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HUMAN:TINF2

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Species (Taxon ID) Homo sapiens (Human). (9606)
Gene Name(s) TINF2 (synonyms: TIN2)
Protein Name(s) TERF1-interacting nuclear factor 2

TRF1-interacting nuclear protein 2

External Links
UniProt Q9BSI4
EMBL AF195512
AK023166
BC005030
BC019343
EU851975
CCDS CCDS41936.1
CCDS41937.1
RefSeq NP_001092744.1
NP_036593.2
UniGene Hs.496191
PDB 3BQO
3BU8
PDBsum 3BQO
3BU8
ProteinModelPortal Q9BSI4
BioGrid 117660
DIP DIP-29413N
IntAct Q9BSI4
MINT MINT-221357
STRING 9606.ENSP00000267415
iPTMnet Q9BSI4
PhosphoSite Q9BSI4
BioMuta TINF2
DMDM 21542262
EPD Q9BSI4
MaxQB Q9BSI4
PaxDb Q9BSI4
PRIDE Q9BSI4
DNASU 26277
Ensembl ENST00000267415
ENST00000399423
GeneID 26277
KEGG hsa:26277
UCSC uc001woa.5
CTD 26277
GeneCards TINF2
GeneReviews TINF2
HGNC HGNC:11824
MalaCards TINF2
MIM 268130
604319
613990
neXtProt NX_Q9BSI4
Orphanet 1775
3322
3088
PharmGKB PA36530
eggNOG ENOG410IHMP
ENOG410Z499
GeneTree ENSGT00400000022326
HOGENOM HOG000247003
HOVERGEN HBG057120
InParanoid Q9BSI4
KO K11112
OMA GGHKERP
PhylomeDB Q9BSI4
TreeFam TF334731
Reactome [www.reactome.org/content/detail/R-HSA-1221632 R-HSA-1221632]
[www.reactome.org/content/detail/R-HSA-171306 R-HSA-171306]
[www.reactome.org/content/detail/R-HSA-2559586 R-HSA-2559586]
SIGNOR Q9BSI4
EvolutionaryTrace Q9BSI4
GeneWiki TINF2
GenomeRNAi 26277
PRO PR:Q9BSI4
Proteomes UP000005640
Bgee Q9BSI4
CleanEx HS_TINF2
ExpressionAtlas Q9BSI4
Genevisible Q9BSI4
GO GO:0000781
GO:0000784
GO:0016363
GO:0000783
GO:0005654
GO:0005634
GO:0010370
GO:0070187
GO:0010521
GO:0042162
GO:0050680
GO:0010836
GO:0051974
GO:0032211
GO:0032206
GO:0034502
GO:0070198
GO:0032202
GO:0016233
GO:0010833
InterPro IPR029400
Pfam PF14973

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

involved_in

GO:0016233

telomere capping

PMID:15133513[1]

ECO:0000305

curator inference used in manual assertion

GO:0032211

P

Seeded From UniProt

complete

involved_in

GO:0010836

negative regulation of protein ADP-ribosylation

PMID:15133513[1]

ECO:0000314

direct assay evidence used in manual assertion

P

has_regulation_target:(UniProtKB:O95271)

Seeded From UniProt

complete

involved_in

GO:0032211

negative regulation of telomere maintenance via telomerase

PMID:15133513[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

has_regulation_target:(UniProtKB:O14746)

Seeded From UniProt

complete

part_of

GO:0000784

nuclear chromosome, telomeric region

PMID:15133513[1]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0000784

nuclear chromosome, telomeric region

PMID:19135898[2]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0070187

shelterin complex

PMID:15383534[3]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0070187

shelterin complex

PMID:23685356[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0000784

nuclear chromosome, telomeric region

PMID:23685356[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0042162

telomeric DNA binding

PMID:23685356[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0070187

shelterin complex

PMID:21852327[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0000784

nuclear chromosome, telomeric region

PMID:24270157[6]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0070198

protein localization to chromosome, telomeric region

PMID:18443218[7]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0050680

negative regulation of epithelial cell proliferation

PMID:15741234[8]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0070198

protein localization to chromosome, telomeric region

PMID:15133513[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

has_direct_input:(UniProtKB:P54274)

Seeded From UniProt

complete

involved_in

GO:0032211

negative regulation of telomere maintenance via telomerase

PMID:10581025[9]

ECO:0000316

genetic interaction evidence used in manual assertion

P

Seeded From UniProt

Missing: with/from

involved_in

GO:0016233

telomere capping

PMID:18443218[7]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0032202

telomere assembly

PMID:16880378[10]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:1904356

regulation of telomere maintenance via telomere lengthening

PMID:18669893[11]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0010370

perinucleolar chromocenter

PMID:15741234[8]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

NOT|enables

GO:0003677

DNA binding

PMID:10581025[9]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0000783

nuclear telomere cap complex

PMID:16880378[10]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0000784

nuclear chromosome, telomeric region

PMID:15380063[12]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0000781

chromosome, telomeric region

PMID:12768206[13]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0000781

chromosome, telomeric region

PMID:10581025[9]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0042162

telomeric DNA binding

PMID:12768206[13]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0016604

nuclear body

GO_REF:0000052

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0016233

telomere capping

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR039098

P

Seeded From UniProt

complete

GO:0070198

protein localization to chromosome, telomeric region

PMID:20404094[14]

ECO:0000314

P

Figure 6: After knockdown of TPP1, introduction of an shRNA-resistant TPP1 restores hTr localization to the telomere Evidence code: IMP

complete
CACAO 12113

part_of

GO:0070187

shelterin complex

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR039098

C

Seeded From UniProt

complete

involved_in

GO:0016233

telomere capping

Reactome:R-HSA-181450
Reactome:R-HSA-176700

ECO:0000304

author statement supported by traceable reference used in manual assertion


P

Seeded From UniProt

complete

part_of

GO:0005654

nucleoplasm

Reactome:R-HSA-3785711
Reactome:R-HSA-181450
Reactome:R-HSA-176700

ECO:0000304

author statement supported by traceable reference used in manual assertion



C

Seeded From UniProt

complete

part_of

GO:0000781

chromosome, telomeric region

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0779
UniProtKB-SubCell:SL-0276

C

Seeded From UniProt

complete

part_of

GO:0005694

chromosome

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0158

C

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0539
UniProtKB-SubCell:SL-0191

C

Seeded From UniProt

complete

part_of

GO:0016363

nuclear matrix

GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-SubCell:SL-0181

C

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 1.2 1.3 1.4 Ye, JZ & de Lange, T (2004) TIN2 is a tankyrase 1 PARP modulator in the TRF1 telomere length control complex. Nat. Genet. 36 618-23 PubMed GONUTS page
  2. Déjardin, J & Kingston, RE (2009) Purification of proteins associated with specific genomic Loci. Cell 136 175-86 PubMed GONUTS page
  3. Liu, D et al. (2004) Telosome, a mammalian telomere-associated complex formed by multiple telomeric proteins. J. Biol. Chem. 279 51338-42 PubMed GONUTS page
  4. 4.0 4.1 4.2 Kappei, D et al. (2013) HOT1 is a mammalian direct telomere repeat-binding protein contributing to telomerase recruitment. EMBO J. 32 1681-701 PubMed GONUTS page
  5. Choi, KH et al. (2011) Characterization of the DNA binding specificity of Shelterin complexes. Nucleic Acids Res. 39 9206-23 PubMed GONUTS page
  6. Grolimund, L et al. (2013) A quantitative telomeric chromatin isolation protocol identifies different telomeric states. Nat Commun 4 2848 PubMed GONUTS page
  7. 7.0 7.1 Kim, SH et al. (2008) Telomere dysfunction and cell survival: roles for distinct TIN2-containing complexes. J. Cell Biol. 181 447-60 PubMed GONUTS page
  8. 8.0 8.1 Kaminker, P et al. (2005) Higher-order nuclear organization in growth arrest of human mammary epithelial cells: a novel role for telomere-associated protein TIN2. J. Cell. Sci. 118 1321-30 PubMed GONUTS page
  9. 9.0 9.1 9.2 Kim, SH et al. (1999) TIN2, a new regulator of telomere length in human cells. Nat. Genet. 23 405-12 PubMed GONUTS page
  10. 10.0 10.1 O'Connor, MS et al. (2006) A critical role for TPP1 and TIN2 interaction in high-order telomeric complex assembly. Proc. Natl. Acad. Sci. U.S.A. 103 11874-9 PubMed GONUTS page
  11. Walne, AJ et al. (2008) TINF2 mutations result in very short telomeres: analysis of a large cohort of patients with dyskeratosis congenita and related bone marrow failure syndromes. Blood 112 3594-600 PubMed GONUTS page
  12. Houghtaling, BR et al. (2004) A dynamic molecular link between the telomere length regulator TRF1 and the chromosome end protector TRF2. Curr. Biol. 14 1621-31 PubMed GONUTS page
  13. 13.0 13.1 Loayza, D & De Lange, T (2003) POT1 as a terminal transducer of TRF1 telomere length control. Nature 423 1013-8 PubMed GONUTS page
  14. Abreu, E et al. (2010) TIN2-tethered TPP1 recruits human telomerase to telomeres in vivo. Mol. Cell. Biol. 30 2971-82 PubMed GONUTS page