    PhosphoSiteiO75943.

    Expressioni

    Tissue specificityi

    Overexpressed in various cancer cell lines and in colon carcinoma (at protein level). Isoform 2 and isoform 3 are the most abundant isoforms in non irradiated cells (at protein level). Ubiquitous at low levels. Highly expressed in testis, where it is expressed within the germinal epithelium of the seminiferous tubuli. Weakly expressed in seminomas (testicular tumors).5 Publications

    Inductioni

    Isoform 1, isoform 3 and isoform 4 are induced by X-ray irradiation.1 Publication

    Gene expression databases

    ArrayExpressiO75943.
    BgeeiO75943.
    CleanExiHS_RAD17.
    GenevestigatoriO75943.

    Organism-specific databases

    HPAiCAB004551.
    HPA005448.

    Interactioni

    Subunit structurei

    Part of a DNA-binding complex containing RFC2, RFC3, RFC4 and RFC5. Interacts with RAD1 and RAD9 within the RAD1-RAD9-HUS1 complex. Interacts with RAD9B, POLE, NHP2L1 and MCM7. DNA damage promotes interaction with ATR or ATM and disrupts interaction with the RAD1-RAD9-HUS1 complex.13 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FZR1Q9UM112EBI-968231,EBI-724997

    Protein-protein interaction databases

    BioGridi111821. 27 interactions.
    DIPiDIP-24254N.
    DIP-34896N.
    IntActiO75943. 7 interactions.
    MINTiMINT-3082919.
    STRINGi9606.ENSP00000370151.

    Structurei

    3D structure databases

    ProteinModelPortaliO75943.
    SMRiO75943. Positions 132-158.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni432 – 681250Interaction with MCM7Add
    BLAST

    Sequence similaritiesi

    Belongs to the rad17/RAD24 family.Curated

    Phylogenomic databases

    eggNOGiCOG0470.
    HOVERGENiHBG059834.
    InParanoidiO75943.
    KOiK06662.
    OMAiAQIAFIQ.
    PhylomeDBiO75943.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR003593. AAA+_ATPase.
    IPR004582. Checkpoint_prot_Rad17_Rad24.
    IPR018324. Checkpoint_prot_Rad24_fun/met.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PANTHERiPTHR12172. PTHR12172. 1 hit.
    SMARTiSM00382. AAA. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR00602. rad24. 1 hit.

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O75943-1) [UniParc]FASTAAdd to Basket

    Also known as: Rad17Sp, FM2

    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

    MSKTFLRPKV SSTKVTDWVD PSFDDFLECS GVSTITATSL GVNNSSHRRK    50
    NGPSTLESSR FPARKRGNLS SLEQIYGLEN SKEYLSENEP WVDKYKPETQ 100
    HELAVHKKKI EEVETWLKAQ VLERQPKQGG SILLITGPPG CGKTTTLKIL 150
    SKEHGIQVQE WINPVLPDFQ KDDFKGMFNT ESSFHMFPYQ SQIAVFKEFL 200
    LRATKYNKLQ MLGDDLRTDK KIILVEDLPN QFYRDSHTLH EVLRKYVRIG 250
    RCPLIFIISD SLSGDNNQRL LFPKEIQEEC SISNISFNPV APTIMMKFLN 300
    RIVTIEANKN GGKITVPDKT SLELLCQGCS GDIRSAINSL QFSSSKGENN 350
    LRPRKKGMSL KSDAVLSKSK RRKKPDRVFE NQEVQAIGGK DVSLFLFRAL 400
    GKILYCKRAS LTELDSPRLP SHLSEYERDT LLVEPEEVVE MSHMPGDLFN 450
    LYLHQNYIDF FMEIDDIVRA SEFLSFADIL SGDWNTRSLL REYSTSIATR 500
    GVMHSNKARG YAHCQGGGSS FRPLHKPQWF LINKKYRENC LAAKALFPDF 550
    CLPALCLQTQ LLPYLALLTI PMRNQAQISF IQDIGRLPLK RHFGRLKMEA 600
    LTDREHGMID PDSGDEAQLN GGHSAEESLG EPTQATVPET WSLPLSQNSA 650
    SELPASQPQP FSAQGDMEEN IIIEDYESDG T 681
    Length:681
    Mass (Da):77,055
    Last modified:March 29, 2005 - v2
    Checksum:i796C2BD48F7995A3
    GO
    Isoform 2 (identifier: O75943-2) [UniParc]FASTAAdd to Basket

    Also known as: Rad17Sp2, FM1

    The sequence of this isoform differs from the canonical sequence as follows:
         1-14: MSKTFLRPKVSSTK → MNQ

    Show »
    Length:670
    Mass (Da):75,836
    Checksum:i2C8053B065996228
    GO
    Isoform 3 (identifier: O75943-3) [UniParc]FASTAAdd to Basket

    Also known as: FM3

    The sequence of this isoform differs from the canonical sequence as follows:
         1-176: Missing.

    Show »
    Length:505
    Mass (Da):57,244
    Checksum:i3F873BE5F9EF5F85
    GO
    Isoform 4 (identifier: O75943-4) [UniParc]FASTAAdd to Basket

    Also known as: FM4

    The sequence of this isoform differs from the canonical sequence as follows:
         1-97: Missing.
         98-99: ET → MN

    Show »
    Length:584
    Mass (Da):66,156
    Checksum:i54FE8CE0D06C1971
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti75 – 751I → V in CAD97683. (PubMed:17974005)Curated
    Sequence conflicti187 – 1871F → L in AAC36334. (PubMed:9933569)Curated
    Sequence conflicti194 – 1941A → S in AAD01620. (PubMed:10208430)Curated
    Sequence conflicti340 – 3401L → P in AAC36334. (PubMed:9933569)Curated
    Sequence conflicti445 – 4451P → S in AAC36334. (PubMed:9933569)Curated
    Sequence conflicti462 – 4621M → T in AAC36334. (PubMed:9933569)Curated
    Sequence conflicti648 – 6481N → D in AAC36334. (PubMed:9933569)Curated
    Sequence conflicti672 – 6721I → M in AAC36334. (PubMed:9933569)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti32 – 321V → I.1 Publication
    Corresponds to variant rs17229831 [ dbSNP | Ensembl ].
    VAR_021574
    Natural varianti487 – 4871R → L.1 Publication
    Corresponds to variant rs17236478 [ dbSNP | Ensembl ].
    VAR_021575
    Natural varianti535 – 5351K → E.1 Publication
    Corresponds to variant rs17236485 [ dbSNP | Ensembl ].
    VAR_021576
    Natural varianti557 – 5571L → R.3 Publications
    Corresponds to variant rs1045051 [ dbSNP | Ensembl ].
    VAR_021577

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 176176Missing in isoform 3. 1 PublicationVSP_013306Add
    BLAST
    Alternative sequencei1 – 9797Missing in isoform 4. 1 PublicationVSP_013307Add
    BLAST
    Alternative sequencei1 – 1414MSKTF…VSSTK → MNQ in isoform 2. 11 PublicationsVSP_013308Add
    BLAST
    Alternative sequencei98 – 992ET → MN in isoform 4. 1 PublicationVSP_013309

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF076838 mRNA. Translation: AAC95520.1.
    AJ004977 mRNA. Translation: CAA06251.1.
    AF112263 mRNA. Translation: AAD38878.1.
    AF085736 mRNA. Translation: AAC36334.1.
    AJ001642 mRNA. Translation: CAA04894.1.
    AJ131296
    , AJ131297, AJ131298, AJ131299, AJ131300, AJ131301, AJ131302, AJ131303, AJ131304, AJ131305, AJ131306, AJ131307, AJ131308 Genomic DNA. Translation: CAB46364.1.
    AF017748 mRNA. Translation: AAD01620.1.
    AF126424 mRNA. Translation: AAD17334.1.
    AF098533 mRNA. Translation: AAC97950.1.
    AF098534 mRNA. Translation: AAC97951.1.
    AL122068 mRNA. Translation: CAB59244.1.
    AK292487 mRNA. Translation: BAF85176.1.
    BX537441 mRNA. Translation: CAD97683.1.
    AY612854 Genomic DNA. Translation: AAT09763.1.
    CH471137 Genomic DNA. Translation: EAW51283.1.
    CH471137 Genomic DNA. Translation: EAW51284.1.
    CH471137 Genomic DNA. Translation: EAW51285.1.
    CH471137 Genomic DNA. Translation: EAW51286.1.
    CH471137 Genomic DNA. Translation: EAW51288.1.
    BC032304 mRNA. Translation: AAH32304.1.
    CCDSiCCDS4003.1. [O75943-1]
    CCDS4004.1. [O75943-2]
    CCDS4005.1. [O75943-4]
    CCDS47226.1. [O75943-3]
    PIRiT34548.
    RefSeqiNP_001265551.1. NM_001278622.1. [O75943-2]
    NP_002864.1. NM_002873.1. [O75943-2]
    NP_579916.1. NM_133338.2. [O75943-2]
    NP_579917.1. NM_133339.2. [O75943-1]
    NP_579918.1. NM_133340.2. [O75943-3]
    NP_579919.1. NM_133341.2. [O75943-4]
    NP_579920.1. NM_133342.2. [O75943-2]
    NP_579921.1. NM_133343.1. [O75943-2]
    NP_579922.1. NM_133344.2. [O75943-2]
    UniGeneiHs.16184.

    Genome annotation databases

    EnsembliENST00000282891; ENSP00000282891; ENSG00000152942. [O75943-4]
    ENST00000305138; ENSP00000303134; ENSG00000152942. [O75943-2]
    ENST00000345306; ENSP00000311227; ENSG00000152942. [O75943-2]
    ENST00000354312; ENSP00000346271; ENSG00000152942. [O75943-2]
    ENST00000354868; ENSP00000346938; ENSG00000152942. [O75943-2]
    ENST00000358030; ENSP00000350725; ENSG00000152942. [O75943-3]
    ENST00000361732; ENSP00000355226; ENSG00000152942. [O75943-2]
    ENST00000380774; ENSP00000370151; ENSG00000152942. [O75943-1]
    ENST00000509734; ENSP00000426191; ENSG00000152942. [O75943-1]
    ENST00000521422; ENSP00000427743; ENSG00000152942. [O75943-3]
    GeneIDi5884.
    KEGGihsa:5884.
    UCSCiuc003jwg.3. human. [O75943-2]
    uc003jwm.3. human. [O75943-1]
    uc003jwn.3. human. [O75943-4]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF076838 mRNA. Translation: AAC95520.1 .
    AJ004977 mRNA. Translation: CAA06251.1 .
    AF112263 mRNA. Translation: AAD38878.1 .
    AF085736 mRNA. Translation: AAC36334.1 .
    AJ001642 mRNA. Translation: CAA04894.1 .
    AJ131296
    , AJ131297 , AJ131298 , AJ131299 , AJ131300 , AJ131301 , AJ131302 , AJ131303 , AJ131304 , AJ131305 , AJ131306 , AJ131307 , AJ131308 Genomic DNA. Translation: CAB46364.1 .
    AF017748 mRNA. Translation: AAD01620.1 .
    AF126424 mRNA. Translation: AAD17334.1 .
    AF098533 mRNA. Translation: AAC97950.1 .
    AF098534 mRNA. Translation: AAC97951.1 .
    AL122068 mRNA. Translation: CAB59244.1 .
    AK292487 mRNA. Translation: BAF85176.1 .
    BX537441 mRNA. Translation: CAD97683.1 .
    AY612854 Genomic DNA. Translation: AAT09763.1 .
    CH471137 Genomic DNA. Translation: EAW51283.1 .
    CH471137 Genomic DNA. Translation: EAW51284.1 .
    CH471137 Genomic DNA. Translation: EAW51285.1 .
    CH471137 Genomic DNA. Translation: EAW51286.1 .
    CH471137 Genomic DNA. Translation: EAW51288.1 .
    BC032304 mRNA. Translation: AAH32304.1 .
    CCDSi CCDS4003.1. [O75943-1 ]
    CCDS4004.1. [O75943-2 ]
    CCDS4005.1. [O75943-4 ]
    CCDS47226.1. [O75943-3 ]
    PIRi T34548.
    RefSeqi NP_001265551.1. NM_001278622.1. [O75943-2 ]
    NP_002864.1. NM_002873.1. [O75943-2 ]
    NP_579916.1. NM_133338.2. [O75943-2 ]
    NP_579917.1. NM_133339.2. [O75943-1 ]
    NP_579918.1. NM_133340.2. [O75943-3 ]
    NP_579919.1. NM_133341.2. [O75943-4 ]
    NP_579920.1. NM_133342.2. [O75943-2 ]
    NP_579921.1. NM_133343.1. [O75943-2 ]
    NP_579922.1. NM_133344.2. [O75943-2 ]
    UniGenei Hs.16184.

    3D structure databases

    ProteinModelPortali O75943.
    SMRi O75943. Positions 132-158.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111821. 27 interactions.
    DIPi DIP-24254N.
    DIP-34896N.
    IntActi O75943. 7 interactions.
    MINTi MINT-3082919.
    STRINGi 9606.ENSP00000370151.

    PTM databases

    PhosphoSitei O75943.

    Proteomic databases

    MaxQBi O75943.
    PaxDbi O75943.
    PRIDEi O75943.

    Protocols and materials databases

    DNASUi 5884.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000282891 ; ENSP00000282891 ; ENSG00000152942 . [O75943-4 ]
    ENST00000305138 ; ENSP00000303134 ; ENSG00000152942 . [O75943-2 ]
    ENST00000345306 ; ENSP00000311227 ; ENSG00000152942 . [O75943-2 ]
    ENST00000354312 ; ENSP00000346271 ; ENSG00000152942 . [O75943-2 ]
    ENST00000354868 ; ENSP00000346938 ; ENSG00000152942 . [O75943-2 ]
    ENST00000358030 ; ENSP00000350725 ; ENSG00000152942 . [O75943-3 ]
    ENST00000361732 ; ENSP00000355226 ; ENSG00000152942 . [O75943-2 ]
    ENST00000380774 ; ENSP00000370151 ; ENSG00000152942 . [O75943-1 ]
    ENST00000509734 ; ENSP00000426191 ; ENSG00000152942 . [O75943-1 ]
    ENST00000521422 ; ENSP00000427743 ; ENSG00000152942 . [O75943-3 ]
    GeneIDi 5884.
    KEGGi hsa:5884.
    UCSCi uc003jwg.3. human. [O75943-2 ]
    uc003jwm.3. human. [O75943-1 ]
    uc003jwn.3. human. [O75943-4 ]

    Organism-specific databases

    CTDi 5884.
    GeneCardsi GC05P068700.
    HGNCi HGNC:9807. RAD17.
    HPAi CAB004551.
    HPA005448.
    MIMi 603139. gene.
    neXtProti NX_O75943.
    PharmGKBi PA34167.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0470.
    HOVERGENi HBG059834.
    InParanoidi O75943.
    KOi K06662.
    OMAi AQIAFIQ.
    PhylomeDBi O75943.

    Enzyme and pathway databases

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

    Miscellaneous databases

    GeneWikii RAD17.
    GenomeRNAii 5884.
    NextBioi 22866.
    PROi O75943.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O75943.
    Bgeei O75943.
    CleanExi HS_RAD17.
    Genevestigatori O75943.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR003593. AAA+_ATPase.
    IPR004582. Checkpoint_prot_Rad17_Rad24.
    IPR018324. Checkpoint_prot_Rad24_fun/met.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    PANTHERi PTHR12172. PTHR12172. 1 hit.
    SMARTi SM00382. AAA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR00602. rad24. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "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] (ISOFORM 2).
    2. "Identification of a human homologue of the Schizosaccharomyces pombe rad17+ checkpoint gene."
      Parker A.E., Van de Weyer I., Laus M.C., Verhasselt P., Luyten W.H.M.L.
      J. Biol. Chem. 273:18340-18346(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, INTERACTION WITH RAD1.
      Tissue: Neuroblastoma.
    3. Erratum
      Parker A.E., Van de Weyer I., Laus M.C., Verhasselt P., Luyten W.H.M.L.
      J. Biol. Chem. 274:24438-24438(1999)
    4. "HRad17, a human homologue of the Schizosaccharomyces pombe checkpoint gene rad17, is overexpressed in colon carcinoma."
      Bao S., Chang M.-S., Auclair D., Sun Y., Wang Y., Wong W.-K., Zhang J., Liu Y., Qian X., Sutherland R., Magi-Galluzi C., Weisberg E., Cheng E.Y.S., Hao L., Sasaki H., Campbell M.S., Kraeft S.-K., Loda M., Lo K.-M., Chen L.B.
      Cancer Res. 59:2023-2028(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, VARIANT ARG-557.
      Tissue: Fibroblast.
    5. "Human and mouse homologs of the Schizosaccharomyces pombe rad17+ cell cycle checkpoint control gene."
      Bluyssen H.A.R., Naus N.C., van Os R.I., Jaspers I., Hoeijmakers J.H.J., de Klein A.
      Genomics 55:219-228(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING.
      Tissue: Thymus.
    6. "Human and mouse RAD17 genes: identification, localization, genomic structure and histological expression pattern in normal testis and seminoma."
      von Deimling F., Scharf J.M., Liehr T., Rothe M., Kelter A.-R., Albers P., Dietrich W.F., Kunkel L.M., Wernert N., Wirth B.
      Hum. Genet. 105:17-27(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
      Tissue: Fetal brain.
    7. "hRAD17, a structural homolog of the Schizosaccharomyces pombe RAD17 cell cycle checkpoint gene, stimulates p53 accumulation."
      Li L., Peterson C.A., Kanter-Smoler G., Wei Y.-F., Ramagli L.S., Sunnerhagen P., Siciliano M.J., Legerski R.J.
      Oncogene 18:1689-1699(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, FUNCTION.
      Tissue: Cervix carcinoma.
    8. "Human hR24L gene is involved in DNA excision repair and recombination repair."
      Han Y., Zhu Y.
      Zhonghua Yi Xue Za Zhi 79:941-943(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Liver.
    9. "Multiple alternative splicing forms of human RAD17 and their differential response to ionizing radiation."
      Chen M.-S., Higashikubo R., Laszlo A., Roti Roti J.
      Gene 277:145-152(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), INDUCTION, TISSUE SPECIFICITY.
      Tissue: Colon and Fibroblast.
    10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Testis.
    11. "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 2).
      Tissue: Testis.
    12. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Fetal brain.
    13. NIEHS SNPs program
      Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ILE-32; LEU-487; GLU-535 AND ARG-557.
    14. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    15. "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 2), VARIANT ARG-557.
      Tissue: Brain.
    16. "HRad17 colocalizes with NHP2L1 in the nucleolus and redistributes after UV irradiation."
      Chang M.-S., Sasaki H., Campbell M.S., Kraeft S.-K., Sutherland R., Yang C.-Y., Liu Y., Auclair D., Hao L., Sonoda H., Ferland L.H., Chen L.B.
      J. Biol. Chem. 274:36544-36549(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NHP2L1.
    17. "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: INTERACTION WITH THE RAD1/RAD9/HUS1 COMPLEX AND RFC3, MUTAGENESIS OF LYS-143.
    18. "ATR/ATM-mediated phosphorylation of human Rad17 is required for genotoxic stress responses."
      Bao S., Tibbetts R.S., Brumbaugh K.M., Fang Y., Richardson D.A., Ali A., Chen S.M., Abraham R.T., Wang X.-F.
      Nature 411:969-974(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ATM; ATR AND RAD1, PHOSPHORYLATION AT SER-646 AND SER-656, MUTAGENESIS OF SER-646 AND SER-656.
    19. "Purification and characterization of human DNA damage checkpoint Rad complexes."
      Lindsey-Boltz L.A., Bermudez V.P., Hurwitz J., Sancar A.
      Proc. Natl. Acad. Sci. U.S.A. 98:11236-11241(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH RFC2; RFC3; RFC4 AND RFC5.
    20. "Phosphorylation of serines 635 and 645 of human Rad17 is cell cycle regulated and is required for G(1)/S checkpoint activation in response to DNA damage."
      Post S.M., Weng Y.-C., Cimprich K., Chen L.B., Xu Y., Lee E.Y.-H.P.
      Proc. Natl. Acad. Sci. U.S.A. 98:13102-13107(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT SER-646 AND SER-656, INTERACTION WITH RFC4, MUTAGENESIS OF SER-191; SER-646 AND SER-656.
    21. "Regulation of ATR substrate selection by Rad17-dependent loading of Rad9 complexes onto chromatin."
      Zou L., Cortez D., Elledge S.J.
      Genes Dev. 16:198-208(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION, MUTAGENESIS OF LYS-143, SUBCELLULAR LOCATION.
    22. "Colocalization of human Rad17 and PCNA in late S phase of the cell cycle upon replication block."
      Dahm K., Huebscher U.
      Oncogene 21:7710-7719(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH RFC4.
    23. "Genomic instability and endoreduplication triggered by RAD17 deletion."
      Wang X., Zou L., Zheng H., Wei Q., Elledge S.J., Li L.
      Genes Dev. 17:965-970(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    24. "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.
    25. "The human checkpoint Rad protein Rad17 is chromatin-associated throughout the cell cycle, localizes to DNA replication sites, and interacts with DNA polymerase epsilon."
      Post S.M., Tomkinson A.E., Lee E.Y.-H.P.
      Nucleic Acids Res. 31:5568-5575(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT SER-646 AND SER-656, MUTAGENESIS OF SER-646 AND SER-656, INTERACTION WITH POLE.
    26. "Biochemical characterization of DNA damage checkpoint complexes: clamp loader and clamp complexes with specificity for 5' recessed DNA."
      Ellison V., Stillman B.
      PLoS Biol. 1:231-243(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RFC2; RFC3; RFC4 AND RFC5, IDENTIFICATION BY MASS SPECTROMETRY.
    27. "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: FUNCTION, INTERACTION WITH RAD1 AND RAD9.
    28. "Requirement of protein phosphatase 5 in DNA-damage-induced ATM activation."
      Ali A., Zhang J., Bao S., Liu I., Otterness D., Dean N.M., Abraham R.T., Wang X.F.
      Genes Dev. 18:249-254(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PPP5C, PHOSPHORYLATION AT SER-646.
    29. "Interaction between human MCM7 and Rad17 proteins is required for replication checkpoint signaling."
      Tsao C.-C., Geisen C., Abraham R.T.
      EMBO J. 23:4660-4669(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MCM7.
    30. "Chromatin association of rad17 is required for an ataxia telangiectasia and rad-related kinase-mediated S-phase checkpoint in response to low-dose ultraviolet radiation."
      Garg R., Callens S., Lim D.-S., Canman C.E., Kastan M.B., Xu B.
      Mol. Cancer Res. 2:362-369(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF LYS-143; SER-646 AND SER-656.
    31. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    32. "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.

    Entry informationi

    Entry nameiRAD17_HUMAN
    AccessioniPrimary (citable) accession number: O75943
    Secondary accession number(s): A8K8X2
    , D3DWA5, O75714, Q7Z3S4, Q9UNK7, Q9UNR7, Q9UNR8, Q9UPF5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 29, 2005
    Last sequence update: March 29, 2005
    Last modified: October 1, 2014
    This is version 127 of the entry and version 2 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

    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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3