| UniProt ID | TINF2_HUMAN | |
|---|---|---|
| UniProt AC | Q9BSI4 | |
| Protein Name | TERF1-interacting nuclear factor 2 | |
| Gene Name | TINF2 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 451 | |
| Subcellular Localization |
Nucleus . Chromosome, telomere . Associated with telomeres. Isoform 1: Nucleus matrix . |
|
| Protein Description | Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded TTAGGG repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways. Plays a role in shelterin complex assembly. Isoform 1 may have additional role in tethering telomeres to the nuclear matrix.. | |
| Protein Sequence | MATPLVAGPAALRFAAAASWQVVRGRCVEHFPRVLEFLRSLRAVAPGLVRYRHHERLCMGLKAKVVVELILQGRPWAQVLKALNHHFPESGPIVRDPKATKQDLRKILEAQETFYQQVKQLSEAPVDLASKLQELEQEYGEPFLAAMEKLLFEYLCQLEKALPTPQAQQLQDVLSWMQPGVSITSSLAWRQYGVDMGWLLPECSVTDSVNLAEPMEQNPPQQQRLALHNPLPKAKPGTHLPQGPSSRTHPEPLAGRHFNLAPLGRRRVQSQWASTRGGHKERPTVMLFPFRNLGSPTQVISKPESKEEHAIYTADLAMGTRAASTGKSKSPCQTLGGRALKENPVDLPATEQKENCLDCYMDPLRLSLLPPRARKPVCPPSLCSSVITIGDLVLDSDEEENGQGEGKESLENYQKTKFDTLIPTLCEYLPPSGHGAIPVSSCDCRDSSRPL | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MATPLVAGP ------CCCCCCCCH | 20.23 | 22814378 | |
| 101 | Methylation | VRDPKATKQDLRKIL CCCCCCCHHHHHHHH | 46.83 | 116253649 | |
| 119 | Ubiquitination | ETFYQQVKQLSEAPV HHHHHHHHHHHHCCC | 40.98 | 29967540 | |
| 122 | Phosphorylation | YQQVKQLSEAPVDLA HHHHHHHHHCCCCHH | 29.26 | 21406692 | |
| 130 | Phosphorylation | EAPVDLASKLQELEQ HCCCCHHHHHHHHHH | 40.99 | 21406692 | |
| 276 | Methylation | QSQWASTRGGHKERP HHCHHHCCCCCCCCC | 46.75 | 12018095 | |
| 295 | Phosphorylation | FPFRNLGSPTQVISK EECCCCCCCCEEECC | 28.13 | 30266825 | |
| 295 (in isoform 2) | Phosphorylation | - | 28.13 | - | |
| 297 | Phosphorylation | FRNLGSPTQVISKPE CCCCCCCCEEECCCC | 36.85 | 30266825 | |
| 301 | Phosphorylation | GSPTQVISKPESKEE CCCCEEECCCCCHHH | 43.21 | 28302921 | |
| 302 | Ubiquitination | SPTQVISKPESKEEH CCCEEECCCCCHHHH | 41.50 | 29967540 | |
| 302 | Sumoylation | SPTQVISKPESKEEH CCCEEECCCCCHHHH | 41.50 | 28112733 | |
| 305 | Phosphorylation | QVISKPESKEEHAIY EEECCCCCHHHHHEE | 54.62 | 28464451 | |
| 306 | Sumoylation | VISKPESKEEHAIYT EECCCCCHHHHHEEE | 66.51 | 28112733 | |
| 312 | Phosphorylation | SKEEHAIYTADLAMG CHHHHHEEEEHHHHC | 9.17 | 25159151 | |
| 313 | Phosphorylation | KEEHAIYTADLAMGT HHHHHEEEEHHHHCC | 13.95 | 29978859 | |
| 324 | Phosphorylation | AMGTRAASTGKSKSP HHCCCCCCCCCCCCC | 36.39 | 30631047 | |
| 328 | Phosphorylation | RAASTGKSKSPCQTL CCCCCCCCCCCCCCC | 39.45 | 30266825 | |
| 330 | Phosphorylation | ASTGKSKSPCQTLGG CCCCCCCCCCCCCCC | 37.69 | 30266825 | |
| 334 | Phosphorylation | KSKSPCQTLGGRALK CCCCCCCCCCCHHHH | 33.80 | 30266825 | |
| 341 | Ubiquitination | TLGGRALKENPVDLP CCCCHHHHHCCCCCC | 55.23 | 33845483 | |
| 341 | Sumoylation | TLGGRALKENPVDLP CCCCHHHHHCCCCCC | 55.23 | 28112733 | |
| 353 | Sumoylation | DLPATEQKENCLDCY CCCCHHHHCCHHHHH | 44.66 | 28112733 | |
| 360 | Phosphorylation | KENCLDCYMDPLRLS HCCHHHHHCCHHHHH | 12.29 | 27642862 | |
| 385 | Phosphorylation | CPPSLCSSVITIGDL CCHHHHCCEEEECCE | 19.28 | 27251275 | |
| 388 | Phosphorylation | SLCSSVITIGDLVLD HHHCCEEEECCEECC | 19.42 | 27251275 | |
| 396 | Phosphorylation | IGDLVLDSDEEENGQ ECCEECCCCCCCCCC | 42.64 | 21712546 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 295 | S | Phosphorylation | Kinase | RPS6KA3 | P51812 | GPS |
| 330 | S | Phosphorylation | Kinase | RPS6KA3 | P51812 | GPS |
| 396 | S | Phosphorylation | Kinase | CSNK2A1 | P68400 | GPS |
| - | K | Ubiquitination | E3 ubiquitin ligase | SIAH2 | O43255 | PMID:22064479 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TINF2_HUMAN !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of TINF2_HUMAN !! | ||||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| 613990 | Dyskeratosis congenita, autosomal dominant, 3 (DKCA3) | |||||
| 268130 | Dyskeratosis congenita, autosomal dominant, 5 (DKCA5) | |||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295, AND MASSSPECTROMETRY. | |
