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RAD1

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:
NCBI GenPept GI number(s): 4506385
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot O60671 O60671
PFAM: - O60671 (Link - using uniprot id)
InterPro: - O60671 (Link - using uniprot id)
CATH: None  
SCOP: None  
PDB: - -


Protein sequence:
MPLLTQQIQDEDDQYSLVASLDNVRNLSTILKAIHFREHATCFATKNGIK
VTVENAKCVQANAFIQAGIFQEFKVQEESVTFRINLTVLLDCLSIFGSSP
MPGTLTALRMCYQGYGYPLMLFLEEGGVVTVCKINTQEPEETLDFDFCST
NVINKIILQSEGLREAFSELDMTSEVLQITMSPDKPYFRLSTFGNAGSSH
LDYPKDSDLMEAFHCNQTQVNRYKISLLKPSTKALVLSCKVSIRTDNRGF
LSLQYMIRNEDGQICFVEYYCCPDEEVPESES

RAD1 (Homo sapiens) is able to recognize following damages:
RAD1 (Homo sapiens) belongs to following protein families:
References:

Title Authors Journal
A human homologue of the Schizosaccharomyces pombe rad1+ checkpoint gene encodes an exonuclease. Parker AE, Van de Weyer I, Laus MC, Oostveen I, Yon J, Verhasselt P, Luyten WH J Biol Chem July 17, 1998
Human and mouse homologs of Schizosaccharomyces pombe rad1(+) and Saccharomyces cerevisiae RAD17: linkage to checkpoint control and mammalian meiosis. Freire R, Murguia JR, Tarsounas M, Lowndes NF, Moens PB, Jackson SP Genes Dev Aug. 15, 1998
HRAD1 and MRAD1 encode mammalian homologues of the fission yeast rad1(+) cell cycle checkpoint control gene. Udell CM, Lee SK, Davey S Nucleic Acids Res Sept. 1, 1998
A human and mouse homolog of the Schizosaccharomyces pombe rad1+ cell cycle checkpoint control gene. Bluyssen HA, van Os RI, Naus NC, Jaspers I, Hoeijmakers JH, de Klein A Genomics Dec. 1, 1998
RAD1, a human structural homolog of the Schizosaccharomyces pombe RAD1 cell cycle checkpoint gene. Marathi UK, Dahlen M, Sunnerhagen P, Romero AV, Ramagli LS, Siciliano MJ, Li L, Legerski RJ Genomics Dec. 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
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
Identification and characterization of a paralog of human cell cycle checkpoint gene HUS1. Hang H, Zhang Y, Dunbrack RL Jr, Wang C, Lieberman HB Genomics April 1, 2002
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
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 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 Nat Genet Feb. 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. 15, 2010.

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