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Protein FULL name: single-strand selective monofunctional uracil DNA glycosylase [Homo sapiens].
SMUG1 (Homo sapiens) is product of expression of
SMUG1
gene.
SMUG1 is involved in:
BER in Homo sapiens
Keywords:
FUNCTION: Responsible for recognizing base lesions in the genome
and initiating base excision DNA repair. Acts as a monofunctional
DNA glycosylase specific for uracil (U) residues in DNA and has a
preference for single-stranded DNA substrates. The activity is
greater against mismatches (U/G) than against matches (U/A).
Excised uracil (U), 5-formyluracil (fU) and uracil derivatives
bearing an oxidized group at C5 [5-hydroxyuracil (hoU) and 5-
hydroxymethyluracil (hmU)] in ssDNA and dsDNA but not analogous
cytosine derivatives (5-hydroxycytosine and 5-formylcytosine) and
other oxidized damage. The activity is damage specificity and salt
concentration-dependent. The general order of the preference for
ssDNA and dsDNA is the following: ssDNA > dsDNA (G pair) = dsDNA
(A pair) at the low salt concentration. At the high concentration
dsDNA (G pair) > dsDNA (A pair) > ssDNA.
INTERACTION:
Q93062:RBPMS; NbExp=1; IntAct=EBI-749970, EBI-740322;
SUBCELLULAR LOCATION: Nucleus.
WEB RESOURCE: Name=NIEHS-SNPs;
[LINK]
Links to other databases:
Protein sequence:
MPQAFLLGSIHEPAGALMEPQPCPGSLAESFLEEELRLNAELSQLQFSEP
VGIIYNPVEYAWEPHRNYVTRYCQGPKEVLFLGMNPGPFGMAQTGVPFGE
VSMVRDWLGIVGPVLTPPQEHPKRPVLGLECPQSEVSGARFWGFFRNLCG
QPEVFFHHCFVHNLCPLLFLAPSGRNLTPAELPAKQREQLLGICDAALCR
QVQLLGVRLVVGVGRLAEQRARRALAGLMPEVQVEGLLHPSPRNPQANKG
WEAVAKERLNELGLLPLLLK
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SMUG1 (Homo sapiens) is able to recognize following damages:
SMUG1 (Homo sapiens) belongs to following protein families:
References:
Title
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Authors
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Journal
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Identification of a new uracil-DNA glycosylase family by expression cloning using synthetic inhibitors.
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Haushalter KA, Todd Stukenberg MW, Kirschner MW, Verdine GL
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Curr Biol
Jan. 25, 1999
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Definitive identification of mammalian 5-hydroxymethyluracil DNA N-glycosylase activity as SMUG1.
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Boorstein RJ, Cummings A Jr, Marenstein DR, Chan MK, Ma Y, Neubert TA, Brown SM, Teebor GW
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J Biol Chem
Nov. 9, 2001
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hUNG2 is the major repair enzyme for removal of uracil from U:A matches, U:G mismatches, and U in single-stranded DNA, with hSMUG1 as a broad specificity backup.
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Kavli B, Sundheim O, Akbari M, Otterlei M, Nilsen H, Skorpen F, Aas PA, Hagen L, Krokan HE, Slupphaug G
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J Biol Chem
Oct. 18, 2002
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Mammalian 5-formyluracil-DNA glycosylase. 2. Role of SMUG1 uracil-DNA glycosylase in repair of 5-formyluracil and other oxidized and deaminated base lesions.
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Masaoka A, Matsubara M, Hasegawa R, Tanaka T, Kurisu S, Terato H, Ohyama Y, Karino N, Matsuda A, Ide H
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Biochemistry
May 6, 2003
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Mutational analysis of the damage-recognition and catalytic mechanism of human SMUG1 DNA glycosylase.
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Matsubara M, Tanaka T, Terato H, Ohmae E, Izumi S, Katayanagi K, Ide H
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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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Last modification of this entry: Oct. 15, 2010.
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