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Cell cycle checkpoint protein RAD17 (hRad17) (RF-C/activator 1 homolog)

 RAD17_HUMAN             Reviewed;         681 AA.
O75943; A8K8X2; D3DWA5; O75714; Q7Z3S4; Q9UNK7; Q9UNR7; Q9UNR8; Q9UPF5;
29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
29-MAR-2005, sequence version 2.
12-AUG-2020, entry version 179.
RecName: Full=Cell cycle checkpoint protein RAD17;
Short=hRad17;
AltName: Full=RF-C/activator 1 homolog;
Name=RAD17; Synonyms=R24L;
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 2).
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).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND INTERACTION
WITH RAD1.
TISSUE=Neuroblastoma;
PubMed=9660800; DOI=10.1074/jbc.273.29.18340;
Parker A.E., Van de Weyer I., Laus M.C., Verhasselt P., Luyten W.H.M.L.;
"Identification of a human homologue of the Schizosaccharomyces pombe
rad17+ checkpoint gene.";
J. Biol. Chem. 273:18340-18346(1998).
[3]
ERRATUM OF PUBMED:9660800.
Parker A.E., Van de Weyer I., Laus M.C., Verhasselt P., Luyten W.H.M.L.;
J. Biol. Chem. 274:24438-24438(1999).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, SUBCELLULAR
LOCATION, AND VARIANT ARG-557.
TISSUE=Fibroblast;
PubMed=10232579;
Bao S., Chang M.-S., Auclair D., Sun Y., Wang Y., Wong W.-K., Zhang J.,
Liu Y., Qian X., Sutherland R., Magi-Galluzi C., Weisberg E., Cheng E.Y.S.,
Hao L., Sasaki H., Campbell M.S., Kraeft S.-K., Loda M., Lo K.-M.,
Chen L.B.;
"HRad17, a human homologue of the Schizosaccharomyces pombe checkpoint gene
rad17, is overexpressed in colon carcinoma.";
Cancer Res. 59:2023-2028(1999).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND ALTERNATIVE SPLICING.
TISSUE=Thymus;
PubMed=9933569; DOI=10.1006/geno.1998.5642;
Bluyssen H.A.R., Naus N.C., van Os R.I., Jaspers I., Hoeijmakers J.H.J.,
de Klein A.;
"Human and mouse homologs of the Schizosaccharomyces pombe rad17+ cell
cycle checkpoint control gene.";
Genomics 55:219-228(1999).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2), AND TISSUE
SPECIFICITY.
TISSUE=Fetal brain;
PubMed=10480350; DOI=10.1007/s004399900067;
von Deimling F., Scharf J.M., Liehr T., Rothe M., Kelter A.-R., Albers P.,
Dietrich W.F., Kunkel L.M., Wernert N., Wirth B.;
"Human and mouse RAD17 genes: identification, localization, genomic
structure and histological expression pattern in normal testis and
seminoma.";
Hum. Genet. 105:17-27(1999).
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND FUNCTION.
TISSUE=Cervix carcinoma;
PubMed=10208430; DOI=10.1038/sj.onc.1202469;
Li L., Peterson C.A., Kanter-Smoler G., Wei Y.-F., Ramagli L.S.,
Sunnerhagen P., Siciliano M.J., Legerski R.J.;
"hRAD17, a structural homolog of the Schizosaccharomyces pombe RAD17 cell
cycle checkpoint gene, stimulates p53 accumulation.";
Oncogene 18:1689-1699(1999).
[8]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Liver;
PubMed=11715513;
Han Y., Zhu Y.;
"Human hR24L gene is involved in DNA excision repair and recombination
repair.";
Zhonghua Yi Xue Za Zhi 79:941-943(1999).
[9]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), INDUCTION, AND TISSUE
SPECIFICITY.
TISSUE=Colon, and Fibroblast;
PubMed=11602352; DOI=10.1016/s0378-1119(01)00692-8;
Chen M.-S., Higashikubo R., Laszlo A., Roti Roti J.;
"Multiple alternative splicing forms of human RAD17 and their differential
response to ionizing radiation.";
Gene 277:145-152(2001).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Testis;
PubMed=11230166; DOI=10.1101/gr.gr1547r;
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and analysis of
500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Testis;
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).
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Fetal brain;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[13]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-32; LEU-487; GLU-535
AND ARG-557.
NIEHS SNPs program;
Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
[14]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[15]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ARG-557.
TISSUE=Brain;
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).
[16]
SUBCELLULAR LOCATION, AND INTERACTION WITH SNU13.
PubMed=10593953; DOI=10.1074/jbc.274.51.36544;
Chang M.-S., Sasaki H., Campbell M.S., Kraeft S.-K., Sutherland R.,
Yang C.-Y., Liu Y., Auclair D., Hao L., Sonoda H., Ferland L.H., Chen L.B.;
"HRad17 colocalizes with NHP2L1 in the nucleolus and redistributes after UV
irradiation.";
J. Biol. Chem. 274:36544-36549(1999).
[17]
INTERACTION WITH THE RAD1/RAD9/HUS1 COMPLEX AND RFC3, AND MUTAGENESIS OF
LYS-143.
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).
[18]
FUNCTION, INTERACTION WITH ATM; ATR AND RAD1, PHOSPHORYLATION AT SER-646
AND SER-656, AND MUTAGENESIS OF SER-646 AND SER-656.
PubMed=11418864; DOI=10.1038/35082110;
Bao S., Tibbetts R.S., Brumbaugh K.M., Fang Y., Richardson D.A., Ali A.,
Chen S.M., Abraham R.T., Wang X.-F.;
"ATR/ATM-mediated phosphorylation of human Rad17 is required for genotoxic
stress responses.";
Nature 411:969-974(2001).
[19]
IDENTIFICATION IN A COMPLEX WITH RFC2; RFC3; RFC4 AND RFC5.
PubMed=11572977; DOI=10.1073/pnas.201373498;
Lindsey-Boltz L.A., Bermudez V.P., Hurwitz J., Sancar A.;
"Purification and characterization of human DNA damage checkpoint Rad
complexes.";
Proc. Natl. Acad. Sci. U.S.A. 98:11236-11241(2001).
[20]
FUNCTION, PHOSPHORYLATION AT SER-646 AND SER-656, INTERACTION WITH RFC4,
AND MUTAGENESIS OF SER-191; SER-646 AND SER-656.
PubMed=11687627; DOI=10.1073/pnas.231364598;
Post S.M., Weng Y.-C., Cimprich K., Chen L.B., Xu Y., Lee E.Y.-H.P.;
"Phosphorylation of serines 635 and 645 of human Rad17 is cell cycle
regulated and is required for G(1)/S checkpoint activation in response to
DNA damage.";
Proc. Natl. Acad. Sci. U.S.A. 98:13102-13107(2001).
[21]
FUNCTION, PHOSPHORYLATION, MUTAGENESIS OF LYS-143, AND SUBCELLULAR
LOCATION.
PubMed=11799063; DOI=10.1101/gad.950302;
Zou L., Cortez D., Elledge S.J.;
"Regulation of ATR substrate selection by Rad17-dependent loading of Rad9
complexes onto chromatin.";
Genes Dev. 16:198-208(2002).
[22]
SUBCELLULAR LOCATION, AND INTERACTION WITH RFC4.
PubMed=12400013; DOI=10.1038/sj.onc.1205872;
Dahm K., Huebscher U.;
"Colocalization of human Rad17 and PCNA in late S phase of the cell cycle
upon replication block.";
Oncogene 21:7710-7719(2002).
[23]
FUNCTION.
PubMed=12672690; DOI=10.1101/gad.1065103;
Wang X., Zou L., Zheng H., Wei Q., Elledge S.J., Li L.;
"Genomic instability and endoreduplication triggered by RAD17 deletion.";
Genes Dev. 17:965-970(2003).
[24]
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).
[25]
FUNCTION, PHOSPHORYLATION AT SER-646 AND SER-656, MUTAGENESIS OF SER-646
AND SER-656, AND INTERACTION WITH POLE.
PubMed=14500819; DOI=10.1093/nar/gkg765;
Post S.M., Tomkinson A.E., Lee E.Y.-H.P.;
"The human checkpoint Rad protein Rad17 is chromatin-associated throughout
the cell cycle, localizes to DNA replication sites, and interacts with DNA
polymerase epsilon.";
Nucleic Acids Res. 31:5568-5575(2003).
[26]
FUNCTION, INTERACTION WITH RFC2; RFC3; RFC4 AND RFC5, AND IDENTIFICATION BY
MASS SPECTROMETRY.
PubMed=14624239; DOI=10.1371/journal.pbio.0000033;
Ellison V., Stillman B.;
"Biochemical characterization of DNA damage checkpoint complexes: clamp
loader and clamp complexes with specificity for 5' recessed DNA.";
PLoS Biol. 1:231-243(2003).
[27]
FUNCTION, AND INTERACTION WITH RAD1 AND RAD9.
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).
[28]
INTERACTION WITH PPP5C, AND PHOSPHORYLATION AT SER-646.
PubMed=14871926; DOI=10.1101/gad.1176004;
Ali A., Zhang J., Bao S., Liu I., Otterness D., Dean N.M., Abraham R.T.,
Wang X.F.;
"Requirement of protein phosphatase 5 in DNA-damage-induced ATM
activation.";
Genes Dev. 18:249-254(2004).
[29]
FUNCTION, AND INTERACTION WITH MCM7.
PubMed=15538388; DOI=10.1038/sj.emboj.7600463;
Tsao C.-C., Geisen C., Abraham R.T.;
"Interaction between human MCM7 and Rad17 proteins is required for
replication checkpoint signaling.";
EMBO J. 23:4660-4669(2004).
[30]
FUNCTION, AND MUTAGENESIS OF LYS-143; SER-646 AND SER-656.
PubMed=15235112;
Garg R., Callens S., Lim D.-S., Canman C.E., Kastan M.B., Xu B.;
"Chromatin association of rad17 is required for an ataxia telangiectasia
and rad-related kinase-mediated S-phase checkpoint in response to low-dose
ultraviolet radiation.";
Mol. Cancer Res. 2:362-369(2004).
[31]
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).
[32]
FUNCTION.
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).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71; SER-86 AND SER-359, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
-!- FUNCTION: Essential for sustained cell growth, maintenance of
chromosomal stability, and ATR-dependent checkpoint activation upon DNA
damage. Has a weak ATPase activity required for binding to chromatin.
Participates in the recruitment of the RAD1-RAD9-HUS1 complex and RHNO1
onto chromatin, and in CHEK1 activation. May also serve as a sensor of
DNA replication progression, and may be involved in homologous
recombination. {ECO:0000269|PubMed:10208430,
ECO:0000269|PubMed:11418864, ECO:0000269|PubMed:11687627,
ECO:0000269|PubMed:11799063, ECO:0000269|PubMed:12578958,
ECO:0000269|PubMed:12672690, ECO:0000269|PubMed:14500819,
ECO:0000269|PubMed:14624239, ECO:0000269|PubMed:15235112,
ECO:0000269|PubMed:15538388, ECO:0000269|PubMed:21659603}.
-!- SUBUNIT: Part of a DNA-binding complex containing RFC2, RFC3, RFC4 and
RFC5. Interacts with RAD1 and RAD9 within the RAD1-RAD9-HUS1 complex.
Interacts with RAD9B, POLE, SNU13 and MCM7. DNA damage promotes
interaction with ATR or ATM and disrupts interaction with the RAD1-
RAD9-HUS1 complex. {ECO:0000269|PubMed:10593953,
ECO:0000269|PubMed:10884395, ECO:0000269|PubMed:11418864,
ECO:0000269|PubMed:11572977, ECO:0000269|PubMed:11687627,
ECO:0000269|PubMed:12400013, ECO:0000269|PubMed:12578958,
ECO:0000269|PubMed:14500819, ECO:0000269|PubMed:14611806,
ECO:0000269|PubMed:14624239, ECO:0000269|PubMed:14871926,
ECO:0000269|PubMed:15538388, ECO:0000269|PubMed:9660800}.
-!- INTERACTION:
O75943; Q9UM11: FZR1; NbExp=2; IntAct=EBI-968231, EBI-724997;
O75943; P49959: MRE11; NbExp=2; IntAct=EBI-968231, EBI-396513;
O75943; O60934: NBN; NbExp=5; IntAct=EBI-968231, EBI-494844;
O75943; Q92878: RAD50; NbExp=2; IntAct=EBI-968231, EBI-495494;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10232579,
ECO:0000269|PubMed:10593953, ECO:0000269|PubMed:11799063,
ECO:0000269|PubMed:12400013}. Note=Phosphorylated form redistributes to
discrete nuclear foci upon DNA damage.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=Rad17Sp, FM2;
IsoId=O75943-1; Sequence=Displayed;
Name=2; Synonyms=Rad17Sp2, FM1;
IsoId=O75943-2; Sequence=VSP_013308;
Name=3; Synonyms=FM3;
IsoId=O75943-3; Sequence=VSP_013306;
Name=4; Synonyms=FM4;
IsoId=O75943-4; Sequence=VSP_013307, VSP_013309;
-!- TISSUE SPECIFICITY: Overexpressed in various cancer cell lines and in
colon carcinoma (at protein level). Isoform 2 and isoform 3 are the
most abundant isoforms in non irradiated cells (at protein level).
Ubiquitous at low levels. Highly expressed in testis, where it is
expressed within the germinal epithelium of the seminiferous tubuli.
Weakly expressed in seminomas (testicular tumors).
{ECO:0000269|PubMed:10208430, ECO:0000269|PubMed:10232579,
ECO:0000269|PubMed:10480350, ECO:0000269|PubMed:11602352,
ECO:0000269|PubMed:9660800}.
-!- INDUCTION: Isoform 1, isoform 3 and isoform 4 are induced by X-ray
irradiation. {ECO:0000269|PubMed:11602352}.
-!- PTM: Phosphorylated. Phosphorylation on Ser-646 and Ser-656 is cell
cycle-regulated, enhanced by genotoxic stress, and required for
activation of checkpoint signaling. Phosphorylation is mediated by ATR
upon UV or replication arrest, whereas it may be mediated both by ATR
and ATM upon ionizing radiation. Phosphorylation on both sites is
required for interaction with RAD1 but dispensable for interaction with
RFC3 or RFC4. {ECO:0000269|PubMed:11418864,
ECO:0000269|PubMed:11687627, ECO:0000269|PubMed:11799063,
ECO:0000269|PubMed:14500819, ECO:0000269|PubMed:14871926}.
-!- SIMILARITY: Belongs to the rad17/RAD24 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/rad17/";
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EMBL; AF076838; AAC95520.1; -; mRNA.
EMBL; AJ004977; CAA06251.1; -; mRNA.
EMBL; AF112263; AAD38878.1; -; mRNA.
EMBL; AF085736; AAC36334.1; -; mRNA.
EMBL; AJ001642; CAA04894.1; -; mRNA.
EMBL; AJ131296; CAB46364.1; -; Genomic_DNA.
EMBL; AJ131297; CAB46364.1; JOINED; Genomic_DNA.
EMBL; AJ131298; CAB46364.1; JOINED; Genomic_DNA.
EMBL; AJ131299; CAB46364.1; JOINED; Genomic_DNA.
EMBL; AJ131300; CAB46364.1; JOINED; Genomic_DNA.
EMBL; AJ131301; CAB46364.1; JOINED; Genomic_DNA.
EMBL; AJ131302; CAB46364.1; JOINED; Genomic_DNA.
EMBL; AJ131303; CAB46364.1; JOINED; Genomic_DNA.
EMBL; AJ131304; CAB46364.1; JOINED; Genomic_DNA.
EMBL; AJ131305; CAB46364.1; JOINED; Genomic_DNA.
EMBL; AJ131306; CAB46364.1; JOINED; Genomic_DNA.
EMBL; AJ131307; CAB46364.1; JOINED; Genomic_DNA.
EMBL; AJ131308; CAB46364.1; JOINED; Genomic_DNA.
EMBL; AF017748; AAD01620.1; -; mRNA.
EMBL; AF126424; AAD17334.1; -; mRNA.
EMBL; AF098533; AAC97950.1; -; mRNA.
EMBL; AF098534; AAC97951.1; -; mRNA.
EMBL; AL122068; CAB59244.1; -; mRNA.
EMBL; AK292487; BAF85176.1; -; mRNA.
EMBL; BX537441; CAD97683.1; -; mRNA.
EMBL; AY612854; AAT09763.1; -; Genomic_DNA.
EMBL; CH471137; EAW51283.1; -; Genomic_DNA.
EMBL; CH471137; EAW51284.1; -; Genomic_DNA.
EMBL; CH471137; EAW51285.1; -; Genomic_DNA.
EMBL; CH471137; EAW51286.1; -; Genomic_DNA.
EMBL; CH471137; EAW51288.1; -; Genomic_DNA.
EMBL; BC032304; AAH32304.1; -; mRNA.
CCDS; CCDS4003.1; -. [O75943-1]
CCDS; CCDS4004.1; -. [O75943-2]
CCDS; CCDS4005.1; -. [O75943-4]
CCDS; CCDS47226.1; -. [O75943-3]
PIR; T34548; T34548.
RefSeq; NP_001265551.1; NM_001278622.1. [O75943-2]
RefSeq; NP_002864.1; NM_002873.1. [O75943-2]
RefSeq; NP_579916.1; NM_133338.2. [O75943-2]
RefSeq; NP_579917.1; NM_133339.2. [O75943-1]
RefSeq; NP_579918.1; NM_133340.2. [O75943-3]
RefSeq; NP_579919.1; NM_133341.2. [O75943-4]
RefSeq; NP_579920.1; NM_133342.2. [O75943-2]
RefSeq; NP_579921.1; NM_133343.1. [O75943-2]
RefSeq; NP_579922.1; NM_133344.2. [O75943-2]
RefSeq; XP_016865168.1; XM_017009679.1.
RefSeq; XP_016865169.1; XM_017009680.1.
RefSeq; XP_016865170.1; XM_017009681.1. [O75943-2]
BioGRID; 111821; 35.
CORUM; O75943; -.
DIP; DIP-24254N; -.
DIP; DIP-34896N; -.
IntAct; O75943; 17.
MINT; O75943; -.
STRING; 9606.ENSP00000426191; -.
iPTMnet; O75943; -.
PhosphoSitePlus; O75943; -.
BioMuta; RAD17; -.
jPOST; O75943; -.
MassIVE; O75943; -.
MaxQB; O75943; -.
PaxDb; O75943; -.
PeptideAtlas; O75943; -.
PRIDE; O75943; -.
ProteomicsDB; 50304; -. [O75943-1]
ProteomicsDB; 50305; -. [O75943-2]
ProteomicsDB; 50306; -. [O75943-3]
ProteomicsDB; 50307; -. [O75943-4]
Antibodypedia; 1389; 621 antibodies.
DNASU; 5884; -.
Ensembl; ENST00000282891; ENSP00000282891; ENSG00000152942. [O75943-4]
Ensembl; ENST00000305138; ENSP00000303134; ENSG00000152942. [O75943-2]
Ensembl; ENST00000345306; ENSP00000311227; ENSG00000152942. [O75943-2]
Ensembl; ENST00000354312; ENSP00000346271; ENSG00000152942. [O75943-2]
Ensembl; ENST00000354868; ENSP00000346938; ENSG00000152942. [O75943-2]
Ensembl; ENST00000358030; ENSP00000350725; ENSG00000152942. [O75943-3]
Ensembl; ENST00000361732; ENSP00000355226; ENSG00000152942. [O75943-2]
Ensembl; ENST00000380774; ENSP00000370151; ENSG00000152942. [O75943-1]
Ensembl; ENST00000509734; ENSP00000426191; ENSG00000152942. [O75943-1]
Ensembl; ENST00000521422; ENSP00000427743; ENSG00000152942. [O75943-3]
Ensembl; ENST00000610770; ENSP00000478167; ENSG00000276618.
Ensembl; ENST00000611523; ENSP00000477962; ENSG00000276618.
Ensembl; ENST00000612044; ENSP00000477996; ENSG00000276618.
Ensembl; ENST00000616488; ENSP00000484854; ENSG00000276618.
Ensembl; ENST00000616683; ENSP00000482775; ENSG00000152942. [O75943-2]
Ensembl; ENST00000616759; ENSP00000479160; ENSG00000276618.
Ensembl; ENST00000620889; ENSP00000482371; ENSG00000276618.
GeneID; 5884; -.
KEGG; hsa:5884; -.
UCSC; uc003jwg.4; human. [O75943-1]
CTD; 5884; -.
DisGeNET; 5884; -.
EuPathDB; HostDB:ENSG00000152942.18; -.
GeneCards; RAD17; -.
HGNC; HGNC:9807; RAD17.
HPA; ENSG00000152942; Low tissue specificity.
MIM; 603139; gene.
neXtProt; NX_O75943; -.
OpenTargets; ENSG00000152942; -.
PharmGKB; PA34167; -.
eggNOG; KOG1970; Eukaryota.
GeneTree; ENSGT00440000039046; -.
HOGENOM; CLU_018598_0_0_1; -.
InParanoid; O75943; -.
KO; K06662; -.
OMA; EPWVDRY; -.
OrthoDB; 674169at2759; -.
PhylomeDB; O75943; -.
PathwayCommons; O75943; -.
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; O75943; -.
BioGRID-ORCS; 5884; 606 hits in 881 CRISPR screens.
ChiTaRS; RAD17; human.
GeneWiki; RAD17; -.
GenomeRNAi; 5884; -.
Pharos; O75943; Tbio.
PRO; PR:O75943; -.
Proteomes; UP000005640; Chromosome 5.
RNAct; O75943; protein.
Bgee; ENSG00000152942; Expressed in testis and 247 other tissues.
ExpressionAtlas; O75943; baseline and differential.
Genevisible; O75943; HS.
GO; GO:0042025; C:host cell nucleus; IEA:InterPro.
GO; GO:0000790; C:nuclear chromatin; IBA:GO_Central.
GO; GO:0005730; C:nucleolus; IDA:GO_Central.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; TAS:ProtInc.
GO; GO:0031389; C:Rad17 RFC-like complex; IEA:InterPro.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
GO; GO:0003689; F:DNA clamp loader activity; IEA:InterPro.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP: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:0000076; P:DNA replication checkpoint; TAS:ProtInc.
GO; GO:0007093; P:mitotic cell cycle checkpoint; IMP:UniProtKB.
GO; GO:0033314; P:mitotic DNA replication checkpoint; IBA:GO_Central.
GO; GO:0008156; P:negative regulation of DNA replication; IMP:UniProtKB.
GO; GO:0042325; P:regulation of phosphorylation; IMP:UniProtKB.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
InterPro; IPR004582; Checkpoint_prot_Rad17_Rad24.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR018324; Rad17/Rad24_fun/met.
PANTHER; PTHR12172; PTHR12172; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00602; rad24; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Cell cycle; DNA damage;
Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome.
CHAIN 1..681
/note="Cell cycle checkpoint protein RAD17"
/id="PRO_0000209948"
NP_BIND 137..144
/note="ATP"
/evidence="ECO:0000255"
REGION 432..681
/note="Interaction with MCM7"
/evidence="ECO:0000269|PubMed:15538388"
MOD_RES 55
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:Q9XT62"
MOD_RES 71
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 86
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 359
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 646
/note="Phosphoserine; by ATR and ATM"
/evidence="ECO:0000269|PubMed:11418864,
ECO:0000269|PubMed:11687627, ECO:0000269|PubMed:14500819,
ECO:0000269|PubMed:14871926"
MOD_RES 656
/note="Phosphoserine; by ATR and ATM"
/evidence="ECO:0000269|PubMed:11418864,
ECO:0000269|PubMed:11687627, ECO:0000269|PubMed:14500819"
VAR_SEQ 1..176
/note="Missing (in isoform 3)"
/evidence="ECO:0000303|PubMed:11602352"
/id="VSP_013306"
VAR_SEQ 1..97
/note="Missing (in isoform 4)"
/evidence="ECO:0000303|PubMed:11602352"
/id="VSP_013307"
VAR_SEQ 1..14
/note="MSKTFLRPKVSSTK -> MNQ (in isoform 2)"
/evidence="ECO:0000303|PubMed:10208430,
ECO:0000303|PubMed:10232579, ECO:0000303|PubMed:10480350,
ECO:0000303|PubMed:11230166, ECO:0000303|PubMed:11602352,
ECO:0000303|PubMed:11715513, ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005,
ECO:0000303|PubMed:9660800, ECO:0000303|PubMed:9878245"
/id="VSP_013308"
VAR_SEQ 98..99
/note="ET -> MN (in isoform 4)"
/evidence="ECO:0000303|PubMed:11602352"
/id="VSP_013309"
VARIANT 32
/note="V -> I (in dbSNP:rs17229831)"
/evidence="ECO:0000269|Ref.13"
/id="VAR_021574"
VARIANT 487
/note="R -> L (in dbSNP:rs17236478)"
/evidence="ECO:0000269|Ref.13"
/id="VAR_021575"
VARIANT 535
/note="K -> E (in dbSNP:rs17236485)"
/evidence="ECO:0000269|Ref.13"
/id="VAR_021576"
VARIANT 557
/note="L -> R (in dbSNP:rs1045051)"
/evidence="ECO:0000269|PubMed:10232579,
ECO:0000269|PubMed:15489334, ECO:0000269|Ref.13"
/id="VAR_021577"
MUTAGEN 143
/note="K->E: Impairs phosphorylation on S-656. Abolishes
interaction with the RAD1-RAD9-HUS1 complex; does not
affect interaction with RFC3."
/evidence="ECO:0000269|PubMed:10884395,
ECO:0000269|PubMed:11799063, ECO:0000269|PubMed:15235112"
MUTAGEN 143
/note="K->G: Impairs phosphorylation. Impairs interaction
with DNA and the RAD1-RAD9-HUS1 complex; does not affect
interaction with RFC3."
/evidence="ECO:0000269|PubMed:10884395,
ECO:0000269|PubMed:11799063, ECO:0000269|PubMed:15235112"
MUTAGEN 191
/note="S->A: No effect on phosphorylation by ATR."
/evidence="ECO:0000269|PubMed:11687627"
MUTAGEN 646
/note="S->A: Reduces by 50% phosphorylation by ATR, and
abolishes interaction with RAD1. Abolishes phosphorylation
by ATR and checkpoint activation without affecting
interaction with RFC3, RFC4, ATM or ATR; when associated
with A-656."
/evidence="ECO:0000269|PubMed:11418864,
ECO:0000269|PubMed:11687627, ECO:0000269|PubMed:14500819,
ECO:0000269|PubMed:15235112"
MUTAGEN 646
/note="S->D: Abolishes interaction with RAD1; when
associated with D-656."
/evidence="ECO:0000269|PubMed:11418864,
ECO:0000269|PubMed:11687627, ECO:0000269|PubMed:14500819,
ECO:0000269|PubMed:15235112"
MUTAGEN 656
/note="S->A: Reduces by 50% phosphorylation by ATR, and
abolishes interaction with RAD1. Abolishes phosphorylation
by ATR and checkpoint activation without affecting
interaction with RFC3, RFC4, ATM or ATR; when associated
with A-646."
/evidence="ECO:0000269|PubMed:11418864,
ECO:0000269|PubMed:11687627, ECO:0000269|PubMed:14500819,
ECO:0000269|PubMed:15235112"
MUTAGEN 656
/note="S->D: Abolishes interaction with RAD1; when
associated with D-646."
/evidence="ECO:0000269|PubMed:11418864,
ECO:0000269|PubMed:11687627, ECO:0000269|PubMed:14500819,
ECO:0000269|PubMed:15235112"
CONFLICT 75
/note="I -> V (in Ref. 12; CAD97683)"
/evidence="ECO:0000305"
CONFLICT 187
/note="F -> L (in Ref. 5; AAC36334)"
/evidence="ECO:0000305"
CONFLICT 194
/note="A -> S (in Ref. 7; AAD01620)"
/evidence="ECO:0000305"
CONFLICT 340
/note="L -> P (in Ref. 5; AAC36334)"
/evidence="ECO:0000305"
CONFLICT 445
/note="P -> S (in Ref. 5; AAC36334)"
/evidence="ECO:0000305"
CONFLICT 462
/note="M -> T (in Ref. 5; AAC36334)"
/evidence="ECO:0000305"
CONFLICT 648
/note="N -> D (in Ref. 5; AAC36334)"
/evidence="ECO:0000305"
CONFLICT 672
/note="I -> M (in Ref. 5; AAC36334)"
/evidence="ECO:0000305"
SEQUENCE 681 AA; 77055 MW; 796C2BD48F7995A3 CRC64;
MSKTFLRPKV SSTKVTDWVD PSFDDFLECS GVSTITATSL GVNNSSHRRK NGPSTLESSR
FPARKRGNLS SLEQIYGLEN SKEYLSENEP WVDKYKPETQ HELAVHKKKI EEVETWLKAQ
VLERQPKQGG SILLITGPPG CGKTTTLKIL SKEHGIQVQE WINPVLPDFQ KDDFKGMFNT
ESSFHMFPYQ SQIAVFKEFL LRATKYNKLQ MLGDDLRTDK KIILVEDLPN QFYRDSHTLH
EVLRKYVRIG RCPLIFIISD SLSGDNNQRL LFPKEIQEEC SISNISFNPV APTIMMKFLN
RIVTIEANKN GGKITVPDKT SLELLCQGCS GDIRSAINSL QFSSSKGENN LRPRKKGMSL
KSDAVLSKSK RRKKPDRVFE NQEVQAIGGK DVSLFLFRAL GKILYCKRAS LTELDSPRLP
SHLSEYERDT LLVEPEEVVE MSHMPGDLFN LYLHQNYIDF FMEIDDIVRA SEFLSFADIL
SGDWNTRSLL REYSTSIATR GVMHSNKARG YAHCQGGGSS FRPLHKPQWF LINKKYRENC
LAAKALFPDF CLPALCLQTQ LLPYLALLTI PMRNQAQISF IQDIGRLPLK RHFGRLKMEA
LTDREHGMID PDSGDEAQLN GGHSAEESLG EPTQATVPET WSLPLSQNSA SELPASQPQP
FSAQGDMEEN IIIEDYESDG T


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Pathways :
WP414: Cell Cycle and Cell Division
WP844: Cell cycle
WP1083: Cell cycle
WP445: G1 to S cell cycle control
WP348: G1 to S cell cycle control
WP179: Cell cycle
WP840: G1 to S cell cycle control
WP1078: G1 to S cell cycle control
WP1393: Cell cycle
WP31: Cell cycle
WP964: Cell cycle
WP1900: Regulation of mitotic cell cycle
WP1782: APC/C-mediated degradation of cell cycle proteins
WP1200: Cell cycle
WP413: G1 to S cell cycle control
WP429: Cell cycle
WP45: G1 to S cell cycle control
WP959: G1 to S cell cycle control
WP190: Cell cycle
WP1775: Cell Cycle Checkpoints
WP1792: Cell Cycle, Mitotic
WP1195: G1 to S cell cycle control
WP1566: Citrate cycle (TCA cycle)
WP2005: Muscle cell TarBase
WP2414: Quercetin and Nf-kB/ AP-1 induced cell apoptosis

Related Genes :
[RAD17 R24L] Cell cycle checkpoint protein RAD17 (hRad17) (RF-C/activator 1 homolog)
[Rad17] Cell cycle checkpoint protein RAD17
[RAD1 REC1] Cell cycle checkpoint protein RAD1 (hRAD1) (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)
[RFC3] Replication factor C subunit 3 (Activator 1 38 kDa subunit) (A1 38 kDa subunit) (Activator 1 subunit 3) (Replication factor C 38 kDa subunit) (RF-C 38 kDa subunit) (RFC38)
[rad17 SPAC14C4.13] Checkpoint protein rad17
[Rad9a Rad9] Cell cycle checkpoint control protein RAD9A (mRAD9) (EC 3.1.11.2) (DNA repair exonuclease rad9 homolog A) (Rad9-like protein)
[RAD17 YOR368W] DNA damage checkpoint control protein RAD17 (DNA repair exonuclease RAD17)
[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 (hHUS1)
[RAD17] Cell cycle checkpoint protein RAD17
[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)
[RFC2] Replication factor C subunit 2 (Activator 1 40 kDa subunit) (A1 40 kDa subunit) (Activator 1 subunit 2) (Replication factor C 40 kDa subunit) (RF-C 40 kDa subunit) (RFC40)
[DDC1 YPL194W] DNA damage checkpoint protein 1
[RFC3 YNL290W N0533] Replication factor C subunit 3 (Replication factor C3) (Activator 1 40 kDa subunit)
[RFC5 YBR087W YBR0810] Replication factor C subunit 5 (Replication factor C5) (Activator 1 40 kDa subunit)
[RFC2 YJR068W J1808] Replication factor C subunit 2 (Replication factor C2) (Activator 1 41 kDa subunit)
[RFC4 YOL094C O0923] Replication factor C subunit 4 (Replication factor C4) (Activator 1 37 kDa subunit)
[RFC4] Replication factor C subunit 4 (Activator 1 37 kDa subunit) (A1 37 kDa subunit) (Activator 1 subunit 4) (Replication factor C 37 kDa subunit) (RF-C 37 kDa subunit) (RFC37)
[RFC5] Replication factor C subunit 5 (Activator 1 36 kDa subunit) (A1 36 kDa subunit) (Activator 1 subunit 5) (Replication factor C 36 kDa subunit) (RF-C 36 kDa subunit) (RFC36)
[Atm] Serine-protein kinase ATM (EC 2.7.11.1) (Ataxia telangiectasia mutated homolog) (A-T mutated homolog)
[Rad1 Rec1] Cell cycle checkpoint protein RAD1 (mRAD1) (EC 3.1.11.2) (DNA repair exonuclease rad1 homolog) (Rad1-like DNA damage checkpoint protein)
[Rfc1 Ibf-1 Recc1] Replication factor C subunit 1 (A1-P145) (Activator 1 140 kDa subunit) (A1 140 kDa subunit) (Activator 1 large subunit) (Activator 1 subunit 1) (Differentiation-specific element-binding protein) (ISRE-binding protein) (Replication factor C 140 kDa subunit) (RF-C 140 kDa subunit) (RFC140) (Replication factor C large subunit)
[Hus1] Checkpoint protein HUS1 (mHUS1)
[CHEK1 CHK1] Serine/threonine-protein kinase Chk1 (EC 2.7.11.1) (CHK1 checkpoint homolog) (Checkpoint kinase-1)
[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)
[RFC1 RFC140] Replication factor C subunit 1 (Activator 1 140 kDa subunit) (A1 140 kDa subunit) (Activator 1 large subunit) (Activator 1 subunit 1) (DNA-binding protein PO-GA) (Replication factor C 140 kDa subunit) (RF-C 140 kDa subunit) (RFC140) (Replication factor C large subunit)
[MEC3 PIP3 PSO9 YLR288C L8003.15] DNA damage checkpoint control protein MEC3
[mat-3 apc-8 cdc-23 pod-4 vex-2 F10C5.1] Cell division cycle protein 23 homolog (Anaphase-promoting complex subunit 8) (APC8) (Metaphase-to-anaphase transition defect protein 3)

Bibliography :