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Q9Z0F6

- RAD9A_MOUSE

UniProt

Q9Z0F6 - RAD9A_MOUSE

Protein

Cell cycle checkpoint control protein RAD9A

Gene

Rad9a

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      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 By similarity.By similarity

    Catalytic activityi

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

    GO - Molecular functioni

    1. 3'-5' exonuclease activity Source: Ensembl
    2. exodeoxyribonuclease III activity Source: UniProtKB-EC
    3. protein binding Source: MGI

    GO - Biological processi

    1. cellular response to ionizing radiation Source: Ensembl
    2. DNA repair Source: InterPro
    3. intra-S DNA damage checkpoint Source: MGI
    4. positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage Source: MGI

    Keywords - Molecular functioni

    Exonuclease, Hydrolase, Nuclease

    Keywords - Biological processi

    DNA damage

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cell cycle checkpoint control protein RAD9A (EC:3.1.11.2)
    Short name:
    mRAD9
    Alternative name(s):
    DNA repair exonuclease rad9 homolog A
    Rad9-like protein
    Gene namesi
    Name:Rad9a
    Synonyms:Rad9
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 19

    Organism-specific databases

    MGIiMGI:1328356. Rad9a.

    Subcellular locationi

    Nucleus By similarity

    GO - Cellular componenti

    1. checkpoint clamp complex Source: InterPro
    2. cytoplasm Source: MGI
    3. nucleus Source: MGI

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 389389Cell cycle checkpoint control protein RAD9APRO_0000225001Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei28 – 281PhosphotyrosineBy similarity
    Modified residuei272 – 2721PhosphoserineBy similarity
    Modified residuei277 – 2771PhosphoserineBy similarity
    Modified residuei341 – 3411PhosphoserineBy similarity
    Modified residuei373 – 3731PhosphoserineBy similarity
    Modified residuei385 – 3851Phosphoserine1 Publication

    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 By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiQ9Z0F6.

    PTM databases

    PhosphoSiteiQ9Z0F6.

    Expressioni

    Tissue specificityi

    Expressed in heart, brain, spleen, lung, liver, skeletal muscle, kidney and testis.1 Publication

    Gene expression databases

    BgeeiQ9Z0F6.
    CleanExiMM_RAD9.
    GenevestigatoriQ9Z0F6.

    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 and RPA2. Interacts with DNAJC7 and RHNO1 By similarity. Interacts with ATAD5.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi202570. 2 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Z0F6.
    SMRiQ9Z0F6. Positions 1-265.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni51 – 9141Possesses 3'-5' exonuclease activityBy similarityAdd
    BLAST
    Regioni266 – 389124Sufficient for interaction with ABL1By similarityAdd
    BLAST

    Sequence similaritiesi

    Belongs to the rad9 family.Curated

    Phylogenomic databases

    eggNOGiNOG236850.
    GeneTreeiENSGT00390000005767.
    HOGENOMiHOG000059650.
    HOVERGENiHBG058989.
    InParanoidiQ9Z0F6.
    KOiK10994.
    OMAiVILRSYQ.
    OrthoDBiEOG70PBXW.
    PhylomeDBiQ9Z0F6.
    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.

    Q9Z0F6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKCLITGGNV KVLGKAVHSL SRIGDELYLE PLKDGLSLRT VNSSRSAYAC    50
    FLFAPLFFQQ YQAASPGQDL LRCKILMKAF LSVFRSLAIV EKSVEKCCIS 100
    LSGSHSHLVV QLHCKYGVKK THNLSFQDCE SLQAVFDPAS CPHLLRTPAR 150
    VLAEAVLSFP LALTEVTLGI GRGRRVILRS YQEEEADSTS KAMVTETSIG 200
    DEDFQQLHAP EGIAVTFCLK EFRGLLSFAE SANLPLTIHF DVPGRPVIFT 250
    IEDSLLDAHF VLATLLEQDS CSQGPCSPKP HQPVPQKQAH STPHLDDFTS 300
    DDIDCYMIAM ETTGGNEGSG AQPSTSLPPV SLASHDLAPT SEEEAEPSTV 350
    PGTPPPKKFR SLFFGSILAP VHSPQGPNPV LAEDSDGEG 389
    Length:389
    Mass (Da):42,059
    Last modified:May 1, 1999 - v1
    Checksum:i2AE8FF75385C668D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF045663 mRNA. Translation: AAC77365.1.
    AF045662 Genomic DNA. Translation: AAC77364.1.
    AK134293 mRNA. Translation: BAE22086.1.
    BC082556 mRNA. Translation: AAH82556.1.
    AF469747 Genomic DNA. Translation: AAL82448.1.
    AF469748 Genomic DNA. Translation: AAL82449.1.
    AF469749 Genomic DNA. Translation: AAL82450.1.
    AF469750 Genomic DNA. Translation: AAL82451.1.
    AF469752 Genomic DNA. Translation: AAL82453.1.
    AF469753 Genomic DNA. Translation: AAL82454.1.
    AF469751 Genomic DNA. Translation: AAL82452.1.
    CCDSiCCDS29422.1.
    RefSeqiNP_035367.1. NM_011237.2.
    UniGeneiMm.277629.

    Genome annotation databases

    EnsembliENSMUST00000025740; ENSMUSP00000025740; ENSMUSG00000024824.
    ENSMUST00000181329; ENSMUSP00000137976; ENSMUSG00000097909.
    GeneIDi19367.
    KEGGimmu:19367.
    UCSCiuc008fzh.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF045663 mRNA. Translation: AAC77365.1 .
    AF045662 Genomic DNA. Translation: AAC77364.1 .
    AK134293 mRNA. Translation: BAE22086.1 .
    BC082556 mRNA. Translation: AAH82556.1 .
    AF469747 Genomic DNA. Translation: AAL82448.1 .
    AF469748 Genomic DNA. Translation: AAL82449.1 .
    AF469749 Genomic DNA. Translation: AAL82450.1 .
    AF469750 Genomic DNA. Translation: AAL82451.1 .
    AF469752 Genomic DNA. Translation: AAL82453.1 .
    AF469753 Genomic DNA. Translation: AAL82454.1 .
    AF469751 Genomic DNA. Translation: AAL82452.1 .
    CCDSi CCDS29422.1.
    RefSeqi NP_035367.1. NM_011237.2.
    UniGenei Mm.277629.

    3D structure databases

    ProteinModelPortali Q9Z0F6.
    SMRi Q9Z0F6. Positions 1-265.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202570. 2 interactions.

    PTM databases

    PhosphoSitei Q9Z0F6.

    Proteomic databases

    PRIDEi Q9Z0F6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000025740 ; ENSMUSP00000025740 ; ENSMUSG00000024824 .
    ENSMUST00000181329 ; ENSMUSP00000137976 ; ENSMUSG00000097909 .
    GeneIDi 19367.
    KEGGi mmu:19367.
    UCSCi uc008fzh.1. mouse.

    Organism-specific databases

    CTDi 5883.
    MGIi MGI:1328356. Rad9a.

    Phylogenomic databases

    eggNOGi NOG236850.
    GeneTreei ENSGT00390000005767.
    HOGENOMi HOG000059650.
    HOVERGENi HBG058989.
    InParanoidi Q9Z0F6.
    KOi K10994.
    OMAi VILRSYQ.
    OrthoDBi EOG70PBXW.
    PhylomeDBi Q9Z0F6.
    TreeFami TF101212.

    Miscellaneous databases

    ChiTaRSi RAD9A. mouse.
    NextBioi 296445.
    PROi Q9Z0F6.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9Z0F6.
    CleanExi MM_RAD9.
    Genevestigatori Q9Z0F6.

    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. "Molecular cloning and tissue-specific expression of Mrad9, a murine orthologue of the Schizosaccharomyces pombe rad9+ checkpoint control gene."
      Hang H., Rauth S.J., Hopkins K.M., Davey S.K., Lieberman H.B.
      J. Cell. Physiol. 177:241-247(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Fetal testis.
    3. "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].
      Strain: C57BL/6.
      Tissue: Eye.
    4. Park Y.-G., Lukes L., Yang H., Debies M.T., Samant R.S., Welch D.R., Lee M., Hunter K.W.
      Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 292-389.
      Strain: AKR/J, C58/J, DBA/2J, FVB/NJ, I/LnJ, MOLF/Ei and NZB/BlNJ.
    5. "Frag1, a homolog of alternative replication factor C subunits, links replication stress surveillance with apoptosis."
      Ishii H., Inageta T., Mimori K., Saito T., Sasaki H., Isobe M., Mori M., Croce C.M., Huebner K., Ozawa K., Furukawa Y.
      Proc. Natl. Acad. Sci. U.S.A. 102:9655-9660(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ATAD5.
    6. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiRAD9A_MOUSE
    AccessioniPrimary (citable) accession number: Q9Z0F6
    Secondary accession number(s): Q8QZZ3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 7, 2006
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 88 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3