UniProt ID | TERF1_HUMAN | |
---|---|---|
UniProt AC | P54274 | |
Protein Name | Telomeric repeat-binding factor 1 | |
Gene Name | TERF1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 439 | |
Subcellular Localization | Nucleus. Cytoplasm, cytoskeleton, spindle. Chromosome, telomere. Colocalizes with telomeric DNA in interphase and prophase cells. Telomeric localization decreases in metaphase, anaphase and telophase. Associates with the mitotic spindle. | |
Protein Description | Binds the telomeric double-stranded 5'-TTAGGG-3' repeat and negatively regulates telomere length. Involved in the regulation of the mitotic spindle. 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.. | |
Protein Sequence | MAEDVSSAAPSPRGCADGRDADPTEEQMAETERNDEEQFECQELLECQVQVGAPEEEEEEEEDAGLVAEAEAVAAGWMLDFLCLSLCRAFRDGRSEDFRRTRNSAEAIIHGLSSLTACQLRTIYICQFLTRIAAGKTLDAQFENDERITPLESALMIWGSIEKEHDKLHEEIQNLIKIQAIAVCMENGNFKEAEEVFERIFGDPNSHMPFKSKLLMIISQKDTFHSFFQHFSYNHMMEKIKSYVNYVLSEKSSTFLMKAAAKVVESKRTRTITSQDKPSGNDVEMETEANLDTRKSVSDKQSAVTESSEGTVSLLRSHKNLFLSKLQHGTQQQDLNKKERRVGTPQSTKKKKESRRATESRIPVSKSQPVTPEKHRARKRQAWLWEEDKNLRSGVRKYGEGNWSKILLHYKFNNRTSVMLKDRWRTMKKLKLISSDSED | |
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 |
---|---|---|---|---|---|
2 | Acetylation | ------MAEDVSSAA ------CCCCHHHCC | 23.00 | 20068231 | |
6 | Phosphorylation | --MAEDVSSAAPSPR --CCCCHHHCCCCCC | 26.95 | 29255136 | |
7 | Phosphorylation | -MAEDVSSAAPSPRG -CCCCHHHCCCCCCC | 28.44 | 29255136 | |
11 | Phosphorylation | DVSSAAPSPRGCADG CHHHCCCCCCCCCCC | 23.62 | 29255136 | |
24 | Phosphorylation | DGRDADPTEEQMAET CCCCCCCCHHHHHHH | 53.34 | 22210691 | |
32 | Ubiquitination | EEQMAETERNDEEQF HHHHHHHHCCHHHHH | 40.78 | 22817900 | |
114 | Phosphorylation | AIIHGLSSLTACQLR HHHHHHHHCHHHHHH | 34.48 | 22210691 | |
122 | Phosphorylation | LTACQLRTIYICQFL CHHHHHHHHHHHHHH | 27.07 | 22817900 | |
136 | Ubiquitination | LTRIAAGKTLDAQFE HHHHHCCCCHHHHCC | 40.98 | 21906983 | |
136 (in isoform 2) | Ubiquitination | - | 40.98 | 21890473 | |
136 (in isoform 1) | Ubiquitination | - | 40.98 | 21890473 | |
149 | Phosphorylation | FENDERITPLESALM CCCCCCCCHHHHHHH | 28.21 | - | |
153 | Phosphorylation | ERITPLESALMIWGS CCCCHHHHHHHHHHC | 34.09 | 20860994 | |
160 | Phosphorylation | SALMIWGSIEKEHDK HHHHHHHCHHHHHHH | 16.75 | 20860994 | |
167 | Ubiquitination | SIEKEHDKLHEEIQN CHHHHHHHHHHHHHH | 54.36 | 29967540 | |
213 | Sumoylation | SHMPFKSKLLMIISQ CCCCCCHHEEEHHCC | 46.35 | 28112733 | |
219 | Phosphorylation | SKLLMIISQKDTFHS HHEEEHHCCHHHHHH | 21.91 | 28112733 | |
225 | Ubiquitination | ISQKDTFHSFFQHFS HCCHHHHHHHHHHCC | 26.28 | 24816145 | |
241 | Acetylation | NHMMEKIKSYVNYVL HHHHHHHHHHHHHHH | 46.96 | 164497481 | |
242 | Phosphorylation | HMMEKIKSYVNYVLS HHHHHHHHHHHHHHC | 37.47 | 20068231 | |
243 | Phosphorylation | MMEKIKSYVNYVLSE HHHHHHHHHHHHHCC | 6.42 | 20068231 | |
249 | Phosphorylation | SYVNYVLSEKSSTFL HHHHHHHCCCCHHHH | 32.69 | 20068231 | |
252 | Phosphorylation | NYVLSEKSSTFLMKA HHHHCCCCHHHHHHH | 30.47 | - | |
253 | Phosphorylation | YVLSEKSSTFLMKAA HHHCCCCHHHHHHHH | 33.96 | - | |
254 | Phosphorylation | VLSEKSSTFLMKAAA HHCCCCHHHHHHHHH | 28.07 | - | |
266 | Phosphorylation | AAAKVVESKRTRTIT HHHHHHHCCCCEEEC | 18.81 | - | |
271 | Phosphorylation | VESKRTRTITSQDKP HHCCCCEEECCCCCC | 28.17 | - | |
273 | Phosphorylation | SKRTRTITSQDKPSG CCCCEEECCCCCCCC | 21.52 | 22817900 | |
287 | Ubiquitination | GNDVEMETEANLDTR CCCCCCCEEECCCCC | 38.80 | 21890473 | |
295 | Acetylation | EANLDTRKSVSDKQS EECCCCCCCCCHHHH | 58.25 | 18526043 | |
296 | Phosphorylation | ANLDTRKSVSDKQSA ECCCCCCCCCHHHHC | 24.46 | - | |
299 | Ubiquitination | DTRKSVSDKQSAVTE CCCCCCCHHHHCEEC | 51.35 | 29967540 | |
300 | Ubiquitination | TRKSVSDKQSAVTES CCCCCCHHHHCEECC | 38.35 | 29967540 | |
300 | Acetylation | TRKSVSDKQSAVTES CCCCCCHHHHCEECC | 38.35 | 18526049 | |
305 | Phosphorylation | SDKQSAVTESSEGTV CHHHHCEECCCHHHH | 29.84 | 20860994 | |
305 | Ubiquitination | SDKQSAVTESSEGTV CHHHHCEECCCHHHH | 29.84 | 29967540 | |
308 | Phosphorylation | QSAVTESSEGTVSLL HHCEECCCHHHHHHH | 33.54 | - | |
311 | Phosphorylation | VTESSEGTVSLLRSH EECCCHHHHHHHHHC | 11.67 | - | |
319 | Ubiquitination | VSLLRSHKNLFLSKL HHHHHHCCHHHHHHH | 57.50 | 29967540 | |
325 | Ubiquitination | HKNLFLSKLQHGTQQ CCHHHHHHHCCCCHH | 55.07 | 29967540 | |
325 | Sumoylation | HKNLFLSKLQHGTQQ CCHHHHHHHCCCCHH | 55.07 | 28112733 | |
329 | Ubiquitination | FLSKLQHGTQQQDLN HHHHHCCCCHHHHCC | 16.56 | 24816145 | |
330 | Phosphorylation | LSKLQHGTQQQDLNK HHHHCCCCHHHHCCH | 22.53 | 23312004 | |
337 | Ubiquitination | TQQQDLNKKERRVGT CHHHHCCHHHHCCCC | 64.41 | 21890473 | |
338 | Ubiquitination | QQQDLNKKERRVGTP HHHHCCHHHHCCCCC | 56.21 | - | |
344 | Phosphorylation | KKERRVGTPQSTKKK HHHHCCCCCHHHHHH | 18.46 | 18625707 | |
346 | Ubiquitination | ERRVGTPQSTKKKKE HHCCCCCHHHHHHHH | 64.67 | 33845483 | |
347 | Phosphorylation | RRVGTPQSTKKKKES HCCCCCHHHHHHHHH | 43.32 | - | |
349 | Ubiquitination | VGTPQSTKKKKESRR CCCCHHHHHHHHHHH | 68.77 | 24816145 | |
358 | Phosphorylation | KKESRRATESRIPVS HHHHHHCCCCCCCCC | 32.45 | 28555341 | |
365 | Phosphorylation | TESRIPVSKSQPVTP CCCCCCCCCCCCCCH | 22.64 | 21712546 | |
366 | Sumoylation | ESRIPVSKSQPVTPE CCCCCCCCCCCCCHH | 54.03 | 28112733 | |
366 | Ubiquitination | ESRIPVSKSQPVTPE CCCCCCCCCCCCCHH | 54.03 | 33845483 | |
367 | Phosphorylation | SRIPVSKSQPVTPEK CCCCCCCCCCCCHHH | 32.01 | 30266825 | |
371 | Phosphorylation | VSKSQPVTPEKHRAR CCCCCCCCHHHHHHH | 32.20 | 30266825 | |
377 | Ubiquitination | VTPEKHRARKRQAWL CCHHHHHHHHHHHHH | 22.52 | 29967540 | |
391 | Ubiquitination | LWEEDKNLRSGVRKY HHHHCCCHHHHCHHH | 5.93 | 21890473 | |
391 (in isoform 2) | Ubiquitination | - | 5.93 | 21890473 | |
397 | Ubiquitination | NLRSGVRKYGEGNWS CHHHHCHHHCCCCCE | 56.02 | 29967540 | |
398 | Phosphorylation | LRSGVRKYGEGNWSK HHHHCHHHCCCCCEE | 15.17 | 30177828 | |
404 | Phosphorylation | KYGEGNWSKILLHYK HHCCCCCEEEEEEEE | 17.51 | 30177828 | |
410 | Phosphorylation | WSKILLHYKFNNRTS CEEEEEEEEECCCCC | 19.76 | 27174698 | |
411 | Ubiquitination | SKILLHYKFNNRTSV EEEEEEEEECCCCCE | 30.76 | 22817900 | |
411 (in isoform 1) | Ubiquitination | - | 30.76 | 21890473 | |
415 | Phosphorylation | LHYKFNNRTSVMLKD EEEEECCCCCEEEHH | 29.49 | 33259812 | |
416 | Phosphorylation | HYKFNNRTSVMLKDR EEEECCCCCEEEHHH | 28.00 | 27174698 | |
417 | Phosphorylation | YKFNNRTSVMLKDRW EEECCCCCEEEHHHH | 11.42 | 18669648 | |
421 | Ubiquitination | NRTSVMLKDRWRTMK CCCCEEEHHHHHHHH | 27.44 | 21890473 | |
434 | Phosphorylation | MKKLKLISSDSED-- HHHHHCCCCCCCC-- | 38.23 | 28450419 | |
435 | Phosphorylation | KKLKLISSDSED--- HHHHCCCCCCCC--- | 37.86 | 18625707 | |
437 | Phosphorylation | LKLISSDSED----- HHCCCCCCCC----- | 45.68 | 28450419 | |
441 | Ubiquitination | SSDSED--------- CCCCCC--------- | 21890473 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
114 | S | Phosphorylation | Kinase | NEK2 | P51955 | PSP |
114 | S | Phosphorylation | Kinase | NEK7 | Q8TDX7 | PSP |
122 | T | Phosphorylation | Kinase | CSNK2A1 | P68400 | GPS |
122 | T | Phosphorylation | Kinase | CK2-FAMILY | - | GPS |
122 | T | Phosphorylation | Kinase | CSNK2B | - | GPS |
219 | S | Phosphorylation | Kinase | ATM | Q13315 | Uniprot |
273 | T | Phosphorylation | Kinase | AKT1 | P31749 | PSP |
344 | T | Phosphorylation | Kinase | CDK1 | P06493 | PSP |
367 | S | Phosphorylation | Kinase | ATM | Q13315 | PSP |
371 | T | Phosphorylation | Kinase | CDK1 | P06493 | PSP |
435 | S | Phosphorylation | Kinase | PLK1 | P53350 | PSP |
- | K | Ubiquitination | E3 ubiquitin ligase | FBXO4 | Q9UKT5 | PMID:20181953 |
- | K | Ubiquitination | E3 ubiquitin ligase | BTRC | Q9Y297 | PMID:24658274 |
- | K | Ubiquitination | E3 ubiquitin ligase | RLIM | Q9NVW2 | PMID:31801865 |
Modified Location | Modified Residue | Modification | Function | Reference |
---|---|---|---|---|
219 | S | Phosphorylation |
| 11375976 |
* 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 TERF1_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 |
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-11, AND MASS SPECTROMETRY. | |
Phosphorylation | |
Reference | PubMed |
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-11, AND MASS SPECTROMETRY. | |
"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-434; SER-435 ANDSER-437, AND MASS SPECTROMETRY. | |
"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-11, AND MASSSPECTROMETRY. | |
"Telomeric protein Pin2/TRF1 as an important ATM target in response todouble strand DNA breaks."; Kishi S., Zhou X.Z., Ziv Y., Khoo C., Hill D.E., Shiloh Y., Lu K.P.; J. Biol. Chem. 276:29282-29291(2001). Cited for: MUTAGENESIS OF SER-219, PHOSPHORYLATION AT SER-219, AND INTERACTIONWITH ATM. |