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HUS1

Protein FULL name:

checkpoint protein HUS1 [Homo sapiens].


HUS1 (Homo sapiens) is product of expression of HUS1 gene.


HUS1 is involved in:

DDS in Homo sapiens
     
BER in Homo sapiens
     


Keywords:



FUNCTION: 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.

SUBUNIT: 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.

INTERACTION: P00492:HPRT1; NbExp=1; IntAct=EBI-1056174, EBI-748210; P25787:PSMA2; NbExp=1; IntAct=EBI-1056174, EBI-603262; O60671:RAD1; NbExp=1; IntAct=EBI-1056174, EBI-721835; Q99638:RAD9A; NbExp=3; IntAct=EBI-1056174, EBI-2606224;

SUBCELLULAR LOCATION: 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.

TISSUE SPECIFICITY: Ubiquitous.

SIMILARITY: Belongs to the HUS1 family.

WEB RESOURCE: Name=NIEHS-SNPs; [LINK]


This protein can be a part of a given complexes:
NCBI GenPept GI number(s): 4758576
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot O60921 O60921
PFAM: - O60921 (Link - using uniprot id)
InterPro: - O60921 (Link - using uniprot id)
CATH: None  
SCOP: None  
PDB: - -


Protein sequence:
MKFRAKIVDGACLNHFTRISNMIAKLAKTCTLRISPDKLNFILCDKLANG
GVSMWCELEQENFFNEFQMEGVSAENNEIYLELTSENLSRALKTAQNARA
LKIKLTNKHFPCLTVSVELLSMSSSSRIVTHDIPIKVIPRKLWKDLQEPV
VPDPDVSIYLPVLKTMKSVVEKMKNISNHLVIEANLDGELNLKIETELVC
VTTHFKDLGNPPLASESTHEDRNVEHMAEVHIDIRKLLQFLAGQQVNPTK
ALCNIVNNKMVHFDLLHEDVSLQYFIPALS

HUS1 (Homo sapiens) is able to recognize following damages:
HUS1 (Homo sapiens) belongs to following protein families:
References:

Title Authors Journal
Hus1p, a conserved fission yeast checkpoint protein, interacts with Rad1p and is phosphorylated in response to DNA damage. Kostrub CF, Knudsen K, Subramani S, Enoch T EMBO J April 1, 1998
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 FB, Lian L, O'Donnell M Genomics Dec. 15, 1998
The human G2 checkpoint control protein hRAD9 is a nuclear phosphoprotein that forms complexes with hRAD1 and hHUS1. St Onge RP, Udell CM, Casselman R, Davey S Mol Biol Cell June 1, 1999
Physical interactions among human checkpoint control proteins HUS1p, RAD1p, and RAD9p, and implications for the regulation of cell cycle progression. Hang H, Lieberman HB Genomics April 1, 2000
HDAC1, a histone deacetylase, forms a complex with Hus1 and Rad9, two G2/M checkpoint Rad proteins. Cai RL, Yan-Neale Y, Cueto MA, Xu H, Cohen D J Biol Chem Sept. 8, 2000
The human checkpoint protein hRad17 interacts with the PCNA-like proteins hRad1, hHus1, and hRad9. Rauen M, Burtelow MA, Dufault VM, Karnitz LM J Biol Chem Sept. 22, 2000
PCNA interacts with hHus1/hRad9 in response to DNA damage and replication inhibition. Komatsu K, Wharton W, Hang H, Wu C, Singh S, Lieberman HB, Pledger WJ, Wang HG Oncogene Nov. 2, 2000
The J domain of Tpr2 regulates its interaction with the proapoptotic and cell-cycle checkpoint protein, Rad9. Xiang SL, Kumano T, Iwasaki SI, Sun X, Yoshioka K, Yamamoto KC Biochem Biophys Res Commun Oct. 5, 2001
Loading of the human 9-1-1 checkpoint complex onto DNA by the checkpoint clamp loader hRad17-replication factor C complex in vitro. Bermudez VP, Lindsey-Boltz LA, Cesare AJ, Maniwa Y, Griffith JD, Hurwitz J, Sancar A Proc Natl Acad Sci U S A Jan. 18, 2003
Expression of mammalian paralogues of HRAD9 and Mrad9 checkpoint control genes in normal and cancerous testicular tissue. Hopkins KM, Wang X, Berlin A, Hang H, Thaker HM, Lieberman HB Cancer Res Sept. 1, 2003
Identification and characterization of RAD9B, a paralog of the RAD9 checkpoint gene. Dufault VM, Oestreich AJ, Vroman BT, Karnitz LM Genomics Dec. 1, 2003
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 MO, Hubscher U Nucleic Acids Res Jan. 1, 2004
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J Genome Res Oct. 1, 2004
The human Rad9-Rad1-Hus1 checkpoint complex stimulates flap endonuclease 1. Wang W, Brandt P, Rossi ML, Lindsey-Boltz L, Podust V, Fanning E, Sancar A, Bambara RA Proc Natl Acad Sci U S A Nov. 1, 2004
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, Hubscher U Biochem J July 1, 2005
Interaction and colocalization of Rad9/Rad1/Hus1 checkpoint complex with replication protein A in human cells. Wu X, Shell SM, Zou Y Oncogene July 7, 2005
The two DNA clamps Rad9/Rad1/Hus1 complex and proliferating cell nuclear antigen differentially regulate flap endonuclease 1 activity. Friedrich-Heineken E, Toueille M, Tannler B, Burki C, Ferrari E, Hottiger MO, Hubscher U J Mol Biol Nov. 11, 2005


Last modification of this entry: Oct. 12, 2010.

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