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Protein FULL name: cell cycle checkpoint protein RAD1 [Homo sapiens].
RAD1 (Homo sapiens) is product of expression of
RAD1
gene.
RAD1 is involved in:
DDS 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. Isoform 1 possesses 3'->5' double
stranded DNA exonuclease activity.
CATALYTIC ACTIVITY: Exonucleolytic cleavage in the 3'- to 5'-
direction to yield nucleoside 5'-phosphates.
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. RAD1 interacts with
POLB, FEN1, HUS1, HUS1B, RAD9A and RAD9B. Interacts with DNAJC7.
INTERACTION:
O60921:HUS1; NbExp=1; IntAct=EBI-721835, EBI-1056174;
Q99638:RAD9A; NbExp=1; IntAct=EBI-721835, EBI-2606224;
SUBCELLULAR LOCATION: Nucleus.
TISSUE SPECIFICITY: Expressed in testis, uterus, bladder, spleen,
ovaries, lung, brain and muscle (at protein level).
SIMILARITY: Belongs to the rad1 family.
SEQUENCE CAUTION:
Sequence=AAC35550.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
Sequence=AAC35550.1; Type=Frameshift; Positions=103;
Sequence=CAA06249.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
Sequence=CAA06249.1; Type=Frameshift; Positions=103;
WEB RESOURCE: Name=NIEHS-SNPs;
[LINK]
This protein can be a part of a given complexes:
Links to other databases:
Protein sequence:
MPLLTQQIQDEDDQYSLVASLDNVRNLSTILKAIHFREHATCFATKNGIK
VTVENAKCVQANAFIQAGIFQEFKVQEESVTFRINLTVLLDCLSIFGSSP
MPGTLTALRMCYQGYGYPLMLFLEEGGVVTVCKINTQEPEETLDFDFCST
NVINKIILQSEGLREAFSELDMTSEVLQITMSPDKPYFRLSTFGNAGSSH
LDYPKDSDLMEAFHCNQTQVNRYKISLLKPSTKALVLSCKVSIRTDNRGF
LSLQYMIRNEDGQICFVEYYCCPDEEVPESES
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RAD1 (Homo sapiens) is able to recognize following damages:
RAD1 (Homo sapiens) belongs to following protein families:
References:
Title
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Authors
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Journal
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A human homologue of the Schizosaccharomyces pombe rad1+ checkpoint gene encodes an exonuclease.
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Parker AE, Van de Weyer I, Laus MC, Oostveen I, Yon J, Verhasselt P, Luyten WH
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J Biol Chem
July 17, 1998
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Human and mouse homologs of Schizosaccharomyces pombe rad1(+) and Saccharomyces cerevisiae RAD17: linkage to checkpoint control and mammalian meiosis.
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Freire R, Murguia JR, Tarsounas M, Lowndes NF, Moens PB, Jackson SP
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Genes Dev
Aug. 15, 1998
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HRAD1 and MRAD1 encode mammalian homologues of the fission yeast rad1(+) cell cycle checkpoint control gene.
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Udell CM, Lee SK, Davey S
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Nucleic Acids Res
Sept. 1, 1998
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A human and mouse homolog of the Schizosaccharomyces pombe rad1+ cell cycle checkpoint control gene.
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Bluyssen HA, van Os RI, Naus NC, Jaspers I, Hoeijmakers JH, de Klein A
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Genomics
Dec. 1, 1998
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RAD1, a human structural homolog of the Schizosaccharomyces pombe RAD1 cell cycle checkpoint gene.
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Marathi UK, Dahlen M, Sunnerhagen P, Romero AV, Ramagli LS, Siciliano MJ, Li L, Legerski RJ
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Genomics
Dec. 1, 1998
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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.
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Dean FB, Lian L, O'Donnell M
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Genomics
Dec. 15, 1998
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The human G2 checkpoint control protein hRAD9 is a nuclear phosphoprotein that forms complexes with hRAD1 and hHUS1.
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St Onge RP, Udell CM, Casselman R, Davey S
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Mol Biol Cell
June 1, 1999
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Physical interactions among human checkpoint control proteins HUS1p, RAD1p, and RAD9p, and implications for the regulation of cell cycle progression.
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Hang H, Lieberman HB
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Genomics
April 1, 2000
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HDAC1, a histone deacetylase, forms a complex with Hus1 and Rad9, two G2/M checkpoint Rad proteins.
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Cai RL, Yan-Neale Y, Cueto MA, Xu H, Cohen D
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J Biol Chem
Sept. 8, 2000
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The human checkpoint protein hRad17 interacts with the PCNA-like proteins hRad1, hHus1, and hRad9.
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Rauen M, Burtelow MA, Dufault VM, Karnitz LM
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J Biol Chem
Sept. 22, 2000
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The J domain of Tpr2 regulates its interaction with the proapoptotic and cell-cycle checkpoint protein, Rad9.
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Xiang SL, Kumano T, Iwasaki SI, Sun X, Yoshioka K, Yamamoto KC
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Biochem Biophys Res Commun
Oct. 5, 2001
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Identification and characterization of a paralog of human cell cycle checkpoint gene HUS1.
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Hang H, Zhang Y, Dunbrack RL Jr, Wang C, Lieberman HB
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Genomics
April 1, 2002
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Loading of the human 9-1-1 checkpoint complex onto DNA by the checkpoint clamp loader hRad17-replication factor C complex in vitro.
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Bermudez VP, Lindsey-Boltz LA, Cesare AJ, Maniwa Y, Griffith JD, Hurwitz J, Sancar A
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Proc Natl Acad Sci U S A
Jan. 18, 2003
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Expression of mammalian paralogues of HRAD9 and Mrad9 checkpoint control genes in normal and cancerous testicular tissue.
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Hopkins KM, Wang X, Berlin A, Hang H, Thaker HM, Lieberman HB
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Cancer Res
Sept. 1, 2003
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Identification and characterization of RAD9B, a paralog of the RAD9 checkpoint gene.
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Dufault VM, Oestreich AJ, Vroman BT, Karnitz LM
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Genomics
Dec. 1, 2003
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The human Rad9/Rad1/Hus1 damage sensor clamp interacts with DNA polymerase beta and increases its DNA substrate utilisation efficiency: implications for DNA repair.
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Toueille M, El-Andaloussi N, Frouin I, Freire R, Funk D, Shevelev I, Friedrich-Heineken E, Villani G, Hottiger MO, Hubscher U
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Nucleic Acids Res
Jan. 1, 2004
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Complete sequencing and characterization of 21,243 full-length human cDNAs.
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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 TO, 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
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Nat Genet
Feb. 1, 2004
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The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
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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
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Genome Res
Oct. 1, 2004
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The human Rad9-Rad1-Hus1 checkpoint complex stimulates flap endonuclease 1.
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Wang W, Brandt P, Rossi ML, Lindsey-Boltz L, Podust V, Fanning E, Sancar A, Bambara RA
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Proc Natl Acad Sci U S A
Nov. 1, 2004
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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.
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Smirnova E, Toueille M, Markkanen E, Hubscher U
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Biochem J
July 1, 2005
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Interaction and colocalization of Rad9/Rad1/Hus1 checkpoint complex with replication protein A in human cells.
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Wu X, Shell SM, Zou Y
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Oncogene
July 7, 2005
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The two DNA clamps Rad9/Rad1/Hus1 complex and proliferating cell nuclear antigen differentially regulate flap endonuclease 1 activity.
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Friedrich-Heineken E, Toueille M, Tannler B, Burki C, Ferrari E, Hottiger MO, Hubscher U
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J Mol Biol
Nov. 11, 2005
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Last modification of this entry: Oct. 15, 2010.
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