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 24-JAN-2024, entry version 184. DE RecName: Full=Cell cycle checkpoint protein RAD1; DE Short=hRAD1; 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). 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). RN [32] {ECO:0007744|PDB:6J8Y} RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH RHNO1; HUS1 AND RP RAD9A, IDENTIFICATION IN THE 9-1-1 COMPLEX, INTERACTION WITH RHNO1, AND RP MUTAGENESIS OF PHE-64; LYS-155; ARG-244; GLN-254; MET-256 AND PHE-266. RX PubMed=31776186; DOI=10.1074/jbc.ac119.011816; RA Hara K., Iida N., Tamafune R., Ohashi E., Sakurai H., Ishikawa Y., RA Hishiki A., Hashimoto H.; RT "Structure of the RAD9-RAD1-HUS1 checkpoint clamp bound to RHINO sheds RT light on the other side of the DNA clamp."; RL J. Biol. Chem. 295:899-904(2020). RN [33] {ECO:0007744|PDB:8GNN} RP X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) IN COMPLEX WITH RAD17; HUS1 AND RP RAD9A. RX PubMed=36841485; DOI=10.1016/j.jbc.2023.103061; RA Hara K., Hishiki A., Hoshino T., Nagata K., Iida N., Sawada Y., Ohashi E., RA Hashimoto H.; RT "The 9-1-1 DNA clamp subunit RAD1 forms specific interactions with clamp RT loader RAD17, revealing functional implications for binding-protein RT RHINO."; RL J. Biol. Chem. 299:103061-103061(2023). 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). CC {ECO:0000269|PubMed:10846170, ECO:0000269|PubMed:10884395, CC ECO:0000269|PubMed:12578958, ECO:0000269|PubMed:15314187, CC ECO:0000269|PubMed:15556996, ECO:0000269|PubMed:15871698, CC ECO:0000269|PubMed:21659603}. 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 PubMed:31776186). The 9-1-1 complex associates with LIG1, POLB, FEN1, CC RAD17, HDAC1, RPA1 and RPA2 (PubMed:10846170, PubMed:10884395, CC PubMed:15314187, PubMed:15556996, PubMed:15871698, PubMed:15897895, CC PubMed:16216273). The 9-1-1 complex associates with the RAD17-RFC CC complex (PubMed:12578958). RAD1 interacts with POLB, FEN1, HUS1, HUS1B, CC RAD9A 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). Interacts CC with RHNO1; interaction is direct (PubMed:31776186). 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 ECO:0000269|PubMed:31776186}. 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 -!- CAUTION: [Isoform 1]: Was reported to possess 3'->5' double stranded CC DNA exonuclease activity (PubMed:9660799). However, this activity was CC not confirmed by other publications (PubMed:9716408). CC {ECO:0000269|PubMed:9660799, ECO:0000269|PubMed:9716408}. 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/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 7Z6H; EM; 3.59 A; B/K=1-282. DR PDB; 8GNN; X-ray; 2.12 A; C=1-282. DR PDBsum; 3A1J; -. DR PDBsum; 3G65; -. DR PDBsum; 3GGR; -. DR PDBsum; 6J8Y; -. DR PDBsum; 7Z6H; -. DR PDBsum; 8GNN; -. DR AlphaFoldDB; O60671; -. DR SMR; O60671; -. DR BioGRID; 111771; 52. 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; 9606-ENSP00000371469; -. DR PeptideAtlas; O60671; -. DR ProteomicsDB; 49514; -. [O60671-1] DR ProteomicsDB; 49515; -. [O60671-2] DR ProteomicsDB; 49516; -. [O60671-3] DR Pumba; O60671; -. DR Antibodypedia; 10031; 371 antibodies from 33 providers. DR CPTC; O60671; 1 antibody. DR DNASU; 5810; -. DR Ensembl; ENST00000325577.8; ENSP00000313467.4; ENSG00000113456.20. [O60671-3] DR Ensembl; ENST00000341754.8; ENSP00000340879.4; ENSG00000113456.20. [O60671-1] DR Ensembl; ENST00000382038.7; ENSP00000371469.2; ENSG00000113456.20. [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 AGR; HGNC:9806; -. 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; WSQAYKF; -. DR OrthoDB; 5473594at2759; -. 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; 408 hits in 1158 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 223 other cell types or tissues. DR ExpressionAtlas; O60671; baseline and differential. DR GO; GO:0030896; C:checkpoint clamp complex; IDA:UniProtKB. 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:HPA. DR GO; GO:0005634; C:nucleus; IC:UniProtKB. DR GO; GO:0008408; F:3'-5' exonuclease activity; IBA:GO_Central. DR GO; GO:0003684; F:damaged DNA binding; TAS:ProtInc. DR GO; GO:0008311; F:double-stranded DNA 3'-5' DNA exonuclease activity; IEA:UniProtKB-EC. 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:0006974; P:DNA damage response; TAS:ProtInc. 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 CDD; cd00577; PCNA; 1. DR Gene3D; 3.70.10.10; -; 1. DR InterPro; IPR003011; Cell_cycle_checkpoint_Rad1. DR InterPro; IPR046938; DNA_clamp_sf. DR InterPro; IPR003021; Rad1_Rec1_Rad17. DR PANTHER; PTHR10870; CELL CYCLE CHECKPOINT PROTEIN RAD1; 1. DR PANTHER; PTHR10870:SF0; CELL CYCLE CHECKPOINT PROTEIN RAD1; 1. DR Pfam; PF02144; Rad1; 1. DR PRINTS; PR01245; RAD1REC1. DR PRINTS; PR01246; RAD1REPAIR. DR SUPFAM; SSF55979; DNA clamp; 1. DR Genevisible; O60671; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; DNA damage; DNA repair; Nucleus; KW 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 64 FT /note="F->A: Reduced binding to RHNO1; when associated with FT A-256 and A-266." FT /evidence="ECO:0000269|PubMed:31776186" FT MUTAGEN 155 FT /note="K->A: Reduced binding to RHNO1; when associated with FT A-244 and A-254." FT /evidence="ECO:0000269|PubMed:31776186" FT MUTAGEN 226..233 FT /note="SLLKPSTK->AAAAAAAA: Abolishes association of the FT 9-1-1 complex with RAD17." FT /evidence="ECO:0000269|PubMed:10884395" FT MUTAGEN 244 FT /note="R->A: Reduced binding to RHNO1; when associated with FT A-155 and A-254." FT /evidence="ECO:0000269|PubMed:31776186" FT MUTAGEN 254 FT /note="Q->A: Reduced binding to RHNO1; when associated with FT A-155 and A-244." FT /evidence="ECO:0000269|PubMed:31776186" FT MUTAGEN 256 FT /note="M->A: Reduced binding to RHNO1; when associated with FT A-64 and A-266." FT /evidence="ECO:0000269|PubMed:31776186" FT MUTAGEN 266 FT /note="F->A: Reduced binding to RHNO1; when associated with FT A-64 and A-256." FT /evidence="ECO:0000269|PubMed:31776186" FT CONFLICT 135 FT /note="N -> T (in Ref. 2; AAC95466)" FT /evidence="ECO:0000305" FT STRAND 16..22 FT /evidence="ECO:0007829|PDB:8GNN" FT HELIX 25..32 FT /evidence="ECO:0007829|PDB:8GNN" FT STRAND 36..44 FT /evidence="ECO:0007829|PDB:8GNN" FT STRAND 46..55 FT /evidence="ECO:0007829|PDB:8GNN" FT TURN 56..58 FT /evidence="ECO:0007829|PDB:8GNN" FT STRAND 59..66 FT /evidence="ECO:0007829|PDB:8GNN" FT HELIX 67..69 FT /evidence="ECO:0007829|PDB:8GNN" FT STRAND 70..78 FT /evidence="ECO:0007829|PDB:8GNN" FT STRAND 80..85 FT /evidence="ECO:0007829|PDB:8GNN" FT HELIX 86..93 FT /evidence="ECO:0007829|PDB:8GNN" FT TURN 94..96 FT /evidence="ECO:0007829|PDB:8GNN" FT STRAND 107..112 FT /evidence="ECO:0007829|PDB:8GNN" FT STRAND 114..117 FT /evidence="ECO:0007829|PDB:3G65" FT STRAND 119..125 FT /evidence="ECO:0007829|PDB:8GNN" FT STRAND 128..134 FT /evidence="ECO:0007829|PDB:8GNN" FT HELIX 149..151 FT /evidence="ECO:0007829|PDB:8GNN" FT STRAND 152..159 FT /evidence="ECO:0007829|PDB:8GNN" FT HELIX 161..168 FT /evidence="ECO:0007829|PDB:8GNN" FT STRAND 174..181 FT /evidence="ECO:0007829|PDB:8GNN" FT STRAND 183..185 FT /evidence="ECO:0007829|PDB:3G65" FT STRAND 187..193 FT /evidence="ECO:0007829|PDB:8GNN" FT STRAND 195..203 FT /evidence="ECO:0007829|PDB:8GNN" FT STRAND 205..207 FT /evidence="ECO:0007829|PDB:3GGR" FT STRAND 210..215 FT /evidence="ECO:0007829|PDB:8GNN" FT STRAND 219..224 FT /evidence="ECO:0007829|PDB:8GNN" FT HELIX 225..228 FT /evidence="ECO:0007829|PDB:8GNN" FT HELIX 229..231 FT /evidence="ECO:0007829|PDB:8GNN" FT HELIX 232..237 FT /evidence="ECO:0007829|PDB:8GNN" FT STRAND 238..246 FT /evidence="ECO:0007829|PDB:8GNN" FT STRAND 247..249 FT /evidence="ECO:0007829|PDB:3GGR" FT STRAND 251..258 FT /evidence="ECO:0007829|PDB:8GNN" FT STRAND 260..262 FT /evidence="ECO:0007829|PDB:3GGR" FT STRAND 264..271 FT /evidence="ECO:0007829|PDB:8GNN" 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 //