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 24-JAN-2024, entry version 176. 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). RN [24] {ECO:0007744|PDB:6J8Y} RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 2-280 IN COMPLEX WITH RHNO1; RAD1 RP AND RAD9A, AND IDENTIFICATION IN THE 9-1-1 COMPLEX. 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 [25] {ECO:0007744|PDB:8GNN} RP X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) OF 2-280 IN COMPLEX WITH RAD17; RAD1 RP AND 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:21659603). The 9-1-1 CC complex is recruited to DNA lesion upon damage by the RAD17-replication CC factor C (RFC) clamp loader complex (PubMed:21659603). Acts then as a CC sliding clamp platform on DNA for several proteins involved in long- CC patch base excision repair (LP-BER) (PubMed:21659603). The 9-1-1 CC complex stimulates DNA polymerase beta (POLB) activity by increasing CC its affinity for the 3'-OH end of the primer-template and stabilizes CC POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavage CC activity on substrates with double, nick, or gap flaps of distinct CC sequences and lengths; and DNA ligase I (LIG1) on long-patch base CC excision repair substrates (PubMed:21659603). The 9-1-1 complex is CC 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:21659603}. CC -!- SUBUNIT: Component of the toroidal 9-1-1 (RAD9-RAD1-HUS1) complex, CC composed of RAD9A, RAD1 and HUS1 (PubMed:10777662, PubMed:10846170, CC PubMed:10359610, PubMed:10884395, PubMed:31776186, PubMed:15871698, CC PubMed:15556996, PubMed:15897895, PubMed:15314187). The 9-1-1 complex CC associates with LIG1, POLB, FEN1, RAD17, HDAC1, RPA1 and RPA2 CC (PubMed:10884395, PubMed:15556996, PubMed:15897895, PubMed:16216273, CC PubMed:15314187). The 9-1-1 complex associates with the RAD17-RFC CC complex (PubMed:12578958). HUS1 interacts with POLB, HDAC1, FEN1, PCNA CC and RAD9B (PubMed:11077446, PubMed:14611806, PubMed:14500360). HUS1 CC does not interact with RAD17 (PubMed:12578958). Interacts with DNAJC7 CC (PubMed:11573955). {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:12578958, CC ECO:0000269|PubMed:14500360, ECO:0000269|PubMed:14611806, CC ECO:0000269|PubMed:15314187, ECO:0000269|PubMed:15556996, CC ECO:0000269|PubMed:15871698, ECO:0000269|PubMed:15897895, CC ECO:0000269|PubMed:16216273, ECO:0000269|PubMed:31776186}. 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 (PubMed:11077446). According to PubMed:11077446, localized also CC in the cytoplasm (PubMed:11077446). DNA damage induces its nuclear CC translocation (PubMed:11077446). Shuttles between the nucleus and the CC cytoplasm (PubMed:11077446). {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="https://atlasgeneticsoncology.org/gene/40899/HUS1"; 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; 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 PDB; 7Z6H; EM; 3.59 A; C=1-280. DR PDB; 8GNN; X-ray; 2.12 A; B=2-280. DR PDBsum; 3A1J; -. DR PDBsum; 3G65; -. DR PDBsum; 3GGR; -. DR PDBsum; 6J8Y; -. DR PDBsum; 7Z6H; -. DR PDBsum; 8GNN; -. DR AlphaFoldDB; O60921; -. DR EMDB; EMD-14527; -. DR SMR; O60921; -. DR BioGRID; 109596; 122. 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; 9606-ENSP00000258774; -. DR PeptideAtlas; O60921; -. DR ProteomicsDB; 4044; -. DR ProteomicsDB; 49670; -. [O60921-1] DR Pumba; O60921; -. DR TopDownProteomics; O60921-1; -. [O60921-1] DR Antibodypedia; 27543; 296 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 AGR; HGNC:5309; -. 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; VCWMRLE; -. DR OrthoDB; 5094542at2759; -. 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; 473 hits in 1177 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 primordial germ cell in gonad and 182 other cell types or tissues. DR ExpressionAtlas; O60921; baseline and differential. DR GO; GO:0030896; C:checkpoint clamp complex; IDA:UniProtKB. 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: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; 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: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 Gene3D; 3.70.10.10; -; 1. DR InterPro; IPR016580; Cell_cycle_HUS1. DR InterPro; IPR046938; DNA_clamp_sf. DR InterPro; IPR007150; Hus1/Mec3. DR PANTHER; PTHR12900:SF4; CHECKPOINT PROTEIN HUS1; 1. DR PANTHER; PTHR12900; MITOTIC AND DNA DAMAGE CHECKPOINT PROTEIN HUS1; 1. DR Pfam; PF04005; Hus1; 1. DR PIRSF; PIRSF011312; Cell_cycle_HUS1; 1. DR SUPFAM; SSF55979; DNA clamp; 1. DR Genevisible; O60921; HS. 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:8GNN" FT HELIX 10..26 FT /evidence="ECO:0007829|PDB:8GNN" FT STRAND 28..34 FT /evidence="ECO:0007829|PDB:8GNN" FT STRAND 36..44 FT /evidence="ECO:0007829|PDB:8GNN" FT STRAND 46..48 FT /evidence="ECO:0007829|PDB:3GGR" FT STRAND 53..59 FT /evidence="ECO:0007829|PDB:8GNN" FT HELIX 60..62 FT /evidence="ECO:0007829|PDB:8GNN" FT STRAND 65..70 FT /evidence="ECO:0007829|PDB:8GNN" FT STRAND 72..74 FT /evidence="ECO:0007829|PDB:8GNN" FT STRAND 79..84 FT /evidence="ECO:0007829|PDB:8GNN" FT HELIX 85..95 FT /evidence="ECO:0007829|PDB:8GNN" FT STRAND 99..119 FT /evidence="ECO:0007829|PDB:8GNN" FT STRAND 122..124 FT /evidence="ECO:0007829|PDB:3A1J" FT STRAND 127..134 FT /evidence="ECO:0007829|PDB:8GNN" FT STRAND 135..137 FT /evidence="ECO:0007829|PDB:3GGR" FT HELIX 140..146 FT /evidence="ECO:0007829|PDB:8GNN" FT STRAND 155..159 FT /evidence="ECO:0007829|PDB:8GNN" FT HELIX 163..174 FT /evidence="ECO:0007829|PDB:8GNN" FT STRAND 178..184 FT /evidence="ECO:0007829|PDB:8GNN" FT STRAND 186..188 FT /evidence="ECO:0007829|PDB:6J8Y" FT STRAND 190..195 FT /evidence="ECO:0007829|PDB:8GNN" FT STRAND 197..205 FT /evidence="ECO:0007829|PDB:8GNN" FT STRAND 216..220 FT /evidence="ECO:0007829|PDB:3GGR" FT STRAND 228..233 FT /evidence="ECO:0007829|PDB:8GNN" FT HELIX 234..242 FT /evidence="ECO:0007829|PDB:8GNN" FT STRAND 249..256 FT /evidence="ECO:0007829|PDB:8GNN" FT TURN 257..259 FT /evidence="ECO:0007829|PDB:8GNN" FT STRAND 260..267 FT /evidence="ECO:0007829|PDB:8GNN" FT STRAND 270..277 FT /evidence="ECO:0007829|PDB:8GNN" 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 //