TERF1

From Wikipedia, the free encyclopedia

Telomeric repeat binding factor (NIMA-interacting) 1

PDB rendering based on 1ba5.

Available structures

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 • chromatin 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 • nucleus • nucleoplasm • cytoplasm • spindle
Biological process	• G2/M transition of mitotic cell cycle • telomere maintenance • age-dependent telomere shortening • induction of apoptosis • activation of cysteine-type endopeptidase activity involved in apoptotic process • telomere maintenance via telomerase • mitosis • mitotic 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

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 8:
73.92 – 73.96 Mb

Chr 1:
15.81 – 15.84 Mb

PubMed search

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.
↑ 2.0 2.1 "Entrez Gene: TERF1 telomeric repeat binding factor (NIMA-interacting) 1".
↑ 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. Cite uses deprecated parameters (help)
↑ 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. Cite uses deprecated parameters (help)
↑ 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. Cite uses deprecated parameters (help)
↑ 6.0 6.1 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. Cite uses deprecated parameters (help)
↑ 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. Cite uses deprecated parameters (help)
↑ 8.0 8.1 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. Cite uses deprecated parameters (help)
↑ 9.0 9.1 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. Cite uses deprecated parameters (help)
↑ 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. Cite uses deprecated parameters (help)
↑ 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. Cite uses deprecated parameters (help)
↑ 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. Cite uses deprecated parameters (help)
↑ 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. Cite uses deprecated parameters (help)
↑ 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. Cite uses deprecated parameters (help)
↑ 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. Cite uses deprecated parameters (help)
↑ 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. Cite uses deprecated parameters (help)

Zhong Z, Shiue L, Kaplan S, de Lange T (1992). "A mammalian factor that binds telomeric TTAGGG repeats in vitro.". Mol. Cell. Biol. 12 (11): 4834–43. PMC 360416. PMID 1406665.
Chong L, van Steensel B, Broccoli D, et al. (1996). "A human telomeric protein.". Science 270 (5242): 1663–7. doi:10.1126/science.270.5242.1663. PMID 7502076.
Lu KP, Hanes SD, Hunter T (1996). "A human peptidyl-prolyl isomerase essential for regulation of mitosis.". Nature 380 (6574): 544–7. doi:10.1038/380544a0. PMID 8606777.
Bilaud T, Koering CE, Binet-Brasselet E, et al. (1996). "The telobox, a Myb-related telomeric DNA binding motif found in proteins from yeast, plants and human.". Nucleic Acids Res. 24 (7): 1294–303. doi:10.1093/nar/24.7.1294. PMC 145771. PMID 8614633.
Broccoli D, Chong L, Oelmann S, et al. (1997). "Comparison of the human and mouse genes encoding the telomeric protein, TRF1: chromosomal localization, expression and conserved protein domains.". Hum. Mol. Genet. 6 (1): 69–76. doi:10.1093/hmg/6.1.69. PMID 9002672.
Bianchi A, Smith S, Chong L, et al. (1997). "TRF1 is a dimer and bends telomeric DNA.". EMBO J. 16 (7): 1785–94. doi:10.1093/emboj/16.7.1785. PMC 1169781. PMID 9130722.
Broccoli D, Smogorzewska A, Chong L, de Lange T (1997). "Human telomeres contain two distinct Myb-related proteins, TRF1 and TRF2.". Nat. Genet. 17 (2): 231–5. doi:10.1038/ng1097-231. PMID 9326950.
Nosaka K, Kawahara M, Masuda M, et al. (1998). "Association of nucleoside diphosphate kinase nm23-H2 with human telomeres.". Biochem. Biophys. Res. Commun. 243 (2): 342–8. doi:10.1006/bbrc.1997.8097. PMID 9480811.
Nishikawa T, Nagadoi A, Yoshimura S, et al. (1998). "Solution structure of the DNA-binding domain of human telomeric protein, hTRF1.". Structure 6 (8): 1057–65. doi:10.1016/S0969-2126(98)00106-3. PMID 9739097.
Smith S, Giriat I, Schmitt A, de Lange T (1998). "Tankyrase, a poly(ADP-ribose) polymerase at human telomeres.". Science 282 (5393): 1484–7. doi:10.1126/science.282.5393.1484. PMID 9822378.
Kim SH, Kaminker P, Campisi J (1999). "TIN2, a new regulator of telomere length in human cells.". Nat. Genet. 23 (4): 405–12. doi:10.1038/70508. PMID 10581025.
Smogorzewska A, van Steensel B, Bianchi A, et al. (2000). "Control of human telomere length by TRF1 and TRF2.". Mol. Cell. Biol. 20 (5): 1659–68. doi:10.1128/MCB.20.5.1659-1668.2000. PMC 85349. PMID 10669743.
Wu G, Lee WH, Chen PL (2000). "NBS1 and TRF1 colocalize at promyelocytic leukemia bodies during late S/G2 phases in immortalized telomerase-negative cells. Implication of NBS1 in alternative lengthening of telomeres.". J. Biol. Chem. 275 (39): 30618–22. doi:10.1074/jbc.C000390200. PMID 10913111.
Chi NW, Lodish HF (2001). "Tankyrase is a golgi-associated mitogen-activated protein kinase substrate that interacts with IRAP in GLUT4 vesicles.". J. Biol. Chem. 275 (49): 38437–44. doi:10.1074/jbc.M007635200. PMID 10988299.
Kishi S, Wulf G, Nakamura M, Lu KP (2001). "Telomeric protein Pin2/TRF1 induces mitotic entry and apoptosis in cells with short telomeres and is down-regulated in human breast tumors.". Oncogene 20 (12): 1497–508. doi:10.1038/sj.onc.1204229. PMID 11313893.
Kishi S, Zhou XZ, Ziv Y, et al. (2001). "Telomeric protein Pin2/TRF1 as an important ATM target in response to double strand DNA breaks.". J. Biol. Chem. 276 (31): 29282–91. doi:10.1074/jbc.M011534200. PMID 11375976.
Fairall L, Chapman L, Moss H, et al. (2001). "Structure of the TRFH dimerization domain of the human telomeric proteins TRF1 and TRF2.". Mol. Cell 8 (2): 351–61. doi:10.1016/S1097-2765(01)00321-5. PMID 11545737.
Zhou XZ, Lu KP (2001). "The Pin2/TRF1-interacting protein PinX1 is a potent telomerase inhibitor.". Cell 107 (3): 347–59. doi:10.1016/S0092-8674(01)00538-4. PMID 11701125.
Nishikawa T, Okamura H, Nagadoi A, et al. (2002). "Solution structure of a telomeric DNA complex of human TRF1.". Structure 9 (12): 1237–51. doi:10.1016/S0969-2126(01)00688-8. PMID 11738049.

PDB gallery

1ba5: DNA-BINDING DOMAIN OF HUMAN TELOMERIC PROTEIN, HTRF1, NMR, 18 STRUCTURES

1h6o: DIMERISATION DOMAIN FROM HUMAN TRF1

1ity: Solution structure of the DNA binding domain of human TRF1

1iv6: Solution Structure of the DNA Complex of Human TRF1

1w0t: HTRF1 DNA-BINDING DOMAIN IN COMPLEX WITH TELOMERIC DNA.

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TERF1

Interactions

References

Further reading