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P54274 (TERF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 162. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Telomeric repeat-binding factor 1
Alternative name(s):
NIMA-interacting protein 2
TTAGGG repeat-binding factor 1
Telomeric protein Pin2/TRF1
Gene names
Name:TERF1
Synonyms:PIN2, TRBF1, TRF, TRF1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length439 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.15

Subunit structure

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. Ref.9 Ref.10 Ref.12 Ref.13 Ref.14 Ref.19 Ref.22 Ref.26 Ref.27 Ref.28

Subcellular location

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. Ref.19 Ref.20

Tissue specificity

Highly expressed and ubiquitous. Isoform Pin2predominates.

Induction

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

Domain

The acidic N-terminal domain binds to the ankyrin repeats of TNKS1 and TNKS2. The C-terminal domain binds microtubules. Ref.27

The TRFH dimerization region mediates the interaction with TINF2. Ref.27

The HTH domain is an independent structural unit and mediates binding to telomeric DNA. Ref.27

Post-translational modification

Phosphorylated preferentially on Ser-219 in an ATM-dependent manner in response to ionizing DNA damage. Ref.9

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. Ref.19 Ref.28

Sequence similarities

Contains 1 HTH myb-type DNA-binding domain.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   Cellular componentChromosome
Cytoplasm
Cytoskeleton
Nucleus
Telomere
   Coding sequence diversityAlternative splicing
   LigandDNA-binding
   PTMAcetylation
ADP-ribosylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processG2/M transition of mitotic cell cycle

Inferred from expression pattern Ref.4. Source: UniProtKB

age-dependent telomere shortening

Inferred from direct assay PubMed 9034193. Source: UniProtKB

mitosis

Inferred from electronic annotation. Source: UniProtKB-KW

mitotic spindle assembly checkpoint

Inferred from mutant phenotype Ref.10. Source: UniProtKB

negative regulation of DNA replication

Inferred from direct assay PubMed 11327863. Source: BHF-UCL

negative regulation of telomerase activity

Inferred from genetic interaction PubMed 11971978. Source: BHF-UCL

negative regulation of telomere maintenance via semi-conservative replication

Non-traceable author statement PubMed 15007108. Source: BHF-UCL

negative regulation of telomere maintenance via telomerase

Inferred from genetic interaction PubMed 11971978. Source: BHF-UCL

positive regulation of apoptotic process

Inferred from direct assay PubMed 11313893PubMed 11313893. Source: UniProtKB

positive regulation of microtubule polymerization

Inferred from direct assay Ref.10. Source: UniProtKB

positive regulation of mitosis

Inferred from mutant phenotype PubMed 11313893. Source: UniProtKB

positive regulation of mitotic cell cycle

Inferred from mutant phenotype Ref.4. Source: UniProtKB

protein homooligomerization

Inferred from direct assay Ref.4. Source: UniProtKB

response to drug

Inferred from electronic annotation. Source: Ensembl

telomere maintenance

Traceable author statement. Source: Reactome

telomere maintenance via telomerase

Inferred from mutant phenotype PubMed 9034193. Source: UniProtKB

telomere maintenance via telomere shortening

Inferred from mutant phenotype PubMed 11971978. Source: BHF-UCL

   Cellular_componentchromosome, telomeric region

Inferred from direct assay PubMed 15380063. Source: BHF-UCL

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

nuclear telomere cap complex

Inferred from direct assay PubMed 16880378. Source: BHF-UCL

nucleolus

Inferred from direct assay. Source: HPA

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 11313893PubMed 1406665Ref.4. Source: UniProtKB

spindle

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionDNA binding

Non-traceable author statement Ref.1. Source: UniProtKB

DNA binding, bending

Inferred from direct assay PubMed 9130722. Source: BHF-UCL

chromatin binding

Inferred from electronic annotation. Source: InterPro

double-stranded telomeric DNA binding

Inferred from direct assay Ref.12Ref.26PubMed 1406665. Source: UniProtKB

microtubule binding

Inferred from direct assay Ref.10. Source: UniProtKB

protein heterodimerization activity

Inferred from direct assay Ref.4. Source: UniProtKB

protein homodimerization activity

Inferred from physical interaction Ref.26. Source: UniProtKB

telomeric DNA binding

Inferred from direct assay PubMed 9034193Ref.4. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P54274-1)

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.
Isoform 2 (identifier: P54274-2)

Also known as: Pin2;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.18
Chain2 – 439438Telomeric repeat-binding factor 1
PRO_0000197129

Regions

Domain375 – 43258HTH myb-type
DNA binding403 – 42826H-T-H motif
Region58 – 268211TRFH dimerization
Region265 – 378114Interaction with RLIM
Motif337 – 35620Nuclear localization signal Potential
Compositional bias2 – 7170Asp/Glu-rich (acidic)
Compositional bias55 – 628Poly-Glu

Amino acid modifications

Modified residue21N-acetylalanine Ref.18 Ref.21
Modified residue111Phosphoserine Ref.16 Ref.21
Modified residue2191Phosphoserine; by ATM Ref.9

Natural variations

Alternative sequence296 – 31520Missing in isoform 2.
VSP_003303

Experimental info

Mutagenesis741A → D: Abolishes dimerization and telomere binding; when associated with P-75. Ref.25
Mutagenesis751A → P: Abolishes dimerization and telomere binding; when associated with D-74. Ref.25
Mutagenesis771W → P: Abolishes telomere binding. Ref.25
Mutagenesis811F → P: Abolishes telomere binding. Ref.25
Mutagenesis901F → P: Diminishes telomere binding.
Mutagenesis1151L → R: Loss of interaction with FBXO4. Ref.28
Mutagenesis1201L → R: Loss of interaction with FBXO4. Ref.28
Mutagenesis2191S → A: Loss of phosphorylation; induction of mitotic entry and apoptosis and increased radiation hypersensitivity of ataxia-telangiectasia cells. Ref.9
Mutagenesis2191S → D or E: Fails to induce apoptosis and decreases radiation hypersensitivity of ataxia-telangiectasia cells (phospho-mimicking mutants). Ref.9
Sequence conflict141G → R in AAB54036. Ref.1
Sequence conflict141G → R in AAB17975. Ref.3
Sequence conflict141G → R in AAB81137. Ref.3
Sequence conflict141G → R in AAB53363. Ref.4
Sequence conflict3381K → E in CAA63768. Ref.8

Secondary structure

.................................... 439
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (TRF1) [UniParc].

Last modified September 23, 2008. Version 3.
Checksum: AB548E7D3124A211

FASTA43950,246
        10         20         30         40         50         60 
MAEDVSSAAP SPRGCADGRD ADPTEEQMAE TERNDEEQFE CQELLECQVQ VGAPEEEEEE 

        70         80         90        100        110        120 
EEDAGLVAEA EAVAAGWMLD FLCLSLCRAF RDGRSEDFRR TRNSAEAIIH GLSSLTACQL 

       130        140        150        160        170        180 
RTIYICQFLT RIAAGKTLDA QFENDERITP LESALMIWGS IEKEHDKLHE EIQNLIKIQA 

       190        200        210        220        230        240 
IAVCMENGNF KEAEEVFERI FGDPNSHMPF KSKLLMIISQ KDTFHSFFQH FSYNHMMEKI 

       250        260        270        280        290        300 
KSYVNYVLSE KSSTFLMKAA AKVVESKRTR TITSQDKPSG NDVEMETEAN LDTRKSVSDK 

       310        320        330        340        350        360 
QSAVTESSEG TVSLLRSHKN LFLSKLQHGT QQQDLNKKER RVGTPQSTKK KKESRRATES 

       370        380        390        400        410        420 
RIPVSKSQPV TPEKHRARKR QAWLWEEDKN LRSGVRKYGE GNWSKILLHY KFNNRTSVML 

       430 
KDRWRTMKKL KLISSDSED 

« Hide

Isoform 2 (Pin2) [UniParc].

Checksum: 4C261E58E09C2AF9
Show »

FASTA41948,239

References

« Hide 'large scale' references
[1]"A human telomeric protein."
Chong L., van Steensel B., Broccoli D., Erdjument-Bromage H., Hanish J., Tempst P., de Lange T.
Science 270:1663-1667(1995) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Inherited mutations in the helicase RTEL1 cause telomere dysfunction and Hoyeraal-Hreidarsson syndrome."
Deng Z., Glousker G., Molczan A., Fox A.J., Lamm N., Dheekollu J., Weizman O.E., Schertzer M., Wang Z., Vladimirova O., Schug J., Aker M., Londono-Vallejo A., Kaestner K.H., Lieberman P.M., Tzfati Y.
Proc. Natl. Acad. Sci. U.S.A. 110:E3408-E3416(2013) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA57573.
RefSeqNP_003209.2. NM_003218.3.
NP_059523.2. NM_017489.2.
UniGeneHs.442707.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP54274.
SMRP54274. Positions 64-266, 373-439.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112872. 298 interactions.
DIPDIP-29412N.
IntActP54274. 31 interactions.
MINTMINT-221323.
STRING9606.ENSP00000276603.

PTM databases

PhosphoSiteP54274.

Polymorphism databases

DMDM206729904.

Proteomic databases

PaxDbP54274.
PRIDEP54274.

Protocols and materials databases

DNASU7013.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000276602; ENSP00000276602; ENSG00000147601. [P54274-2]
ENST00000276603; ENSP00000276603; ENSG00000147601. [P54274-1]
GeneID7013.
KEGGhsa:7013.
UCSCuc003xzd.2. human. [P54274-1]
uc003xze.2. human. [P54274-2]

Organism-specific databases

CTD7013.
GeneCardsGC08P073921.
H-InvDBHIX0007582.
HGNCHGNC:11728. TERF1.
HPAHPA048379.
MIM600951. gene.
neXtProtNX_P54274.
PharmGKBPA36445.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG72230.
HOGENOMHOG000132847.
HOVERGENHBG054097.
InParanoidP54274.
KOK11110.
OMAYQLRTVY.
OrthoDBEOG7DFXCF.
PhylomeDBP54274.
TreeFamTF333209.

Enzyme and pathway databases

ReactomeREACT_111183. Meiosis.
REACT_115566. Cell Cycle.
REACT_120956. Cellular responses to stress.

Gene expression databases

ArrayExpressP54274.
BgeeP54274.
CleanExHS_TERF1.
GenevestigatorP54274.

Family and domain databases

Gene3D1.10.10.60. 1 hit.
1.25.40.210. 1 hit.
InterProIPR009057. Homeodomain-like.
IPR017930. Myb_dom.
IPR001005. SANT/Myb.
IPR017357. Telomere_repeat-bd-1/2.
IPR013867. Telomere_rpt-bd_fac_dimer_dom.
[Graphical view]
PfamPF00249. Myb_DNA-binding. 1 hit.
PF08558. TRF. 1 hit.
[Graphical view]
PIRSFPIRSF038016. Telomere_bd-1_Pin2. 1 hit.
ProDomPD014243. Telomere_repeat-bd_fac_dimer. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00717. SANT. 1 hit.
[Graphical view]
SUPFAMSSF46689. SSF46689. 1 hit.
SSF63600. SSF63600. 1 hit.
PROSITEPS51294. HTH_MYB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTERF1. human.
EvolutionaryTraceP54274.
GeneWikiTERF1.
GenomeRNAi7013.
NextBio27395.
PROP54274.
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Entry information

Entry nameTERF1_HUMAN
AccessionPrimary (citable) accession number: P54274
Secondary accession number(s): A7XP29 expand/collapse secondary AC list , Q15553, Q8NHT6, Q93029
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: September 23, 2008
Last modified: April 16, 2014
This is version 162 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM