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O60921

- HUS1_HUMAN

UniProt

O60921 - HUS1_HUMAN

Protein

Checkpoint protein HUS1

Gene

HUS1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 1 (01 Aug 1998)
      Previous versions | rss
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    Functioni

    Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair. The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex. Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER). 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. The 9-1-1 complex is necessary for the recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring during the S phase.1 Publication

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. cellular response to DNA damage stimulus Source: ProtInc
    2. cellular response to ionizing radiation Source: UniProtKB
    3. DNA damage checkpoint Source: UniProtKB
    4. DNA repair Source: ProtInc
    5. DNA replication Source: Reactome
    6. double-strand break repair via homologous recombination Source: Ensembl
    7. embryo development Source: Ensembl
    8. mitotic cell cycle checkpoint Source: Ensembl
    9. negative regulation of DNA replication Source: Ensembl
    10. protein phosphorylation Source: Ensembl
    11. regulation of protein phosphorylation Source: Ensembl
    12. response to UV Source: Ensembl

    Keywords - Biological processi

    DNA damage

    Enzyme and pathway databases

    ReactomeiREACT_6769. Activation of ATR in response to replication stress.
    SignaLinkiO60921.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Checkpoint protein HUS1
    Short name:
    hHUS1
    Gene namesi
    Name:HUS1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:5309. HUS1.

    Subcellular locationi

    Nucleus. Cytoplasm
    Note: In discrete nuclear foci upon DNA damage. According to PubMed:14500360, localized also in the cytoplasm. DNA damage induces its nuclear translocation. Shuttles between the nucleus and the cytoplasm.

    GO - Cellular componenti

    1. checkpoint clamp complex Source: InterPro
    2. cytoplasm Source: UniProtKB-SubCell
    3. nucleolus Source: InterPro
    4. nucleoplasm Source: Reactome
    5. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29564.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 280280Checkpoint protein HUS1PRO_0000225003Add
    BLAST

    Proteomic databases

    MaxQBiO60921.
    PaxDbiO60921.
    PRIDEiO60921.

    PTM databases

    PhosphoSiteiO60921.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Gene expression databases

    ArrayExpressiO60921.
    BgeeiO60921.
    CleanExiHS_HUS1.
    GenevestigatoriO60921.

    Organism-specific databases

    HPAiHPA026787.

    Interactioni

    Subunit structurei

    Component of the toroidal 9-1-1 (RAD9-RAD1-HUS1) complex, composed of RAD9A, RAD1 and HUS1. The 9-1-1 complex associates with LIG1, POLB, FEN1, RAD17, HDAC1, RPA1 and RPA2. The 9-1-1 complex associates with the RAD17-RFC complex. HUS1 interacts with POLB, HDAC1, FEN1, PCNA, RAD1, RAD9A and RAD9B. HUS1 does not interact with RAD17. Interacts with DNAJC7.13 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RAD1O606714EBI-1056174,EBI-721835
    RAD9AQ996385EBI-1056174,EBI-2606224

    Protein-protein interaction databases

    BioGridi109596. 21 interactions.
    DIPiDIP-40929N.
    IntActiO60921. 4 interactions.
    MINTiMINT-134822.
    STRINGi9606.ENSP00000258774.

    Structurei

    Secondary structure

    1
    280
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 76
    Helixi10 – 2617
    Beta strandi28 – 347
    Beta strandi36 – 438
    Beta strandi46 – 483
    Beta strandi53 – 597
    Helixi60 – 623
    Beta strandi65 – 706
    Beta strandi72 – 743
    Beta strandi79 – 846
    Helixi85 – 917
    Helixi92 – 976
    Beta strandi98 – 1069
    Beta strandi108 – 1103
    Beta strandi112 – 1198
    Beta strandi122 – 1243
    Beta strandi128 – 1347
    Beta strandi135 – 1373
    Helixi140 – 1467
    Beta strandi155 – 1595
    Helixi163 – 17412
    Beta strandi178 – 1847
    Beta strandi186 – 1883
    Beta strandi190 – 1956
    Beta strandi197 – 2059
    Beta strandi216 – 2205
    Beta strandi228 – 2336
    Helixi234 – 24310
    Beta strandi249 – 2568
    Turni257 – 2593
    Beta strandi260 – 26910
    Beta strandi271 – 2777

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3A1JX-ray2.50B1-280[»]
    3G65X-ray2.90C1-280[»]
    3GGRX-ray3.20B2-280[»]
    ProteinModelPortaliO60921.
    SMRiO60921. Positions 3-280.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO60921.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the HUS1 family.Curated

    Phylogenomic databases

    eggNOGiNOG250864.
    HOGENOMiHOG000253011.
    HOVERGENiHBG053069.
    InParanoidiO60921.
    KOiK10903.
    OMAiCMILYVY.
    PhylomeDBiO60921.
    TreeFamiTF314491.

    Family and domain databases

    InterProiIPR016580. Cell_cycle_HUS1.
    IPR007150. Hus1/Mec3.
    [Graphical view]
    PANTHERiPTHR12900. PTHR12900. 1 hit.
    PfamiPF04005. Hus1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF011312. Cell_cycle_HUS1. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O60921-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MKFRAKIVDG ACLNHFTRIS NMIAKLAKTC TLRISPDKLN FILCDKLANG    50
    GVSMWCELEQ ENFFNEFQME GVSAENNEIY LELTSENLSR ALKTAQNARA 100
    LKIKLTNKHF PCLTVSVELL SMSSSSRIVT HDIPIKVIPR KLWKDLQEPV 150
    VPDPDVSIYL PVLKTMKSVV EKMKNISNHL VIEANLDGEL NLKIETELVC 200
    VTTHFKDLGN PPLASESTHE DRNVEHMAEV HIDIRKLLQF LAGQQVNPTK 250
    ALCNIVNNKM VHFDLLHEDV SLQYFIPALS 280
    Length:280
    Mass (Da):31,691
    Last modified:August 1, 1998 - v1
    Checksum:i9C3ED2FD35C2ACB3
    GO
    Isoform 2 (identifier: O60921-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-21: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:259
    Mass (Da):29,287
    Checksum:iD97AE567F923089B
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti126 – 1261S → G.
    Corresponds to variant rs2307261 [ dbSNP | Ensembl ].
    VAR_033999
    Natural varianti147 – 1471Q → K.1 Publication
    Corresponds to variant rs2307254 [ dbSNP | Ensembl ].
    VAR_025414
    Natural varianti221 – 2211D → E.1 Publication
    Corresponds to variant rs3176588 [ dbSNP | Ensembl ].
    VAR_025415

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2121Missing in isoform 2. 1 PublicationVSP_056702Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y16893 mRNA. Translation: CAA76518.1.
    AF076844 mRNA. Translation: AAC95526.1.
    AF110393 mRNA. Translation: AAD25350.1.
    AK294117 mRNA. Translation: BAG57450.1.
    AC019066 Genomic DNA. No translation available.
    AC069282 Genomic DNA. No translation available.
    AC104696 Genomic DNA. No translation available.
    CR536552 mRNA. Translation: CAG38789.1.
    BT019481 mRNA. Translation: AAV38288.1.
    BT019482 mRNA. Translation: AAV38289.1.
    AF503165 Genomic DNA. Translation: AAM18968.1.
    BC007013 mRNA. Translation: AAH07013.1.
    CCDSiCCDS34635.1.
    RefSeqiNP_004498.1. NM_004507.3.
    UniGeneiHs.152983.

    Genome annotation databases

    EnsembliENST00000258774; ENSP00000258774; ENSG00000136273.
    ENST00000432325; ENSP00000416588; ENSG00000136273.
    ENST00000436444; ENSP00000403844; ENSG00000136273.
    GeneIDi3364.
    KEGGihsa:3364.
    UCSCiuc003tod.2. human.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs
    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y16893 mRNA. Translation: CAA76518.1 .
    AF076844 mRNA. Translation: AAC95526.1 .
    AF110393 mRNA. Translation: AAD25350.1 .
    AK294117 mRNA. Translation: BAG57450.1 .
    AC019066 Genomic DNA. No translation available.
    AC069282 Genomic DNA. No translation available.
    AC104696 Genomic DNA. No translation available.
    CR536552 mRNA. Translation: CAG38789.1 .
    BT019481 mRNA. Translation: AAV38288.1 .
    BT019482 mRNA. Translation: AAV38289.1 .
    AF503165 Genomic DNA. Translation: AAM18968.1 .
    BC007013 mRNA. Translation: AAH07013.1 .
    CCDSi CCDS34635.1.
    RefSeqi NP_004498.1. NM_004507.3.
    UniGenei Hs.152983.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3A1J X-ray 2.50 B 1-280 [» ]
    3G65 X-ray 2.90 C 1-280 [» ]
    3GGR X-ray 3.20 B 2-280 [» ]
    ProteinModelPortali O60921.
    SMRi O60921. Positions 3-280.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109596. 21 interactions.
    DIPi DIP-40929N.
    IntActi O60921. 4 interactions.
    MINTi MINT-134822.
    STRINGi 9606.ENSP00000258774.

    PTM databases

    PhosphoSitei O60921.

    Proteomic databases

    MaxQBi O60921.
    PaxDbi O60921.
    PRIDEi O60921.

    Protocols and materials databases

    DNASUi 3364.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000258774 ; ENSP00000258774 ; ENSG00000136273 .
    ENST00000432325 ; ENSP00000416588 ; ENSG00000136273 .
    ENST00000436444 ; ENSP00000403844 ; ENSG00000136273 .
    GeneIDi 3364.
    KEGGi hsa:3364.
    UCSCi uc003tod.2. human.

    Organism-specific databases

    CTDi 3364.
    GeneCardsi GC07M047735.
    H-InvDB HIX0033836.
    HGNCi HGNC:5309. HUS1.
    HPAi HPA026787.
    MIMi 603760. gene.
    neXtProti NX_O60921.
    PharmGKBi PA29564.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG250864.
    HOGENOMi HOG000253011.
    HOVERGENi HBG053069.
    InParanoidi O60921.
    KOi K10903.
    OMAi CMILYVY.
    PhylomeDBi O60921.
    TreeFami TF314491.

    Enzyme and pathway databases

    Reactomei REACT_6769. Activation of ATR in response to replication stress.
    SignaLinki O60921.

    Miscellaneous databases

    EvolutionaryTracei O60921.
    GeneWikii HUS1.
    GenomeRNAii 3364.
    NextBioi 13320.
    PROi O60921.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O60921.
    Bgeei O60921.
    CleanExi HS_HUS1.
    Genevestigatori O60921.

    Family and domain databases

    InterProi IPR016580. Cell_cycle_HUS1.
    IPR007150. Hus1/Mec3.
    [Graphical view ]
    PANTHERi PTHR12900. PTHR12900. 1 hit.
    Pfami PF04005. Hus1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF011312. Cell_cycle_HUS1. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Hus1p, a conserved fission yeast checkpoint protein, interacts with Rad1p and is phosphorylated in response to DNA damage."
      Kostrub C.F., Knudsen K., Subramani S., Enoch T.
      EMBO J. 17:2055-2066(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "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."
      Dean F.B., Lian L., O'Donnell M.
      Genomics 54:424-436(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Physical interaction among human checkpoint control proteins HUS1p, RAD1p, and RAD9p, and implications for the regulation of cell cycle progression."
      Hang H., Lieberman H.B.
      Genomics 65:24-33(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH RAD1 AND RAD9A, TISSUE SPECIFICITY.
      Tissue: T-cell.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      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.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    6. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      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.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    7. NIEHS SNPs program
      Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LYS-147 AND GLU-221.
    8. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Urinary bladder.
    10. "The human G2 checkpoint control protein hRAD9 is a nuclear phosphoprotein that forms complexes with hRAD1 and hHUS1."
      St Onge R.P., Udell C.M., Casselman R., Davey S.
      Mol. Biol. Cell 10:1985-1995(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAD1 AND RAD9A.
    11. "HDAC1, a histone deacetylase, forms a complex with Hus1 and Rad9, two G2/M checkpoint Rad proteins."
      Cai R.L., Yan-Neale Y., Cueto M.A., Xu H., Cohen D.
      J. Biol. Chem. 275:27909-27916(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE 9-1-1 COMPLEX ASSOCIATED WITH HDAC1, INTERACTION WITH HDAC1, SUBCELLULAR LOCATION.
    12. "The human checkpoint protein hRad17 interacts with the PCNA-like proteins hRad1, hHus1, and hRad9."
      Rauen M., Burtelow M.A., Dufault V.M., Karnitz L.M.
      J. Biol. Chem. 275:29767-29771(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE 9-1-1 COMPLEX ASSOCIATED WITH RAD17.
    13. "PCNA interacts with hHus1/hRad9 in response to DNA damage and replication inhibition."
      Komatsu K., Wharton W., Hang H., Wu C., Singh S., Lieberman H.B., Pledger W.J., Wang H.-G.
      Oncogene 19:5291-5297(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PCNA, SUBCELLULAR LOCATION.
    14. "The J domain of Tpr2 regulates its interaction with the proapoptotic and cell-cycle checkpoint protein, Rad9."
      Xiang S.L., Kumano T., Iwasaki S.I., Sun X., Yoshioka K., Yamamoto K.C.
      Biochem. Biophys. Res. Commun. 287:932-940(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DNAJC7.
    15. "Expression of mammalian paralogues of HRAD9 and Mrad9 checkpoint control genes in normal and cancerous testicular tissue."
      Hopkins K.M., Wang X., Berlin A., Hang H., Thaker H.M., Lieberman H.B.
      Cancer Res. 63:5291-5298(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAD9B.
    16. "Identification and characterization of RAD9B, a paralog of the RAD9 checkpoint gene."
      Dufault V.M., Oestreich A.J., Vroman B.T., Karnitz L.M.
      Genomics 82:644-651(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAD9B.
    17. "Loading of the human 9-1-1 checkpoint complex onto DNA by the checkpoint clamp loader hRad17-replication factor C complex in vitro."
      Bermudez V.P., Lindsey-Boltz L.A., Cesare A.J., Maniwa Y., Griffith J.D., Hurwitz J., Sancar A.
      Proc. Natl. Acad. Sci. U.S.A. 100:1633-1638(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: ASSOCIATION OF THE 9-1-1 COMPLEX WITH THE RAD17-RFC COMPLEX, LACK OF INTERACTION WITH RAD17, ELECTRON MICROSCOPY OF THE 9-1-1 AND RAD17-RFC COMPLEXES BOUND TO DNA.
    18. "The human Rad9/Rad1/Hus1 damage sensor clamp interacts with DNA polymerase beta and increases its DNA substrate utilisation efficiency: implications for DNA repair."
      Toueille M., El-Andaloussi N., Frouin I., Freire R., Funk D., Shevelev I., Friedrich-Heineken E., Villani G., Hottiger M.O., Huebscher U.
      Nucleic Acids Res. 32:3316-3324(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE 9-1-1 COMPLEX ASSOCIATED WITH POLB, INTERACTION WITH POLB.
    19. Cited for: IDENTIFICATION IN THE 9-1-1 COMPLEX ASSOCIATED WITH FEN1.
    20. "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."
      Smirnova E., Toueille M., Markkanen E., Huebscher U.
      Biochem. J. 389:13-17(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE 9-1-1 COMPLEX ASSOCIATED WITH LIG1.
    21. "The two DNA clamps Rad9/Rad1/Hus1 complex and proliferating cell nuclear antigen differentially regulate flap endonuclease 1 activity."
      Friedrich-Heineken E., Toueille M., Taennler B., Buerki C., Ferrari E., Hottiger M.O., Huebscher U.
      J. Mol. Biol. 353:980-989(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE 9-1-1 COMPLEX ASSOCIATED WITH FEN1, INTERACTION WITH FEN1.
    22. "Interaction and colocalization of Rad9/Rad1/Hus1 checkpoint complex with replication protein A in human cells."
      Wu X., Shell S.M., Zou Y.
      Oncogene 24:4728-4735(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE 9-1-1 COMPLEX ASSOCIATED WITH RPA1 AND RPA2.
    23. "A DNA damage response screen identifies RHINO, a 9-1-1 and TopBP1 interacting protein required for ATR signaling."
      Cotta-Ramusino C., McDonald E.R. III, Hurov K., Sowa M.E., Harper J.W., Elledge S.J.
      Science 332:1313-1317(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiHUS1_HUMAN
    AccessioniPrimary (citable) accession number: O60921
    Secondary accession number(s): B4DFI9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 7, 2006
    Last sequence update: August 1, 1998
    Last modified: October 1, 2014
    This is version 111 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3