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do over; "They would like to take it over again" (同)take_over
an event that repeats; "the events today were a repeat of yesterdays" (同)repetition
to say again or imitate; "followers echoing the cries of their leaders" (同)echo
to say, state, or perform again; "She kept reiterating her request" (同)reiterate, ingeminate, iterate, restate, retell
executed with proper legal authority; "a binding contract"
the protective covering on the front, back, and spine of a book; "the book had a leather binding" (同)book binding, cover, back
strip sewn over or along an edge for reinforcement or decoration
the capacity to attract and hold something
any of a large group of nitrogenous organic compounds that are essential constituents of living cells; consist of polymers of amino acids; essential in the diet of animals for growth and for repair of tissues; can be obtained from meat and eggs and milk and legumes; "a diet high in protein"

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〈自分がすでに一度言ったこと)‘を'『繰り返して言う』 / 〈他人の言ったこと〉‘を'おうむ返しに言う;…‘を'他の人に繰り返して言う / …‘を'『暗記して言う』,暗唱する / …‘を'繰り返して行う(do again) / (食べたあとで)〈食物の〉味が残る / 〈小数が〉循環する / 繰り返すこと,反復すること / 繰り返されるもの,(公演の)再演;(番組の)再放送 / 反復楽節;反復記号(∥: :∥)
義務的な,拘束力ある / 〈U〉しばること;〈C〉しばる物 / 〈C〉製本,装丁 / 〈U〉縁(‘ふち')取り材料
蛋白(たんばく)質
繰り返して言われる(行われる)

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2012/07/24 00:55:07」(JST)

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Telomeric repeat-binding factor 1 is a protein that in humans is encoded by the TERF1 gene.^[1]^[2]

This gene encodes a telomere specific protein which is a component of the telomere nucleoprotein complex. This protein is present at telomeres throughout the cell cycle and functions as an inhibitor of telomerase, acting in cis to limit the elongation of individual chromosome ends. The protein structure contains a C-terminal Myb motif, a dimerization domain near its N-terminus and an acidic N-terminus. Two transcripts of this gene are alternatively spliced products.^[2]

Interactions

TERF1 has been shown to interact with SALL1,^[3] MAPRE1,^[4] NME1,^[5] TNKS2,^[6]^[7]^[8] Ataxia telangiectasia mutated,^[9] TINF2,^[10]^[11]^[12] TNKS,^[6]^[8]^[13]^[14]^[15] PINX1^[16] and Abl gene.^[9]

References

^ Shen M, Haggblom C, Vogt M, Hunter T, Lu KP (January 1998). "Characterization and cell cycle regulation of the related human telomeric proteins Pin2 and TRF1 suggest a role in mitosis". Proc Natl Acad Sci U S A 94 (25): 13618–23. DOI:10.1073/pnas.94.25.13618. PMC 28355. PMID 9391075. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=28355.
^ ^a ^b "Entrez Gene: TERF1 telomeric repeat binding factor (NIMA-interacting) 1". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7013.
^ Netzer, C; Rieger L, Brero A, Zhang C D, Hinzke M, Kohlhase J, Bohlander S K (Dec. 2001). "SALL1, the gene mutated in Townes-Brocks syndrome, encodes a transcriptional repressor which interacts with TRF1/PIN2 and localizes to pericentromeric heterochromatin". Hum. Mol. Genet. (England) 10 (26): 3017–24. DOI:10.1093/hmg/10.26.3017. ISSN 0964-6906. PMID 11751684.
^ Nakamura, Masafumi; Zhou X Z, Kishi Shuji, Lu K P (March 2002). "Involvement of the telomeric protein Pin2/TRF1 in the regulation of the mitotic spindle". FEBS Lett. (Netherlands) 514 (2-3): 193–8. DOI:10.1016/S0014-5793(02)02363-3. ISSN 0014-5793. PMID 11943150.
^ Nosaka, K; Kawahara M, Masuda M, Satomi Y, Nishino H (February 1998). "Association of nucleoside diphosphate kinase nm23-H2 with human telomeres". Biochem. Biophys. Res. Commun. (UNITED STATES) 243 (2): 342–8. DOI:10.1006/bbrc.1997.8097. ISSN 0006-291X. PMID 9480811.
^ ^a ^b Cook, Brandoch D; Dynek Jasmin N, Chang William, Shostak Grigoriy, Smith Susan (January 2002). "Role for the related poly(ADP-Ribose) polymerases tankyrase 1 and 2 at human telomeres". Mol. Cell. Biol. (United States) 22 (1): 332–42. DOI:10.1128/MCB.22.1.332-342.2002. ISSN 0270-7306. PMC 134233. PMID 11739745. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=134233.
^ Chi, N W; Lodish H F (Dec. 2000). "Tankyrase is a golgi-associated mitogen-activated protein kinase substrate that interacts with IRAP in GLUT4 vesicles". J. Biol. Chem. (UNITED STATES) 275 (49): 38437–44. DOI:10.1074/jbc.M007635200. ISSN 0021-9258. PMID 10988299.
^ ^a ^b Sbodio, Juan I; Lodish Harvey F, Chi Nai-Wen (February 2002). "Tankyrase-2 oligomerizes with tankyrase-1 and binds to both TRF1 (telomere-repeat-binding factor 1) and IRAP (insulin-responsive aminopeptidase)". Biochem. J. (England) 361 (Pt 3): 451–9. DOI:10.1042/0264-6021:3610451. ISSN 0264-6021. PMC 1222327. PMID 11802774. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1222327.
^ ^a ^b Kishi, S; Zhou X Z, Ziv Y, Khoo C, Hill D E, Shiloh Y, Lu K P (August 2001). "Telomeric protein Pin2/TRF1 as an important ATM target in response to double strand DNA breaks". J. Biol. Chem. (United States) 276 (31): 29282–91. DOI:10.1074/jbc.M011534200. ISSN 0021-9258. PMID 11375976.
^ Liu, Dan; Safari Amin, O'Connor Matthew S, Chan Doug W, Laegeler Andrew, Qin Jun, Songyang Zhou (July 2004). "PTOP interacts with POT1 and regulates its localization to telomeres". Nat. Cell Biol. (England) 6 (7): 673–80. DOI:10.1038/ncb1142. ISSN 1465-7392. PMID 15181449.
^ Stelzl, Ulrich; Worm Uwe, Lalowski Maciej, Haenig Christian, Brembeck Felix H, Goehler Heike, Stroedicke Martin, Zenkner Martina, Schoenherr Anke, Koeppen Susanne, Timm Jan, Mintzlaff Sascha, Abraham Claudia, Bock Nicole, Kietzmann Silvia, Goedde Astrid, Toksöz Engin, Droege Anja, Krobitsch Sylvia, Korn Bernhard, Birchmeier Walter, Lehrach Hans, Wanker Erich E (September 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell (United States) 122 (6): 957–68. DOI:10.1016/j.cell.2005.08.029. ISSN 0092-8674. PMID 16169070.
^ Kim, S H; Kaminker P, Campisi J (Dec. 1999). "TIN2, a new regulator of telomere length in human cells". Nat. Genet. (UNITED STATES) 23 (4): 405–12. DOI:10.1038/70508. ISSN 1061-4036. PMID 10581025.
^ Seimiya, Hiroyuki; Smith Susan (April 2002). "The telomeric poly(ADP-ribose) polymerase, tankyrase 1, contains multiple binding sites for telomeric repeat binding factor 1 (TRF1) and a novel acceptor, 182-kDa tankyrase-binding protein (TAB182)". J. Biol. Chem. (United States) 277 (16): 14116–26. DOI:10.1074/jbc.M112266200. ISSN 0021-9258. PMID 11854288.
^ Sbodio, Juan I; Chi Nai-Wen (August 2002). "Identification of a tankyrase-binding motif shared by IRAP, TAB182, and human TRF1 but not mouse TRF1. NuMA contains this RXXPDG motif and is a novel tankyrase partner". J. Biol. Chem. (United States) 277 (35): 31887–92. DOI:10.1074/jbc.M203916200. ISSN 0021-9258. PMID 12080061.
^ Smith, S; Giriat I, Schmitt A, de Lange T (November 1998). "Tankyrase, a poly(ADP-ribose) polymerase at human telomeres". Science (UNITED STATES) 282 (5393): 1484–7. DOI:10.1126/science.282.5393.1484. ISSN 0036-8075. PMID 9822378.
^ Zhou, X Z; Lu K P (November 2001). "The Pin2/TRF1-interacting protein PinX1 is a potent telomerase inhibitor". Cell (United States) 107 (3): 347–59. DOI:10.1016/S0092-8674(01)00538-4. ISSN 0092-8674. PMID 11701125.

UpToDate Contents

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English Journal

How proteins bind to DNA: target discrimination and dynamic sequence search by the telomeric protein TRF1.

Wieczór M1, Czub J1.
Nucleic acids research.Nucleic Acids Res.2017 Jul 27;45(13):7643-7654. doi: 10.1093/nar/gkx534.
PMID 28633355

Rho GDP-dissociation inhibitor α is a potential prognostic biomarker and controls telomere regulation in colorectal cancer.

Huang D1,2, Lu W3, Zou S2, Wang H1, Jiang Y4, Zhang X4, Li P4, Songyang Z4, Wang L1,2, Wang J1,2, Huang J4, Fang L1,2.
Cancer science.Cancer Sci.2017 Jul;108(7):1293-1302. doi: 10.1111/cas.13259. Epub 2017 May 31.
PMID 28417530

Tankyrase-Binding Protein TNKS1BP1 Regulates Actin Cytoskeleton Rearrangement and Cancer Cell Invasion.

Ohishi T1,2, Yoshida H1, Katori M3, Migita T1, Muramatsu Y1, Miyake M1, Ishikawa Y3, Saiura A4, Iemura SI5, Natsume T5, Seimiya H6.
Cancer research.Cancer Res.2017 May 1;77(9):2328-2338. doi: 10.1158/0008-5472.CAN-16-1846. Epub 2017 Feb 15.
PMID 28202517

Japanese Journal

血液学におけるテロメアとテロメレース

東京女子医科大学雑誌 83(E2), E520-E538, 2013-03-31
NAID 110009575062

A Novel Pair of Terminal Protein and Telomere-Associated Protein for Replication of the Linear Chromosome of Streptomyces griseus IFO13350

Bioscience, biotechnology, and biochemistry 72(11), 2973-2980, 2008-11-23
NAID 10027534196

<集談会記録>ヒト胃癌におけるテロメア関連因子およびDNA修復酵素の発現 : ヒト胃癌におけるTRF1,TRF2およびTIN2の発現解析ヒト胃癌におけるMRE11 complex(MRE11,Rad50,NBS1)およびhRAP1の発現解析(学位論文抄録)

広島大学医学雑誌 50(2), 95, 2002-04-28
NAID 110000210212

「テロメア反復結合タンパク質1」

Telomeric repeat binding factor (NIMA-interacting) 1
	; PDB rendering based on 1ba5.
Available structures
PDB	Ortholog search: PDBe, RCSB
List of PDB id codes
	1BA5, 1H6O, 1ITY, 1IV6, 1W0T, 3BQO, 3L82
Identifiers
Symbols	TERF1; PIN2; TRBF1; TRF; TRF1; hTRF1-AS; t-TRF1
External IDs	OMIM: 600951 MGI: 109634 HomoloGene: 7570 GeneCards: TERF1 Gene
Gene Ontology
Molecular function	• DNA binding; • double-stranded telomeric DNA binding; • protein binding; • microtubule binding; • DNA binding, bending; • cysteine-type endopeptidase activator activity involved in apoptotic process; • telomerase inhibitor activity; • telomeric DNA binding; • protein homodimerization activity; • protein heterodimerization activity;
Cellular component	• chromosome, telomeric region; • nuclear telomere cap complex; • nuclear telomere cap complex; • nucleus; • nucleus; • nucleoplasm; • chromosome; • cytoplasm; • spindle; • spindle; • cytoskeleton;
Biological process	• G2/M transition of mitotic cell cycle; • telomere maintenance; • age-dependent telomere shortening; • regulation of transcription, DNA-dependent; • induction of apoptosis; • activation of cysteine-type endopeptidase activity involved in apoptotic process; • telomere maintenance via telomerase; • telomere maintenance via telomerase; • cell cycle; • mitosis; • mitotic cell cycle spindle assembly checkpoint; • negative regulation of DNA replication; • telomere maintenance via telomere shortening; • positive regulation of microtubule polymerization; • negative regulation of telomere maintenance via telomerase; • negative regulation of telomere maintenance via semi-conservative replication; • response to drug; • positive regulation of mitosis; • positive regulation of mitotic cell cycle; • protein homooligomerization; • cell division; • negative regulation of telomerase activity;
	Sources: Amigo / QuickGO
Orthologs
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