RAD9A_MOUSE
ID RAD9A_MOUSE Reviewed; 389 AA.
AC Q9Z0F6; Q8QZZ3;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Cell cycle checkpoint control protein RAD9A;
DE Short=mRAD9;
DE EC=3.1.11.2;
DE AltName: Full=DNA repair exonuclease rad9 homolog A;
DE AltName: Full=Rad9-like protein;
GN Name=Rad9a; Synonyms=Rad9;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RX PubMed=9766521;
RX DOI=10.1002/(sici)1097-4652(199811)177:2<241::aid-jcp6>3.0.co;2-n;
RA Hang H., Rauth S.J., Hopkins K.M., Davey S.K., Lieberman H.B.;
RT "Molecular cloning and tissue-specific expression of Mrad9, a murine
RT orthologue of the Schizosaccharomyces pombe rad9+ checkpoint control
RT gene.";
RL J. Cell. Physiol. 177:241-247(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Fetal testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 292-389.
RC STRAIN=AKR/J, C58/J, DBA/2J, FVB/NJ, I/LnJ, MOLF/EiJ, and NZB/BlNJ;
RA Park Y.-G., Lukes L., Yang H., Debies M.T., Samant R.S., Welch D.R.,
RA Lee M., Hunter K.W.;
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INTERACTION WITH ATAD5.
RX PubMed=15983387; DOI=10.1073/pnas.0504222102;
RA Ishii H., Inageta T., Mimori K., Saito T., Sasaki H., Isobe M., Mori M.,
RA Croce C.M., Huebner K., Ozawa K., Furukawa Y.;
RT "Frag1, a homolog of alternative replication factor C subunits, links
RT replication stress surveillance with apoptosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:9655-9660(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-373 AND SER-385, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Component of the 9-1-1 cell-cycle checkpoint response complex
CC that plays a major role in DNA repair. The 9-1-1 complex is recruited
CC to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp
CC loader complex. Acts then as a sliding clamp platform on DNA for
CC several proteins involved in long-patch base excision repair (LP-BER).
CC The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by
CC increasing its affinity for the 3'-OH end of the primer-template and
CC stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1
CC cleavage activity on substrates with double, nick, or gap flaps of
CC distinct sequences and lengths; and DNA ligase I (LIG1) on long-patch
CC base excision repair substrates. The 9-1-1 complex is necessary for the
CC recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring
CC during the S phase. RAD9A possesses 3'->5' double stranded DNA
CC exonuclease activity (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield
CC nucleoside 5'-phosphates.; EC=3.1.11.2;
CC -!- SUBUNIT: Component of the toroidal 9-1-1 (RAD9-RAD1-HUS1) complex,
CC composed of RAD9A, RAD1 and HUS1. The 9-1-1 complex associates with
CC LIG1, POLB, FEN1, RAD17, HDAC1, RPA1 and RPA2. The 9-1-1 complex
CC associates with the RAD17-RFC complex. RAD9A interacts with BCL2L1,
CC FEN1, PRKCD, RAD9B, HUS1, RAD1, ABL1, RPA1 and RPA2. Interacts with
CC DNAJC7 and RHNO1 (By similarity). Interacts with ATAD5. {ECO:0000250,
CC ECO:0000269|PubMed:15983387}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in heart, brain, spleen, lung, liver,
CC skeletal muscle, kidney and testis. {ECO:0000269|PubMed:9766521}.
CC -!- PTM: Constitutively phosphorylated on serine and threonine amino acids
CC in absence of DNA damage. Hyperphosphorylated by PRKCD and ABL1 upon
CC DNA damage. Its phosphorylation by PRKCD may be required for the
CC formation of the 9-1-1 complex (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the rad9 family. {ECO:0000305}.
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DR EMBL; AF045663; AAC77365.1; -; mRNA.
DR EMBL; AF045662; AAC77364.1; -; Genomic_DNA.
DR EMBL; AK134293; BAE22086.1; -; mRNA.
DR EMBL; BC082556; AAH82556.1; -; mRNA.
DR EMBL; AF469747; AAL82448.1; -; Genomic_DNA.
DR EMBL; AF469748; AAL82449.1; -; Genomic_DNA.
DR EMBL; AF469749; AAL82450.1; -; Genomic_DNA.
DR EMBL; AF469750; AAL82451.1; -; Genomic_DNA.
DR EMBL; AF469752; AAL82453.1; -; Genomic_DNA.
DR EMBL; AF469753; AAL82454.1; -; Genomic_DNA.
DR EMBL; AF469751; AAL82452.1; -; Genomic_DNA.
DR CCDS; CCDS29422.1; -.
DR RefSeq; NP_035367.1; NM_011237.2.
DR AlphaFoldDB; Q9Z0F6; -.
DR SMR; Q9Z0F6; -.
DR BioGRID; 202570; 2.
DR STRING; 10090.ENSMUSP00000025740; -.
DR iPTMnet; Q9Z0F6; -.
DR PhosphoSitePlus; Q9Z0F6; -.
DR EPD; Q9Z0F6; -.
DR jPOST; Q9Z0F6; -.
DR MaxQB; Q9Z0F6; -.
DR PaxDb; Q9Z0F6; -.
DR PeptideAtlas; Q9Z0F6; -.
DR PRIDE; Q9Z0F6; -.
DR ProteomicsDB; 255024; -.
DR Antibodypedia; 1880; 1155 antibodies from 38 providers.
DR DNASU; 19367; -.
DR Ensembl; ENSMUST00000025740; ENSMUSP00000025740; ENSMUSG00000024824.
DR GeneID; 19367; -.
DR KEGG; mmu:19367; -.
DR UCSC; uc008fzh.1; mouse.
DR CTD; 5883; -.
DR MGI; MGI:1328356; Rad9a.
DR VEuPathDB; HostDB:ENSMUSG00000024824; -.
DR eggNOG; KOG2810; Eukaryota.
DR GeneTree; ENSGT00390000005767; -.
DR HOGENOM; CLU_049242_0_0_1; -.
DR InParanoid; Q9Z0F6; -.
DR OMA; AMMTEMS; -.
DR OrthoDB; 1176140at2759; -.
DR PhylomeDB; Q9Z0F6; -.
DR TreeFam; TF101212; -.
DR Reactome; R-MMU-176187; Activation of ATR in response to replication stress.
DR Reactome; R-MMU-5685938; HDR through Single Strand Annealing (SSA).
DR Reactome; R-MMU-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-MMU-69473; G2/M DNA damage checkpoint.
DR BioGRID-ORCS; 19367; 34 hits in 105 CRISPR screens.
DR ChiTaRS; Rad9a; mouse.
DR PRO; PR:Q9Z0F6; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q9Z0F6; protein.
DR Bgee; ENSMUSG00000024824; Expressed in undifferentiated genital tubercle and 71 other tissues.
DR ExpressionAtlas; Q9Z0F6; baseline and differential.
DR Genevisible; Q9Z0F6; MM.
DR GO; GO:0030896; C:checkpoint clamp complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0008408; F:3'-5' exonuclease activity; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0008853; F:exodeoxyribonuclease III activity; IEA:UniProtKB-EC.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0017124; F:SH3 domain binding; ISO:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:MGI.
DR GO; GO:0071479; P:cellular response to ionizing radiation; ISO:MGI.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; ISO:MGI.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0000076; P:DNA replication checkpoint signaling; IBA:GO_Central.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IMP:MGI.
DR GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; IGI:MGI.
DR GO; GO:1902231; P:positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage; IMP:MGI.
DR InterPro; IPR026584; Rad9.
DR InterPro; IPR007268; Rad9/Ddc1.
DR PANTHER; PTHR15237; PTHR15237; 1.
DR Pfam; PF04139; Rad9; 1.
DR PIRSF; PIRSF009303; Cell_cycle_RAD9; 1.
PE 1: Evidence at protein level;
KW DNA damage; Exonuclease; Hydrolase; Nuclease; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..389
FT /note="Cell cycle checkpoint control protein RAD9A"
FT /id="PRO_0000225001"
FT REGION 51..91
FT /note="Possesses 3'-5' exonuclease activity"
FT /evidence="ECO:0000250"
FT REGION 266..389
FT /note="Sufficient for interaction with ABL1"
FT /evidence="ECO:0000250"
FT REGION 271..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 312..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 28
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q99638"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99638"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99638"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99638"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
SQ SEQUENCE 389 AA; 42059 MW; 2AE8FF75385C668D CRC64;
MKCLITGGNV KVLGKAVHSL SRIGDELYLE PLKDGLSLRT VNSSRSAYAC FLFAPLFFQQ
YQAASPGQDL LRCKILMKAF LSVFRSLAIV EKSVEKCCIS LSGSHSHLVV QLHCKYGVKK
THNLSFQDCE SLQAVFDPAS CPHLLRTPAR VLAEAVLSFP LALTEVTLGI GRGRRVILRS
YQEEEADSTS KAMVTETSIG DEDFQQLHAP EGIAVTFCLK EFRGLLSFAE SANLPLTIHF
DVPGRPVIFT IEDSLLDAHF VLATLLEQDS CSQGPCSPKP HQPVPQKQAH STPHLDDFTS
DDIDCYMIAM ETTGGNEGSG AQPSTSLPPV SLASHDLAPT SEEEAEPSTV PGTPPPKKFR
SLFFGSILAP VHSPQGPNPV LAEDSDGEG
