TERF2IP

Protein-coding gene in the species Homo sapiens
TERF2IP
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1FEX, 3K6G, 4RQI

Identifiers
AliasesTERF2IP, DRIP5, RAP1, TERF2 interacting protein
External IDsOMIM: 605061; MGI: 1929871; HomoloGene: 10357; GeneCards: TERF2IP; OMA:TERF2IP - orthologs
Gene location (Human)
Chromosome 16 (human)
Chr.Chromosome 16 (human)[1]
Chromosome 16 (human)
Genomic location for TERF2IP
Genomic location for TERF2IP
Band16q23.1Start75,647,773 bp[1]
End75,761,872 bp[1]
Gene location (Mouse)
Chromosome 8 (mouse)
Chr.Chromosome 8 (mouse)[2]
Chromosome 8 (mouse)
Genomic location for TERF2IP
Genomic location for TERF2IP
Band8|8 E1Start112,738,030 bp[2]
End112,747,160 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • middle temporal gyrus

  • Brodmann area 23

  • Pars compacta

  • pars reticulata

  • superior vestibular nucleus

  • pons

  • internal globus pallidus

  • lateral nuclear group of thalamus

  • Brodmann area 9

  • superior frontal gyrus
Top expressed in
  • ventromedial nucleus

  • supraoptic nucleus

  • paraventricular nucleus of hypothalamus

  • dorsomedial hypothalamic nucleus

  • lateral hypothalamus

  • ventral tegmental area

  • arcuate nucleus

  • dorsal tegmental nucleus

  • mammillary body

  • habenula
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • DNA binding
  • telomeric DNA binding
  • protein binding
  • G-rich strand telomeric DNA binding
  • phosphatase binding
Cellular component
  • nuclear telomere cap complex
  • nuclear envelope
  • chromosome
  • shelterin complex
  • telomere
  • nuclear chromosome
  • Mre11 complex
  • nucleus
  • nucleoplasm
  • cytosol
  • nuclear body
  • cytoplasm
Biological process
  • negative regulation of DNA recombination at telomere
  • telomere maintenance via telomerase
  • protection from non-homologous end joining at telomere
  • regulation of double-strand break repair via homologous recombination
  • transcription, DNA-templated
  • positive regulation of peptidyl-serine phosphorylation
  • protein localization to chromosome, telomeric region
  • positive regulation of protein acetylation
  • telomere maintenance via telomere lengthening
  • positive regulation of NF-kappaB transcription factor activity
  • positive regulation of I-kappaB kinase/NF-kappaB signaling
  • telomere maintenance
  • telomere capping
  • negative regulation of protein phosphorylation
  • regulation of transcription, DNA-templated
  • regulation of telomere maintenance
  • negative regulation of telomere maintenance
  • positive regulation of NIK/NF-kappaB signaling
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

54386

57321

Ensembl

ENSG00000166848

ENSMUSG00000033430

UniProt

Q9NYB0

Q91VL8

RefSeq (mRNA)

NM_018975

NM_020584

RefSeq (protein)

NP_061848

NP_065609

Location (UCSC)Chr 16: 75.65 – 75.76 MbChr 8: 112.74 – 112.75 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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.[5][6]

Interactions

TERF2IP has been shown to interact with Ku80,[7] Rad50[7] and TERF2.[5][7][8] Upon interaction, TERF2IP/TERF2 complex has been shown to bind to telomeric junction sites with higher affinity[9]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000166848 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000033430 – 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. ^ a b Li B, Oestreich S, de Lange T (May 2000). "Identification of human Rap1: implications for telomere evolution". Cell. 101 (5): 471–83. doi:10.1016/S0092-8674(00)80858-2. PMID 10850490. S2CID 7956545.
  6. ^ "Entrez Gene: TERF2IP telomeric repeat binding factor 2, interacting protein".
  7. ^ a b c O'Connor MS, Safari A, Liu D, Qin J, Songyang Z (July 2004). "The human Rap1 protein complex and modulation of telomere length". The Journal of Biological Chemistry. 279 (27): 28585–91. doi:10.1074/jbc.M312913200. PMID 15100233.
  8. ^ Zhu XD, Küster B, Mann M, Petrini JH, de Lange T (July 2000). "Cell-cycle-regulated association of RAD50/MRE11/NBS1 with TRF2 and human telomeres". Nature Genetics. 25 (3): 347–52. doi:10.1038/77139. PMID 10888888. S2CID 6689794.
  9. ^ Arat NÖ, Griffith JD (December 2012). "Human Rap1 interacts directly with telomeric DNA and regulates TRF2 localization at the telomere". The Journal of Biological Chemistry. 287 (50): 41583–94. doi:10.1074/jbc.M112.415984. PMC 3516710. PMID 23086976.

Further reading

  • Zhu XD, Küster B, Mann M, Petrini JH, de Lange T (July 2000). "Cell-cycle-regulated association of RAD50/MRE11/NBS1 with TRF2 and human telomeres". Nature Genetics. 25 (3): 347–52. doi:10.1038/77139. PMID 10888888. S2CID 6689794.
  • Hanaoka S, Nagadoi A, Yoshimura S, Aimoto S, Li B, de Lange T, Nishimura Y (September 2001). "NMR structure of the hRap1 Myb motif reveals a canonical three-helix bundle lacking the positive surface charge typical of Myb DNA-binding domains". Journal of Molecular Biology. 312 (1): 167–75. doi:10.1006/jmbi.2001.4924. PMID 11545594.
  • Loayza D, De Lange T (June 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.
  • Li B, de Lange T (December 2003). "Rap1 affects the length and heterogeneity of human telomeres". Molecular Biology of the Cell. 14 (12): 5060–8. doi:10.1091/mbc.E03-06-0403. PMC 284807. PMID 14565979.
  • Zhu XD, Niedernhofer L, Kuster B, Mann M, Hoeijmakers JH, de Lange T (December 2003). "ERCC1/XPF removes the 3' overhang from uncapped telomeres and represses formation of telomeric DNA-containing double minute chromosomes". Molecular Cell. 12 (6): 1489–98. doi:10.1016/S1097-2765(03)00478-7. PMID 14690602.
  • O'Connor MS, Safari A, Liu D, Qin J, Songyang Z (July 2004). "The human Rap1 protein complex and modulation of telomere length". The Journal of Biological Chemistry. 279 (27): 28585–91. doi:10.1074/jbc.M312913200. PMID 15100233.
  • Liu D, Safari A, O'Connor MS, Chan DW, Laegeler A, Qin J, Songyang Z (July 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.
  • Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP (August 2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proceedings of the National Academy of Sciences of the United States of America. 101 (33): 12130–5. Bibcode:2004PNAS..10112130B. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
  • Ye JZ, Donigian JR, van Overbeek M, Loayza D, Luo Y, Krutchinsky AN, Chait BT, de Lange T (November 2004). "TIN2 binds TRF1 and TRF2 simultaneously and stabilizes the TRF2 complex on telomeres". The Journal of Biological Chemistry. 279 (45): 47264–71. doi:10.1074/jbc.M409047200. PMID 15316005.
  • Liu D, O'Connor MS, Qin J, Songyang Z (December 2004). "Telosome, a mammalian telomere-associated complex formed by multiple telomeric proteins". The Journal of Biological Chemistry. 279 (49): 51338–42. doi:10.1074/jbc.M409293200. PMID 15383534.
  • Wan D, Gong Y, Qin W, Zhang P, Li J, Wei L, Zhou X, Li H, Qiu X, Zhong F, He L, Yu J, Yao G, Jiang H, Qian L, Yu Y, Shu H, Chen X, Xu H, Guo M, Pan Z, Chen Y, Ge C, Yang S, Gu J (November 2004). "Large-scale cDNA transfection screening for genes related to cancer development and progression". Proceedings of the National Academy of Sciences of the United States of America. 101 (44): 15724–9. Bibcode:2004PNAS..10115724W. doi:10.1073/pnas.0404089101. PMC 524842. PMID 15498874.
  • Antoine K, Ferbus D, Kolahgar G, Prospéri MT, Goubin G (July 2005). "Zinc finger protein overexpressed in colon carcinoma interacts with the telomeric protein hRap1". Journal of Cellular Biochemistry. 95 (4): 763–8. doi:10.1002/jcb.20487. PMID 15838871. S2CID 10264323.
  • Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
  • Beausoleil SA, Villén J, Gerber SA, Rush J, Gygi SP (October 2006). "A probability-based approach for high-throughput protein phosphorylation analysis and site localization". Nature Biotechnology. 24 (10): 1285–92. doi:10.1038/nbt1240. PMID 16964243. S2CID 14294292.
  • Wu Y, Zacal NJ, Rainbow AJ, Zhu XD (February 2007). "XPF with mutations in its conserved nuclease domain is defective in DNA repair but functions in TRF2-mediated telomere shortening". DNA Repair. 6 (2): 157–66. doi:10.1016/j.dnarep.2006.09.005. PMID 17055345.
  • Bae NS, Baumann P (May 2007). "A RAP1/TRF2 complex inhibits nonhomologous end-joining at human telomeric DNA ends". Molecular Cell. 26 (3): 323–34. doi:10.1016/j.molcel.2007.03.023. PMID 17499040.
  • Cai Y, Kandula V, Kosuru R, Ye X, Irwin MG, Xia Z (Oct 2017). "Decoding telomere protein Rap1: its telomeric and nontelomeric functions and potential implications in diabetic cardiomyopathy". Cell Cycle. 16 (19): 1765–1773. doi:10.1080/15384101.2017.1371886. PMC 5628636. PMID 28853973.
  • Cai Y, Liu H, Song E, Wang L, Xu J, He Y, Xia Z (Mar 2021). "Deficiency of telomere-associated repressor activator protein 1 precipitates cardiac aging in mice via p53/PPARα signaling". Theranostics. 11 (10): 4710–4727. doi:10.7150/thno.51739. PMC 7978321. PMID 33754023.
  • v
  • t
  • e
  • 1fex: SOLUTION STRUCTURE OF MYB-DOMAIN OF HUMAN RAP1
    1fex: SOLUTION STRUCTURE OF MYB-DOMAIN OF HUMAN RAP1


Stub icon

This article on a gene on human chromosome 16 is a stub. You can help Wikipedia by expanding it.

  • v
  • t
  • e