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HomoloGene:8264. Gene conserved in Boreoeutheria Download , Links
Genes identified as putative homologs of one another during the construction of HomoloGene.

Proteins used in sequence comparisons and their conserved domain architectures.

TINF2,  H.sapiens
TERF1 (TRF1)-interacting nuclear factor 2
451 aa
TINF2,  P.troglodytes
TERF1 (TRF1)-interacting nuclear factor 2
453 aa
TINF2,  M.mulatta
TERF1 (TRF1)-interacting nuclear factor 2
451 aa
TINF2,  C.lupus
TERF1 (TRF1)-interacting nuclear factor 2
465 aa
TINF2,  B.taurus
TERF1 (TRF1)-interacting nuclear factor 2
451 aa
Tinf2,  M.musculus
Terf1 (TRF1)-interacting nuclear factor 2
414 aa
Tinf2,  R.norvegicus
TERF1 (TRF1)-interacting nuclear factor 2
397 aa

Protein Alignments
Protein multiple alignment, pairwise similarity scores and evolutionary distances.

Show Multiple Alignment

Show Pairwise Alignment Scores

Pairwise alignments generated using BLAST
Regenerate Alignments

Phenotypic information for the genes in this entry imported from model organism databases.

Dyskeratosis congenita, autosomal dominant.

Articles associated with genes and sequences of this homology group.

TINF2 mutations in children with severe aplastic anemia.
Du HY, et al. Pediatr Blood Cancer 52, 687 (2009).

Conserved Domains
Conserved Domains from CDD found in protein sequences by rpsblast searching.
TIN2_TBM (cd11741)
  TRF-binding motif region of TRF-Interacting Nuclear factor 2.
TIN2_N (cl18929)
  TIN2 is one of the six proteins of shelterin complex, which acts to protect telomeres from DNA damage repair machinery. TIN2 binds directly to TRF1 and TRF2 and stabilizes TRF2 complex-telomere binding by tethering it to the TRF1 complex. TIN2 binding to TRF2 is primarily via the TRF binding motif (TBM) region and the N-terminus, while the far C-terminal region has lower affinity. The TIN2 TBM, but not the N-terminal region, is involved in TIN2 binding to TRF1. Truncation of the TIN2 N-terminus in mouse results in telomere elongation, suggesting a negative regulatory function of this region. Three shelterin components (TRF1, TRF2, POT1) bind DNA and 3 components (TIN2, RAP1, TPP1) are recruited by these DNA binding factors. TRF1 activity at telomeres is regulated in part by selective ubiquitination and degradation. Ubiquitination of TRF1 is mediated by Fbx4, which binds TRF1 in the TRFH domain, via a small GTPase module. When bound to telomeres, TIN2 acts to protect TRF1 from SCF-Fbx4 mediated ubiquitination. F-box proteins act in substrate recognition as part of Skp1-Cul1-Rbx1-F- box (SCF) protein complexes. Tankyrase-mediated ADP-ribosylation releases TRF1 from telomeres, rendering them susceptible to ubiquitination and degradation, promoting telomere elongation. TIN2 also binds PIP1, which recruits POT1 to telomeres.

Related Homology Resources
Links to curated and computed homology information found in other databases.
Orthology group for M.musculus Tinf2 includes H.sapiens TINF2 and R.norvegicus Tinf2.

Links to UniGene entries found by comparing the homologous proteins against the transcript database.

Mammalia - mammals (9 transcripts, 9 species)




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