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P54274

- TERF1_HUMAN

UniProt

P54274 - TERF1_HUMAN

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Protein
Telomeric repeat-binding factor 1
Gene
TERF1, PIN2, TRBF1, TRF, TRF1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi403 – 42826H-T-H motif
Add
BLAST

GO - Molecular functioni

  1. DNA binding Source: UniProtKB
  2. DNA binding, bending Source: BHF-UCL
  3. chromatin binding Source: InterPro
  4. double-stranded telomeric DNA binding Source: UniProtKB
  5. microtubule binding Source: UniProtKB
  6. protein binding Source: UniProtKB
  7. protein heterodimerization activity Source: UniProtKB
  8. protein homodimerization activity Source: UniProtKB
  9. telomeric DNA binding Source: UniProtKB

GO - Biological processi

  1. G2/M transition of mitotic cell cycle Source: UniProtKB
  2. age-dependent telomere shortening Source: UniProtKB
  3. mitotic nuclear division Source: UniProtKB-KW
  4. mitotic spindle assembly checkpoint Source: UniProtKB
  5. negative regulation of DNA replication Source: BHF-UCL
  6. negative regulation of telomerase activity Source: BHF-UCL
  7. negative regulation of telomere maintenance via semi-conservative replication Source: BHF-UCL
  8. negative regulation of telomere maintenance via telomerase Source: BHF-UCL
  9. positive regulation of apoptotic process Source: UniProtKB
  10. positive regulation of microtubule polymerization Source: UniProtKB
  11. positive regulation of mitosis Source: UniProtKB
  12. positive regulation of mitotic cell cycle Source: UniProtKB
  13. protein homooligomerization Source: UniProtKB
  14. response to drug Source: Ensembl
  15. telomere maintenance Source: Reactome
  16. telomere maintenance via telomerase Source: UniProtKB
  17. telomere maintenance via telomere shortening Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

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 1
Alternative name(s):
NIMA-interacting protein 2
TTAGGG repeat-binding factor 1
Telomeric protein Pin2/TRF1
Gene namesi
Name:TERF1
Synonyms:PIN2, TRBF1, TRF, TRF1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:11728. TERF1.

Subcellular locationi

Nucleus. Cytoplasmcytoskeletonspindle. Chromosometelomere
Note: Colocalizes with telomeric DNA in interphase and prophase cells. Telomeric localization decreases in metaphase, anaphase and telophase. Associates with the mitotic spindle.2 Publications

GO - Cellular componenti

  1. chromosome, telomeric region Source: BHF-UCL
  2. cytoplasm Source: UniProtKB-KW
  3. nuclear telomere cap complex Source: BHF-UCL
  4. nucleolus Source: HPA
  5. nucleoplasm Source: Reactome
  6. nucleus Source: UniProtKB
  7. spindle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Cytoskeleton, Nucleus, Telomere

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi74 – 741A → D: Abolishes dimerization and telomere binding; when associated with P-75. 1 Publication
Mutagenesisi75 – 751A → P: Abolishes dimerization and telomere binding; when associated with D-74. 1 Publication
Mutagenesisi77 – 771W → P: Abolishes telomere binding. 1 Publication
Mutagenesisi81 – 811F → P: Abolishes telomere binding. 1 Publication
Mutagenesisi90 – 901F → P: Diminishes telomere binding.
Mutagenesisi115 – 1151L → R: Loss of interaction with FBXO4. 1 Publication
Mutagenesisi120 – 1201L → R: Loss of interaction with FBXO4. 1 Publication
Mutagenesisi219 – 2191S → A: Loss of phosphorylation; induction of mitotic entry and apoptosis and increased radiation hypersensitivity of ataxia-telangiectasia cells. 1 Publication
Mutagenesisi219 – 2191S → D or E: Fails to induce apoptosis and decreases radiation hypersensitivity of ataxia-telangiectasia cells (phospho-mimicking mutants). 1 Publication

Organism-specific databases

PharmGKBiPA36445.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 439438Telomeric repeat-binding factor 1
PRO_0000197129Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei11 – 111Phosphoserine2 Publications
Modified residuei219 – 2191Phosphoserine; by ATM1 Publication

Post-translational modificationi

Phosphorylated preferentially on Ser-219 in an ATM-dependent manner in response to ionizing DNA damage.1 Publication
ADP-ribosylation by TNKS1 or TNKS2 diminishes its ability to bind to telomeric DNA.
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.2 Publications

Keywords - PTMi

Acetylation, ADP-ribosylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP54274.
PaxDbiP54274.
PRIDEiP54274.

PTM databases

PhosphoSiteiP54274.

Expressioni

Tissue specificityi

Highly expressed and ubiquitous. Isoform Pin2 predominates.

Inductioni

Expression is tightly regulated during the cell cycle; levels are low in G1 and S phase and increase during G2 phase and mitosis.

Gene expression databases

ArrayExpressiP54274.
BgeeiP54274.
CleanExiHS_TERF1.
GenevestigatoriP54274.

Organism-specific databases

HPAiHPA048379.

Interactioni

Subunit structurei

Homodimer; can contain both isoforms. Found in a complex with POT1; TINF2 and TNKS1. Interacts with ATM, TINF2, TNKS1, TNKS2, PINX1, NEK2 and MAPRE1. Component of the shelterin complex (telosome) composed of TERF1, TERF2, TINF2, TERF2IP ACD and POT1. Interacts with RLIM (via N-terminus). Interacts with FBXO4. Interaction with TINF2 protects against interaction with FBXO4 and subsequent polyubiquitination and proteasomal degradation. Interacts with GNL3L; this interaction promotes homodimerization. Interacts with TIN2. Interacts with RTEL1. Interactions with GNL3L and TIN2 are mutually exclusive. Interacts with CCDC79/TERB1 By similarity.10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ATMQ133155EBI-711018,EBI-495465
BLMP541323EBI-710997,EBI-621372
FBXO4Q9UKT5-13EBI-711018,EBI-960421
MAPRE1Q156912EBI-710997,EBI-1004115
STAG1Q8WVM74EBI-710997,EBI-1175097
TINF2Q9BSI4-32EBI-710997,EBI-717418
TNKS2Q9H2K22EBI-710997,EBI-4398527

Protein-protein interaction databases

BioGridi112872. 300 interactions.
DIPiDIP-29412N.
IntActiP54274. 31 interactions.
MINTiMINT-221323.
STRINGi9606.ENSP00000276603.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi63 – 9230
Helixi95 – 11016
Beta strandi113 – 1153
Helixi117 – 13317
Turni134 – 1363
Beta strandi143 – 1453
Helixi150 – 1589
Helixi167 – 18620
Helixi190 – 20011
Beta strandi203 – 2053
Helixi211 – 2199
Helixi226 – 2305
Helixi233 – 25119
Beta strandi252 – 2543
Helixi255 – 26511
Beta strandi377 – 3793
Helixi385 – 39814
Helixi403 – 4097
Helixi417 – 42812

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BA5NMR-A378-430[»]
1H6OX-ray2.90A62-265[»]
1ITYNMR-A371-439[»]
1IV6NMR-A371-439[»]
1W0TX-ray2.00A/B379-431[»]
3BQOX-ray2.00A58-268[»]
3L82X-ray2.40A58-268[»]
ProteinModelPortaliP54274.
SMRiP54274. Positions 64-266, 373-439.

Miscellaneous databases

EvolutionaryTraceiP54274.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini375 – 43258HTH myb-type
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni58 – 268211TRFH dimerization
Add
BLAST
Regioni265 – 378114Interaction with RLIM
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi337 – 35620Nuclear localization signal Reviewed prediction
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2 – 7170Asp/Glu-rich (acidic)
Add
BLAST
Compositional biasi55 – 628Poly-Glu

Domaini

The acidic N-terminal domain binds to the ankyrin repeats of TNKS1 and TNKS2. The C-terminal domain binds microtubules.1 Publication
The TRFH dimerization region mediates the interaction with TINF2.1 Publication
The HTH domain is an independent structural unit and mediates binding to telomeric DNA.1 Publication

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG72230.
HOGENOMiHOG000132847.
HOVERGENiHBG054097.
InParanoidiP54274.
KOiK11110.
OMAiYQLRTVY.
OrthoDBiEOG7DFXCF.
PhylomeDBiP54274.
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.
IPR017357. Telomere_repeat-bd-1/2.
IPR013867. Telomere_rpt-bd_fac_dimer_dom.
[Graphical view]
PfamiPF00249. Myb_DNA-binding. 1 hit.
PF08558. TRF. 1 hit.
[Graphical view]
PIRSFiPIRSF038016. Telomere_bd-1_Pin2. 1 hit.
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.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P54274-1) [UniParc]FASTAAdd to Basket

Also known as: TRF1

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

MAEDVSSAAP SPRGCADGRD ADPTEEQMAE TERNDEEQFE CQELLECQVQ    50
VGAPEEEEEE EEDAGLVAEA EAVAAGWMLD FLCLSLCRAF RDGRSEDFRR 100
TRNSAEAIIH GLSSLTACQL RTIYICQFLT RIAAGKTLDA QFENDERITP 150
LESALMIWGS IEKEHDKLHE EIQNLIKIQA IAVCMENGNF KEAEEVFERI 200
FGDPNSHMPF KSKLLMIISQ KDTFHSFFQH FSYNHMMEKI KSYVNYVLSE 250
KSSTFLMKAA AKVVESKRTR TITSQDKPSG NDVEMETEAN LDTRKSVSDK 300
QSAVTESSEG TVSLLRSHKN LFLSKLQHGT QQQDLNKKER RVGTPQSTKK 350
KKESRRATES RIPVSKSQPV TPEKHRARKR QAWLWEEDKN LRSGVRKYGE 400
GNWSKILLHY KFNNRTSVML KDRWRTMKKL KLISSDSED 439
Length:439
Mass (Da):50,246
Last modified:September 23, 2008 - v3
Checksum:iAB548E7D3124A211
GO
Isoform 2 (identifier: P54274-2) [UniParc]FASTAAdd to Basket

Also known as: Pin2

The sequence of this isoform differs from the canonical sequence as follows:
     296-315: Missing.

Show »
Length:419
Mass (Da):48,239
Checksum:i4C261E58E09C2AF9
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei296 – 31520Missing in isoform 2.
VSP_003303Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 141G → R in AAB54036. 1 Publication
Sequence conflicti14 – 141G → R in AAB17975. 1 Publication
Sequence conflicti14 – 141G → R in AAB81137. 1 Publication
Sequence conflicti14 – 141G → R in AAB53363. 1 Publication
Sequence conflicti338 – 3381K → E in CAA63768. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U40705 mRNA. Translation: AAB54036.1.
AF003001 mRNA. Translation: AAB81137.1.
AH003684 Genomic DNA. Translation: AAB17975.1.
U74382 mRNA. Translation: AAB53363.1.
EU088287 Genomic DNA. Translation: ABV02580.1.
AC022893 Genomic DNA. No translation available.
BC029378 mRNA. Translation: AAH29378.1.
X93511 mRNA. Translation: CAA63768.1.
CCDSiCCDS6210.1. [P54274-2]
CCDS6211.1. [P54274-1]
PIRiA57573.
RefSeqiNP_003209.2. NM_003218.3. [P54274-2]
NP_059523.2. NM_017489.2. [P54274-1]
UniGeneiHs.442707.

Genome annotation databases

EnsembliENST00000276602; ENSP00000276602; ENSG00000147601. [P54274-2]
ENST00000276603; ENSP00000276603; ENSG00000147601. [P54274-1]
GeneIDi7013.
KEGGihsa:7013.
UCSCiuc003xzd.2. human. [P54274-1]
uc003xze.2. human. [P54274-2]

Polymorphism databases

DMDMi206729904.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

NIEHS SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U40705 mRNA. Translation: AAB54036.1 .
AF003001 mRNA. Translation: AAB81137.1 .
AH003684 Genomic DNA. Translation: AAB17975.1 .
U74382 mRNA. Translation: AAB53363.1 .
EU088287 Genomic DNA. Translation: ABV02580.1 .
AC022893 Genomic DNA. No translation available.
BC029378 mRNA. Translation: AAH29378.1 .
X93511 mRNA. Translation: CAA63768.1 .
CCDSi CCDS6210.1. [P54274-2 ]
CCDS6211.1. [P54274-1 ]
PIRi A57573.
RefSeqi NP_003209.2. NM_003218.3. [P54274-2 ]
NP_059523.2. NM_017489.2. [P54274-1 ]
UniGenei Hs.442707.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BA5 NMR - A 378-430 [» ]
1H6O X-ray 2.90 A 62-265 [» ]
1ITY NMR - A 371-439 [» ]
1IV6 NMR - A 371-439 [» ]
1W0T X-ray 2.00 A/B 379-431 [» ]
3BQO X-ray 2.00 A 58-268 [» ]
3L82 X-ray 2.40 A 58-268 [» ]
ProteinModelPortali P54274.
SMRi P54274. Positions 64-266, 373-439.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112872. 300 interactions.
DIPi DIP-29412N.
IntActi P54274. 31 interactions.
MINTi MINT-221323.
STRINGi 9606.ENSP00000276603.

PTM databases

PhosphoSitei P54274.

Polymorphism databases

DMDMi 206729904.

Proteomic databases

MaxQBi P54274.
PaxDbi P54274.
PRIDEi P54274.

Protocols and materials databases

DNASUi 7013.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000276602 ; ENSP00000276602 ; ENSG00000147601 . [P54274-2 ]
ENST00000276603 ; ENSP00000276603 ; ENSG00000147601 . [P54274-1 ]
GeneIDi 7013.
KEGGi hsa:7013.
UCSCi uc003xzd.2. human. [P54274-1 ]
uc003xze.2. human. [P54274-2 ]

Organism-specific databases

CTDi 7013.
GeneCardsi GC08P073921.
H-InvDB HIX0007582.
HGNCi HGNC:11728. TERF1.
HPAi HPA048379.
MIMi 600951. gene.
neXtProti NX_P54274.
PharmGKBi PA36445.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG72230.
HOGENOMi HOG000132847.
HOVERGENi HBG054097.
InParanoidi P54274.
KOi K11110.
OMAi YQLRTVY.
OrthoDBi EOG7DFXCF.
PhylomeDBi P54274.
TreeFami TF333209.

Enzyme and pathway databases

Reactomei REACT_169185. DNA Damage/Telomere Stress Induced Senescence.
REACT_75792. Meiotic synapsis.
REACT_7963. Packaging Of Telomere Ends.

Miscellaneous databases

ChiTaRSi TERF1. human.
EvolutionaryTracei P54274.
GeneWikii TERF1.
GenomeRNAii 7013.
NextBioi 27395.
PROi P54274.
SOURCEi Search...

Gene expression databases

ArrayExpressi P54274.
Bgeei P54274.
CleanExi HS_TERF1.
Genevestigatori P54274.

Family and domain databases

Gene3Di 1.10.10.60. 1 hit.
1.25.40.210. 1 hit.
InterProi IPR009057. Homeodomain-like.
IPR017930. Myb_dom.
IPR001005. SANT/Myb.
IPR017357. Telomere_repeat-bd-1/2.
IPR013867. Telomere_rpt-bd_fac_dimer_dom.
[Graphical view ]
Pfami PF00249. Myb_DNA-binding. 1 hit.
PF08558. TRF. 1 hit.
[Graphical view ]
PIRSFi PIRSF038016. Telomere_bd-1_Pin2. 1 hit.
ProDomi PD014243. Telomere_repeat-bd_fac_dimer. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00717. SANT. 1 hit.
[Graphical view ]
SUPFAMi SSF46689. SSF46689. 1 hit.
SSF63600. SSF63600. 1 hit.
PROSITEi PS51294. HTH_MYB. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
    Tissue: Cervix carcinoma.
  2. de Lange T.
    Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 14.
  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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-138 (ISOFORM1/2).
  4. "Characterization and cell cycle regulation of the related human telomeric proteins Pin2 and TRF1 suggest a role in mitosis."
    Shen M., Haggblom C., Vogt M., Hunter T., Lu K.P.
    Proc. Natl. Acad. Sci. U.S.A. 94:13618-13623(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Cervix carcinoma.
  5. NIEHS SNPs program
    Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  6. "DNA sequence and analysis of human chromosome 8."
    Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
    , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
    Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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: Liver.
  8. "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 329-439 (ISOFORMS 1/2).
    Tissue: Cervix carcinoma.
  9. "Telomeric protein Pin2/TRF1 as an important ATM target in response to double 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) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF SER-219, PHOSPHORYLATION AT SER-219, INTERACTION WITH ATM.
  10. "Involvement of the telomeric protein Pin2/TRF1 in the regulation of the mitotic spindle."
    Nakamura M., Zhen Zhou X., Kishi S., Ping Lu K.
    FEBS Lett. 514:193-198(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAPRE1 AND WITH THE MITOTIC SPINDLE.
  11. "Role for the related poly(ADP-Ribose) polymerases tankyrase 1 and 2 at human telomeres."
    Cook B.D., Dynek J.N., Chang W., Shostak G., Smith S.
    Mol. Cell. Biol. 22:332-342(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: ADP-RIBOSYLATION.
  12. "POT1 as a terminal transducer of TRF1 telomere length control."
    Loayza D., De Lange T.
    Nature 423:1013-1018(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH POT1; TINF2 AND TNKS1.
  13. "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.
  14. "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.
  15. "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.
  16. "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-11, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  19. "Ubiquitin ligase RLIM modulates telomere length homeostasis through a proteolysis of TRF1."
    Her Y.R., Chung I.K.
    J. Biol. Chem. 284:8557-8566(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RLIM, SUBCELLULAR LOCATION, UBIQUITINATION.
  20. "GNL3L stabilizes the TRF1 complex and promotes mitotic transition."
    Zhu Q., Meng L., Hsu J.K., Lin T., Teishima J., Tsai R.Y.
    J. Cell Biol. 185:827-839(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  21. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. Cited for: INTERACTION WITH RTEL1.
  23. "Solution structure of the DNA-binding domain of human telomeric protein, hTRF1."
    Nishikawa T., Nagadoi A., Yoshimura S., Aimoto S., Nishimura Y.
    Structure 6:1057-1065(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 378-430.
  24. "Solution structure of a telomeric DNA complex of human TRF1."
    Nishikawa T., Okamura H., Nagadoi A., Koenig P., Rhodes D., Nishimura Y.
    Structure 9:1237-1251(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 371-439.
  25. "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 (2.9 ANGSTROMS) OF 48-268, MUTAGENESIS OF ALA-74; ALA-75; TRP-77 AND PHE-81.
  26. "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 (2.0 ANGSTROMS) OF 379-431 IN COMPLEX WITH TELOMERIC DNA, SUBUNIT.
  27. "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 (2.0 ANGSTROMS) OF 58-268 IN COMPLEX WITH TINF2, INTERACTION WITH TINF2 AND PINX1, DOMAIN TRFH DIMERIZATION, SUBUNIT.
  28. "Structural basis of selective ubiquitination of TRF1 by SCFFbx4."
    Zeng Z., Wang W., Yang Y., Chen Y., Yang X., Diehl J.A., Liu X., Lei M.
    Dev. Cell 18:214-225(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 58-268 IN COMPLEX WITH FBXO4, MUTAGENESIS OF LEU-115 AND LEU-120, INTERACTION WITH TINF2, SUBUNIT, UBIQUITINATION.

Entry informationi

Entry nameiTERF1_HUMAN
AccessioniPrimary (citable) accession number: P54274
Secondary accession number(s): A7XP29
, Q15553, Q8NHT6, Q93029
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: September 23, 2008
Last modified: September 3, 2014
This is version 166 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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