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Protein Page:
TRF2 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
TRF2 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. Homodimer. Component of the shelterin complex (telosome) composed of TERF1, TERF2, TINF2, TERF2IP/RAP1, ACD and POT1. Interacts with TERF2IP. Interacts with NBN. Interacts with SLX4/BTBD12. Interacts with DCLRE1B/Apollo and TERF2IP/RAP1; the interaction is direct. Ubiquitous. Highly expressed in spleen, thymus, prostate, uterus, testis, small intestine, colon and peripheral blood leukocytes. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: DNA repair, damage; DNA binding protein
Cellular Component: male germ cell nucleus; nucleoplasm; Golgi apparatus; chromosome, telomeric region; nuclear telomere cap complex; Mre11 complex; cytoplasm; nucleolus; nucleus
Molecular Function: protein C-terminus binding; protein binding; protein homodimerization activity; telomeric DNA binding; double-stranded telomeric DNA binding; chromatin binding
Biological Process: negative regulation of telomere maintenance; telomere capping; in utero embryonic development; negative regulation of telomere maintenance via semi-conservative replication; telomeric loop formation; positive regulation of telomere maintenance; telomere maintenance via telomerase; age-dependent telomere shortening; cell cycle; telomere maintenance; protection from non-homologous end joining at telomere
Reference #:  Q15554 (UniProtKB)
Alt. Names/Synonyms: Telomeric DNA-binding protein; telomeric repeat binding factor 2; telomeric repeat binding protein 2; Telomeric repeat-binding factor 2; TERF2; TRBF2; TRF2; TTAGGG repeat-binding factor 2
Gene Symbols: TERF2
Molecular weight: 59,594 Da
Basal Isoelectric point: 9.38  Predict pI for various phosphorylation states
CST Pathways:  G2/M DNA Damage Checkpoint
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

TRF2

Protein Structure Not Found.


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Sites Implicated In
intracellular localization: T230‑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


 SS 

SS: 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.


 MS 

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


       human

 
0 1 G30 SQPRKRPGREGGEGA
1 0 R55-me GSSDGSGrAAGrrAS
1 0 R59-me GSGrAAGrrASrSSG
1 0 R60-me SGrAAGrrASrSSGr
1 0 R63-me AAGrrASrSSGrArr
1 0 R67-me rASrSSGrArrGrHE
1 0 R69-me SrSSGrArrGrHEPG
1 0 R70-me rSSGrArrGrHEPGL
1 0 R72-me SGrArrGrHEPGLGG
0 12 K211-ac VIICIKNkEFEkASK
0 11 K215-ac IKNkEFEkASKILKK
0 3 T229-p KHMSKDPttQKLRND
2 0 T230-p HMSKDPttQKLRNDL
0 1 S288-p MAKKALKsEsAASST
0 1 S290-p KKALKsEsAASSTGK
0 1 R312-m2 GPVEKPPrEPArQLR
0 1 R316-m2 KPPrEPArQLRNPPt
0 1 T323-p rQLRNPPttIGMMTL
0 1 T324-p QLRNPPttIGMMTLK
1 0 K335-ac MTLKAAFkTLsGAQD
0 1 K335-ub MTLKAAFkTLsGAQD
0 1 S338-p KAAFkTLsGAQDSEA
0 4 L362 LVLPTQALPAsPALK
0 4 A364 LPTQALPAsPALKNK
1 115 S365-p PTQALPAsPALKNKR
0 1 A367 QALPAsPALKNKRPR
0 8 K397 SELQPKNKRMTISRL
0 1 S402 KNKRMTISRLVLEED
0 4 S410-p RLVLEEDsQStEPSA
0 1 S412 VLEEDsQStEPSAGL
0 3 T413-p LEEDsQStEPSAGLN
0 2 S416 DsQStEPSAGLNSsQ
0 1 S421 EPSAGLNSsQEAAsA
0 3 S422-p PSAGLNSsQEAAsAP
0 3 S427-p NSsQEAAsAPPSkPT
0 1 P429 sQEAAsAPPSkPTVL
0 1 K432-ub AAsAPPSkPTVLNQP
0 1 K444-ub NQPLPGEkNPKVPKG
0 1 V466 VEEKETWVEEDELFQ
0 1 N485 PDEDSTTNITKkQKW
1 0 K489-ac STTNITKkQKWTVEE
1 0 K530-ac NRTAVMIkDRWRTMK
  mouse

 
S30-p SQPRKRPsREGGEGG
R58 GSSDSSGRAASRRAS
R62 SSGRAASRRASRSGG
R63 SGRAASRRASRSGGR
R66 AASRRASRSGGRARR
R70 RASRSGGRARRGRHE
R72 SRSGGRARRGRHEPG
R73 RSGGRARRGRHEPGL
R75 GGRARRGRHEPGLGG
K214-ac VIICIKNkEFEkASK
K218-ac IKNkEFEkASKILKK
T232 KYMSKDPTTQKLRTD
T233 YMSKDPTTQKLRTDL
S291 MAKKALKSESAASST
S293 KKALKSESAASSTMR
R313 EPVEKPLREPPSRQP
R318 PLREPPSRQPQNPPA
A325 RQPQNPPATIGIRTL
T326 QPQNPPATIGIRTLK
K337 RTLKAAFKALSTAQD
K337 RTLKAAFKALSTAQD
S340 KAAFKALSTAQDSEA
S364-p LVLANLAsPssPAHK
S366-p LANLAsPssPAHKHK
S367-p ANLAsPssPAHKHKR
A369 LAsPssPAHKHKRPR
S399-p SDRQPRNsPMTIsRL
S404-p RNsPMTIsRLLLEED
S412-p RLLLEEDsQstEPsP
S414-p LLEEDsQstEPsPGL
T415-p LEEDsQstEPsPGLN
S418-p DsQstEPsPGLNssH
S423-p EPsPGLNssHKAMsA
S424-p PsPGLNssHKAMsAS
S429-p NssHKAMsASKPRAL
S431 sHKAMsASKPRALNQ
K432 HKAMsASKPRALNQP
K444 NQPHPGEKKPKASKD
L466 LEEKEVWLEEDQLFE
S484-p PGEDRSSsLTRKQKW
K488 RSSsLTRKQKWTIEE
K529 NRTAVMIKDRWRTMK
  rat

 
- gap
R13 GSSDNGGRAANRRAS
R17 NGGRAANRRASRSGG
R18 GGRAANRRASRSGGR
R21 AANRRASRSGGRARR
R25 RASRSGGRARRGRHE
R27 SRSGGRARRGRHEPG
R28 RSGGRARRGRHEPGL
R30 GGRARRGRHEPGLGG
K169 VIICIKNKEFEKASK
K173 IKNKEFEKASKILKK
T187 KYMSKDPTTQKVRTD
T188 YMSKDPTTQKVRTDL
S246 MAKKALRSESAASST
S248 KKALRSESAASSTMK
R268 EPVEKPLREPPRQPR
R272 KPLREPPRQPRNPPT
T279 RQPRNPPTTIGLRTV
T280 QPRNPPTTIGLRTVK
K291 RTVKAAFKALSTAQD
K291 RTVKAAFKALSTAQD
S294 KAAFKALSTAQDSEA
S318 LVLPNLASPSSPtHK
S320 LPNLASPSSPtHKNK
S321 PNLASPSSPtHKNKR
T323-p LASPSSPtHKNKRPR
N353 SERQPRNNRMTISRL
S358 RNNRMTISRLVLEED
S366 RLVLEEDSQSSEPSP
S368 VLEEDSQSSEPSPDL
S369 LEEDSQSSEPSPDLN
S372 DSQSSEPSPDLNSSR
S377 EPSPDLNSSRQALSA
S378 PSPDLNSSRQALSAs
S383 NSSRQALSAsPSKPR
S385-p SRQALSAsPSKPRAL
K388 ALSAsPSKPRALNQP
K400 NQPHTGEKNPKASKD
S422-p LEEKEVWsEEDQLFE
N440 PGEDKSSNLARKQKW
K444 KSSNLARKQKWTIEE
K485 NRTAVMIKDRWRTMK
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