RAD9A_HUMAN
ID RAD9A_HUMAN Reviewed; 391 AA.
AC Q99638; B2RCZ8; Q6FI29; Q96C41;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Cell cycle checkpoint control protein RAD9A;
DE Short=hRAD9;
DE EC=3.1.11.2;
DE AltName: Full=DNA repair exonuclease rad9 homolog A;
GN Name=RAD9A;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8943031; DOI=10.1073/pnas.93.24.13890;
RA Lieberman H.B., Hopkins K.M., Nass M., Demetrick D., Davey S.;
RT "A human homolog of the Schizosaccharomyces pombe rad9+ checkpoint control
RT gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:13890-13895(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS PHE-3; ALA-100; ARG-239 AND
RP THR-307.
RG NIEHS SNPs program;
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [7]
RP PROTEIN SEQUENCE OF 270-280; 326-329; 373-383 AND 385-390, IDENTIFICATION
RP BY MASS SPECTROMETRY, PHOSPHORYLATION AT SER-272; SER-277; SER-328;
RP SER-341; SER-375; SER-380 AND SER-387, AND MUTAGENESIS OF SER-272; SER-277;
RP SER-328; SER-341; SER-375; SER-380 AND SER-387.
RX PubMed=12709442; DOI=10.1074/jbc.m301544200;
RA Roos-Mattjus P., Hopkins K.M., Oestreich A.J., Vroman B.T., Johnson K.L.,
RA Naylor S., Lieberman H.B., Karnitz L.M.;
RT "Phosphorylation of human Rad9 is required for genotoxin-activated
RT checkpoint signaling.";
RL J. Biol. Chem. 278:24428-24437(2003).
RN [8]
RP INTERACTION WITH HUS1 AND RAD1.
RX PubMed=10359610; DOI=10.1091/mbc.10.6.1985;
RA St Onge R.P., Udell C.M., Casselman R., Davey S.;
RT "The human G2 checkpoint control protein hRAD9 is a nuclear phosphoprotein
RT that forms complexes with hRAD1 and hHUS1.";
RL Mol. Biol. Cell 10:1985-1995(1999).
RN [9]
RP INTERACTION WITH HUS1 AND RAD1.
RX PubMed=10777662; DOI=10.1006/geno.2000.6142;
RA Hang H., Lieberman H.B.;
RT "Physical interaction among human checkpoint control proteins HUS1p, RAD1p,
RT and RAD9p, and implications for the regulation of cell cycle progression.";
RL Genomics 65:24-33(2000).
RN [10]
RP FUNCTION IN EXONUCLEASE ACTIVITY.
RX PubMed=10713044; DOI=10.1074/jbc.275.11.7451;
RA Bessho T., Sancar A.;
RT "Human DNA damage checkpoint protein hRAD9 is a 3' to 5' exonuclease.";
RL J. Biol. Chem. 275:7451-7454(2000).
RN [11]
RP IDENTIFICATION IN THE 9-1-1 COMPLEX ASSOCIATED WITH HDAC1.
RX PubMed=10846170; DOI=10.1074/jbc.m000168200;
RA Cai R.L., Yan-Neale Y., Cueto M.A., Xu H., Cohen D.;
RT "HDAC1, a histone deacetylase, forms a complex with Hus1 and Rad9, two G2/M
RT checkpoint Rad proteins.";
RL J. Biol. Chem. 275:27909-27916(2000).
RN [12]
RP IDENTIFICATION IN THE 9-1-1 COMPLEX ASSOCIATED WITH RAD17.
RX PubMed=10884395; DOI=10.1074/jbc.m005782200;
RA Rauen M., Burtelow M.A., Dufault V.M., Karnitz L.M.;
RT "The human checkpoint protein hRad17 interacts with the PCNA-like proteins
RT hRad1, hHus1, and hRad9.";
RL J. Biol. Chem. 275:29767-29771(2000).
RN [13]
RP INTERACTION WITH DNAJC7.
RX PubMed=11573955; DOI=10.1006/bbrc.2001.5685;
RA Xiang S.L., Kumano T., Iwasaki S.I., Sun X., Yoshioka K., Yamamoto K.C.;
RT "The J domain of Tpr2 regulates its interaction with the proapoptotic and
RT cell-cycle checkpoint protein, Rad9.";
RL Biochem. Biophys. Res. Commun. 287:932-940(2001).
RN [14]
RP INTERACTION WITH ABL1 AND BCL2L1, PHOSPHORYLATION, PHOSPHORYLATION AT
RP TYR-28, AND MUTAGENESIS OF TYR-28.
RX PubMed=11971963; DOI=10.1128/mcb.22.10.3292-3300.2002;
RA Yoshida K., Komatsu K., Wang H.-G., Kufe D.;
RT "c-Abl tyrosine kinase regulates the human Rad9 checkpoint protein in
RT response to DNA damage.";
RL Mol. Cell. Biol. 22:3292-3300(2002).
RN [15]
RP INTERACTION WITH RAD9B.
RX PubMed=14500360;
RA Hopkins K.M., Wang X., Berlin A., Hang H., Thaker H.M., Lieberman H.B.;
RT "Expression of mammalian paralogues of HRAD9 and Mrad9 checkpoint control
RT genes in normal and cancerous testicular tissue.";
RL Cancer Res. 63:5291-5298(2003).
RN [16]
RP INTERACTION WITH PRKCD, PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=12628935; DOI=10.1093/emboj/cdg134;
RA Yoshida K., Wang H.-G., Miki Y., Kufe D.;
RT "Protein kinase Cdelta is responsible for constitutive and DNA damage-
RT induced phosphorylation of Rad9.";
RL EMBO J. 22:1431-1441(2003).
RN [17]
RP ASSOCIATION OF THE 9-1-1 COMPLEX WITH THE RAD17-RFC COMPLEX, AND ELECTRON
RP MICROSCOPY OF THE 9-1-1 AND RAD17-RFC COMPLEXES BOUND TO DNA.
RX PubMed=12578958; DOI=10.1073/pnas.0437927100;
RA Bermudez V.P., Lindsey-Boltz L.A., Cesare A.J., Maniwa Y., Griffith J.D.,
RA Hurwitz J., Sancar A.;
RT "Loading of the human 9-1-1 checkpoint complex onto DNA by the checkpoint
RT clamp loader hRad17-replication factor C complex in vitro.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1633-1638(2003).
RN [18]
RP IDENTIFICATION IN THE 9-1-1 COMPLEX ASSOCIATED WITH POLB.
RX PubMed=15314187; DOI=10.1093/nar/gkh652;
RA Toueille M., El-Andaloussi N., Frouin I., Freire R., Funk D., Shevelev I.,
RA Friedrich-Heineken E., Villani G., Hottiger M.O., Huebscher U.;
RT "The human Rad9/Rad1/Hus1 damage sensor clamp interacts with DNA polymerase
RT beta and increases its DNA substrate utilisation efficiency: implications
RT for DNA repair.";
RL Nucleic Acids Res. 32:3316-3324(2004).
RN [19]
RP IDENTIFICATION IN THE 9-1-1 COMPLEX ASSOCIATED WITH FEN1.
RX PubMed=15556996; DOI=10.1073/pnas.0407686101;
RA Wang W., Brandt P., Rossi M.L., Lindsey-Boltz L., Podust V., Fanning E.,
RA Sancar A., Bambara R.A.;
RT "The human Rad9-Rad1-Hus1 checkpoint complex stimulates flap endonuclease
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:16762-16767(2004).
RN [20]
RP IDENTIFICATION IN THE 9-1-1 COMPLEX ASSOCIATED WITH LIG1.
RX PubMed=15871698; DOI=10.1042/bj20050211;
RA Smirnova E., Toueille M., Markkanen E., Huebscher U.;
RT "The human checkpoint sensor and alternative DNA clamp Rad9-Rad1-Hus1
RT modulates the activity of DNA ligase I, a component of the long-patch base
RT excision repair machinery.";
RL Biochem. J. 389:13-17(2005).
RN [21]
RP IDENTIFICATION IN THE 9-1-1 COMPLEX ASSOCIATED WITH FEN1, AND INTERACTION
RP WITH FEN1.
RX PubMed=16216273; DOI=10.1016/j.jmb.2005.09.018;
RA Friedrich-Heineken E., Toueille M., Taennler B., Buerki C., Ferrari E.,
RA Hottiger M.O., Huebscher U.;
RT "The two DNA clamps Rad9/Rad1/Hus1 complex and proliferating cell nuclear
RT antigen differentially regulate flap endonuclease 1 activity.";
RL J. Mol. Biol. 353:980-989(2005).
RN [22]
RP IDENTIFICATION IN THE 9-1-1 COMPLEX ASSOCIATED WITH RPA1 AND RPA2, AND
RP INTERACTION WITH RPA1 AND RPA2.
RX PubMed=15897895; DOI=10.1038/sj.onc.1208674;
RA Wu X., Shell S.M., Zou Y.;
RT "Interaction and colocalization of Rad9/Rad1/Hus1 checkpoint complex with
RT replication protein A in human cells.";
RL Oncogene 24:4728-4735(2005).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375; SER-380 AND SER-387, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277 AND SER-387, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [25]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277; SER-375 AND SER-387, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277; SER-375 AND SER-387, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [28]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [30]
RP FUNCTION, INTERACTION WITH RHNO1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=21659603; DOI=10.1126/science.1203430;
RA Cotta-Ramusino C., McDonald E.R. III, Hurov K., Sowa M.E., Harper J.W.,
RA Elledge S.J.;
RT "A DNA damage response screen identifies RHINO, a 9-1-1 and TopBP1
RT interacting protein required for ATR signaling.";
RL Science 332:1313-1317(2011).
RN [31]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328 AND SER-387, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [32]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
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. Its phosphorylation by PRKCD may be required for
CC the formation of the 9-1-1 complex. {ECO:0000269|PubMed:10713044,
CC ECO:0000269|PubMed:21659603}.
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, ATAD5 and RPA2. Interacts
CC with DNAJC7 and RHNO1. {ECO:0000269|PubMed:10359610,
CC ECO:0000269|PubMed:10777662, ECO:0000269|PubMed:10846170,
CC ECO:0000269|PubMed:10884395, ECO:0000269|PubMed:11573955,
CC ECO:0000269|PubMed:11971963, ECO:0000269|PubMed:12628935,
CC ECO:0000269|PubMed:14500360, ECO:0000269|PubMed:15314187,
CC ECO:0000269|PubMed:15556996, ECO:0000269|PubMed:15871698,
CC ECO:0000269|PubMed:15897895, ECO:0000269|PubMed:16216273,
CC ECO:0000269|PubMed:21659603}.
CC -!- INTERACTION:
CC Q99638; O60921: HUS1; NbExp=13; IntAct=EBI-2606224, EBI-1056174;
CC Q99638; O60671: RAD1; NbExp=2; IntAct=EBI-2606224, EBI-721835;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12628935}.
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. {ECO:0000269|PubMed:11971963,
CC ECO:0000269|PubMed:12628935, ECO:0000269|PubMed:12709442}.
CC -!- SIMILARITY: Belongs to the rad9 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/rad9a/";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/RAD9AID42031ch11q13.html";
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DR EMBL; U53174; AAB39928.1; -; mRNA.
DR EMBL; CR536508; CAG38746.1; -; mRNA.
DR EMBL; AY766122; AAU89725.1; -; Genomic_DNA.
DR EMBL; AK315348; BAG37745.1; -; mRNA.
DR EMBL; CH471076; EAW74605.1; -; Genomic_DNA.
DR EMBL; BC014848; AAH14848.1; -; mRNA.
DR CCDS; CCDS8159.1; -.
DR RefSeq; NP_001230153.1; NM_001243224.1.
DR RefSeq; NP_004575.1; NM_004584.2.
DR PDB; 3A1J; X-ray; 2.50 A; A=1-266.
DR PDB; 3G65; X-ray; 2.90 A; A=1-270.
DR PDB; 3GGR; X-ray; 3.20 A; A=1-270.
DR PDB; 6HM5; X-ray; 2.33 A; B=380-390.
DR PDB; 6J8Y; X-ray; 2.40 A; A=1-270.
DR PDBsum; 3A1J; -.
DR PDBsum; 3G65; -.
DR PDBsum; 3GGR; -.
DR PDBsum; 6HM5; -.
DR PDBsum; 6J8Y; -.
DR AlphaFoldDB; Q99638; -.
DR SMR; Q99638; -.
DR BioGRID; 111820; 63.
DR ComplexPortal; CPX-1829; Checkpoint clamp complex.
DR CORUM; Q99638; -.
DR DIP; DIP-24255N; -.
DR DIP; DIP-40930N; -.
DR IntAct; Q99638; 10.
DR MINT; Q99638; -.
DR STRING; 9606.ENSP00000311360; -.
DR iPTMnet; Q99638; -.
DR PhosphoSitePlus; Q99638; -.
DR BioMuta; RAD9A; -.
DR DMDM; 74717382; -.
DR EPD; Q99638; -.
DR jPOST; Q99638; -.
DR MassIVE; Q99638; -.
DR MaxQB; Q99638; -.
DR PaxDb; Q99638; -.
DR PeptideAtlas; Q99638; -.
DR PRIDE; Q99638; -.
DR ProteomicsDB; 78371; -.
DR Antibodypedia; 1880; 1155 antibodies from 38 providers.
DR CPTC; Q99638; 1 antibody.
DR DNASU; 5883; -.
DR Ensembl; ENST00000307980.7; ENSP00000311360.2; ENSG00000172613.8.
DR GeneID; 5883; -.
DR KEGG; hsa:5883; -.
DR MANE-Select; ENST00000307980.7; ENSP00000311360.2; NM_004584.3; NP_004575.1.
DR UCSC; uc001okr.4; human.
DR CTD; 5883; -.
DR DisGeNET; 5883; -.
DR GeneCards; RAD9A; -.
DR HGNC; HGNC:9827; RAD9A.
DR HPA; ENSG00000172613; Low tissue specificity.
DR MIM; 603761; gene.
DR neXtProt; NX_Q99638; -.
DR OpenTargets; ENSG00000172613; -.
DR PharmGKB; PA294; -.
DR VEuPathDB; HostDB:ENSG00000172613; -.
DR eggNOG; KOG2810; Eukaryota.
DR GeneTree; ENSGT00390000005767; -.
DR InParanoid; Q99638; -.
DR OMA; AMMTEMS; -.
DR OrthoDB; 1176140at2759; -.
DR PhylomeDB; Q99638; -.
DR TreeFam; TF101212; -.
DR PathwayCommons; Q99638; -.
DR Reactome; R-HSA-176187; Activation of ATR in response to replication stress.
DR Reactome; R-HSA-5685938; HDR through Single Strand Annealing (SSA).
DR Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-HSA-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
DR Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-HSA-69473; G2/M DNA damage checkpoint.
DR Reactome; R-HSA-9709570; Impaired BRCA2 binding to RAD51.
DR SignaLink; Q99638; -.
DR SIGNOR; Q99638; -.
DR BioGRID-ORCS; 5883; 564 hits in 1088 CRISPR screens.
DR ChiTaRS; RAD9A; human.
DR EvolutionaryTrace; Q99638; -.
DR GeneWiki; RAD9A; -.
DR GenomeRNAi; 5883; -.
DR Pharos; Q99638; Tbio.
DR PRO; PR:Q99638; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q99638; protein.
DR Bgee; ENSG00000172613; Expressed in right uterine tube and 133 other tissues.
DR ExpressionAtlas; Q99638; baseline and differential.
DR Genevisible; Q99638; HS.
DR GO; GO:0030896; C:checkpoint clamp complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IDA:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0008853; F:exodeoxyribonuclease III activity; IEA:UniProtKB-EC.
DR GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0017124; F:SH3 domain binding; IPI:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR GO; GO:0071479; P:cellular response to ionizing radiation; IDA:UniProtKB.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IMP:UniProtKB.
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; IEA:Ensembl.
DR GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; IBA:GO_Central.
DR GO; GO:1902231; P:positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Ensembl.
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 3D-structure; Direct protein sequencing; DNA damage; Exonuclease;
KW Hydrolase; Nuclease; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..391
FT /note="Cell cycle checkpoint control protein RAD9A"
FT /id="PRO_0000225000"
FT REGION 51..91
FT /note="Possesses 3'-5' exonuclease activity"
FT REGION 266..391
FT /note="Sufficient for interaction with ABL1"
FT /evidence="ECO:0000269|PubMed:11971963"
FT REGION 268..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 28
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:11971963"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12709442"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12709442,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12709442,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12709442"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12709442,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12709442,
FT ECO:0007744|PubMed:17081983"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12709442,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT VARIANT 3
FT /note="C -> F (in dbSNP:rs11575913)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_025410"
FT VARIANT 71
FT /note="L -> Q (in dbSNP:rs2422490)"
FT /id="VAR_051724"
FT VARIANT 100
FT /note="S -> A (in dbSNP:rs2066492)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_025411"
FT VARIANT 239
FT /note="H -> R (in dbSNP:rs17880039)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_025412"
FT VARIANT 307
FT /note="M -> T (in dbSNP:rs17882466)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_025413"
FT MUTAGEN 28
FT /note="Y->F: Abolishes phosphorylation by ABL1."
FT /evidence="ECO:0000269|PubMed:11971963"
FT MUTAGEN 272
FT /note="S->A: Complete loss of phosphorylation and no loss
FT of interaction with the 9-1-1 complex; when associated with
FT A-277; A-328; A-341; A-375; A-380 and A-387."
FT /evidence="ECO:0000269|PubMed:12709442"
FT MUTAGEN 277
FT /note="S->A: Complete loss of phosphorylation and no loss
FT of interaction with the 9-1-1 complex; when associated with
FT A-272; A-328; A-341; A-375; A-380 and A-387."
FT /evidence="ECO:0000269|PubMed:12709442"
FT MUTAGEN 328
FT /note="S->A: Complete loss of phosphorylation and no loss
FT of interaction with the 9-1-1 complex; when associated with
FT A-272; A-277; A-341; A-375; A-380 and A-387."
FT /evidence="ECO:0000269|PubMed:12709442"
FT MUTAGEN 341
FT /note="S->A: Complete loss of phosphorylation and no loss
FT of interaction with the 9-1-1 complex; when associated with
FT A-272; A-277; A-328; A-375; A-380 and A-387."
FT /evidence="ECO:0000269|PubMed:12709442"
FT MUTAGEN 375
FT /note="S->A: Complete loss of phosphorylation and no loss
FT of interaction with the 9-1-1 complex; when associated with
FT A-272; A-277; A-328; A-341; A-380 and A-387."
FT /evidence="ECO:0000269|PubMed:12709442"
FT MUTAGEN 380
FT /note="S->A: Complete loss of phosphorylation and no loss
FT of interaction with the 9-1-1 complex; when associated with
FT A-272; A-277; A-328; A-341; A-375 and A-387."
FT /evidence="ECO:0000269|PubMed:12709442"
FT MUTAGEN 387
FT /note="S->A: Complete loss of phosphorylation and no loss
FT of interaction with the 9-1-1 complex; when associated with
FT A-272; A-277; A-328; A-341; A-375 and A-380."
FT /evidence="ECO:0000269|PubMed:12709442"
FT CONFLICT 12
FT /note="V -> A (in Ref. 2; CAG38746)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="E -> A (in Ref. 6; AAH14848)"
FT /evidence="ECO:0000305"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:6J8Y"
FT HELIX 9..20
FT /evidence="ECO:0007829|PDB:6J8Y"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:6J8Y"
FT STRAND 25..32
FT /evidence="ECO:0007829|PDB:6J8Y"
FT STRAND 35..41
FT /evidence="ECO:0007829|PDB:6J8Y"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:6J8Y"
FT STRAND 47..53
FT /evidence="ECO:0007829|PDB:6J8Y"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:6J8Y"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:6J8Y"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:3A1J"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:6J8Y"
FT HELIX 77..83
FT /evidence="ECO:0007829|PDB:6J8Y"
FT HELIX 87..92
FT /evidence="ECO:0007829|PDB:6J8Y"
FT STRAND 94..100
FT /evidence="ECO:0007829|PDB:6J8Y"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:3GGR"
FT STRAND 107..114
FT /evidence="ECO:0007829|PDB:6J8Y"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:6J8Y"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:6J8Y"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:6J8Y"
FT STRAND 142..148
FT /evidence="ECO:0007829|PDB:6J8Y"
FT HELIX 149..156
FT /evidence="ECO:0007829|PDB:6J8Y"
FT STRAND 165..171
FT /evidence="ECO:0007829|PDB:6J8Y"
FT TURN 172..174
FT /evidence="ECO:0007829|PDB:6J8Y"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:6J8Y"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:3GGR"
FT STRAND 194..199
FT /evidence="ECO:0007829|PDB:6J8Y"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:6J8Y"
FT STRAND 205..208
FT /evidence="ECO:0007829|PDB:6J8Y"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:6J8Y"
FT HELIX 219..230
FT /evidence="ECO:0007829|PDB:6J8Y"
FT TURN 231..233
FT /evidence="ECO:0007829|PDB:6J8Y"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:6J8Y"
FT STRAND 241..245
FT /evidence="ECO:0007829|PDB:3GGR"
FT STRAND 247..252
FT /evidence="ECO:0007829|PDB:6J8Y"
FT STRAND 254..262
FT /evidence="ECO:0007829|PDB:6J8Y"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:3G65"
FT STRAND 382..384
FT /evidence="ECO:0007829|PDB:6HM5"
SQ SEQUENCE 391 AA; 42547 MW; 4D4D6D4C6E1057D3 CRC64;
MKCLVTGGNV KVLGKAVHSL SRIGDELYLE PLEDGLSLRT VNSSRSAYAC FLFAPLFFQQ
YQAATPGQDL LRCKILMKSF LSVFRSLAML EKTVEKCCIS LNGRSSRLVV QLHCKFGVRK
THNLSFQDCE SLQAVFDPAS CPHMLRAPAR VLGEAVLPFS PALAEVTLGI GRGRRVILRS
YHEEEADSTA KAMVTEMCLG EEDFQQLQAQ EGVAITFCLK EFRGLLSFAE SANLNLSIHF
DAPGRPAIFT IKDSLLDGHF VLATLSDTDS HSQDLGSPER HQPVPQLQAH STPHPDDFAN
DDIDSYMIAM ETTIGNEGSR VLPSISLSPG PQPPKSPGPH SEEEDEAEPS TVPGTPPPKK
FRSLFFGSIL APVRSPQGPS PVLAEDSEGE G
