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Q99638

- RAD9A_HUMAN

UniProt

Q99638 - RAD9A_HUMAN

Protein

Cell cycle checkpoint control protein RAD9A

Gene

RAD9A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      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. RAD9A possesses 3'->5' double stranded DNA exonuclease activity. Its phosphorylation by PRKCD may be required for the formation of the 9-1-1 complex.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. enzyme binding Source: UniProtKB
    3. exodeoxyribonuclease III activity Source: UniProtKB-EC
    4. histone deacetylase binding Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. protein kinase binding Source: UniProtKB
    7. SH3 domain binding Source: UniProtKB

    GO - Biological processi

    1. cellular response to DNA damage stimulus Source: UniProtKB
    2. cellular response to ionizing radiation Source: UniProtKB
    3. DNA damage checkpoint Source: UniProtKB
    4. DNA repair Source: ProtInc
    5. DNA replication Source: Reactome
    6. DNA replication checkpoint Source: ProtInc
    7. intra-S DNA damage checkpoint Source: Ensembl
    8. nucleic acid phosphodiester bond hydrolysis Source: GOC
    9. positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage Source: Ensembl

    Keywords - Molecular functioni

    Exonuclease, Hydrolase, Nuclease

    Keywords - Biological processi

    DNA damage

    Enzyme and pathway databases

    ReactomeiREACT_6769. Activation of ATR in response to replication stress.
    SignaLinkiQ99638.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cell cycle checkpoint control protein RAD9A (EC:3.1.11.2)
    Short name:
    hRAD9
    Alternative name(s):
    DNA repair exonuclease rad9 homolog A
    Gene namesi
    Name:RAD9A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:9827. RAD9A.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. checkpoint clamp complex Source: InterPro
    2. cytoplasm Source: Ensembl
    3. nucleoplasm Source: Reactome
    4. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi28 – 281Y → F: Abolishes phosphorylation by ABL1. 1 Publication
    Mutagenesisi272 – 2721S → A: Complete loss of phosphorylation and no loss of interaction with the 9-1-1 complex; when associated with A-277; A-328; A-341; A-375; A-380 and A-387. 1 Publication
    Mutagenesisi277 – 2771S → A: Complete loss of phosphorylation and no loss of interaction with the 9-1-1 complex; when associated with A-272; A-328; A-341; A-375; A-380 and A-387. 1 Publication
    Mutagenesisi328 – 3281S → A: Complete loss of phosphorylation and no loss of interaction with the 9-1-1 complex; when associated with A-272; A-277; A-341; A-375; A-380 and A-387. 1 Publication
    Mutagenesisi341 – 3411S → A: Complete loss of phosphorylation and no loss of interaction with the 9-1-1 complex; when associated with A-272; A-277; A-328; A-375; A-380 and A-387. 1 Publication
    Mutagenesisi375 – 3751S → A: Complete loss of phosphorylation and no loss of interaction with the 9-1-1 complex; when associated with A-272; A-277; A-328; A-341; A-380 and A-387. 1 Publication
    Mutagenesisi380 – 3801S → A: Complete loss of phosphorylation and no loss of interaction with the 9-1-1 complex; when associated with A-272; A-277; A-328; A-341; A-375 and A-387. 1 Publication
    Mutagenesisi387 – 3871S → A: Complete loss of phosphorylation and no loss of interaction with the 9-1-1 complex; when associated with A-272; A-277; A-328; A-341; A-375 and A-380. 1 Publication

    Organism-specific databases

    PharmGKBiPA294.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 391391Cell cycle checkpoint control protein RAD9APRO_0000225000Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei28 – 281Phosphotyrosine1 Publication
    Modified residuei272 – 2721Phosphoserine1 Publication
    Modified residuei277 – 2771Phosphoserine4 Publications
    Modified residuei328 – 3281Phosphoserine1 Publication
    Modified residuei341 – 3411Phosphoserine1 Publication
    Modified residuei375 – 3751Phosphoserine4 Publications
    Modified residuei380 – 3801Phosphoserine2 Publications
    Modified residuei387 – 3871Phosphoserine6 Publications

    Post-translational modificationi

    Constitutively phosphorylated on serine and threonine amino acids in absence of DNA damage. Hyperphosphorylated by PRKCD and ABL1 upon DNA damage. Its phosphorylation by PRKCD may be required for the formation of the 9-1-1 complex.8 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ99638.
    PaxDbiQ99638.
    PeptideAtlasiQ99638.
    PRIDEiQ99638.

    PTM databases

    PhosphoSiteiQ99638.

    Expressioni

    Gene expression databases

    ArrayExpressiQ99638.
    BgeeiQ99638.
    CleanExiHS_RAD9A.
    GenevestigatoriQ99638.

    Organism-specific databases

    HPAiHPA006725.
    HPA048155.

    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. RAD9A interacts with BCL2L1, FEN1, PRKCD, RAD9B, HUS1, RAD1, ABL1, RPA1, ATAD5 and RPA2. Interacts with DNAJC7 and RHNO1.14 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HUS1O609215EBI-2606224,EBI-1056174
    RAD1O606712EBI-2606224,EBI-721835

    Protein-protein interaction databases

    BioGridi111820. 27 interactions.
    DIPiDIP-24255N.
    DIP-40930N.
    IntActiQ99638. 7 interactions.
    MINTiMINT-134869.
    STRINGi9606.ENSP00000311360.

    Structurei

    Secondary structure

    1
    391
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 65
    Helixi8 – 2114
    Beta strandi25 – 328
    Beta strandi35 – 417
    Beta strandi47 – 537
    Helixi55 – 573
    Beta strandi58 – 625
    Beta strandi66 – 683
    Beta strandi73 – 764
    Helixi77 – 848
    Helixi87 – 937
    Beta strandi94 – 1007
    Beta strandi106 – 1149
    Helixi115 – 1173
    Beta strandi119 – 1257
    Helixi138 – 1403
    Beta strandi142 – 1487
    Helixi149 – 1568
    Beta strandi165 – 1706
    Helixi172 – 1743
    Beta strandi176 – 1816
    Beta strandi187 – 1893
    Beta strandi194 – 1996
    Helixi201 – 2033
    Beta strandi205 – 2084
    Beta strandi214 – 2185
    Helixi219 – 23113
    Beta strandi235 – 2406
    Beta strandi241 – 2455
    Beta strandi247 – 2526
    Beta strandi254 – 2629
    Beta strandi267 – 2693

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3A1JX-ray2.50A1-266[»]
    3G65X-ray2.90A1-270[»]
    3GGRX-ray3.20A1-270[»]
    ProteinModelPortaliQ99638.
    SMRiQ99638. Positions 1-266.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ99638.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni51 – 9141Possesses 3'-5' exonuclease activityAdd
    BLAST
    Regioni266 – 391126Sufficient for interaction with ABL1Add
    BLAST

    Sequence similaritiesi

    Belongs to the rad9 family.Curated

    Phylogenomic databases

    eggNOGiNOG236850.
    HOGENOMiHOG000059650.
    HOVERGENiHBG058989.
    InParanoidiQ99638.
    KOiK10994.
    OMAiVILRSYQ.
    OrthoDBiEOG70PBXW.
    PhylomeDBiQ99638.
    TreeFamiTF101212.

    Family and domain databases

    InterProiIPR026584. Rad9.
    IPR007268. Rad9/Ddc1.
    [Graphical view]
    PANTHERiPTHR15237. PTHR15237. 1 hit.
    PfamiPF04139. Rad9. 1 hit.
    [Graphical view]
    PIRSFiPIRSF009303. Cell_cycle_RAD9. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q99638-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKCLVTGGNV KVLGKAVHSL SRIGDELYLE PLEDGLSLRT VNSSRSAYAC    50
    FLFAPLFFQQ YQAATPGQDL LRCKILMKSF LSVFRSLAML EKTVEKCCIS 100
    LNGRSSRLVV QLHCKFGVRK THNLSFQDCE SLQAVFDPAS CPHMLRAPAR 150
    VLGEAVLPFS PALAEVTLGI GRGRRVILRS YHEEEADSTA KAMVTEMCLG 200
    EEDFQQLQAQ EGVAITFCLK EFRGLLSFAE SANLNLSIHF DAPGRPAIFT 250
    IKDSLLDGHF VLATLSDTDS HSQDLGSPER HQPVPQLQAH STPHPDDFAN 300
    DDIDSYMIAM ETTIGNEGSR VLPSISLSPG PQPPKSPGPH SEEEDEAEPS 350
    TVPGTPPPKK FRSLFFGSIL APVRSPQGPS PVLAEDSEGE G 391
    Length:391
    Mass (Da):42,547
    Last modified:May 1, 1997 - v1
    Checksum:i4D4D6D4C6E1057D3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti12 – 121V → A in CAG38746. 1 PublicationCurated
    Sequence conflicti130 – 1301E → A in AAH14848. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti3 – 31C → F.1 Publication
    VAR_025410
    Natural varianti71 – 711L → Q.
    Corresponds to variant rs2422490 [ dbSNP | Ensembl ].
    VAR_051724
    Natural varianti100 – 1001S → A.1 Publication
    Corresponds to variant rs2066492 [ dbSNP | Ensembl ].
    VAR_025411
    Natural varianti239 – 2391H → R.1 Publication
    Corresponds to variant rs17880039 [ dbSNP | Ensembl ].
    VAR_025412
    Natural varianti307 – 3071M → T.1 Publication
    Corresponds to variant rs17882466 [ dbSNP | Ensembl ].
    VAR_025413

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U53174 mRNA. Translation: AAB39928.1.
    CR536508 mRNA. Translation: CAG38746.1.
    AY766122 Genomic DNA. Translation: AAU89725.1.
    AK315348 mRNA. Translation: BAG37745.1.
    CH471076 Genomic DNA. Translation: EAW74605.1.
    BC014848 mRNA. Translation: AAH14848.1.
    CCDSiCCDS8159.1.
    RefSeqiNP_001230153.1. NM_001243224.1.
    NP_004575.1. NM_004584.2.
    UniGeneiHs.655354.

    Genome annotation databases

    EnsembliENST00000307980; ENSP00000311360; ENSG00000172613.
    GeneIDi5883.
    KEGGihsa:5883.
    UCSCiuc001okr.3. human.

    Polymorphism databases

    DMDMi74717382.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs
    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U53174 mRNA. Translation: AAB39928.1 .
    CR536508 mRNA. Translation: CAG38746.1 .
    AY766122 Genomic DNA. Translation: AAU89725.1 .
    AK315348 mRNA. Translation: BAG37745.1 .
    CH471076 Genomic DNA. Translation: EAW74605.1 .
    BC014848 mRNA. Translation: AAH14848.1 .
    CCDSi CCDS8159.1.
    RefSeqi NP_001230153.1. NM_001243224.1.
    NP_004575.1. NM_004584.2.
    UniGenei Hs.655354.

    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 A 1-266 [» ]
    3G65 X-ray 2.90 A 1-270 [» ]
    3GGR X-ray 3.20 A 1-270 [» ]
    ProteinModelPortali Q99638.
    SMRi Q99638. Positions 1-266.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111820. 27 interactions.
    DIPi DIP-24255N.
    DIP-40930N.
    IntActi Q99638. 7 interactions.
    MINTi MINT-134869.
    STRINGi 9606.ENSP00000311360.

    PTM databases

    PhosphoSitei Q99638.

    Polymorphism databases

    DMDMi 74717382.

    Proteomic databases

    MaxQBi Q99638.
    PaxDbi Q99638.
    PeptideAtlasi Q99638.
    PRIDEi Q99638.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000307980 ; ENSP00000311360 ; ENSG00000172613 .
    GeneIDi 5883.
    KEGGi hsa:5883.
    UCSCi uc001okr.3. human.

    Organism-specific databases

    CTDi 5883.
    GeneCardsi GC11P067159.
    HGNCi HGNC:9827. RAD9A.
    HPAi HPA006725.
    HPA048155.
    MIMi 603761. gene.
    neXtProti NX_Q99638.
    PharmGKBi PA294.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG236850.
    HOGENOMi HOG000059650.
    HOVERGENi HBG058989.
    InParanoidi Q99638.
    KOi K10994.
    OMAi VILRSYQ.
    OrthoDBi EOG70PBXW.
    PhylomeDBi Q99638.
    TreeFami TF101212.

    Enzyme and pathway databases

    Reactomei REACT_6769. Activation of ATR in response to replication stress.
    SignaLinki Q99638.

    Miscellaneous databases

    ChiTaRSi RAD9A. human.
    EvolutionaryTracei Q99638.
    GeneWikii RAD9A.
    GenomeRNAii 5883.
    NextBioi 22862.
    PROi Q99638.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q99638.
    Bgeei Q99638.
    CleanExi HS_RAD9A.
    Genevestigatori Q99638.

    Family and domain databases

    InterProi IPR026584. Rad9.
    IPR007268. Rad9/Ddc1.
    [Graphical view ]
    PANTHERi PTHR15237. PTHR15237. 1 hit.
    Pfami PF04139. Rad9. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF009303. Cell_cycle_RAD9. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "A human homolog of the Schizosaccharomyces pombe rad9+ checkpoint control gene."
      Lieberman H.B., Hopkins K.M., Nass M., Demetrick D., Davey S.
      Proc. Natl. Acad. Sci. U.S.A. 93:13890-13895(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. NIEHS SNPs program
      Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS PHE-3; ALA-100; ARG-239 AND THR-307.
    4. "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].
      Tissue: Trachea.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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].
      Tissue: Testis.
    7. "Phosphorylation of human Rad9 is required for genotoxin-activated checkpoint signaling."
      Roos-Mattjus P., Hopkins K.M., Oestreich A.J., Vroman B.T., Johnson K.L., Naylor S., Lieberman H.B., Karnitz L.M.
      J. Biol. Chem. 278:24428-24437(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 270-280; 326-329; 373-383 AND 385-390, IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT SER-272; SER-277; SER-328; SER-341; SER-375; SER-380 AND SER-387, MUTAGENESIS OF SER-272; SER-277; SER-328; SER-341; SER-375; SER-380 AND SER-387.
    8. "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 RAD1.
    9. "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 RAD1.
    10. "Human DNA damage checkpoint protein hRAD9 is a 3' to 5' exonuclease."
      Bessho T., Sancar A.
      J. Biol. Chem. 275:7451-7454(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN EXONUCLEASE ACTIVITY.
    11. "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.
    12. "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.
    13. "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.
    14. "c-Abl tyrosine kinase regulates the human Rad9 checkpoint protein in response to DNA damage."
      Yoshida K., Komatsu K., Wang H.-G., Kufe D.
      Mol. Cell. Biol. 22:3292-3300(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ABL1 AND BCL2L1, PHOSPHORYLATION, PHOSPHORYLATION AT TYR-28, MUTAGENESIS OF TYR-28.
    15. "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.
    16. "Protein kinase Cdelta is responsible for constitutive and DNA damage-induced phosphorylation of Rad9."
      Yoshida K., Wang H.-G., Miki Y., Kufe D.
      EMBO J. 22:1431-1441(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PRKCD, PHOSPHORYLATION, SUBCELLULAR LOCATION.
    17. "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.
    18. "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.
    19. Cited for: IDENTIFICATION IN THE 9-1-1 COMPLEX ASSOCIATED WITH FEN1.
    20. "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.
    21. "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.
    22. "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, INTERACTION WITH RPA1 AND RPA2.
    23. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375; SER-380 AND SER-387, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    24. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277 AND SER-387, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    25. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277; SER-375 AND SER-387, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    27. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277; SER-375 AND SER-387, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    28. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    29. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387, 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, INTERACTION WITH RHNO1, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiRAD9A_HUMAN
    AccessioniPrimary (citable) accession number: Q99638
    Secondary accession number(s): B2RCZ8, Q6FI29, Q96C41
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 7, 2006
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 105 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: 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