TINF2

Last updated
TINF2
Protein TINF2 PDB 3BQO.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases TINF2 , DKCA3, TIN2, TERF1 interacting nuclear factor 2
External IDs OMIM: 604319 MGI: 107246 HomoloGene: 8264 GeneCards: TINF2
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001099274
NM_012461
NM_001363668

NM_145705

RefSeq (protein)

NP_001092744
NP_036593
NP_001350597

NP_663751

Location (UCSC) Chr 14: 24.24 – 24.24 Mb Chr 14: 55.91 – 55.92 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

TERF1-interacting nuclear factor 2 is a protein that in humans is encoded by the TINF2 gene. [5] [6] TINF2 is a component of the shelterin protein complex found at the end of telomeres. [7]

Contents

Interactions

TINF2 has been shown to interact with ACD, [8] [9] POT1 [8] [9] [10] and TERF1. [5] [9] [11]

Related Research Articles

<span class="mw-page-title-main">Telomere</span> Region of repetitive nucleotide sequences on chromosomes

A telomere is a region of repetitive nucleotide sequences associated with specialized proteins at the ends of linear chromosomes. Telomeres are a widespread genetic feature most commonly found in eukaryotes. In most, if not all species possessing them, they protect the terminal regions of chromosomal DNA from progressive degradation and ensure the integrity of linear chromosomes by preventing DNA repair systems from mistaking the very ends of the DNA strand for a double-strand break.

<span class="mw-page-title-main">Ku70</span> Protein-coding gene in the species Homo sapiens

Ku70 is a protein that, in humans, is encoded by the XRCC6 gene.

<span class="mw-page-title-main">MRE11A</span> Protein-coding gene in the species Homo sapiens

Double-strand break repair protein MRE11 is an enzyme that in humans is encoded by the MRE11 gene. The gene has been designated MRE11A to distinguish it from the pseudogene MRE11B that is nowadays named MRE11P1.

<span class="mw-page-title-main">Telomeric repeat-binding factor 2</span> Protein

Telomeric repeat-binding factor 2 is a protein that is present at telomeres throughout the cell cycle. It is also known as TERF2, TRF2, and TRBF2, and is encoded in humans by the TERF2 gene. It is a component of the shelterin nucleoprotein complex and a second negative regulator of telomere length, playing a key role in the protective activity of telomeres. It was first reported in 1997 in the lab of Titia de Lange, where a DNA sequence similar, but not identical, to TERF1 was discovered, with respect to the Myb-domain. De Lange isolated the new Myb-containing protein sequence and called it TERF2.

<span class="mw-page-title-main">Telomeric repeat-binding factor 1</span> Protein-coding gene in humans

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

<span class="mw-page-title-main">Rad50</span> Protein-coding gene in the species Homo sapiens

DNA repair protein RAD50, also known as RAD50, is a protein that in humans is encoded by the RAD50 gene.

<span class="mw-page-title-main">POT1</span> Protein-coding gene in the species Homo sapiens

Protection of telomeres protein 1 is a protein that in humans is encoded by the POT1 gene.

<span class="mw-page-title-main">MAPRE1</span> Protein-coding gene in the species Homo sapiens

Microtubule-associated protein RP/EB family member 1 is a protein that in humans is encoded by the MAPRE1 gene.

<span class="mw-page-title-main">Tankyrase</span> Enzyme

Tankyrase, also known as tankyrase 1, is an enzyme that in humans is encoded by the TNKS gene. It inhibits the binding of TERF1 to telomeric DNA. Tankyrase attracts substantial interest in cancer research through its interaction with AXIN1 and AXIN2, which are negative regulators of pro-oncogenic β-catenin signaling. Importantly, activity in the β-catenin destruction complex can be increased by tankyrase inhibitors and thus such inhibitors are a potential therapeutic option to reduce the growth of β-catenin-dependent cancers.

<span class="mw-page-title-main">ACD (gene)</span> Protein-coding gene in the species Homo sapiens

Adrenocortical dysplasia protein homolog is a protein that in humans is encoded by the ACD gene.

<span class="mw-page-title-main">TERF2IP</span> Protein-coding gene in the species Homo sapiens

Telomeric repeat-binding factor 2-interacting protein 1 also known as repressor activator protein 1 (Rap1) is a protein that in humans is encoded by the TERF2IP gene.

<span class="mw-page-title-main">PINX1</span> Protein-coding gene in the species Homo sapiens

PIN2/TERF1-interacting telomerase inhibitor 1, also known as PINX1, is a human gene. PINX1 is also known as PIN2 interacting protein 1. PINX1 is a telomerase inhibitor and a possible tumor suppressor.

<span class="mw-page-title-main">Tankyrase 2</span> Protein-coding gene in the species Homo sapiens

Tankyrase-2 is an enzyme that in humans is encoded by the TNKS2 gene.

<span class="mw-page-title-main">TELO2</span> Human protein

Telomere length regulation protein TEL2 homolog is a protein that in humans is encoded by the TELO2 gene.

<span class="mw-page-title-main">DCLRE1B</span> Protein-coding gene in the species Homo sapiens

DNA cross-link repair 1B protein is a protein that in humans is encoded by the DCLRE1B gene.

Telomere-binding proteins function to bind telomeric DNA in various species. In particular, telomere-binding protein refers to TTAGGG repeat binding factor-1 (TERF1) and TTAGGG repeat binding factor-2 (TERF2). Telomere sequences in humans are composed of TTAGGG sequences which provide protection and replication of chromosome ends to prevent degradation. Telomere-binding proteins can generate a T-loop to protect chromosome ends. TRFs are double-stranded proteins which are known to induce bending, looping, and pairing of DNA which aids in the formation of T-loops. They directly bind to TTAGGG repeat sequence in the DNA. There are also subtelomeric regions present for regulation. However, in humans, there are six subunits forming a complex known as shelterin.

Shelterin is a protein complex known to protect telomeres in many eukaryotes from DNA repair mechanisms, as well as to regulate telomerase activity. In mammals and other vertebrates, telomeric DNA consists of repeating double-stranded 5'-TTAGGG-3' (G-strand) sequences along with the 3'-AATCCC-5' (C-strand) complement, ending with a 50-400 nucleotide 3' (G-strand) overhang. Much of the final double-stranded portion of the telomere forms a T-loop (Telomere-loop) that is invaded by the 3' (G-strand) overhang to form a small D-loop (Displacement-loop).

<span class="mw-page-title-main">Titia de Lange</span> Dutch geneticist

Titia de Lange is the Director of the Anderson Center for Cancer Research, the Leon Hess professor and the head of Laboratory Cell Biology and Genetics at Rockefeller University.

<span class="mw-page-title-main">Telomeric repeat–containing RNA</span> Long non-coding RNA transcribed from telomeres

Telomeric repeat–containing RNA (TERRA) is a long non-coding RNA transcribed from telomeres - repetitive nucleotide regions found on the ends of chromosomes that function to protect DNA from deterioration or fusion with neighboring chromosomes. TERRA has been shown to be ubiquitously expressed in almost all cell types containing linear chromosomes - including humans, mice, and yeasts. While the exact function of TERRA is still an active area of research, it is generally believed to play a role in regulating telomerase activity as well as maintaining the heterochromatic state at the ends of chromosomes. TERRA interaction with other associated telomeric proteins has also been shown to help regulate telomere integrity in a length-dependent manner.

Telomeres, the caps on the ends of eukaryotic chromosomes, play critical roles in cellular aging and cancer. An important facet to how telomeres function in these roles is their involvement in cell cycle regulation.

References

  1. 1 2 3 ENSG00000284915 GRCh38: Ensembl release 89: ENSG00000092330, ENSG00000284915 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000007589 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. 1 2 Kim SH, Kaminker P, Campisi J (Dec 1999). "TIN2, a new regulator of telomere length in human cells". Nature Genetics. 23 (4): 405–12. doi:10.1038/70508. PMC   4940194 . PMID   10581025.
  6. "Entrez Gene: TINF2 TERF1 (TRF1)-interacting nuclear factor 2".
  7. Savage SA, Giri N, Baerlocher GM, Orr N, Lansdorp PM, Alter BP (Feb 2008). "TINF2, a component of the shelterin telomere protection complex, is mutated in dyskeratosis congenita". American Journal of Human Genetics. 82 (2): 501–9. doi:10.1016/j.ajhg.2007.10.004. PMC   2427222 . PMID   18252230.
  8. 1 2 Ye JZ, Hockemeyer D, Krutchinsky AN, Loayza D, Hooper SM, Chait BT, de Lange T (Jul 2004). "POT1-interacting protein PIP1: a telomere length regulator that recruits POT1 to the TIN2/TRF1 complex". Genes & Development. 18 (14): 1649–54. doi:10.1101/gad.1215404. PMC   478187 . PMID   15231715.
  9. 1 2 3 Liu D, Safari A, O'Connor MS, Chan DW, Laegeler A, Qin J, Songyang Z (Jul 2004). "PTOP interacts with POT1 and regulates its localization to telomeres". Nature Cell Biology. 6 (7): 673–80. doi:10.1038/ncb1142. PMID   15181449. S2CID   11543383.
  10. Loayza D, De Lange T (Jun 2003). "POT1 as a terminal transducer of TRF1 telomere length control". Nature. 423 (6943): 1013–8. Bibcode:2003Natur.423.1013L. doi:10.1038/nature01688. PMID   12768206. S2CID   4370276.
  11. Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE (Sep 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi: 10.1016/j.cell.2005.08.029 . PMID   16169070.

Further reading