HUS1_HUMAN
ID HUS1_HUMAN Reviewed; 280 AA.
AC O60921; B4DFI9;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Checkpoint protein HUS1;
DE Short=hHUS1;
GN Name=HUS1;
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).
RX PubMed=9524127; DOI=10.1093/emboj/17.7.2055;
RA Kostrub C.F., Knudsen K., Subramani S., Enoch T.;
RT "Hus1p, a conserved fission yeast checkpoint protein, interacts with Rad1p
RT and is phosphorylated in response to DNA damage.";
RL EMBO J. 17:2055-2066(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH RAD1 AND RAD9A,
RP AND TISSUE SPECIFICITY.
RC TISSUE=T-cell;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LYS-147 AND GLU-221.
RG NIEHS SNPs program;
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Urinary bladder;
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 [10]
RP INTERACTION WITH RAD1 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 [11]
RP IDENTIFICATION IN THE 9-1-1 COMPLEX ASSOCIATED WITH HDAC1, INTERACTION WITH
RP HDAC1, AND SUBCELLULAR LOCATION.
RX PubMed=10846170; DOI=10.1074/jbc.m000168200;
RA Cai R.L., Yan-Neale Y., Cueto M.A., Xu H., Cohen D.;
RT "HDAC1, a histone deacetylase, forms a complex with Hus1 and Rad9, two G2/M
RT checkpoint Rad proteins.";
RL J. Biol. Chem. 275:27909-27916(2000).
RN [12]
RP IDENTIFICATION IN THE 9-1-1 COMPLEX ASSOCIATED WITH RAD17.
RX PubMed=10884395; DOI=10.1074/jbc.m005782200;
RA Rauen M., Burtelow M.A., Dufault V.M., Karnitz L.M.;
RT "The human checkpoint protein hRad17 interacts with the PCNA-like proteins
RT hRad1, hHus1, and hRad9.";
RL J. Biol. Chem. 275:29767-29771(2000).
RN [13]
RP INTERACTION WITH PCNA, AND SUBCELLULAR LOCATION.
RX PubMed=11077446; DOI=10.1038/sj.onc.1203901;
RA Komatsu K., Wharton W., Hang H., Wu C., Singh S., Lieberman H.B.,
RA Pledger W.J., Wang H.-G.;
RT "PCNA interacts with hHus1/hRad9 in response to DNA damage and replication
RT inhibition.";
RL Oncogene 19:5291-5297(2000).
RN [14]
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 [15]
RP INTERACTION WITH RAD9B.
RX PubMed=14500360;
RA Hopkins K.M., Wang X., Berlin A., Hang H., Thaker H.M., Lieberman H.B.;
RT "Expression of mammalian paralogues of HRAD9 and Mrad9 checkpoint control
RT genes in normal and cancerous testicular tissue.";
RL Cancer Res. 63:5291-5298(2003).
RN [16]
RP INTERACTION WITH 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 [17]
RP ASSOCIATION OF THE 9-1-1 COMPLEX WITH THE RAD17-RFC COMPLEX, LACK OF
RP INTERACTION WITH RAD17, AND ELECTRON MICROSCOPY OF THE 9-1-1 AND RAD17-RFC
RP COMPLEXES BOUND TO DNA.
RX PubMed=12578958; DOI=10.1073/pnas.0437927100;
RA Bermudez V.P., Lindsey-Boltz L.A., Cesare A.J., Maniwa Y., Griffith J.D.,
RA Hurwitz J., Sancar A.;
RT "Loading of the human 9-1-1 checkpoint complex onto DNA by the checkpoint
RT clamp loader hRad17-replication factor C complex in vitro.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1633-1638(2003).
RN [18]
RP IDENTIFICATION IN THE 9-1-1 COMPLEX ASSOCIATED WITH POLB, AND INTERACTION
RP WITH POLB.
RX PubMed=15314187; DOI=10.1093/nar/gkh652;
RA Toueille M., El-Andaloussi N., Frouin I., Freire R., Funk D., Shevelev I.,
RA Friedrich-Heineken E., Villani G., Hottiger M.O., Huebscher U.;
RT "The human Rad9/Rad1/Hus1 damage sensor clamp interacts with DNA polymerase
RT beta and increases its DNA substrate utilisation efficiency: implications
RT for DNA repair.";
RL Nucleic Acids Res. 32:3316-3324(2004).
RN [19]
RP IDENTIFICATION IN THE 9-1-1 COMPLEX ASSOCIATED WITH FEN1.
RX PubMed=15556996; DOI=10.1073/pnas.0407686101;
RA Wang W., Brandt P., Rossi M.L., Lindsey-Boltz L., Podust V., Fanning E.,
RA Sancar A., Bambara R.A.;
RT "The human Rad9-Rad1-Hus1 checkpoint complex stimulates flap endonuclease
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:16762-16767(2004).
RN [20]
RP IDENTIFICATION IN THE 9-1-1 COMPLEX ASSOCIATED WITH LIG1.
RX PubMed=15871698; DOI=10.1042/bj20050211;
RA Smirnova E., Toueille M., Markkanen E., Huebscher U.;
RT "The human checkpoint sensor and alternative DNA clamp Rad9-Rad1-Hus1
RT modulates the activity of DNA ligase I, a component of the long-patch base
RT excision repair machinery.";
RL Biochem. J. 389:13-17(2005).
RN [21]
RP IDENTIFICATION IN THE 9-1-1 COMPLEX ASSOCIATED WITH FEN1, AND INTERACTION
RP WITH FEN1.
RX PubMed=16216273; DOI=10.1016/j.jmb.2005.09.018;
RA Friedrich-Heineken E., Toueille M., Taennler B., Buerki C., Ferrari E.,
RA Hottiger M.O., Huebscher U.;
RT "The two DNA clamps Rad9/Rad1/Hus1 complex and proliferating cell nuclear
RT antigen differentially regulate flap endonuclease 1 activity.";
RL J. Mol. Biol. 353:980-989(2005).
RN [22]
RP IDENTIFICATION IN THE 9-1-1 COMPLEX ASSOCIATED WITH RPA1 AND RPA2.
RX PubMed=15897895; DOI=10.1038/sj.onc.1208674;
RA Wu X., Shell S.M., Zou Y.;
RT "Interaction and colocalization of Rad9/Rad1/Hus1 checkpoint complex with
RT replication protein A in human cells.";
RL Oncogene 24:4728-4735(2005).
RN [23]
RP 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).
CC -!- FUNCTION: Component of the 9-1-1 cell-cycle checkpoint response complex
CC that plays a major role in DNA repair. The 9-1-1 complex is recruited
CC to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp
CC loader complex. Acts then as a sliding clamp platform on DNA for
CC several proteins involved in long-patch base excision repair (LP-BER).
CC The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by
CC increasing its affinity for the 3'-OH end of the primer-template and
CC stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1
CC cleavage activity on substrates with double, nick, or gap flaps of
CC distinct sequences and lengths; and DNA ligase I (LIG1) on long-patch
CC base excision repair substrates. The 9-1-1 complex is necessary for the
CC recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring
CC during the S phase. {ECO:0000269|PubMed:21659603}.
CC -!- SUBUNIT: Component of the toroidal 9-1-1 (RAD9-RAD1-HUS1) complex,
CC composed of RAD9A, RAD1 and HUS1. The 9-1-1 complex associates with
CC LIG1, POLB, FEN1, RAD17, HDAC1, RPA1 and RPA2. The 9-1-1 complex
CC associates with the RAD17-RFC complex. HUS1 interacts with POLB, HDAC1,
CC FEN1, PCNA, RAD1, RAD9A and RAD9B. HUS1 does not interact with RAD17.
CC Interacts with DNAJC7. {ECO:0000269|PubMed:10359610,
CC ECO:0000269|PubMed:10777662, ECO:0000269|PubMed:10846170,
CC ECO:0000269|PubMed:10884395, ECO:0000269|PubMed:11077446,
CC ECO:0000269|PubMed:11573955, 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 O60921; Q504U0: C4orf46; NbExp=6; IntAct=EBI-1056174, EBI-6657981;
CC O60921; Q9BTE7: DCUN1D5; NbExp=5; IntAct=EBI-1056174, EBI-3924013;
CC O60921; Q9Y3R0-3: GRIP1; NbExp=3; IntAct=EBI-1056174, EBI-12193965;
CC O60921; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-1056174, EBI-741158;
CC O60921; O60671: RAD1; NbExp=5; IntAct=EBI-1056174, EBI-721835;
CC O60921; Q99638: RAD9A; NbExp=13; IntAct=EBI-1056174, EBI-2606224;
CC O60921; O00560: SDCBP; NbExp=3; IntAct=EBI-1056174, EBI-727004;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10846170,
CC ECO:0000269|PubMed:11077446}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:11077446}. Note=In discrete nuclear foci upon DNA
CC damage. According to PubMed:11077446, localized also in the cytoplasm.
CC DNA damage induces its nuclear translocation. Shuttles between the
CC nucleus and the cytoplasm. {ECO:0000269|PubMed:11077446}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O60921-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O60921-2; Sequence=VSP_056702;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10777662}.
CC -!- SIMILARITY: Belongs to the HUS1 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/hus1/";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/HUS1ID40899ch7p12.html";
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DR EMBL; Y16893; CAA76518.1; -; mRNA.
DR EMBL; AF076844; AAC95526.1; -; mRNA.
DR EMBL; AF110393; AAD25350.1; -; mRNA.
DR EMBL; AK294117; BAG57450.1; -; mRNA.
DR EMBL; AC019066; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC069282; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC104696; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR536552; CAG38789.1; -; mRNA.
DR EMBL; BT019481; AAV38288.1; -; mRNA.
DR EMBL; BT019482; AAV38289.1; -; mRNA.
DR EMBL; AF503165; AAM18968.1; -; Genomic_DNA.
DR EMBL; BC007013; AAH07013.1; -; mRNA.
DR CCDS; CCDS34635.1; -. [O60921-1]
DR CCDS; CCDS87501.1; -. [O60921-2]
DR RefSeq; NP_004498.1; NM_004507.3. [O60921-1]
DR RefSeq; XP_016867604.1; XM_017012115.1.
DR PDB; 3A1J; X-ray; 2.50 A; B=1-280.
DR PDB; 3G65; X-ray; 2.90 A; C=1-280.
DR PDB; 3GGR; X-ray; 3.20 A; B=2-280.
DR PDB; 6J8Y; X-ray; 2.40 A; B=2-280.
DR PDBsum; 3A1J; -.
DR PDBsum; 3G65; -.
DR PDBsum; 3GGR; -.
DR PDBsum; 6J8Y; -.
DR AlphaFoldDB; O60921; -.
DR SMR; O60921; -.
DR BioGRID; 109596; 115.
DR ComplexPortal; CPX-1829; Checkpoint clamp complex.
DR CORUM; O60921; -.
DR DIP; DIP-40929N; -.
DR IntAct; O60921; 22.
DR MINT; O60921; -.
DR STRING; 9606.ENSP00000258774; -.
DR iPTMnet; O60921; -.
DR PhosphoSitePlus; O60921; -.
DR BioMuta; HUS1; -.
DR EPD; O60921; -.
DR jPOST; O60921; -.
DR MassIVE; O60921; -.
DR MaxQB; O60921; -.
DR PaxDb; O60921; -.
DR PeptideAtlas; O60921; -.
DR PRIDE; O60921; -.
DR ProteomicsDB; 4044; -.
DR ProteomicsDB; 49670; -. [O60921-1]
DR TopDownProteomics; O60921-1; -. [O60921-1]
DR Antibodypedia; 27543; 261 antibodies from 30 providers.
DR CPTC; O60921; 1 antibody.
DR DNASU; 3364; -.
DR Ensembl; ENST00000258774.10; ENSP00000258774.5; ENSG00000136273.13. [O60921-1]
DR Ensembl; ENST00000432325.5; ENSP00000416588.1; ENSG00000136273.13. [O60921-2]
DR Ensembl; ENST00000458191.5; ENSP00000400727.1; ENSG00000136273.13. [O60921-2]
DR GeneID; 3364; -.
DR KEGG; hsa:3364; -.
DR MANE-Select; ENST00000258774.10; ENSP00000258774.5; NM_004507.4; NP_004498.1.
DR UCSC; uc003tod.3; human. [O60921-1]
DR CTD; 3364; -.
DR DisGeNET; 3364; -.
DR GeneCards; HUS1; -.
DR HGNC; HGNC:5309; HUS1.
DR HPA; ENSG00000136273; Low tissue specificity.
DR MIM; 603760; gene.
DR neXtProt; NX_O60921; -.
DR OpenTargets; ENSG00000136273; -.
DR PharmGKB; PA29564; -.
DR VEuPathDB; HostDB:ENSG00000136273; -.
DR eggNOG; KOG3999; Eukaryota.
DR GeneTree; ENSGT00390000000706; -.
DR HOGENOM; CLU_035754_1_0_1; -.
DR InParanoid; O60921; -.
DR OMA; PWASEDG; -.
DR PhylomeDB; O60921; -.
DR TreeFam; TF314491; -.
DR BRENDA; 2.3.2.27; 2681.
DR PathwayCommons; O60921; -.
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; O60921; -.
DR BioGRID-ORCS; 3364; 442 hits in 1098 CRISPR screens.
DR ChiTaRS; HUS1; human.
DR EvolutionaryTrace; O60921; -.
DR GeneWiki; HUS1; -.
DR GenomeRNAi; 3364; -.
DR Pharos; O60921; Tbio.
DR PRO; PR:O60921; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; O60921; protein.
DR Bgee; ENSG00000136273; Expressed in monocyte and 181 other tissues.
DR ExpressionAtlas; O60921; baseline and differential.
DR Genevisible; O60921; HS.
DR GO; GO:0030896; C:checkpoint clamp complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:InterPro.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0035861; C:site of double-strand break; IBA:GO_Central.
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; TAS:ProtInc.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IEA:Ensembl.
DR GO; GO:0044778; P:meiotic DNA integrity checkpoint signaling; IBA:GO_Central.
DR GO; GO:0033314; P:mitotic DNA replication checkpoint signaling; IBA:GO_Central.
DR GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; IBA:GO_Central.
DR GO; GO:0006289; P:nucleotide-excision repair; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:Ensembl.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:0009411; P:response to UV; IEA:Ensembl.
DR GO; GO:0000723; P:telomere maintenance; IBA:GO_Central.
DR InterPro; IPR016580; Cell_cycle_HUS1.
DR InterPro; IPR007150; Hus1/Mec3.
DR Pfam; PF04005; Hus1; 1.
DR PIRSF; PIRSF011312; Cell_cycle_HUS1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; DNA damage; Nucleus;
KW Reference proteome.
FT CHAIN 1..280
FT /note="Checkpoint protein HUS1"
FT /id="PRO_0000225003"
FT VAR_SEQ 1..21
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056702"
FT VARIANT 126
FT /note="S -> G (in dbSNP:rs2307261)"
FT /id="VAR_033999"
FT VARIANT 147
FT /note="Q -> K (in dbSNP:rs2307254)"
FT /evidence="ECO:0000269|Ref.7"
FT /id="VAR_025414"
FT VARIANT 221
FT /note="D -> E (in dbSNP:rs3176588)"
FT /evidence="ECO:0000269|Ref.7"
FT /id="VAR_025415"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:6J8Y"
FT HELIX 10..26
FT /evidence="ECO:0007829|PDB:6J8Y"
FT STRAND 28..34
FT /evidence="ECO:0007829|PDB:6J8Y"
FT STRAND 36..44
FT /evidence="ECO:0007829|PDB:6J8Y"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:3GGR"
FT STRAND 53..59
FT /evidence="ECO:0007829|PDB:6J8Y"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:6J8Y"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:6J8Y"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:6J8Y"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:6J8Y"
FT HELIX 85..95
FT /evidence="ECO:0007829|PDB:6J8Y"
FT STRAND 99..119
FT /evidence="ECO:0007829|PDB:6J8Y"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:3A1J"
FT STRAND 127..134
FT /evidence="ECO:0007829|PDB:6J8Y"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:3GGR"
FT HELIX 140..146
FT /evidence="ECO:0007829|PDB:6J8Y"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:6J8Y"
FT HELIX 163..174
FT /evidence="ECO:0007829|PDB:6J8Y"
FT STRAND 178..184
FT /evidence="ECO:0007829|PDB:6J8Y"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:6J8Y"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:6J8Y"
FT STRAND 197..205
FT /evidence="ECO:0007829|PDB:6J8Y"
FT STRAND 216..220
FT /evidence="ECO:0007829|PDB:3GGR"
FT STRAND 228..233
FT /evidence="ECO:0007829|PDB:6J8Y"
FT HELIX 234..242
FT /evidence="ECO:0007829|PDB:6J8Y"
FT STRAND 249..256
FT /evidence="ECO:0007829|PDB:6J8Y"
FT TURN 257..259
FT /evidence="ECO:0007829|PDB:6J8Y"
FT STRAND 260..266
FT /evidence="ECO:0007829|PDB:6J8Y"
FT STRAND 268..277
FT /evidence="ECO:0007829|PDB:6J8Y"
SQ SEQUENCE 280 AA; 31691 MW; 9C3ED2FD35C2ACB3 CRC64;
MKFRAKIVDG ACLNHFTRIS NMIAKLAKTC TLRISPDKLN FILCDKLANG GVSMWCELEQ
ENFFNEFQME GVSAENNEIY LELTSENLSR ALKTAQNARA LKIKLTNKHF PCLTVSVELL
SMSSSSRIVT HDIPIKVIPR KLWKDLQEPV VPDPDVSIYL PVLKTMKSVV EKMKNISNHL
VIEANLDGEL NLKIETELVC VTTHFKDLGN PPLASESTHE DRNVEHMAEV HIDIRKLLQF
LAGQQVNPTK ALCNIVNNKM VHFDLLHEDV SLQYFIPALS
