UniProt ID | TERF2_HUMAN | |
---|---|---|
UniProt AC | Q15554 | |
Protein Name | Telomeric repeat-binding factor 2 | |
Gene Name | TERF2 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 542 | |
Subcellular Localization | Nucleus . Chromosome, telomere . Colocalizes with telomeric DNA in interphase cells and is located at chromosome ends during metaphase. | |
Protein Description | Binds the telomeric double-stranded 5'-TTAGGG-3' repeat and plays a central role in telomere maintenance and protection against end-to-end fusion of chromosomes. In addition to its telomeric DNA-binding role, required to recruit a number of factors and enzymes required for telomere protection, including the shelterin complex, TERF2IP/RAP1 and DCLRE1B/Apollo. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded 5'-TTAGGG-3' 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. Together with DCLRE1B/Apollo, plays a key role in telomeric loop (T loop) formation by generating 3' single-stranded overhang at the leading end telomeres: T loops have been proposed to protect chromosome ends from degradation and repair. Required both to recruit DCLRE1B/Apollo to telomeres and activate the exonuclease activity of DCLRE1B/Apollo. Preferentially binds to positive supercoiled DNA. Together with DCLRE1B/Apollo, required to control the amount of DNA topoisomerase (TOP1, TOP2A and TOP2B) needed for telomere replication during fork passage and prevent aberrant telomere topology. Recruits TERF2IP/RAP1 to telomeres, thereby participating in to repressing homology-directed repair (HDR), which can affect telomere length.. | |
Protein Sequence | MAAGAGTAGPASGPGVVRDPAASQPRKRPGREGGEGARRSDTMAGGGGSSDGSGRAAGRRASRSSGRARRGRHEPGLGGPAERGAGEARLEEAVNRWVLKFYFHEALRAFRGSRYGDFRQIRDIMQALLVRPLGKEHTVSRLLRVMQCLSRIEEGENLDCSFDMEAELTPLESAINVLEMIKTEFTLTEAVVESSRKLVKEAAVIICIKNKEFEKASKILKKHMSKDPTTQKLRNDLLNIIREKNLAHPVIQNFSYETFQQKMLRFLESHLDDAEPYLLTMAKKALKSESAASSTGKEDKQPAPGPVEKPPREPARQLRNPPTTIGMMTLKAAFKTLSGAQDSEAAFAKLDQKDLVLPTQALPASPALKNKRPRKDENESSAPADGEGGSELQPKNKRMTISRLVLEEDSQSTEPSAGLNSSQEAASAPPSKPTVLNQPLPGEKNPKVPKGKWNSSNGVEEKETWVEEDELFQVQAAPDEDSTTNITKKQKWTVEESEWVKAGVQKYGEGNWAAISKNYPFVNRTAVMIKDRWRTMKRLGMN | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
12 | Phosphorylation | AGTAGPASGPGVVRD CCCCCCCCCCCCCCC | 28.86 | 22210691 | |
18 (in isoform 3) | Methylation | - | 35.68 | - | |
28 (in isoform 3) | Methylation | - | 45.58 | - | |
40 | Phosphorylation | GGEGARRSDTMAGGG CCCCCCCCCCCCCCC | 55.57 | 28985074 | |
42 | Phosphorylation | EGARRSDTMAGGGGS CCCCCCCCCCCCCCC | 29.46 | 28111955 | |
49 | Phosphorylation | TMAGGGGSSDGSGRA CCCCCCCCCCCCCHH | 38.05 | 28111955 | |
50 | Phosphorylation | MAGGGGSSDGSGRAA CCCCCCCCCCCCHHH | 63.61 | 28111955 | |
53 | Phosphorylation | GGGSSDGSGRAAGRR CCCCCCCCCHHHCCH | 38.86 | 28111955 | |
55 (in isoform 3) | Methylation | - | 8.45 | - | |
55 | Methylation | GSSDGSGRAAGRRAS CCCCCCCHHHCCHHH | 8.45 | 20676309 | |
59 (in isoform 3) | Asymmetric dimethylarginine | - | 7.43 | - | |
59 (in isoform 3) | Methylation | - | 7.43 | - | |
59 | Methylation | GSGRAAGRRASRSSG CCCHHHCCHHHCCCC | 7.43 | 19596784 | |
60 (in isoform 3) | Methylation | - | 11.48 | - | |
60 | Methylation | SGRAAGRRASRSSGR CCHHHCCHHHCCCCC | 11.48 | 19596784 | |
63 (in isoform 3) | Methylation | - | 39.23 | - | |
63 | Methylation | AAGRRASRSSGRARR HHCCHHHCCCCCCCC | 39.23 | 20676329 | |
67 (in isoform 3) | Methylation | - | 10.19 | - | |
67 | Methylation | RASRSSGRARRGRHE HHHCCCCCCCCCCCC | 10.19 | 20676305 | |
69 (in isoform 3) | Methylation | - | 40.99 | - | |
69 | Methylation | SRSSGRARRGRHEPG HCCCCCCCCCCCCCC | 40.99 | 20676325 | |
70 (in isoform 3) | Methylation | - | 15.26 | - | |
70 | Methylation | RSSGRARRGRHEPGL CCCCCCCCCCCCCCC | 15.26 | 20676317 | |
72 (in isoform 3) | Methylation | - | 42.13 | - | |
72 | Methylation | SGRARRGRHEPGLGG CCCCCCCCCCCCCCC | 42.13 | 20676321 | |
93 | Ubiquitination | GEARLEEAVNRWVLK CHHHHHHHHHHHHHH | 54.74 | - | |
135 (in isoform 3) | Ubiquitination | - | 3.81 | - | |
169 | Acetylation | FDMEAELTPLESAIN CCCEEEECCHHHHHH | 59.80 | - | |
169 | Phosphorylation | FDMEAELTPLESAIN CCCEEEECCHHHHHH | 59.80 | 29888752 | |
173 | Acetylation | AELTPLESAINVLEM EEECCHHHHHHHHHH | 64.38 | - | |
173 | Phosphorylation | AELTPLESAINVLEM EEECCHHHHHHHHHH | 64.38 | 29888752 | |
188 | Phosphorylation | IKTEFTLTEAVVESS HHCCCCHHHHHHHHH | 29.15 | 16223874 | |
188 (in isoform 3) | Phosphorylation | - | 29.15 | - | |
211 (in isoform 3) | Acetylation | - | 19.39 | - | |
211 | Acetylation | VIICIKNKEFEKASK EEEEECCHHHHHHHH | 19.39 | 20167786 | |
215 (in isoform 3) | Acetylation | - | 41.78 | - | |
215 | Acetylation | IKNKEFEKASKILKK ECCHHHHHHHHHHHH | 41.78 | 20167786 | |
225 | Phosphorylation | KILKKHMSKDPTTQK HHHHHHCCCCCCHHH | 5.51 | 29083192 | |
229 (in isoform 3) | Phosphorylation | - | 9.92 | - | |
229 | Phosphorylation | KHMSKDPTTQKLRND HHCCCCCCHHHHHHH | 9.92 | - | |
230 (in isoform 3) | Phosphorylation | - | 47.88 | - | |
230 | Phosphorylation | HMSKDPTTQKLRNDL HCCCCCCHHHHHHHH | 47.88 | 22817900 | |
232 | Ubiquitination | SKDPTTQKLRNDLLN CCCCCHHHHHHHHHH | 21.23 | 29967540 | |
241 | Ubiquitination | RNDLLNIIREKNLAH HHHHHHHHHHCCCCC | 27.97 | - | |
242 | Ubiquitination | NDLLNIIREKNLAHP HHHHHHHHHCCCCCH | 49.79 | - | |
253 | Ubiquitination | LAHPVIQNFSYETFQ CCCHHHCCCCHHHHH | 50.18 | 23000965 | |
257 | Ubiquitination | VIQNFSYETFQQKML HHCCCCHHHHHHHHH | 59.38 | 21890473 | |
280 | Phosphorylation | DAEPYLLTMAKKALK CHHHHHHHHHHHHHH | 45.80 | 24719451 | |
287 (in isoform 3) | Sumoylation | - | 19.06 | - | |
287 | Sumoylation | TMAKKALKSESAASS HHHHHHHHCCHHHHC | 19.06 | 28112733 | |
288 (in isoform 3) | Phosphorylation | - | 1.61 | - | |
288 | Phosphorylation | MAKKALKSESAASST HHHHHHHCCHHHHCC | 1.61 | - | |
290 (in isoform 3) | Phosphorylation | - | 22.65 | - | |
290 | Phosphorylation | KKALKSESAASSTGK HHHHHCCHHHHCCCC | 22.65 | - | |
293 | Ubiquitination | LKSESAASSTGKEDK HHCCHHHHCCCCCCC | 43.78 | 21890473 | |
294 | Phosphorylation | KSESAASSTGKEDKQ HCCHHHHCCCCCCCC | 21.50 | 28985074 | |
297 | Ubiquitination | SAASSTGKEDKQPAP HHHHCCCCCCCCCCC | 30.30 | 24816145 | |
312 (in isoform 3) | Dimethylation | - | 36.05 | - | |
312 | Methylation | GPVEKPPREPARQLR CCCCCCCCCHHHHHC | 36.05 | 24411731 | |
316 (in isoform 3) | Dimethylation | - | 18.25 | - | |
316 | Methylation | KPPREPARQLRNPPT CCCCCHHHHHCCCCC | 18.25 | 24411739 | |
323 | Phosphorylation | RQLRNPPTTIGMMTL HHHCCCCCCHHHHHH | 14.57 | 18669648 | |
323 (in isoform 3) | Phosphorylation | - | 14.57 | - | |
324 (in isoform 3) | Phosphorylation | - | 43.66 | - | |
324 | Phosphorylation | QLRNPPTTIGMMTLK HHCCCCCCHHHHHHH | 43.66 | 23403867 | |
329 | Phosphorylation | PTTIGMMTLKAAFKT CCCHHHHHHHHHHHH | 63.29 | 23403867 | |
331 | Ubiquitination | TIGMMTLKAAFKTLS CHHHHHHHHHHHHHC | 49.65 | 23000965 | |
334 | Ubiquitination | MMTLKAAFKTLSGAQ HHHHHHHHHHHCCCC | 66.29 | 23000965 | |
335 (in isoform 3) | Acetylation | - | 66.97 | - | |
335 (in isoform 3) | Ubiquitination | - | 66.97 | - | |
335 | Ubiquitination | MTLKAAFKTLSGAQD HHHHHHHHHHCCCCC | 66.97 | 21890473 | |
335 | Acetylation | MTLKAAFKTLSGAQD HHHHHHHHHHCCCCC | 66.97 | 25953088 | |
335 | Sumoylation | MTLKAAFKTLSGAQD HHHHHHHHHHCCCCC | 66.97 | 28112733 | |
338 (in isoform 3) | Phosphorylation | - | 43.30 | - | |
338 | Phosphorylation | KAAFKTLSGAQDSEA HHHHHHHCCCCCHHH | 43.30 | - | |
338 | Ubiquitination | KAAFKTLSGAQDSEA HHHHHHHCCCCCHHH | 43.30 | 21890473 | |
349 | Ubiquitination | DSEAAFAKLDQKDLV CHHHHHHHCCCCCCC | 55.49 | 32015554 | |
353 | Sumoylation | AFAKLDQKDLVLPTQ HHHHCCCCCCCCCCC | 63.24 | 28112733 | |
354 | Ubiquitination | FAKLDQKDLVLPTQA HHHCCCCCCCCCCCC | 43.80 | 22817900 | |
359 | Phosphorylation | QKDLVLPTQALPASP CCCCCCCCCCCCCCH | 1.32 | 23927012 | |
365 (in isoform 3) | Phosphorylation | - | 52.88 | 23822953 | |
365 | Phosphorylation | PTQALPASPALKNKR CCCCCCCCHHHCCCC | 52.88 | 29255136 | |
366 | Ubiquitination | TQALPASPALKNKRP CCCCCCCHHHCCCCC | 59.82 | 22817900 | |
368 | Phosphorylation | ALPASPALKNKRPRK CCCCCHHHCCCCCCC | 29.34 | 17525332 | |
369 | Ubiquitination | LPASPALKNKRPRKD CCCCHHHCCCCCCCC | 67.69 | 22817900 | |
369 | Sumoylation | LPASPALKNKRPRKD CCCCHHHCCCCCCCC | 67.69 | 28112733 | |
372 | Ubiquitination | SPALKNKRPRKDENE CHHHCCCCCCCCCCC | 42.37 | 23503661 | |
375 | Ubiquitination | LKNKRPRKDENESSA HCCCCCCCCCCCCCC | 36.89 | 24816145 | |
375 | Sumoylation | LKNKRPRKDENESSA HCCCCCCCCCCCCCC | 36.89 | 28112733 | |
378 | Ubiquitination | KRPRKDENESSAPAD CCCCCCCCCCCCCCC | 38.40 | 24816145 | |
379 | Phosphorylation | RPRKDENESSAPADG CCCCCCCCCCCCCCC | 38.14 | 18669648 | |
380 | Phosphorylation | PRKDENESSAPADGE CCCCCCCCCCCCCCC | 30.85 | 17525332 | |
380 (in isoform 3) | Phosphorylation | - | 30.85 | - | |
390 | Ubiquitination | PADGEGGSELQPKNK CCCCCCCCCCCCCCC | 50.94 | 21906983 | |
402 | Ubiquitination | KNKRMTISRLVLEED CCCCCEEEEEEEECC | 81.89 | 2190698 | |
410 (in isoform 3) | Phosphorylation | - | 49.69 | - | |
410 | Phosphorylation | RLVLEEDSQSTEPSA EEEEECCCCCCCCCC | 49.69 | 23401153 | |
412 | Phosphorylation | VLEEDSQSTEPSAGL EEECCCCCCCCCCCC | 38.76 | 30108239 | |
413 (in isoform 3) | Phosphorylation | - | 24.86 | - | |
413 | Phosphorylation | LEEDSQSTEPSAGLN EECCCCCCCCCCCCC | 24.86 | 30108239 | |
416 | Phosphorylation | DSQSTEPSAGLNSSQ CCCCCCCCCCCCCCH | 30.11 | 30108239 | |
421 | Phosphorylation | EPSAGLNSSQEAASA CCCCCCCCCHHHHHC | 51.70 | 30108239 | |
422 (in isoform 3) | Phosphorylation | - | 45.97 | - | |
422 | Phosphorylation | PSAGLNSSQEAASAP CCCCCCCCHHHHHCC | 45.97 | 17525332 | |
427 (in isoform 3) | Phosphorylation | - | 44.38 | 27251275 | |
427 | Phosphorylation | NSSQEAASAPPSKPT CCCHHHHHCCCCCCC | 44.38 | 20068231 | |
431 | Phosphorylation | EAASAPPSKPTVLNQ HHHHCCCCCCCCCCC | 38.75 | 29449344 | |
432 (in isoform 3) | Ubiquitination | - | 3.07 | - | |
432 | Ubiquitination | AASAPPSKPTVLNQP HHHCCCCCCCCCCCC | 3.07 | 22817900 | |
434 | Phosphorylation | SAPPSKPTVLNQPLP HCCCCCCCCCCCCCC | 23.31 | 28122231 | |
435 | Ubiquitination | APPSKPTVLNQPLPG CCCCCCCCCCCCCCC | 8.59 | 22817900 | |
444 (in isoform 3) | Ubiquitination | - | 5.85 | - | |
444 | Ubiquitination | NQPLPGEKNPKVPKG CCCCCCCCCCCCCCC | 5.85 | 22817900 | |
446 | Acetylation | PLPGEKNPKVPKGKW CCCCCCCCCCCCCCC | 49.78 | - | |
447 (in isoform 3) | Acetylation | - | 48.76 | - | |
447 | Ubiquitination | LPGEKNPKVPKGKWN CCCCCCCCCCCCCCC | 48.76 | 22817900 | |
447 | Acetylation | LPGEKNPKVPKGKWN CCCCCCCCCCCCCCC | 48.76 | - | |
449 | Acetylation | GEKNPKVPKGKWNSS CCCCCCCCCCCCCCC | 54.43 | - | |
450 | Ubiquitination | EKNPKVPKGKWNSSN CCCCCCCCCCCCCCC | 11.81 | 22817900 | |
452 | Acetylation | NPKVPKGKWNSSNGV CCCCCCCCCCCCCCC | 8.15 | 25953088 | |
452 | Sumoylation | NPKVPKGKWNSSNGV CCCCCCCCCCCCCCC | 8.15 | 28112733 | |
453 | Ubiquitination | PKVPKGKWNSSNGVE CCCCCCCCCCCCCCC | 48.72 | 23503661 | |
456 (in isoform 3) | Phosphorylation | - | 60.62 | - | |
456 | Phosphorylation | PKGKWNSSNGVEEKE CCCCCCCCCCCCCCC | 60.62 | 28985074 | |
488 (in isoform 3) | Acetylation | - | 24.12 | - | |
488 | Acetylation | DSTTNITKKQKWTVE CCCCCCCCCCCEEEC | 24.12 | 18197706 | |
489 (in isoform 3) | Acetylation | - | 44.44 | - | |
489 | Acetylation | STTNITKKQKWTVEE CCCCCCCCCCEEECH | 44.44 | 18197706 | |
491 | Acetylation | TNITKKQKWTVEESE CCCCCCCCEEECHHH | 15.38 | 18197706 | |
495 | Acetylation | KKQKWTVEESEWVKA CCCCEEECHHHHHHH | 43.81 | - | |
530 (in isoform 3) | Acetylation | - | - | ||
530 | Acetylation | NRTAVMIKDRWRTMK CCEEEEHHHHHHHHH | 18197706 | ||
537 | Acetylation | KDRWRTMKRLGMN-- HHHHHHHHHHCCC-- | 18197706 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
20 | S | Phosphorylation | Kinase | CHEK2 | O96017 | GPS |
230 | T | Phosphorylation | Kinase | ATM | Q13315 | Uniprot |
365 | S | Phosphorylation | Kinase | CDK2 | P24941 | PSP |
365 | S | Phosphorylation | Kinase | MAPK1 | P28482 | GPS |
- | K | Ubiquitination | E3 ubiquitin ligase | SIAH1 | Q8IUQ4 | PMID:21057505 |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TERF2_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 TERF2_HUMAN !! |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
There are no disease associations of PTM sites. | ||||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Acetylation | |
Reference | PubMed |
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-169, AND MASS SPECTROMETRY. | |
Phosphorylation | |
Reference | PubMed |
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323, AND MASSSPECTROMETRY. | |
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323, AND MASSSPECTROMETRY. | |
"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-323, AND MASSSPECTROMETRY. | |
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323, AND MASSSPECTROMETRY. | |
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323, AND MASSSPECTROMETRY. | |
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-368 AND SER-380, ANDMASS SPECTROMETRY. | |
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323, AND MASSSPECTROMETRY. | |
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323, AND MASSSPECTROMETRY. | |
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323, AND MASSSPECTROMETRY. |