Welcome! Click here to login or here to register.
 |
|||||||||||||||||||
|
|||||||||||||||||||
 |
|||||||||||||||||||
NTH |
Protein FULL name:
endonuclease III-like protein 1 [Homo sapiens].
NTH (Homo sapiens) is product of expression of NTHL1 gene.
NTH is involved in:
BER in Homo sapiens
Keywords:
FUNCTION: Has both an apurinic and/or apyrimidinic endonuclease activity and a DNA N-glycosylase activity. Incises damaged DNA at cytosines, thymines and guanines. Acts on a damaged strand, 5' from the damaged site. Required for the repair of both oxidative DNA damage and spontaneous mutagenic lesions.
CATALYTIC ACTIVITY: The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.
COFACTOR: Binds 1 4Fe-4S cluster. The cluster is not important for the catalytic activity, but which is probably involved in the proper positioning of the enzyme along the DNA strand.
INTERACTION: O14556:GAPDHS; NbExp=1; IntAct=EBI-1049350, EBI-1057431; P12883:MYH7; NbExp=1; IntAct=EBI-1049350, EBI-519141; P36639:NUDT1; NbExp=1; IntAct=EBI-1049350, EBI-1048967; Q9HC36:RNMTL1; NbExp=1; IntAct=EBI-1049350, EBI-1045440;
SUBCELLULAR LOCATION: Nucleus.
TISSUE SPECIFICITY: Widely expressed with highest levels in heart and lowest levels in lung and liver.
DEVELOPMENTAL STAGE: Expression levels are regulated during the cell cycle with increased levels during early and mid S-phase.
SIMILARITY: Belongs to the nth/mutY family.
CAUTION: It is uncertain whether Met-1, Met-9 or Met-16 is the initiator.
SEQUENCE CAUTION: Sequence=AAC51136.1; Type=Erroneous initiation; Sequence=AAH03014.1; Type=Erroneous initiation; Sequence=BAA19413.1; Type=Erroneous initiation; Sequence=BAA32695.1; Type=Erroneous initiation;
WEB RESOURCE: Name=NIEHS-SNPs; [LINK]
| NCBI GenPept GI number(s): |
4505471 29840795 |
| Species: | Homo sapiens |
Links to other databases:
| Database | ID | Link |
| Uniprot | P78549 |
P78549 |
| PFAM: | - |
P78549 (Link - using uniprot id) |
| InterPro: | - |
P78549 (Link - using uniprot id) |
| CATH: | - | - |
| SCOP: | - | - |
| PDB: | - | - |
Protein sequence:
|
MCSPQESGMTALSARMLTRSRSLGPGAGPRGCREEPGPLRRREAAAEARK SHSPVKRPRKAQRLRVAYEGSDSEKGEGAEPLKVPVWEPQDWQQQLVNIR AMRNKKDAPVDHLGTEHCYDSSAPPKVRRYQVLLSLMLSSQTKDQVTAGA MQRLRARGLTVDSILQTDDATLGKLIYPVGFWRSKVKYIKQTSAILQQHY GGDIPASVAELVALPGVGPKMAHLAMAVAWGTVSGIAVDTHVHRIANRLR WTKKATKSPEETRAALEEWLPRELWHEINGLLVGFGQQTCLPVHPRCHAC LNQALCPAAQGL |
NTH (Homo sapiens) is able to recognize following damages:
NTH (Homo sapiens) belongs to following protein families:
References:
| Title | Authors | Journal |
| Cloning and characterization of a functional human homolog of Escherichia coli endonuclease III. | Aspinwall R, Rothwell DG, Roldan-Arjona T, Anselmino C, Ward CJ, Cheadle JP, Sampson JR, Lindahl T, Harris PC, Hickson ID | Proc Natl Acad Sci U S A Feb. 7, 1997 |
| Cloning and expression of the cDNA encoding the human homologue of the DNA repair enzyme, Escherichia coli endonuclease III. | Hilbert TP, Chaung W, Boorstein RJ, Cunningham RP, Teebor GW | J Biol Chem March 7, 1997 |
| Purification and characterization of human NTH1, a homolog of Escherichia coli endonuclease III. Direct identification of Lys-212 as the active nucleophilic residue. | Ikeda S, Biswas T, Roy R, Izumi T, Boldogh I, Kurosky A, Sarker AH, Seki S, Mitra S | J Biol Chem Aug. 21, 1998 |
| Genomic structure and sequence of a human homologue (NTHL1/NTH1) of Escherichia coli endonuclease III with those of the adjacent parts of TSC2 and SLC9A3R2 genes. | Imai K, Sarker AH, Akiyama K, Ikeda S, Yao M, Tsutsui K, Shohmori T, Seki S | Gene Nov. 19, 1998 |
| Cell-cycle regulation, intracellular sorting and induced overexpression of the human NTH1 DNA glycosylase involved in removal of formamidopyrimidine residues from DNA. | Luna L, Bjoras M, Hoff E, Rognes T, Seeberg E | Mutat Res July 25, 2000 |
| Differential intracellular localization of the human and mouse endonuclease III homologs and analysis of the sorting signals. | Ikeda S, Kohmoto T, Tabata R, Seki Y | DNA Repair (Amst) Oct. 1, 2002 |
| 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 sequence and analysis of duplication-rich human chromosome 16. | Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA | Nature Dec. 23, 2004 |
Last modification of this entry: Oct. 15, 2010.
Add your own comment!
There is no comment yet.
|
|
|
|