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Cell cycle checkpoint protein RAD1 (hRAD1) (EC 3.1.11.2) (DNA repair exonuclease rad1 homolog) (Rad1-like DNA damage checkpoint protein)

 RAD1_HUMAN              Reviewed;         282 AA.
O60671; O75572; O95304; Q1W161; Q5KSM0; Q5KSM1; Q9UEP1;
07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
01-AUG-1998, sequence version 1.
12-AUG-2020, entry version 168.
RecName: Full=Cell cycle checkpoint protein RAD1;
Short=hRAD1;
EC=3.1.11.2 {ECO:0000269|PubMed:9660799};
AltName: Full=DNA repair exonuclease rad1 homolog;
AltName: Full=Rad1-like DNA damage checkpoint protein;
Name=RAD1; Synonyms=REC1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=9716408; DOI=10.1101/gad.12.16.2560;
Freire R., Murguia J.R., Tarsounas M., Lowndes N.F., Moens P.B.,
Jackson S.P.;
"Human and mouse homologs of Schizosaccharomyces pombe rad1(+) and
Saccharomyces cerevisiae RAD17: linkage to checkpoint control and mammalian
meiosis.";
Genes Dev. 12:2560-2573(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9828137; DOI=10.1006/geno.1998.5582;
Bluyssen H.A.R., van Os R.I., Naus N.C., Jaspers I., Hoeijmakers J.H.J.,
de Klein A.;
"A human and mouse homolog of the Schizosaccharomyces pombe rad1+ cell
cycle checkpoint control gene.";
Genomics 54:331-337(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Cervix carcinoma;
PubMed=9828139; DOI=10.1006/geno.1998.5589;
Marathi U.K., Dahlen M., Sunnerhagen P., Romero A.V., Ramagli L.S.,
Siciliano M.J., Li L., Legerski R.J.;
"RAD1, a human structural homolog of the Schizosaccharomyces pombe RAD1
cell cycle checkpoint gene.";
Genomics 54:344-347(1998).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
PubMed=9878245; DOI=10.1006/geno.1998.5587;
Dean F.B., Lian L., O'Donnell M.;
"cDNA cloning and gene mapping of human homologs for Schizosaccharomyces
pombe rad17, rad1, and hus1 and cloning of homologs from mouse,
Caenorhabditis elegans, and Drosophila melanogaster.";
Genomics 54:424-436(1998).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND FUNCTION IN EXONUCLEASE
ACTIVITY.
PubMed=9660799; DOI=10.1074/jbc.273.29.18332;
Parker A.E., Van de Weyer I., Laus M.C., Oostveen I., Yon J.,
Verhasselt P., Luyten W.H.M.L.;
"A human homologue of the Schizosaccharomyces pombe rad1+ checkpoint gene
encodes an exonuclease.";
J. Biol. Chem. 273:18332-18339(1998).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9705507; DOI=10.1093/nar/26.17.3971;
Udell C.M., Lee S.K., Davey S.;
"HRAD1 and MRad1 encode mammalian homologues of the fission yeast rad1+
cell cycle checkpoint control gene.";
Nucleic Acids Res. 26:3971-3976(1998).
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Hao L., Chang M., Liu J., Chen L.B.;
"Identification and cloning of Hrad1, a human homolog of the
Schizosaccharomyces pombe checkpoint protein.";
Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Shannon M.E., Naureckiene S., Stubbs L., Holloman W.K., Thelen M.P.;
"Mammalian REC1, encoding a 3'-5' exonuclease, is differentially expressed
during meiosis.";
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLN-39 AND GLY-281.
NIEHS SNPs program;
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Bone marrow, Placenta, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[14]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 104-188 AND 223-282.
Saegusa K.K., Suga T.K., Imai T.;
"Identification of novel polymorphisms in the RAD1 gene.";
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
[15]
INTERACTION WITH HUS1 AND RAD9A.
PubMed=10359610; DOI=10.1091/mbc.10.6.1985;
St Onge R.P., Udell C.M., Casselman R., Davey S.;
"The human G2 checkpoint control protein hRAD9 is a nuclear phosphoprotein
that forms complexes with hRAD1 and hHUS1.";
Mol. Biol. Cell 10:1985-1995(1999).
[16]
INTERACTION WITH HUS1 AND RAD9A.
PubMed=10777662; DOI=10.1006/geno.2000.6142;
Hang H., Lieberman H.B.;
"Physical interaction among human checkpoint control proteins HUS1p, RAD1p,
and RAD9p, and implications for the regulation of cell cycle progression.";
Genomics 65:24-33(2000).
[17]
FUNCTION, AND IDENTIFICATION IN THE 9-1-1 COMPLEX ASSOCIATED WITH HDAC1.
PubMed=10846170; DOI=10.1074/jbc.m000168200;
Cai R.L., Yan-Neale Y., Cueto M.A., Xu H., Cohen D.;
"HDAC1, a histone deacetylase, forms a complex with Hus1 and Rad9, two G2/M
checkpoint Rad proteins.";
J. Biol. Chem. 275:27909-27916(2000).
[18]
FUNCTION, IDENTIFICATION IN THE 9-1-1 COMPLEX ASSOCIATED WITH RAD17, AND
MUTAGENESIS OF 226-SER--LYS-233.
PubMed=10884395; DOI=10.1074/jbc.m005782200;
Rauen M., Burtelow M.A., Dufault V.M., Karnitz L.M.;
"The human checkpoint protein hRad17 interacts with the PCNA-like proteins
hRad1, hHus1, and hRad9.";
J. Biol. Chem. 275:29767-29771(2000).
[19]
INTERACTION WITH DNAJC7.
PubMed=11573955; DOI=10.1006/bbrc.2001.5685;
Xiang S.L., Kumano T., Iwasaki S.I., Sun X., Yoshioka K., Yamamoto K.C.;
"The J domain of Tpr2 regulates its interaction with the proapoptotic and
cell-cycle checkpoint protein, Rad9.";
Biochem. Biophys. Res. Commun. 287:932-940(2001).
[20]
INTERACTION WITH HUS1B.
PubMed=11944979; DOI=10.1006/geno.2002.6737;
Hang H., Zhang Y., Dunbrack R.L. Jr., Wang C., Lieberman H.B.;
"Identification and characterization of a paralog of human cell cycle
checkpoint gene HUS1.";
Genomics 79:487-492(2002).
[21]
INTERACTION WITH RAD9B.
PubMed=14500360;
Hopkins K.M., Wang X., Berlin A., Hang H., Thaker H.M., Lieberman H.B.;
"Expression of mammalian paralogues of HRAD9 and Mrad9 checkpoint control
genes in normal and cancerous testicular tissue.";
Cancer Res. 63:5291-5298(2003).
[22]
INTERACTION WITH RAD9B.
PubMed=14611806; DOI=10.1016/s0888-7543(03)00200-3;
Dufault V.M., Oestreich A.J., Vroman B.T., Karnitz L.M.;
"Identification and characterization of RAD9B, a paralog of the RAD9
checkpoint gene.";
Genomics 82:644-651(2003).
[23]
FUNCTION, ASSOCIATION OF THE 9-1-1 COMPLEX WITH THE RAD17-RFC COMPLEX, AND
ELECTRON MICROSCOPY OF THE 9-1-1 AND RAD17-RFC COMPLEXES BOUND TO DNA.
PubMed=12578958; DOI=10.1073/pnas.0437927100;
Bermudez V.P., Lindsey-Boltz L.A., Cesare A.J., Maniwa Y., Griffith J.D.,
Hurwitz J., Sancar A.;
"Loading of the human 9-1-1 checkpoint complex onto DNA by the checkpoint
clamp loader hRad17-replication factor C complex in vitro.";
Proc. Natl. Acad. Sci. U.S.A. 100:1633-1638(2003).
[24]
FUNCTION, IDENTIFICATION IN THE 9-1-1 COMPLEX ASSOCIATED WITH POLB, AND
INTERACTION WITH POLB.
PubMed=15314187; DOI=10.1093/nar/gkh652;
Toueille M., El-Andaloussi N., Frouin I., Freire R., Funk D., Shevelev I.,
Friedrich-Heineken E., Villani G., Hottiger M.O., Huebscher U.;
"The human Rad9/Rad1/Hus1 damage sensor clamp interacts with DNA polymerase
beta and increases its DNA substrate utilisation efficiency: implications
for DNA repair.";
Nucleic Acids Res. 32:3316-3324(2004).
[25]
FUNCTION, AND IDENTIFICATION IN THE 9-1-1 COMPLEX ASSOCIATED WITH FEN1.
PubMed=15556996; DOI=10.1073/pnas.0407686101;
Wang W., Brandt P., Rossi M.L., Lindsey-Boltz L., Podust V., Fanning E.,
Sancar A., Bambara R.A.;
"The human Rad9-Rad1-Hus1 checkpoint complex stimulates flap endonuclease
1.";
Proc. Natl. Acad. Sci. U.S.A. 101:16762-16767(2004).
[26]
FUNCTION, AND IDENTIFICATION IN THE 9-1-1 COMPLEX ASSOCIATED WITH LIG1.
PubMed=15871698; DOI=10.1042/bj20050211;
Smirnova E., Toueille M., Markkanen E., Huebscher U.;
"The human checkpoint sensor and alternative DNA clamp Rad9-Rad1-Hus1
modulates the activity of DNA ligase I, a component of the long-patch base
excision repair machinery.";
Biochem. J. 389:13-17(2005).
[27]
IDENTIFICATION IN THE 9-1-1 COMPLEX ASSOCIATED WITH FEN1, AND INTERACTION
WITH FEN1.
PubMed=16216273; DOI=10.1016/j.jmb.2005.09.018;
Friedrich-Heineken E., Toueille M., Taennler B., Buerki C., Ferrari E.,
Hottiger M.O., Huebscher U.;
"The two DNA clamps Rad9/Rad1/Hus1 complex and proliferating cell nuclear
antigen differentially regulate flap endonuclease 1 activity.";
J. Mol. Biol. 353:980-989(2005).
[28]
IDENTIFICATION IN THE 9-1-1 COMPLEX ASSOCIATED WITH RPA1 AND RPA2.
PubMed=15897895; DOI=10.1038/sj.onc.1208674;
Wu X., Shell S.M., Zou Y.;
"Interaction and colocalization of Rad9/Rad1/Hus1 checkpoint complex with
replication protein A in human cells.";
Oncogene 24:4728-4735(2005).
[29]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[30]
FUNCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=21659603; DOI=10.1126/science.1203430;
Cotta-Ramusino C., McDonald E.R. III, Hurov K., Sowa M.E., Harper J.W.,
Elledge S.J.;
"A DNA damage response screen identifies RHINO, a 9-1-1 and TopBP1
interacting protein required for ATR signaling.";
Science 332:1313-1317(2011).
[31]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-terminal
acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
-!- FUNCTION: Component of the 9-1-1 cell-cycle checkpoint response complex
that plays a major role in DNA repair (PubMed:10846170,
PubMed:10884395). The 9-1-1 complex is recruited to DNA lesion upon
damage by the RAD17-replication factor C (RFC) clamp loader complex
(PubMed:12578958). Acts then as a sliding clamp platform on DNA for
several proteins involved in long-patch base excision repair (LP-BER)
(PubMed:15871698). The 9-1-1 complex stimulates DNA polymerase beta
(POLB) activity by increasing its affinity for the 3'-OH end of the
primer-template and stabilizes POLB to those sites where LP-BER
proceeds; endonuclease FEN1 cleavage activity on substrates with
double, nick, or gap flaps of distinct sequences and lengths; and DNA
ligase I (LIG1) on long-patch base excision repair substrates
(PubMed:15314187, PubMed:15556996, PubMed:15871698). The 9-1-1 complex
is necessary for the recruitment of RHNO1 to sites of double-stranded
breaks (DSB) occurring during the S phase (PubMed:21659603). Isoform 1
possesses 3'->5' double stranded DNA exonuclease activity
(PubMed:9660799). {ECO:0000269|PubMed:10846170,
ECO:0000269|PubMed:10884395, ECO:0000269|PubMed:12578958,
ECO:0000269|PubMed:15314187, ECO:0000269|PubMed:15556996,
ECO:0000269|PubMed:15871698, ECO:0000269|PubMed:21659603,
ECO:0000269|PubMed:9660799}.
-!- CATALYTIC ACTIVITY:
Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield
nucleoside 5'-phosphates.; EC=3.1.11.2;
Evidence={ECO:0000269|PubMed:9660799};
-!- SUBUNIT: Component of the toroidal 9-1-1 (RAD9-RAD1-HUS1) complex,
composed of RAD9A, RAD1 and HUS1 (PubMed:10846170, PubMed:10884395).
The 9-1-1 complex associates with LIG1, POLB, FEN1, RAD17, HDAC1, RPA1
and RPA2 (PubMed:10846170, PubMed:10884395, PubMed:15314187,
PubMed:15556996, PubMed:15871698, PubMed:15897895, PubMed:16216273).
The 9-1-1 complex associates with the RAD17-RFC complex
(PubMed:12578958). RAD1 interacts with POLB, FEN1, HUS1, HUS1B, RAD9A
and RAD9B (PubMed:10359610, PubMed:10777662, PubMed:11944979,
PubMed:14500360, PubMed:14611806, PubMed:15314187, PubMed:15556996,
PubMed:16216273). Interacts with DNAJC7 (PubMed:11573955).
{ECO:0000269|PubMed:10359610, ECO:0000269|PubMed:10777662,
ECO:0000269|PubMed:10846170, ECO:0000269|PubMed:10884395,
ECO:0000269|PubMed:11573955, ECO:0000269|PubMed:11944979,
ECO:0000269|PubMed:12578958, ECO:0000269|PubMed:14500360,
ECO:0000269|PubMed:14611806, ECO:0000269|PubMed:15314187,
ECO:0000269|PubMed:15556996, ECO:0000269|PubMed:15871698,
ECO:0000269|PubMed:15897895, ECO:0000269|PubMed:16216273}.
-!- INTERACTION:
O60671; O60921: HUS1; NbExp=5; IntAct=EBI-721835, EBI-1056174;
O60671; Q99638: RAD9A; NbExp=2; IntAct=EBI-721835, EBI-2606224;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9716408}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=Hrad1A;
IsoId=O60671-1; Sequence=Displayed;
Name=2; Synonyms=Hrad1B;
IsoId=O60671-2; Sequence=VSP_017334;
Name=3;
IsoId=O60671-3; Sequence=VSP_017335, VSP_017336;
-!- TISSUE SPECIFICITY: Expressed in testis, uterus, bladder, spleen,
ovaries, lung, brain and muscle (at protein level).
{ECO:0000269|PubMed:9716408}.
-!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a
premature stop codon in the mRNA, leading to nonsense-mediated mRNA
decay. {ECO:0000305}.
-!- SIMILARITY: Belongs to the rad1 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC35550.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
Sequence=AAC35550.1; Type=Frameshift; Evidence={ECO:0000305};
Sequence=CAA06249.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
Sequence=CAA06249.1; Type=Frameshift; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/rad1/";
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EMBL; AF074717; AAC98093.1; -; mRNA.
EMBL; AF073524; AAC95466.1; -; mRNA.
EMBL; AF030933; AAC95427.1; -; mRNA.
EMBL; AF076841; AAC95523.1; -; mRNA.
EMBL; AF090170; AAC95603.1; -; mRNA.
EMBL; AJ004974; CAA06248.1; -; mRNA.
EMBL; AJ004975; CAA06249.1; ALT_SEQ; mRNA.
EMBL; AF011905; AAC27243.1; -; mRNA.
EMBL; AF058392; AAC14138.1; -; mRNA.
EMBL; AF084512; AAC35549.1; -; mRNA.
EMBL; AF084513; AAC35550.1; ALT_SEQ; mRNA.
EMBL; AK002112; BAG51017.1; -; mRNA.
EMBL; BT006908; AAP35554.1; -; mRNA.
EMBL; DQ451401; ABD96829.1; -; Genomic_DNA.
EMBL; CH471119; EAW55904.1; -; Genomic_DNA.
EMBL; BC006837; AAH06837.1; -; mRNA.
EMBL; BC009804; AAH09804.1; -; mRNA.
EMBL; BC037857; AAH37857.1; -; mRNA.
EMBL; AB183821; BAD86789.1; -; Genomic_DNA.
EMBL; AB183822; BAD86790.1; -; Genomic_DNA.
CCDS; CCDS3905.1; -. [O60671-1]
RefSeq; NP_002844.1; NM_002853.3. [O60671-1]
PDB; 3A1J; X-ray; 2.50 A; C=13-275.
PDB; 3G65; X-ray; 2.90 A; B=1-282.
PDB; 3GGR; X-ray; 3.20 A; C=1-282.
PDB; 6J8Y; X-ray; 2.40 A; C=1-282.
PDBsum; 3A1J; -.
PDBsum; 3G65; -.
PDBsum; 3GGR; -.
PDBsum; 6J8Y; -.
SMR; O60671; -.
BioGRID; 111771; 35.
ComplexPortal; CPX-1829; Checkpoint clamp complex.
CORUM; O60671; -.
DIP; DIP-46061N; -.
IntAct; O60671; 9.
STRING; 9606.ENSP00000371469; -.
BindingDB; O60671; -.
ChEMBL; CHEMBL3309116; -.
iPTMnet; O60671; -.
PhosphoSitePlus; O60671; -.
BioMuta; RAD1; -.
EPD; O60671; -.
jPOST; O60671; -.
MassIVE; O60671; -.
MaxQB; O60671; -.
PaxDb; O60671; -.
PeptideAtlas; O60671; -.
PRIDE; O60671; -.
ProteomicsDB; 49514; -. [O60671-1]
ProteomicsDB; 49515; -. [O60671-2]
ProteomicsDB; 49516; -. [O60671-3]
Antibodypedia; 10031; 319 antibodies.
DNASU; 5810; -.
Ensembl; ENST00000325577; ENSP00000313467; ENSG00000113456. [O60671-3]
Ensembl; ENST00000341754; ENSP00000340879; ENSG00000113456. [O60671-1]
Ensembl; ENST00000382038; ENSP00000371469; ENSG00000113456. [O60671-1]
GeneID; 5810; -.
KEGG; hsa:5810; -.
UCSC; uc003jix.4; human. [O60671-1]
CTD; 5810; -.
DisGeNET; 5810; -.
EuPathDB; HostDB:ENSG00000113456.18; -.
GeneCards; RAD1; -.
HGNC; HGNC:9806; RAD1.
HPA; ENSG00000113456; Low tissue specificity.
MIM; 603153; gene.
neXtProt; NX_O60671; -.
OpenTargets; ENSG00000113456; -.
PharmGKB; PA34166; -.
eggNOG; KOG3194; Eukaryota.
GeneTree; ENSGT00500000044913; -.
HOGENOM; CLU_035332_2_1_1; -.
InParanoid; O60671; -.
KO; K02830; -.
OMA; TCELTTY; -.
PhylomeDB; O60671; -.
TreeFam; TF101211; -.
PathwayCommons; O60671; -.
Reactome; R-HSA-176187; Activation of ATR in response to replication stress.
Reactome; R-HSA-5685938; HDR through Single Strand Annealing (SSA).
Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
Reactome; R-HSA-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
Reactome; R-HSA-69473; G2/M DNA damage checkpoint.
SIGNOR; O60671; -.
BioGRID-ORCS; 5810; 331 hits in 878 CRISPR screens.
ChiTaRS; RAD1; human.
EvolutionaryTrace; O60671; -.
GeneWiki; RAD1_homolog; -.
GenomeRNAi; 5810; -.
Pharos; O60671; Tchem.
PRO; PR:O60671; -.
Proteomes; UP000005640; Chromosome 5.
RNAct; O60671; protein.
Bgee; ENSG00000113456; Expressed in secondary oocyte and 254 other tissues.
ExpressionAtlas; O60671; baseline and differential.
Genevisible; O60671; HS.
GO; GO:0030896; C:checkpoint clamp complex; IBA:GO_Central.
GO; GO:0005694; C:chromosome; IDA:UniProtKB.
GO; GO:0042025; C:host cell nucleus; IEA:InterPro.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IC:UniProtKB.
GO; GO:0008408; F:3'-5' exonuclease activity; IDA:UniProtKB.
GO; GO:0003684; F:damaged DNA binding; TAS:ProtInc.
GO; GO:0008853; F:exodeoxyribonuclease III activity; IEA:UniProtKB-EC.
GO; GO:0006974; P:cellular response to DNA damage stimulus; TAS:ProtInc.
GO; GO:0071479; P:cellular response to ionizing radiation; IDA:UniProtKB.
GO; GO:0000077; P:DNA damage checkpoint; IMP:UniProtKB.
GO; GO:0006281; P:DNA repair; IBA:GO_Central.
GO; GO:0006260; P:DNA replication; TAS:Reactome.
GO; GO:0051598; P:meiotic recombination checkpoint; IGI:UniProtKB.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0021762; P:substantia nigra development; HEP:UniProtKB.
InterPro; IPR003011; Cell_cycle_checkpoint_Rad1.
InterPro; IPR003021; Rad1_Rec1_Rad17.
PANTHER; PTHR10870; PTHR10870; 1.
Pfam; PF02144; Rad1; 1.
PRINTS; PR01245; RAD1REC1.
PRINTS; PR01246; RAD1REPAIR.
1: Evidence at protein level;
3D-structure; Alternative splicing; DNA damage; DNA repair; Exonuclease;
Hydrolase; Nuclease; Nucleus; Polymorphism; Reference proteome.
CHAIN 1..282
/note="Cell cycle checkpoint protein RAD1"
/id="PRO_0000225005"
VAR_SEQ 67..102
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:9660799, ECO:0000303|Ref.8"
/id="VSP_017334"
VAR_SEQ 67..68
/note="AG -> GL (in isoform 3)"
/evidence="ECO:0000303|PubMed:9878245"
/id="VSP_017335"
VAR_SEQ 69..282
/note="Missing (in isoform 3)"
/evidence="ECO:0000303|PubMed:9878245"
/id="VSP_017336"
VARIANT 33
/note="A -> G (in dbSNP:rs2308951)"
/id="VAR_051718"
VARIANT 39
/note="H -> Q (in dbSNP:rs41271673)"
/evidence="ECO:0000269|Ref.11"
/id="VAR_055376"
VARIANT 104
/note="T -> S (in dbSNP:rs1805328)"
/id="VAR_051719"
VARIANT 114
/note="G -> D (in dbSNP:rs2308957)"
/id="VAR_051720"
VARIANT 281
/note="E -> G (in dbSNP:rs1805327)"
/evidence="ECO:0000269|Ref.11"
/id="VAR_051721"
MUTAGEN 226..233
/note="SLLKPSTK->AAAAAAAA: Abolishes association of the 9-
1-1 complex with RAD17."
/evidence="ECO:0000269|PubMed:10884395"
CONFLICT 135
/note="N -> T (in Ref. 2; AAC95466)"
/evidence="ECO:0000305"
STRAND 17..22
/evidence="ECO:0000244|PDB:6J8Y"
HELIX 25..32
/evidence="ECO:0000244|PDB:6J8Y"
STRAND 36..45
/evidence="ECO:0000244|PDB:6J8Y"
STRAND 48..55
/evidence="ECO:0000244|PDB:6J8Y"
TURN 56..58
/evidence="ECO:0000244|PDB:6J8Y"
STRAND 59..66
/evidence="ECO:0000244|PDB:6J8Y"
TURN 67..69
/evidence="ECO:0000244|PDB:6J8Y"
STRAND 70..78
/evidence="ECO:0000244|PDB:6J8Y"
STRAND 80..85
/evidence="ECO:0000244|PDB:6J8Y"
HELIX 86..93
/evidence="ECO:0000244|PDB:6J8Y"
TURN 94..96
/evidence="ECO:0000244|PDB:6J8Y"
STRAND 107..112
/evidence="ECO:0000244|PDB:6J8Y"
STRAND 114..117
/evidence="ECO:0000244|PDB:3G65"
STRAND 119..125
/evidence="ECO:0000244|PDB:6J8Y"
STRAND 128..134
/evidence="ECO:0000244|PDB:6J8Y"
HELIX 149..151
/evidence="ECO:0000244|PDB:6J8Y"
STRAND 152..160
/evidence="ECO:0000244|PDB:6J8Y"
HELIX 161..163
/evidence="ECO:0000244|PDB:6J8Y"
HELIX 164..167
/evidence="ECO:0000244|PDB:6J8Y"
STRAND 172..181
/evidence="ECO:0000244|PDB:6J8Y"
STRAND 183..185
/evidence="ECO:0000244|PDB:3G65"
STRAND 187..194
/evidence="ECO:0000244|PDB:6J8Y"
STRAND 197..203
/evidence="ECO:0000244|PDB:6J8Y"
STRAND 205..207
/evidence="ECO:0000244|PDB:3GGR"
STRAND 210..215
/evidence="ECO:0000244|PDB:6J8Y"
STRAND 219..224
/evidence="ECO:0000244|PDB:6J8Y"
HELIX 225..228
/evidence="ECO:0000244|PDB:6J8Y"
HELIX 231..237
/evidence="ECO:0000244|PDB:6J8Y"
STRAND 238..248
/evidence="ECO:0000244|PDB:6J8Y"
STRAND 251..258
/evidence="ECO:0000244|PDB:6J8Y"
STRAND 260..262
/evidence="ECO:0000244|PDB:3GGR"
STRAND 264..271
/evidence="ECO:0000244|PDB:6J8Y"
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


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Pathways :
WP414: Cell Cycle and Cell Division
WP707: DNA damage response
WP1579: DNA damage response
WP1530: miRNA regulation of DNA Damage Response
WP2087: miRNA regulation of DNA Damage Response
WP1566: Citrate cycle (TCA cycle)
WP1678: Nucleotide excision repair
WP1625: Base excision repair
WP1672: Mismatch repair
WP1657: Glycerolipid metabolism
WP1493: Carbon assimilation C4 pathway
WP1700: Selenoamino acid metabolism
WP1200: Cell cycle
WP1775: Cell Cycle Checkpoints
WP31: Cell cycle
WP1663: Homologous recombination
WP1888: Post-translational protein modification
WP232: G Protein Signaling Pathways
WP1078: G1 to S cell cycle control
WP179: Cell cycle
WP1673: Naphthalene and anthracene degradation
WP1900: Regulation of mitotic cell cycle
WP525: Mitochondrial Unfolded-Protein Response
WP1613: 1,4-Dichlorobenzene degradation
WP2371: Parkinsons Disease Pathway

Related Genes :
[RAD1 REC1] Cell cycle checkpoint protein RAD1 (hRAD1) (EC 3.1.11.2) (DNA repair exonuclease rad1 homolog) (Rad1-like DNA damage checkpoint protein)
[Rad1 Rec1] Cell cycle checkpoint protein RAD1 (mRAD1) (EC 3.1.11.2) (DNA repair exonuclease rad1 homolog) (Rad1-like DNA damage checkpoint protein)
[RAD9A] Cell cycle checkpoint control protein RAD9A (hRAD9) (EC 3.1.11.2) (DNA repair exonuclease rad9 homolog A)
[RAD1 YPL022W] DNA repair protein RAD1
[Rad9a Rad9] Cell cycle checkpoint control protein RAD9A (mRAD9) (EC 3.1.11.2) (DNA repair exonuclease rad9 homolog A) (Rad9-like protein)
[RAD17 R24L] Cell cycle checkpoint protein RAD17 (hRad17) (RF-C/activator 1 homolog)
[lem-3 rad-1 F42H11.2] Ankyrin repeat and LEM domain-containing protein 1 homolog (EC 3.1.-.-) (LEM-domain containing protein 3)
[HUS1] Checkpoint protein HUS1 (hHUS1)
[RAD1] Cell cycle checkpoint protein RAD1 (EC 3.1.11.2) (DNA repair exonuclease rad1 homolog)
[RAD17 YOR368W] DNA damage checkpoint control protein RAD17 (DNA repair exonuclease RAD17)
[Rad17] Cell cycle checkpoint protein RAD17
[MEC1 ESR1 SAD3 YBR136W YBR1012] Serine/threonine-protein kinase MEC1 (EC 2.7.11.1) (ATR homolog) (DNA-damage checkpoint kinase MEC1) (Mitosis entry checkpoint protein 1)
[CHEK1 CHK1] Serine/threonine-protein kinase Chk1 (EC 2.7.11.1) (CHK1 checkpoint homolog) (Cell cycle checkpoint kinase) (Checkpoint kinase-1)
[Hus1] Checkpoint protein HUS1 (mHUS1)
[TEL1 YBL088C YBL0706] Serine/threonine-protein kinase TEL1 (EC 2.7.11.1) (ATM homolog) (DNA-damage checkpoint kinase TEL1) (Telomere length regulation protein 1)
[tel1 SPCC23B6.03c] Serine/threonine-protein kinase tel1 (EC 2.7.11.1) (ATM homolog) (DNA-damage checkpoint kinase tel1) (Telomere length regulation protein 1)
[crb2 rhp9 SPBC342.05] DNA repair protein crb2 (Checkpoint mediator protein crb2) (Cut5-repeat binding protein 2) (RAD9 protein homolog)
[topbp1-A cut5] DNA topoisomerase 2-binding protein 1-A (Cut5 protein) (DNA topoisomerase II-binding protein 1-A) (TopBP1-A) (XtopBP)
[CHEK2 CDS1 CHK2 RAD53] Serine/threonine-protein kinase Chk2 (EC 2.7.11.1) (CHK2 checkpoint homolog) (Cds1 homolog) (Hucds1) (hCds1) (Checkpoint kinase 2)
[Chek1 Chk1] Serine/threonine-protein kinase Chk1 (EC 2.7.11.1) (CHK1 checkpoint homolog) (Checkpoint kinase-1)
[Chek1 Chk1] Serine/threonine-protein kinase Chk1 (EC 2.7.11.1) (CHK1 checkpoint homolog) (Checkpoint kinase-1)
[rad16 rad10 rad20 swi9 SPCC970.01] DNA repair protein rad16 (EC 3.1.-.-)
[MSH3 YCR092C YCR1152 YCR92C] DNA mismatch repair protein MSH3 (Mismatch-binding protein) (MBP) (MutS protein homolog 3)
[MSH2 YOL090W O0935] DNA mismatch repair protein MSH2 (MutS protein homolog 2)
[DDC1 YPL194W] DNA damage checkpoint protein 1
[chek1 chk1] Serine/threonine-protein kinase Chk1 (EC 2.7.11.1) (CHK1 checkpoint homolog) (Checkpoint kinase-1) (xChk1)
[CHEK1 CHK1] Serine/threonine-protein kinase Chk1 (EC 2.7.11.1) (CHK1 checkpoint homolog) (Checkpoint kinase-1)
[MEC3 PIP3 PSO9 YLR288C L8003.15] DNA damage checkpoint control protein MEC3
[MRE11 HNGS1 MRE11A] Double-strand break repair protein MRE11 (EC 3.1.-.-) (Double-strand break repair protein MRE11A) (Meiotic recombination 11 homolog 1) (MRE11 homolog 1) (Meiotic recombination 11 homolog A) (MRE11 homolog A)
[BUB1B BUBR1 MAD3L SSK1] Mitotic checkpoint serine/threonine-protein kinase BUB1 beta (EC 2.7.11.1) (MAD3/BUB1-related protein kinase) (hBUBR1) (Mitotic checkpoint kinase MAD3L) (Protein SSK1)

Bibliography :