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Protein

Telomeric repeat-binding factor 2

Gene

TERF2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi512 – 53726H-T-H motifPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • chromatin binding Source: InterPro
  • double-stranded telomeric DNA binding Source: BHF-UCL
  • protein C-terminus binding Source: UniProtKB
  • protein homodimerization activity Source: BHF-UCL
  • telomeric DNA binding Source: UniProtKB

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • cellular senescence Source: BHF-UCL
  • in utero embryonic development Source: Ensembl
  • negative regulation of beta-galactosidase activity Source: BHF-UCL
  • negative regulation of cellular senescence Source: BHF-UCL
  • negative regulation of gene expression Source: BHF-UCL
  • negative regulation of telomere maintenance Source: UniProtKB
  • negative regulation of telomere maintenance via semi-conservative replication Source: BHF-UCL
  • negative regulation of telomere single strand break repair Source: BHF-UCL
  • positive regulation of gene expression Source: BHF-UCL
  • positive regulation of nitric-oxide synthase activity Source: BHF-UCL
  • positive regulation of telomere maintenance Source: Ensembl
  • protection from non-homologous end joining at telomere Source: BHF-UCL
  • protein localization to chromosome, telomeric region Source: BHF-UCL
  • regulation of telomere maintenance Source: CACAO
  • telomere capping Source: BHF-UCL
  • telomere maintenance Source: UniProtKB
  • telomere maintenance via telomerase Source: BHF-UCL
  • telomeric loop formation Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

Cell cycle

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_169185. DNA Damage/Telomere Stress Induced Senescence.
REACT_75792. Meiotic synapsis.
REACT_7963. Packaging Of Telomere Ends.

Names & Taxonomyi

Protein namesi
Recommended name:
Telomeric repeat-binding factor 2
Alternative name(s):
TTAGGG repeat-binding factor 2
Telomeric DNA-binding protein
Gene namesi
Name:TERF2
Synonyms:TRBF2, TRF2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:11729. TERF2.

Subcellular locationi

GO - Cellular componenti

  • chromosome, telomeric region Source: UniProtKB
  • cytoplasm Source: HPA
  • Golgi apparatus Source: HPA
  • male germ cell nucleus Source: Ensembl
  • nuclear chromosome, telomeric region Source: GO_Central
  • nuclear telomere cap complex Source: BHF-UCL
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus, Telomere

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36446.

Polymorphism and mutation databases

DMDMi21542277.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 542542Telomeric repeat-binding factor 2PRO_0000197131Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei59 – 591Asymmetric dimethylarginine; by PRMT11 Publication
Modified residuei60 – 601Omega-N-methylarginine1 Publication
Modified residuei230 – 2301Phosphothreonine; by ATM1 Publication
Modified residuei365 – 3651Phosphoserine7 Publications

Post-translational modificationi

Phosphorylated upon DNA damage, most probably by ATM. Phosphorylated TERF2 is not bound to telomeric DNA, and rapidly localizes to damage sites.1 Publication
Methylated by PRMT1 at multiple arginines within the N-terminal Arg-rich region. Methylation may control association with telomeres.1 Publication

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

MaxQBiQ15554.
PaxDbiQ15554.
PRIDEiQ15554.

PTM databases

PhosphoSiteiQ15554.

Expressioni

Tissue specificityi

Ubiquitous. Highly expressed in spleen, thymus, prostate, uterus, testis, small intestine, colon and peripheral blood leukocytes.

Gene expression databases

BgeeiQ15554.
CleanExiHS_TERF2.
ExpressionAtlasiQ15554. baseline and differential.
GenevisibleiQ15554. HS.

Organism-specific databases

HPAiCAB010451.
HPA001907.
HPA002735.

Interactioni

Subunit structurei

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.12 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BLMP541328EBI-706637,EBI-621372
DCLRE1BQ9H8166EBI-706637,EBI-3508943
EBNA1P032113EBI-706637,EBI-996522From a different organism.
ORC1Q134152EBI-706637,EBI-374847
ORC2Q134163EBI-706637,EBI-374957
POT1Q9NUX53EBI-706637,EBI-752420
SLX4Q8IY925EBI-706637,EBI-2370740
TERF2IPQ9NYB07EBI-706637,EBI-750109
TINF2Q9BSI4-34EBI-706637,EBI-717418
WRNQ141918EBI-706637,EBI-368417

Protein-protein interaction databases

BioGridi112873. 251 interactions.
DIPiDIP-34052N.
IntActiQ15554. 21 interactions.
MINTiMINT-2831307.
STRINGi9606.ENSP00000254942.

Structurei

Secondary structure

1
542
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni87 – 893Combined sources
Helixi90 – 11122Combined sources
Helixi115 – 12814Combined sources
Helixi137 – 15317Combined sources
Turni154 – 1563Combined sources
Beta strandi163 – 1653Combined sources
Helixi170 – 18415Combined sources
Helixi189 – 20921Combined sources
Helixi213 – 22311Combined sources
Helixi228 – 2303Combined sources
Helixi231 – 24313Combined sources
Turni244 – 2463Combined sources
Helixi249 – 2524Combined sources
Helixi256 – 26813Combined sources
Helixi277 – 2859Combined sources
Turni286 – 2883Combined sources
Helixi327 – 33812Combined sources
Helixi343 – 35210Combined sources
Turni482 – 4854Combined sources
Beta strandi487 – 4893Combined sources
Helixi494 – 50714Combined sources
Helixi512 – 5187Combined sources
Helixi526 – 53813Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H6PX-ray2.20A/B85-287[»]
1VF9NMR-A480-542[»]
1VFCNMR-A480-542[»]
1W0UX-ray1.80A/B488-542[»]
1XG1NMR-A480-542[»]
3BU8X-ray2.15A/B84-318[»]
3BUAX-ray2.50A/B/C/D84-287[»]
3K6GX-ray1.95D/E/F317-358[»]
3SJMX-ray1.35A/B483-542[»]
4M7CX-ray2.05A/B87-286[»]
ProteinModelPortaliQ15554.
SMRiQ15554. Positions 85-291, 323-358, 488-542.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15554.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini484 – 54158HTH myb-typePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni84 – 287204TRFH dimerizationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi371 – 3755Nuclear localization signalSequence Analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi55 – 7218Arg-rich (basic)Add
BLAST

Domaini

The TRFH dimerization region mediates the interaction with DCLRE1B/Apollo but not TINF2.1 Publication
The HTH domain is an independent structural unit and mediates binding to telomeric DNA.1 Publication

Sequence similaritiesi

Contains 1 HTH myb-type DNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG44337.
GeneTreeiENSGT00530000063796.
HOGENOMiHOG000154547.
HOVERGENiHBG108560.
InParanoidiQ15554.
KOiK11111.
OMAiITKKQKW.
OrthoDBiEOG7DFXCF.
TreeFamiTF333209.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
1.25.40.210. 1 hit.
InterProiIPR009057. Homeodomain-like.
IPR017930. Myb_dom.
IPR001005. SANT/Myb.
IPR013867. Telomere_rpt-bd_fac_dimer_dom.
IPR030657. TERF2.
[Graphical view]
PANTHERiPTHR21717:SF13. PTHR21717:SF13. 1 hit.
PfamiPF00249. Myb_DNA-binding. 1 hit.
PF08558. TRF. 1 hit.
[Graphical view]
ProDomiPD014243. Telomere_repeat-bd_fac_dimer. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00717. SANT. 1 hit.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 1 hit.
SSF63600. SSF63600. 1 hit.
PROSITEiPS51294. HTH_MYB. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q15554-3) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAAGAGTAGP ASGPGVVRDP AASQPRKRPG REGGEGARRS DTMAGGGGSS
60 70 80 90 100
DGSGRAAGRR ASRSSGRARR GRHEPGLGGP AERGAGEARL EEAVNRWVLK
110 120 130 140 150
FYFHEALRAF RGSRYGDFRQ IRDIMQALLV RPLGKEHTVS RLLRVMQCLS
160 170 180 190 200
RIEEGENLDC SFDMEAELTP LESAINVLEM IKTEFTLTEA VVESSRKLVK
210 220 230 240 250
EAAVIICIKN KEFEKASKIL KKHMSKDPTT QKLRNDLLNI IREKNLAHPV
260 270 280 290 300
IQNFSYETFQ QKMLRFLESH LDDAEPYLLT MAKKALKSES AASSTGKEDK
310 320 330 340 350
QPAPGPVEKP PREPARQLRN PPTTIGMMTL KAAFKTLSGA QDSEAAFAKL
360 370 380 390 400
DQKDLVLPTQ ALPASPALKN KRPRKDENES SAPADGEGGS ELQPKNKRMT
410 420 430 440 450
ISRLVLEEDS QSTEPSAGLN SSQEAASAPP SKPTVLNQPL PGEKNPKVPK
460 470 480 490 500
GKWNSSNGVE EKETWVEEDE LFQVQAAPDE DSTTNITKKQ KWTVEESEWV
510 520 530 540
KAGVQKYGEG NWAAISKNYP FVNRTAVMIK DRWRTMKRLG MN
Length:542
Mass (Da):59,594
Last modified:April 16, 2014 - v3
Checksum:i3A278AC6B594C43A
GO
Isoform 2 (identifier: Q15554-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     281-293: MAKKALKSESAAS → VRLGPSPITMVCP
     294-542: Missing.

Note: No experimental confirmation available.
Show »
Length:293
Mass (Da):32,298
Checksum:iF9B31F886F3D3C23
GO

Sequence cautioni

The sequence AAB81135.1 differs from that shown.Contaminating sequence. The N-terminus may be contaminated with vector sequence.Curated
The sequence AAB81135.1 differs from that shown. Reason: Frameshift at position 36. Curated
The sequence AAH24890.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti455 – 4551S → G.
Corresponds to variant rs35874485 [ dbSNP | Ensembl ].
VAR_050196

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei281 – 29313MAKKA…ESAAS → VRLGPSPITMVCP in isoform 2. 1 PublicationVSP_003304Add
BLAST
Alternative sequencei294 – 542249Missing in isoform 2. 1 PublicationVSP_003305Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC026464 Genomic DNA. No translation available.
BC024890 mRNA. Translation: AAH24890.1. Different initiation.
AF002999 mRNA. Translation: AAB81135.1. Sequence problems.
U95970 mRNA. Translation: AAD00821.1.
X93512 mRNA. Translation: CAA63769.1.
CCDSiCCDS10879.2. [Q15554-3]
PIRiS67923.
RefSeqiNP_005643.2. NM_005652.4. [Q15554-3]
UniGeneiHs.63335.

Genome annotation databases

EnsembliENST00000254942; ENSP00000254942; ENSG00000132604.
ENST00000567296; ENSP00000454955; ENSG00000132604. [Q15554-4]
GeneIDi7014.
KEGGihsa:7014.
UCSCiuc002exd.4. human. [Q15554-3]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC026464 Genomic DNA. No translation available.
BC024890 mRNA. Translation: AAH24890.1. Different initiation.
AF002999 mRNA. Translation: AAB81135.1. Sequence problems.
U95970 mRNA. Translation: AAD00821.1.
X93512 mRNA. Translation: CAA63769.1.
CCDSiCCDS10879.2. [Q15554-3]
PIRiS67923.
RefSeqiNP_005643.2. NM_005652.4. [Q15554-3]
UniGeneiHs.63335.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H6PX-ray2.20A/B85-287[»]
1VF9NMR-A480-542[»]
1VFCNMR-A480-542[»]
1W0UX-ray1.80A/B488-542[»]
1XG1NMR-A480-542[»]
3BU8X-ray2.15A/B84-318[»]
3BUAX-ray2.50A/B/C/D84-287[»]
3K6GX-ray1.95D/E/F317-358[»]
3SJMX-ray1.35A/B483-542[»]
4M7CX-ray2.05A/B87-286[»]
ProteinModelPortaliQ15554.
SMRiQ15554. Positions 85-291, 323-358, 488-542.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112873. 251 interactions.
DIPiDIP-34052N.
IntActiQ15554. 21 interactions.
MINTiMINT-2831307.
STRINGi9606.ENSP00000254942.

PTM databases

PhosphoSiteiQ15554.

Polymorphism and mutation databases

DMDMi21542277.

Proteomic databases

MaxQBiQ15554.
PaxDbiQ15554.
PRIDEiQ15554.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000254942; ENSP00000254942; ENSG00000132604.
ENST00000567296; ENSP00000454955; ENSG00000132604. [Q15554-4]
GeneIDi7014.
KEGGihsa:7014.
UCSCiuc002exd.4. human. [Q15554-3]

Organism-specific databases

CTDi7014.
GeneCardsiGC16M069389.
HGNCiHGNC:11729. TERF2.
HPAiCAB010451.
HPA001907.
HPA002735.
MIMi602027. gene.
neXtProtiNX_Q15554.
PharmGKBiPA36446.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG44337.
GeneTreeiENSGT00530000063796.
HOGENOMiHOG000154547.
HOVERGENiHBG108560.
InParanoidiQ15554.
KOiK11111.
OMAiITKKQKW.
OrthoDBiEOG7DFXCF.
TreeFamiTF333209.

Enzyme and pathway databases

ReactomeiREACT_169185. DNA Damage/Telomere Stress Induced Senescence.
REACT_75792. Meiotic synapsis.
REACT_7963. Packaging Of Telomere Ends.

Miscellaneous databases

ChiTaRSiTERF2. human.
EvolutionaryTraceiQ15554.
GeneWikiiTERF2.
GenomeRNAii7014.
NextBioi27401.
PROiQ15554.
SOURCEiSearch...

Gene expression databases

BgeeiQ15554.
CleanExiHS_TERF2.
ExpressionAtlasiQ15554. baseline and differential.
GenevisibleiQ15554. HS.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
1.25.40.210. 1 hit.
InterProiIPR009057. Homeodomain-like.
IPR017930. Myb_dom.
IPR001005. SANT/Myb.
IPR013867. Telomere_rpt-bd_fac_dimer_dom.
IPR030657. TERF2.
[Graphical view]
PANTHERiPTHR21717:SF13. PTHR21717:SF13. 1 hit.
PfamiPF00249. Myb_DNA-binding. 1 hit.
PF08558. TRF. 1 hit.
[Graphical view]
ProDomiPD014243. Telomere_repeat-bd_fac_dimer. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00717. SANT. 1 hit.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 1 hit.
SSF63600. SSF63600. 1 hit.
PROSITEiPS51294. HTH_MYB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Adrenal cortex.
  3. "Human telomeres contain two distinct Myb-related proteins, TRF1 and TRF2."
    Broccoli D., Smogorzewska A., Chong L., de Lange T.
    Nat. Genet. 17:231-235(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-542 (ISOFORM 1).
    Tissue: Mammary carcinoma.
  4. "Telomeric localization of TRF2, a novel human telobox protein."
    Bilaud T., Brun C., Ancelin K., Koering C.E., Larouche T., Gilson E.
    Nat. Genet. 17:236-239(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 83-542 (ISOFORM 1).
    Tissue: Cervix carcinoma.
  5. "The telobox, a Myb-related telomeric DNA binding motif found in proteins from yeast, plants and human."
    Bilaud T., Koering C.E., Binet-Brasselet E., Ancelin K., Pollice A., Gasser S.M., Gilson E.
    Nucleic Acids Res. 24:1294-1303(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 480-542 (ISOFORM 1).
    Tissue: Cervix carcinoma.
  6. "TRF2 protects human telomeres from end-to-end fusions."
    van Steensel B., Smogorzewska A., de Lange T.
    Cell 92:401-413(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Cell-cycle-regulated association of RAD50/MRE11/NBS1 with TRF2 and human telomeres."
    Zhu X.-D., Kuester B., Mann M., Petrini J.H.J., de Lange T.
    Nat. Genet. 25:347-352(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NBN.
  8. "TIN2 binds TRF1 and TRF2 simultaneously and stabilizes the TRF2 complex on telomeres."
    Ye J.Z.-S., Donigian J.R., van Overbeek M., Loayza D., Luo Y., Krutchinsky A.N., Chait B.T., de Lange T.
    J. Biol. Chem. 279:47264-47271(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE SHELTERIN COMPLEX.
  9. "Telosome, a mammalian telomere-associated complex formed by multiple telomeric proteins."
    Liu D., O'Connor M.S., Qin J., Songyang Z.
    J. Biol. Chem. 279:51338-51342(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE SHELTERIN COMPLEX.
  10. "Shelterin: the protein complex that shapes and safeguards human telomeres."
    de Lange T.
    Genes Dev. 19:2100-2110(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE SHELTERIN COMPLEX.
  11. "DNA damage-induced phosphorylation of the human telomere-associated protein TRF2."
    Tanaka H., Mendonca M.S., Bradshaw P.S., Hoelz D.J., Malkas L.H., Meyn M.S., Gilley D.
    Proc. Natl. Acad. Sci. U.S.A. 102:15539-15544(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-230 BY ATM.
  12. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Apollo, an Artemis-related nuclease, interacts with TRF2 and protects human telomeres in S phase."
    van Overbeek M., de Lange T.
    Curr. Biol. 16:1295-1302(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DCLRE1B.
  14. "The Apollo 5' exonuclease functions together with TRF2 to protect telomeres from DNA repair."
    Lenain C., Bauwens S., Amiard S., Brunori M., Giraud-Panis M.J., Gilson E.
    Curr. Biol. 16:1303-1310(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DCLRE1B.
  15. "hSnm1B is a novel telomere-associated protein."
    Freibaum B.D., Counter C.M.
    J. Biol. Chem. 281:15033-15036(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DCLRE1B.
  16. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. "Endogenous hSNM1B/Apollo interacts with TRF2 and stimulates ATM in response to ionizing radiation."
    Demuth I., Bradshaw P.S., Lindner A., Anders M., Heinrich S., Kallenbach J., Schmelz K., Digweed M., Meyn M.S., Concannon P.
    DNA Repair 7:1192-1201(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DCLRE1B.
  18. "The protein hSnm1B is stabilized when bound to the telomere-binding protein TRF2."
    Freibaum B.D., Counter C.M.
    J. Biol. Chem. 283:23671-23676(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DCLRE1B.
  19. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Mammalian BTBD12/SLX4 assembles a Holliday junction resolvase and is required for DNA repair."
    Svendsen J.M., Smogorzewska A., Sowa M.E., O'Connell B.C., Gygi S.P., Elledge S.J., Harper J.W.
    Cell 138:63-77(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SLX4.
  22. "Arginine methylation regulates telomere length and stability."
    Mitchell T.R., Glenfield K., Jeyanthan K., Zhu X.D.
    Mol. Cell. Biol. 29:4918-4934(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT ARG-59 AND ARG-60 BY PRMT1.
  23. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals 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) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  24. Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH DCLRE1B, DNA-BINDING.
  25. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  26. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  27. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  29. "Structure of the TRFH dimerization domain of the human telomeric proteins TRF1 and TRF2."
    Fairall L., Chapman L., Moss H., de Lange T., Rhodes D.
    Mol. Cell 8:351-361(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
  30. "How the human telomeric proteins TRF1 and TRF2 recognize telomeric DNA: a view from high-resolution crystal structures."
    Court R., Chapman L., Fairall L., Rhodes D.
    EMBO Rep. 6:39-45(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 488-542 IN COMPLEX WITH TELOMERIC DNA, SUBUNIT.
  31. "A shared docking motif in TRF1 and TRF2 used for differential recruitment of telomeric proteins."
    Chen Y., Yang Y., van Overbeek M., Donigian J.R., Baciu P., de Lange T., Lei M.
    Science 319:1092-1096(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 84-318 IN COMPLEX WITH TINF2 AND DCLRE1B, DOMAIN TRFH DIMERIZATION.

Entry informationi

Entry nameiTERF2_HUMAN
AccessioniPrimary (citable) accession number: Q15554
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: April 16, 2014
Last modified: July 22, 2015
This is version 165 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.