RAD1_HUMAN
ID RAD1_HUMAN Reviewed; 282 AA.
AC O60671; O75572; O95304; Q1W161; Q5KSM0; Q5KSM1; Q9UEP1;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Cell cycle checkpoint protein RAD1;
DE Short=hRAD1;
DE EC=3.1.11.2 {ECO:0000269|PubMed:9660799};
DE AltName: Full=DNA repair exonuclease rad1 homolog;
DE AltName: Full=Rad1-like DNA damage checkpoint protein;
GN Name=RAD1; Synonyms=REC1;
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] (ISOFORM 1), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=9716408; DOI=10.1101/gad.12.16.2560;
RA Freire R., Murguia J.R., Tarsounas M., Lowndes N.F., Moens P.B.,
RA Jackson S.P.;
RT "Human and mouse homologs of Schizosaccharomyces pombe rad1(+) and
RT Saccharomyces cerevisiae RAD17: linkage to checkpoint control and mammalian
RT meiosis.";
RL Genes Dev. 12:2560-2573(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9828137; DOI=10.1006/geno.1998.5582;
RA Bluyssen H.A.R., van Os R.I., Naus N.C., Jaspers I., Hoeijmakers J.H.J.,
RA de Klein A.;
RT "A human and mouse homolog of the Schizosaccharomyces pombe rad1+ cell
RT cycle checkpoint control gene.";
RL Genomics 54:331-337(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Cervix carcinoma;
RX PubMed=9828139; DOI=10.1006/geno.1998.5589;
RA Marathi U.K., Dahlen M., Sunnerhagen P., Romero A.V., Ramagli L.S.,
RA Siciliano M.J., Li L., Legerski R.J.;
RT "RAD1, a human structural homolog of the Schizosaccharomyces pombe RAD1
RT cell cycle checkpoint gene.";
RL Genomics 54:344-347(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
RX PubMed=9878245; DOI=10.1006/geno.1998.5587;
RA Dean F.B., Lian L., O'Donnell M.;
RT "cDNA cloning and gene mapping of human homologs for Schizosaccharomyces
RT pombe rad17, rad1, and hus1 and cloning of homologs from mouse,
RT Caenorhabditis elegans, and Drosophila melanogaster.";
RL Genomics 54:424-436(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND FUNCTION IN EXONUCLEASE
RP ACTIVITY.
RX PubMed=9660799; DOI=10.1074/jbc.273.29.18332;
RA Parker A.E., Van de Weyer I., Laus M.C., Oostveen I., Yon J.,
RA Verhasselt P., Luyten W.H.M.L.;
RT "A human homologue of the Schizosaccharomyces pombe rad1+ checkpoint gene
RT encodes an exonuclease.";
RL J. Biol. Chem. 273:18332-18339(1998).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9705507; DOI=10.1093/nar/26.17.3971;
RA Udell C.M., Lee S.K., Davey S.;
RT "HRAD1 and MRad1 encode mammalian homologues of the fission yeast rad1+
RT cell cycle checkpoint control gene.";
RL Nucleic Acids Res. 26:3971-3976(1998).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Hao L., Chang M., Liu J., Chen L.B.;
RT "Identification and cloning of Hrad1, a human homolog of the
RT Schizosaccharomyces pombe checkpoint protein.";
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RA Shannon M.E., Naureckiene S., Stubbs L., Holloman W.K., Thelen M.P.;
RT "Mammalian REC1, encoding a 3'-5' exonuclease, is differentially expressed
RT during meiosis.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLN-39 AND GLY-281.
RG NIEHS SNPs program;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [12]
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 [13]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow, Placenta, and 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 [14]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 104-188 AND 223-282.
RA Saegusa K.K., Suga T.K., Imai T.;
RT "Identification of novel polymorphisms in the RAD1 gene.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [15]
RP INTERACTION WITH HUS1 AND RAD9A.
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 [16]
RP INTERACTION WITH HUS1 AND RAD9A.
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 [17]
RP FUNCTION, AND 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 [18]
RP FUNCTION, IDENTIFICATION IN THE 9-1-1 COMPLEX ASSOCIATED WITH RAD17, AND
RP MUTAGENESIS OF 226-SER--LYS-233.
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 [19]
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 [20]
RP INTERACTION WITH HUS1B.
RX PubMed=11944979; DOI=10.1006/geno.2002.6737;
RA Hang H., Zhang Y., Dunbrack R.L. Jr., Wang C., Lieberman H.B.;
RT "Identification and characterization of a paralog of human cell cycle
RT checkpoint gene HUS1.";
RL Genomics 79:487-492(2002).
RN [21]
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 [22]
RP INTERACTION WITH RAD9B.
RX PubMed=14611806; DOI=10.1016/s0888-7543(03)00200-3;
RA Dufault V.M., Oestreich A.J., Vroman B.T., Karnitz L.M.;
RT "Identification and characterization of RAD9B, a paralog of the RAD9
RT checkpoint gene.";
RL Genomics 82:644-651(2003).
RN [23]
RP FUNCTION, ASSOCIATION OF THE 9-1-1 COMPLEX WITH THE RAD17-RFC COMPLEX, AND
RP ELECTRON 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 [24]
RP FUNCTION, IDENTIFICATION IN THE 9-1-1 COMPLEX ASSOCIATED WITH POLB, AND
RP INTERACTION 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 [25]
RP FUNCTION, AND 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 [26]
RP FUNCTION, AND 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 [27]
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 [28]
RP IDENTIFICATION IN THE 9-1-1 COMPLEX ASSOCIATED 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 [29]
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 [30]
RP FUNCTION, 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Component of the 9-1-1 cell-cycle checkpoint response complex
CC that plays a major role in DNA repair (PubMed:10846170,
CC PubMed:10884395). The 9-1-1 complex is recruited to DNA lesion upon
CC damage by the RAD17-replication factor C (RFC) clamp loader complex
CC (PubMed:12578958). Acts then as a sliding clamp platform on DNA for
CC several proteins involved in long-patch base excision repair (LP-BER)
CC (PubMed:15871698). The 9-1-1 complex stimulates DNA polymerase beta
CC (POLB) activity by increasing its affinity for the 3'-OH end of the
CC primer-template and stabilizes POLB to those sites where LP-BER
CC proceeds; endonuclease FEN1 cleavage activity on substrates with
CC double, nick, or gap flaps of distinct sequences and lengths; and DNA
CC ligase I (LIG1) on long-patch base excision repair substrates
CC (PubMed:15314187, PubMed:15556996, PubMed:15871698). The 9-1-1 complex
CC is necessary for the recruitment of RHNO1 to sites of double-stranded
CC breaks (DSB) occurring during the S phase (PubMed:21659603). Isoform 1
CC possesses 3'->5' double stranded DNA exonuclease activity
CC (PubMed:9660799). {ECO:0000269|PubMed:10846170,
CC ECO:0000269|PubMed:10884395, ECO:0000269|PubMed:12578958,
CC ECO:0000269|PubMed:15314187, ECO:0000269|PubMed:15556996,
CC ECO:0000269|PubMed:15871698, ECO:0000269|PubMed:21659603,
CC ECO:0000269|PubMed:9660799}.
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 Evidence={ECO:0000269|PubMed:9660799};
CC -!- SUBUNIT: Component of the toroidal 9-1-1 (RAD9-RAD1-HUS1) complex,
CC composed of RAD9A, RAD1 and HUS1 (PubMed:10846170, PubMed:10884395).
CC The 9-1-1 complex associates with LIG1, POLB, FEN1, RAD17, HDAC1, RPA1
CC and RPA2 (PubMed:10846170, PubMed:10884395, PubMed:15314187,
CC PubMed:15556996, PubMed:15871698, PubMed:15897895, PubMed:16216273).
CC The 9-1-1 complex associates with the RAD17-RFC complex
CC (PubMed:12578958). RAD1 interacts with POLB, FEN1, HUS1, HUS1B, RAD9A
CC and RAD9B (PubMed:10359610, PubMed:10777662, PubMed:11944979,
CC PubMed:14500360, PubMed:14611806, PubMed:15314187, PubMed:15556996,
CC PubMed:16216273). Interacts with DNAJC7 (PubMed:11573955).
CC {ECO:0000269|PubMed:10359610, ECO:0000269|PubMed:10777662,
CC ECO:0000269|PubMed:10846170, ECO:0000269|PubMed:10884395,
CC ECO:0000269|PubMed:11573955, ECO:0000269|PubMed:11944979,
CC ECO:0000269|PubMed:12578958, ECO:0000269|PubMed:14500360,
CC ECO:0000269|PubMed:14611806, ECO:0000269|PubMed:15314187,
CC ECO:0000269|PubMed:15556996, ECO:0000269|PubMed:15871698,
CC ECO:0000269|PubMed:15897895, ECO:0000269|PubMed:16216273}.
CC -!- INTERACTION:
CC O60671; O60921: HUS1; NbExp=5; IntAct=EBI-721835, EBI-1056174;
CC O60671; O60260-5: PRKN; NbExp=6; IntAct=EBI-721835, EBI-21251460;
CC O60671; Q99638: RAD9A; NbExp=2; IntAct=EBI-721835, EBI-2606224;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9716408}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Hrad1A;
CC IsoId=O60671-1; Sequence=Displayed;
CC Name=2; Synonyms=Hrad1B;
CC IsoId=O60671-2; Sequence=VSP_017334;
CC Name=3;
CC IsoId=O60671-3; Sequence=VSP_017335, VSP_017336;
CC -!- TISSUE SPECIFICITY: Expressed in testis, uterus, bladder, spleen,
CC ovaries, lung, brain and muscle (at protein level).
CC {ECO:0000269|PubMed:9716408}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the rad1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC35550.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAC35550.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA06249.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA06249.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/rad1/";
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DR EMBL; AF074717; AAC98093.1; -; mRNA.
DR EMBL; AF073524; AAC95466.1; -; mRNA.
DR EMBL; AF030933; AAC95427.1; -; mRNA.
DR EMBL; AF076841; AAC95523.1; -; mRNA.
DR EMBL; AF090170; AAC95603.1; -; mRNA.
DR EMBL; AJ004974; CAA06248.1; -; mRNA.
DR EMBL; AJ004975; CAA06249.1; ALT_SEQ; mRNA.
DR EMBL; AF011905; AAC27243.1; -; mRNA.
DR EMBL; AF058392; AAC14138.1; -; mRNA.
DR EMBL; AF084512; AAC35549.1; -; mRNA.
DR EMBL; AF084513; AAC35550.1; ALT_SEQ; mRNA.
DR EMBL; AK002112; BAG51017.1; -; mRNA.
DR EMBL; BT006908; AAP35554.1; -; mRNA.
DR EMBL; DQ451401; ABD96829.1; -; Genomic_DNA.
DR EMBL; CH471119; EAW55904.1; -; Genomic_DNA.
DR EMBL; BC006837; AAH06837.1; -; mRNA.
DR EMBL; BC009804; AAH09804.1; -; mRNA.
DR EMBL; BC037857; AAH37857.1; -; mRNA.
DR EMBL; AB183821; BAD86789.1; -; Genomic_DNA.
DR EMBL; AB183822; BAD86790.1; -; Genomic_DNA.
DR CCDS; CCDS3905.1; -. [O60671-1]
DR RefSeq; NP_002844.1; NM_002853.3. [O60671-1]
DR PDB; 3A1J; X-ray; 2.50 A; C=13-275.
DR PDB; 3G65; X-ray; 2.90 A; B=1-282.
DR PDB; 3GGR; X-ray; 3.20 A; C=1-282.
DR PDB; 6J8Y; X-ray; 2.40 A; C=1-282.
DR PDBsum; 3A1J; -.
DR PDBsum; 3G65; -.
DR PDBsum; 3GGR; -.
DR PDBsum; 6J8Y; -.
DR AlphaFoldDB; O60671; -.
DR SMR; O60671; -.
DR BioGRID; 111771; 49.
DR ComplexPortal; CPX-1829; Checkpoint clamp complex.
DR CORUM; O60671; -.
DR DIP; DIP-46061N; -.
DR IntAct; O60671; 20.
DR MINT; O60671; -.
DR STRING; 9606.ENSP00000371469; -.
DR BindingDB; O60671; -.
DR ChEMBL; CHEMBL3309116; -.
DR iPTMnet; O60671; -.
DR PhosphoSitePlus; O60671; -.
DR BioMuta; RAD1; -.
DR EPD; O60671; -.
DR jPOST; O60671; -.
DR MassIVE; O60671; -.
DR MaxQB; O60671; -.
DR PaxDb; O60671; -.
DR PeptideAtlas; O60671; -.
DR PRIDE; O60671; -.
DR ProteomicsDB; 49514; -. [O60671-1]
DR ProteomicsDB; 49515; -. [O60671-2]
DR ProteomicsDB; 49516; -. [O60671-3]
DR Antibodypedia; 10031; 358 antibodies from 33 providers.
DR CPTC; O60671; 1 antibody.
DR DNASU; 5810; -.
DR Ensembl; ENST00000325577.8; ENSP00000313467.4; ENSG00000113456.19. [O60671-3]
DR Ensembl; ENST00000341754.8; ENSP00000340879.4; ENSG00000113456.19. [O60671-1]
DR Ensembl; ENST00000382038.7; ENSP00000371469.2; ENSG00000113456.19. [O60671-1]
DR GeneID; 5810; -.
DR KEGG; hsa:5810; -.
DR MANE-Select; ENST00000382038.7; ENSP00000371469.2; NM_002853.4; NP_002844.1.
DR UCSC; uc003jix.4; human. [O60671-1]
DR CTD; 5810; -.
DR DisGeNET; 5810; -.
DR GeneCards; RAD1; -.
DR HGNC; HGNC:9806; RAD1.
DR HPA; ENSG00000113456; Low tissue specificity.
DR MIM; 603153; gene.
DR neXtProt; NX_O60671; -.
DR OpenTargets; ENSG00000113456; -.
DR PharmGKB; PA34166; -.
DR VEuPathDB; HostDB:ENSG00000113456; -.
DR eggNOG; KOG3194; Eukaryota.
DR GeneTree; ENSGT00500000044913; -.
DR HOGENOM; CLU_035332_2_1_1; -.
DR InParanoid; O60671; -.
DR OMA; QITMSPE; -.
DR PhylomeDB; O60671; -.
DR TreeFam; TF101211; -.
DR PathwayCommons; O60671; -.
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; O60671; -.
DR SIGNOR; O60671; -.
DR BioGRID-ORCS; 5810; 377 hits in 1079 CRISPR screens.
DR ChiTaRS; RAD1; human.
DR EvolutionaryTrace; O60671; -.
DR GeneWiki; RAD1_homolog; -.
DR GenomeRNAi; 5810; -.
DR Pharos; O60671; Tchem.
DR PRO; PR:O60671; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; O60671; protein.
DR Bgee; ENSG00000113456; Expressed in secondary oocyte and 222 other tissues.
DR ExpressionAtlas; O60671; baseline and differential.
DR Genevisible; O60671; HS.
DR GO; GO:0030896; C:checkpoint clamp complex; IBA:GO_Central.
DR GO; GO:0005694; C:chromosome; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IC:UniProtKB.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IDA:UniProtKB.
DR GO; GO:0003684; F:damaged DNA binding; TAS:ProtInc.
DR GO; GO:0008853; F:exodeoxyribonuclease III activity; IEA:UniProtKB-EC.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; TAS:ProtInc.
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:0051598; P:meiotic recombination checkpoint signaling; IGI:UniProtKB.
DR GO; GO:0021762; P:substantia nigra development; HEP:UniProtKB.
DR InterPro; IPR003011; Cell_cycle_checkpoint_Rad1.
DR InterPro; IPR003021; Rad1_Rec1_Rad17.
DR PANTHER; PTHR10870; PTHR10870; 1.
DR Pfam; PF02144; Rad1; 1.
DR PRINTS; PR01245; RAD1REC1.
DR PRINTS; PR01246; RAD1REPAIR.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; DNA damage; DNA repair; Exonuclease;
KW Hydrolase; Nuclease; Nucleus; Reference proteome.
FT CHAIN 1..282
FT /note="Cell cycle checkpoint protein RAD1"
FT /id="PRO_0000225005"
FT VAR_SEQ 67..102
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9660799, ECO:0000303|Ref.8"
FT /id="VSP_017334"
FT VAR_SEQ 67..68
FT /note="AG -> GL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9878245"
FT /id="VSP_017335"
FT VAR_SEQ 69..282
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9878245"
FT /id="VSP_017336"
FT VARIANT 33
FT /note="A -> G (in dbSNP:rs2308951)"
FT /id="VAR_051718"
FT VARIANT 39
FT /note="H -> Q (in dbSNP:rs41271673)"
FT /evidence="ECO:0000269|Ref.11"
FT /id="VAR_055376"
FT VARIANT 104
FT /note="T -> S (in dbSNP:rs1805328)"
FT /id="VAR_051719"
FT VARIANT 114
FT /note="G -> D (in dbSNP:rs2308957)"
FT /id="VAR_051720"
FT VARIANT 281
FT /note="E -> G (in dbSNP:rs1805327)"
FT /evidence="ECO:0000269|Ref.11"
FT /id="VAR_051721"
FT MUTAGEN 226..233
FT /note="SLLKPSTK->AAAAAAAA: Abolishes association of the 9-
FT 1-1 complex with RAD17."
FT /evidence="ECO:0000269|PubMed:10884395"
FT CONFLICT 135
FT /note="N -> T (in Ref. 2; AAC95466)"
FT /evidence="ECO:0000305"
FT STRAND 17..22
FT /evidence="ECO:0007829|PDB:6J8Y"
FT HELIX 25..32
FT /evidence="ECO:0007829|PDB:6J8Y"
FT STRAND 36..45
FT /evidence="ECO:0007829|PDB:6J8Y"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:6J8Y"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:6J8Y"
FT STRAND 59..66
FT /evidence="ECO:0007829|PDB:6J8Y"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:6J8Y"
FT STRAND 70..78
FT /evidence="ECO:0007829|PDB:6J8Y"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:6J8Y"
FT HELIX 86..93
FT /evidence="ECO:0007829|PDB:6J8Y"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:6J8Y"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:6J8Y"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:3G65"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:6J8Y"
FT STRAND 128..134
FT /evidence="ECO:0007829|PDB:6J8Y"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:6J8Y"
FT STRAND 152..160
FT /evidence="ECO:0007829|PDB:6J8Y"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:6J8Y"
FT HELIX 164..167
FT /evidence="ECO:0007829|PDB:6J8Y"
FT STRAND 172..181
FT /evidence="ECO:0007829|PDB:6J8Y"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:3G65"
FT STRAND 187..194
FT /evidence="ECO:0007829|PDB:6J8Y"
FT STRAND 197..203
FT /evidence="ECO:0007829|PDB:6J8Y"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:3GGR"
FT STRAND 210..215
FT /evidence="ECO:0007829|PDB:6J8Y"
FT STRAND 219..224
FT /evidence="ECO:0007829|PDB:6J8Y"
FT HELIX 225..228
FT /evidence="ECO:0007829|PDB:6J8Y"
FT HELIX 231..237
FT /evidence="ECO:0007829|PDB:6J8Y"
FT STRAND 238..248
FT /evidence="ECO:0007829|PDB:6J8Y"
FT STRAND 251..258
FT /evidence="ECO:0007829|PDB:6J8Y"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:3GGR"
FT STRAND 264..271
FT /evidence="ECO:0007829|PDB:6J8Y"
SQ SEQUENCE 282 AA; 31827 MW; 075FBD4CF8A4FDB2 CRC64;
MPLLTQQIQD EDDQYSLVAS LDNVRNLSTI LKAIHFREHA TCFATKNGIK VTVENAKCVQ
ANAFIQAGIF QEFKVQEESV TFRINLTVLL DCLSIFGSSP MPGTLTALRM CYQGYGYPLM
LFLEEGGVVT VCKINTQEPE ETLDFDFCST NVINKIILQS EGLREAFSEL DMTSEVLQIT
MSPDKPYFRL STFGNAGSSH LDYPKDSDLM EAFHCNQTQV NRYKISLLKP STKALVLSCK
VSIRTDNRGF LSLQYMIRNE DGQICFVEYY CCPDEEVPES ES
