TERF1
entrez
7013
canonical
uniprot
P54274
canonical
ensembl
ENSG00000147601
resolver
ensp
ENSP00000276602
resolver
ensp
ENSP00000276603
resolver
ensp
ENSP00000503453
resolver
ensp
ENSP00000504760
resolver
ensp
ENSP00000569384
resolver
ensp
ENSP00000582818
resolver
ensp
ENSP00000732982
resolver
ensp
ENSP00000732995
resolver
enst
ENST00000678860
resolver
enst
ENST00000679115
resolver
genesymbol
TERF1
resolver
genesymbol_syn
PIN2
resolver
genesymbol_syn
TRBF1
resolver
genesymbol_syn
TRF
resolver
genesymbol_syn
TRF1
resolver
hgnc
HGNC:11728
resolver
uniprot
A0A7I2V5T5
resolver
uniprot
A0A7I2YQE7
resolver
uniprot
A7XP29
resolver
uniprot
Q15553
resolver
uniprot
Q8NHT6
resolver
uniprot
Q93029
resolver
uniprot_entry
A0A7I2V5T5_HUMAN
resolver
uniprot_entry
A0A7I2YQE7_HUMAN
resolver
uniprot_entry
TERF1_HUMAN
resolver
uniprot_sec
A7XP29
resolver
uniprot_sec
Q15553
resolver
uniprot_sec
Q8NHT6
resolver
uniprot_sec
Q93029
resolver
amino_acid_sequence
MAEDVSSAAPSPRGCADGRDADPTEEQMAETERNDEEQFECQELLECQVQVGAPEEEEEEEEDAGLVAEAEAVAAGWMLDFLCLSLCRAFRDGRSEDFRRTRNSAEAIIHGLSSLTACQLRTIYICQFLTRIAAGKTLDAQFENDERITPLESALMIWGSIEKEHDKLHEEIQNLIKIQAIAVCMENGNFKEAEEVFERIFGDPNSHMPFKSKLLMIISQKDTFHSFFQHFSYNHMMEKIKSYVNYVLSEKSSTFLMKAAAKVVESKRTRTITSQDKPSGNDVEMETEANLDTRKSVSDKQSAVTESSEGTVSLLRSHKNLFLSKLQHGTQQQDLNKKERRVGTPQSTKKKKESRRATESRIPVSKSQPVTPEKHRARKRQAWLWEEDKNLRSGVRKYGEGNWSKILLHYKFNNRTSVMLKDRWRTMKKLKLISSDSED
uniprot
proteins
function
FUNCTION: Binds the telomeric double-stranded 5'-TTAGGG-3' repeat and negatively regulates telomere length (PubMed:31595153). 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. {ECO:0000269|PubMed:16166375, ECO:0000269|PubMed:31595153}.
uniprot
proteins
mass_dalton
50246
uniprot
proteins
mutagenesis
MUTAGEN 74; /note="A->D: Abolishes dimerization and telomere binding; when associated with P-75."; /evidence="ECO:0000269|PubMed:11545737"; MUTAGEN 75; /note="A->P: Abolishes dimerization and telomere binding; when associated with D-74."; /evidence="ECO:0000269|PubMed:11545737"; MUTAGEN 77; /note="W->P: Abolishes telomere binding."; /evidence="ECO:0000269|PubMed:11545737"; MUTAGEN 81; /note="F->P: Abolishes telomere binding."; /evidence="ECO:0000269|PubMed:11545737"; MUTAGEN 90; /note="F->P: Diminishes telomere binding."; /evidence="ECO:0000269|PubMed:11545737"; MUTAGEN 115; /note="L->R: Loss of interaction with FBXO4."; /evidence="ECO:0000269|PubMed:20159592"; MUTAGEN 120; /note="L->R: Loss of interaction with FBXO4."; /evidence="ECO:0000269|PubMed:20159592"; MUTAGEN 219; /note="S->A: Loss of phosphorylation; induction of mitotic entry and apoptosis and increased radiation hypersensitivity of ataxia-telangiectasia cells."; /evidence="ECO:0000269|PubMed:11375976"; MUTAGEN 219; /note="S->D,E: Fails to induce apoptosis and decreases radiation hypersensitivity of ataxia-telangiectasia cells (phospho-mimicking mutants)."; /evidence="ECO:0000269|PubMed:11375976
uniprot
proteins
post_translational_modification
PTM: Phosphorylated preferentially on Ser-219 in an ATM-dependent manner in response to ionizing DNA damage. {ECO:0000269|PubMed:11375976}.; PTM: ADP-ribosylation by TNKS1 or TNKS2 diminishes its ability to bind to telomeric DNA.; PTM: Ubiquitinated by RLIM/RNF12, leading to its degradation by the proteasome. Ubiquitinated by a SCF (SKP1-CUL1-F-box protein) ubiquitin-protein ligase complex, leading to its degradation by the proteasome. {ECO:0000269|PubMed:19164295, ECO:0000269|PubMed:20159592}.
uniprot
proteins
pubmed
11375976
uniprot
proteins
pubmed
11545737
uniprot
proteins
pubmed
11738049
uniprot
proteins
pubmed
11739745
uniprot
proteins
pubmed
11943150
uniprot
proteins
pubmed
12768206
uniprot
proteins
pubmed
15316005
uniprot
proteins
pubmed
15383534
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15608617
uniprot
proteins
pubmed
16166375
uniprot
proteins
pubmed
16421571
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
18202258
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19164295
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19487455
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20159592
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23959892
uniprot
proteins
pubmed
24692559
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
31595153
uniprot
proteins
pubmed
7502076
uniprot
proteins
pubmed
8614633
uniprot
proteins
pubmed
9326950
uniprot
proteins
pubmed
9391075
uniprot
proteins
pubmed
9739097
uniprot
proteins
sequence_length
439
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24692559}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:11943150}. Chromosome, telomere {ECO:0000269|PubMed:24692559}. Note=Colocalizes with telomeric DNA in interphase and prophase cells. Telomeric localization decreases in metaphase, anaphase and telophase. Associates with the mitotic spindle (PubMed:11943150). Colocalizes with TRIOBP isoform 1 at the telomeres in interphase (PubMed:24692559). {ECO:0000269|PubMed:11943150, ECO:0000269|PubMed:24692559}.
uniprot
proteins