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Protein Page:
TRF1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
TRF1 a telomeric repeat binding factor. Binds the telomeric double-stranded TTAGGG repeat and negatively regulates telomere length. Colocalizes with telomeric DNA in interphase and metaphase cells and is located at chromosome ends during metaphase. Involved in the regulation of the mitotic spindle. Expression is tightly regulated during the cell cycle; levels are low in G1 and S phase and increase during G2 phase and mitosis. Two splice variant isoforms have been described. Note: This description may include information from UniProtKB.
Protein type: DNA-binding
Chromosomal Location of Human Ortholog: 8q21.11
Cellular Component: nuclear chromosome, telomeric region; nuclear telomere cap complex; nucleolus; nucleoplasm; nucleus
Molecular Function: DNA bending activity; double-stranded telomeric DNA binding; protein binding; protein homodimerization activity; telomerase activity; telomeric DNA binding; ubiquitin binding
Biological Process: negative regulation of DNA replication; negative regulation of telomerase activity; negative regulation of telomere maintenance via telomerase; telomere capping; telomere maintenance; telomere maintenance via telomerase; telomeric loop formation
Reference #:  P54274 (UniProtKB)
Alt. Names/Synonyms: FLJ41416; hTRF1-AS; NIMA-interacting protein 2; PIN2; t-TRF1; Telomeric protein Pin2/TRF1; telomeric repeat binding factor (NIMA-interacting) 1; telomeric repeat binding factor 1; telomeric repeat binding protein 1; Telomeric repeat-binding factor 1; TERF1; TRBF1; TRF; TRF1; TTAGGG repeat-binding factor 1
Gene Symbols: TERF1
Molecular weight: 50,246 Da
Basal Isoelectric point: 5.99  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

TRF1

Protein Structure Not Found.
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Sites Implicated In
apoptosis, induced: S435‑p
apoptosis, inhibited: S219‑p
intracellular localization: T122‑p, S367‑p, T371‑p
molecular association, regulation: T122‑p
phosphorylation: T344‑p, T371‑p
protein stabilization: T122‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment



 LTP 

LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 2 S7‑p _MAEDVSsAAPsPRG
0 10 S11‑p DVSsAAPsPRGCADG
0 1 T24 DGRDADPTEEQMAET
2 0 T122‑p LTACQLRtIYICQFL
0 2 K136‑ub LTRIAAGkTLDAQFE
0 1 T149‑p FENDERItPLESALM
0 1 S160‑p SALMIWGsIEKEHDK
1 0 S219‑p SKLLMIIsQKDTFHS
0 1 S252‑p NYVLSEKsstFLMKA
0 1 S253‑p YVLSEKsstFLMKAA
0 1 T254‑p VLSEKsstFLMKAAA
1 0 T273‑p SKRTRTItSQDKPSG
0 1 S274 KRTRTItSQDKPSGN
0 1 N281 SQDKPSGNDVEMETE
0 1 V283 DKPSGNDVEMETEAN
0 1 K295‑ac EANLDTRksVSDkQS
0 2 S296‑p ANLDTRksVSDkQSA
0 1 K300‑ac TRksVSDkQSAVTES
0 1 S308‑p QSAVTESsEGtVSLL
0 1 T311‑p VTESsEGtVSLLRSH
0 1 S324 SHKNLFLSKLQHGTQ
1 0 T344‑p KKERRVGtPQsTKKK
0 2 S347‑p RRVGtPQsTKKKKES
0 1 T358‑p KKESRRAtESRIPVS
2 0 S367‑p SRIPVSKsQPVtPEK
4 6 T371‑p VSKsQPVtPEKHRAR
0 1 K411‑ub SKILLHYkFNNRTSV
0 3 S434‑p MKKLKLIssDsED__
1 4 S435‑p KKLKLIssDsED___
0 4 S437‑p LKLIssDsED_____
  mouse

 
S7 _MAETVSSAARDAPS
D11 TVSSAARDAPSREGW
S23 EGWTDSDSPEQEEVG
T109 LTAYQLKTVYICQFL
K123 LTRVASGKALDAQFE
T136 FEVDERITPLESALM
S147 SALMIWNSIEKEHDK
S206 RKLLKIISQKDVFHS
S239 GDVLSEKSSTFLMKA
S240 DVLSEKSSTFLMKAA
T241 VLSEKSSTFLMKAAT
A260 NEKARTQAsKDRPDA
S261‑p EKARTQAsKDRPDAt
T268‑p sKDRPDAtNtGMDTE
T270‑p DRPDAtNtGMDTEVG
K282 EVGLNKEKSVNGQQS
S283 VGLNKEKSVNGQQST
Q287 KEKSVNGQQSTETEP
L295 QSTETEPLVDTVSSI
T298 ETEPLVDTVSSIRSH
S310 RSHKNALSQLKHRRA
T330 RNEARTGTLQCETTM
C333 ARTGTLQCETTMERN
S344 MERNRRTSGRNRLCV
N354 NRLCVSENQPDTDDK
T358 VSENQPDTDDKSGRR
K398 AKILSHYKFNNRTSV
S421 MKRLKLIS_______
- gap
- gap
  rat

 
S7 _MAGTVTSAAPGARS
G11 TVTSAAPGARSNAGG
S23‑p AGGTSADsPEKEAAR
T109 LTAYQLKTVYICQFL
K123 LTRVAAGKSLDAQFE
T136 FEVDERITPLESALM
S147 SALMIWDSIEKEHDK
S206 RKLLKIISQKDVFHV
S239 ECVLNEKSSTFLMKA
S240 CVLNEKSSTFLMKAA
T241 VLNEKSSTFLMKAAT
A260 NEKARTVASEDKAKA
S261 EKARTVASEDKAKAT
T268 SEDKAKATNTGTETE
T270 DKAKATNTGTETEVN
E282 EVNSNKGESVNGQQS
S283 VNSNKGESVNGQQSV
Q287 KGESVNGQQSVETES
L295 QSVETESLVDTGSSV
T298 ETESLVDTGSSVRSH
S310‑p RSHKNALsPLKSRRL
T330 RNEARTGTLQCEIAT
C333 ARTGTLQCEIATKRN
S344 TKRNRRTSGGNRLRI
N354 NRLRISKNQPDTNEK
T358 ISKNQPDTNEKHGRR
K398 AKILSHYKFNNRTSV
S421 MRRLRLIS_______
- gap
- gap
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