Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Telomeric repeat-binding factor 2-interacting protein 1  

UniProtKB / Swiss-Prot ID :  TE2IP_MOUSE

Gene Name (Synonyms) : 
Terf2ip, Rap1 MNCb-0448, MNCb-0628  

Species :  Mus musculus (Mouse). 

Subcellular Localization :  Nucleus. Cytoplasm. Chromosome. Chromosome, telomere. Note=Associates with chromosomes, both at telomeres and in extratelomeric sites. Also exists as a cytoplasmic form, where it associates with the IKK complex. 

Protein Function :  Acts both as a regulator of telomere function and as a transcription regulator. Involved in the regulation of telomere length and protection as a component of the shelterin complex (telosome). In contrast to other components of the shelterin complex, it is dispensible for telomere capping and does not participate in the protection of telomeres against non-homologous end-joining (NHEJ)-mediated repair. Instead, it is required to negatively regulate telomere recombination and is essential for repressing homology-directed repair (HDR), which can affect telomere length. Does not bind DNA directly: recruited to telomeric double-stranded 5'-TTAGGG-3' repeats via its interaction with TERF2. Independently of its function in telomeres, also acts as a transcription regulator: recruited to extratelomeric 5'- TTAGGG-3' sites via its association with TERF2 or other factors, and regulates gene expression. When cytoplasmic, associates with the I-kappa-B-kinase (IKK) complex and acts as a regulator of the NF-kappa-B signaling by promoting IKK-mediated phosphorylation of RELA/p65, leading to activate expression of NF-kappa-B target genes. 

Protein Sequence MAEAMDLGKDPNGPTHSSTLFVREDGSAMSFYVRPSSAKRRLSTLILHGGGTVCRVQEPGAVLLAQPGEA...
Predicted Secondary Structure CCCCHHCCCCCCCCCCCCEEEEEECCCEEEEEECCCCHHHHEEEEEEECCCCEEEEECCCEEEEECCCHH...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
151PhosphoserineENARSPSSV
HCCCCCCCC
27.07Phosphositeplus
Link-
200PhosphoserineNAPVSPSSQ
CCCCCCCHH
20.29PhosphoELM
Link-
200PhosphoserineNAPVSPSSQ
CCCCCCCHH
20.29Phosphositeplus
Link-
200PhosphoserineNAPVSPSSQ
CCCCCCCHH
20.29SysPTM
Link-
200Phosphoserine.NAPVSPSSQ
CCCCCCCHH
20.29UniProtKB
Link-
203PhosphoserineVSPSSQKLK
CCCCHHHHH
34.42Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Drug Reference
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures