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Database: UniProt
Entry: D3ZXM2_RAT
LinkDB: D3ZXM2_RAT
Original site: D3ZXM2_RAT 
ID   D3ZXM2_RAT              Unreviewed;       392 AA.
AC   D3ZXM2;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   RecName: Full=Cell cycle checkpoint control protein {ECO:0000256|PIRNR:PIRNR009303};
GN   Name=Rad9a {ECO:0000313|Ensembl:ENSRNOP00000025317.4,
GN   ECO:0000313|RGD:2319938};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000025317.4, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000025317.4, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000025317.4,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0007829|PubMed:22673903}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
RN   [3] {ECO:0000313|Ensembl:ENSRNOP00000025317.4}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000025317.4};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the rad9 family. {ECO:0000256|ARBA:ARBA00008494,
CC       ECO:0000256|PIRNR:PIRNR009303}.
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DR   RefSeq; XP_002725812.1; XM_002725766.5.
DR   RefSeq; XP_002728900.1; XM_002728854.5.
DR   AlphaFoldDB; D3ZXM2; -.
DR   SMR; D3ZXM2; -.
DR   STRING; 10116.ENSRNOP00000025317; -.
DR   PhosphoSitePlus; D3ZXM2; -.
DR   PaxDb; 10116-ENSRNOP00000025317; -.
DR   Ensembl; ENSRNOT00000025317.6; ENSRNOP00000025317.4; ENSRNOG00000018729.6.
DR   GeneID; 100361529; -.
DR   KEGG; rno:100361529; -.
DR   UCSC; RGD:2319938; rat.
DR   AGR; RGD:2319938; -.
DR   CTD; 5883; -.
DR   RGD; 2319938; Rad9a.
DR   eggNOG; KOG2810; Eukaryota.
DR   GeneTree; ENSGT00390000005767; -.
DR   HOGENOM; CLU_049242_0_0_1; -.
DR   OMA; YQLHDAL; -.
DR   OrthoDB; 3061362at2759; -.
DR   TreeFam; TF101212; -.
DR   Reactome; R-RNO-176187; Activation of ATR in response to replication stress.
DR   Reactome; R-RNO-5685938; HDR through Single Strand Annealing (SSA).
DR   Reactome; R-RNO-5693607; Processing of DNA double-strand break ends.
DR   Reactome; R-RNO-6804756; Regulation of TP53 Activity through Phosphorylation.
DR   Reactome; R-RNO-69473; G2/M DNA damage checkpoint.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000018729; Expressed in spleen and 18 other cell types or tissues.
DR   GO; GO:0030896; C:checkpoint clamp complex; ISO:RGD.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; ISO:RGD.
DR   GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR   GO; GO:0042826; F:histone deacetylase binding; ISO:RGD.
DR   GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR   GO; GO:0017124; F:SH3 domain binding; ISO:RGD.
DR   GO; GO:0071479; P:cellular response to ionizing radiation; ISO:RGD.
DR   GO; GO:0000077; P:DNA damage checkpoint signaling; ISO:RGD.
DR   GO; GO:0006974; P:DNA damage response; ISO:RGD.
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; ISO:RGD.
DR   GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; ISO:RGD.
DR   GO; GO:1902231; P:positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage; ISO:RGD.
DR   CDD; cd00577; PCNA; 1.
DR   Gene3D; 3.70.10.10; -; 1.
DR   InterPro; IPR046938; DNA_clamp_sf.
DR   InterPro; IPR026584; Rad9.
DR   InterPro; IPR007268; Rad9/Ddc1.
DR   PANTHER; PTHR15237:SF1; CELL CYCLE CHECKPOINT CONTROL PROTEIN RAD9A; 1.
DR   PANTHER; PTHR15237; DNA REPAIR PROTEIN RAD9; 1.
DR   Pfam; PF04139; Rad9; 1.
DR   PIRSF; PIRSF009303; Cell_cycle_RAD9; 1.
DR   SUPFAM; SSF55979; DNA clamp; 1.
PE   1: Evidence at protein level;
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494}.
SQ   SEQUENCE   392 AA;  42850 MW;  2EC3E5F10F4C3D05 CRC64;
     MKCLITGGNV KVLGKAVHSL SRIGDELYLE PLKDGLSLRT VNSSRSAYAC FLFAPLFFQQ
     YQEASPGQDL LRCKILMKSF LSVFRSLATV EKTVEKCCIS LSGSNSHLVV QLHCKYGVKK
     THNLSFQDCE SLQAVFDPAS CPHLLRTPAR VLAEAVLSFP LALTEVTLGI GRGRRVILRS
     YQEEEADSTS KAMVTETSIG EEDFQQLHAP EGRAVTFCLK EFRGLLSFAE SANLPLTIHF
     DVPGRPVIFT VEDSLLDAHF VLATLLEQDS CSQDLCSPKP HQPVPQKQPH STPHSDDFTN
     DDIDCYMIAM ETTVGNESSR AQPSTSLPPV PQASHDLAPP SEEEEEEAEP STVPGTPPPK
     KFRSLFFGSI LAPIHSPQGP NPVLAEDSDG EG
//
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