P54274 (TERF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	439 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Binds the telomeric double-stranded TTAGGG 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 TTAGGG 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. Interactions with GNL3L and TIN2 are mutually exclusive By similarity. Ref.9 Ref.10 Ref.12 Ref.13 Ref.14 Ref.18 Ref.24 Ref.25 Ref.26
Subcellular location	Nucleus. Cytoplasm › cytoskeleton › spindle. Chromosome › telomere. Note: Colocalizes with telomeric DNA in interphase and prophase cells. Telomeric localization decreases in metaphase, anaphase and telophase. Associates with the mitotic spindle. Ref.18 Ref.19
Tissue specificity	Highly expressed and ubiquitous. Isoform Pin2 predominates.
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.25 The TRFH dimerization region mediates the interaction with TINF2. Ref.25 The HTH domain is an independent structural unit and mediates binding to telomeric DNA. Ref.25
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.18 Ref.26
Sequence similarities	Contains 1 HTH myb-type DNA-binding domain.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Chromosome Cytoplasm Cytoskeleton Nucleus Telomere
Coding sequence diversity	Alternative splicing
Ligand	DNA-binding
PTM	ADP-ribosylation Acetylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	G2/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 cell division Inferred from electronic annotation. Source: UniProtKB-KW induction of apoptosis Inferred from direct assay PubMed 11313893PubMed 11313893. 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 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 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: Compara 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_component	chromosome, telomeric region Inferred from direct assay PubMed 9034193Ref.4PubMed 11313893. Source: UniProtKB cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW nuclear telomere cap complex Inferred from direct assay PubMed 16880378. Source: BHF-UCL nucleoplasm Traceable author statement. Source: Reactome nucleus Inferred from direct assay PubMed 1406665Ref.4. Source: UniProtKB spindle Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	DNA binding, bending Inferred from direct assay PubMed 9130722. Source: BHF-UCL chromatin binding Inferred from electronic annotation. Source: InterPro cysteine-type endopeptidase activator activity involved in apoptotic process Inferred from direct assay PubMed 11313893. Source: UniProtKB double-stranded telomeric DNA binding Inferred from direct assay Ref.12Ref.24PubMed 1406665. Source: UniProtKB microtubule binding Inferred from direct assay Ref.10. Source: UniProtKB protein heterodimerization activity Inferred from direct assay Ref.4. Source: UniProtKB telomerase inhibitor activity Inferred from genetic interaction PubMed 11971978. Source: BHF-UCL telomeric DNA binding Inferred from direct assay Ref.4. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ATM	Q13315	5	EBI-711018,EBI-495465
BLM	P54132	3	EBI-710997,EBI-621372
FBXO4	Q9UKT5-1	3	EBI-711018,EBI-960421
MAPRE1	Q15691	2	EBI-710997,EBI-1004115
TINF2	Q9BSI4-3	2	EBI-710997,EBI-717418
TNKS2	Q9H2K2	2	EBI-710997,EBI-4398527

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.20

Chain

2 – 439

438

Telomeric repeat-binding factor 1

PRO_0000197129

Regions

Domain

375 – 432

58

HTH myb-type

DNA binding

403 – 428

26

H-T-H motif

Region

58 – 268

211

TRFH dimerization

Region

265 – 378

114

Interaction with RLIM

Motif

337 – 356

20

Nuclear localization signal Potential

Compositional bias

2 – 71

70

Asp/Glu-rich (acidic)

Compositional bias

55 – 62

8

Poly-Glu

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.20

Modified residue

11

1

Phosphoserine Ref.16 Ref.20

Modified residue

219

1

Phosphoserine; by ATM Ref.9

Natural variations

Alternative sequence

296 – 315

20

Missing in isoform 2.

VSP_003303

Experimental info

Mutagenesis

74

1

A → D: Abolishes dimerization and telomere binding; when associated with P-75. Ref.23

Mutagenesis

75

1

A → P: Abolishes dimerization and telomere binding; when associated with D-74. Ref.23

Mutagenesis

77

1

W → P: Abolishes telomere binding. Ref.23

Mutagenesis

81

1

F → P: Abolishes telomere binding. Ref.23

Mutagenesis

90

1

F → P: Diminishes telomere binding.

Mutagenesis

115

1

L → R: Loss of interaction with FBXO4. Ref.26

Mutagenesis

120

1

L → R: Loss of interaction with FBXO4. Ref.26

Mutagenesis

219

1

S → A: Loss of phosphorylation; induction of mitotic entry and apoptosis and increased radiation hypersensitivity of ataxia-telangiectasia cells. Ref.9

Mutagenesis

219

1

S → D or E: Fails to induce apoptosis and decreases radiation hypersensitivity of ataxia-telangiectasia cells (phospho-mimicking mutants). Ref.9

Sequence conflict

14

1

G → R in AAB54036. Ref.1

Sequence conflict

14

1

G → R in AAB17975. Ref.3

Sequence conflict

14

1

G → R in AAB81137. Ref.3

Sequence conflict

14

1

G → R in AAB53363. Ref.4

Sequence conflict

338

1

K → E in CAA63768. Ref.8

Secondary structure

1

.

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439

Helix Strand Turn

Details...

Helix

63 – 92

30

Helix

95 – 110

16

Beta strand

113 – 115

3

Helix

117 – 133

17

Turn

134 – 136

3

Beta strand

143 – 145

3

Helix

150 – 158

9

Helix

167 – 186

20

Helix

190 – 200

11

Beta strand

203 – 205

3

Helix

211 – 219

9

Helix

226 – 230

5

Helix

233 – 251

19

Beta strand

252 – 254

3

Helix

255 – 265

11

Beta strand

377 – 379

3

Helix

385 – 398

14

Helix

403 – 409

7

Helix

417 – 428

12

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (TRF1) [UniParc]. Last modified September 23, 2008. Version 3. Checksum: AB548E7D3124A211	FASTA	439	50,246
	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
	Isoform 2 (Pin2) [UniParc]. Checksum: 4C261E58E09C2AF9	FASTA	419	48,239
	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 LDTRKRSHKN 310 320 330 340 350 360 LFLSKLQHGT QQQDLNKKER RVGTPQSTKK KKESRRATES RIPVSKSQPV TPEKHRARKR 370 380 390 400 410 QAWLWEEDKN LRSGVRKYGE GNWSKILLHY KFNNRTSVML KDRWRTMKKL KLISSDSED

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. 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]	"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.
[19]	"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.
[20]	"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, MASS SPECTROMETRY, CLEAVAGE OF INITIATOR METHIONINE. Tissue: Cervix carcinoma.
[21]	"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.
[22]	"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.
[23]	"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.
[24]	"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.
[25]	"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.
[26]	"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

NIEHS SNPs

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.

IPI

IPI00005539.
IPI00220583.

PIR

A57573.

RefSeq

NP_003209.2. NM_003218.3.
NP_059523.2. NM_017489.2.

UniGene

Hs.442707.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P54274.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29412N.

IntAct

P54274. 24 interactions.

MINT

MINT-221323.

STRING

9606.ENSP00000276603.

PTM databases

PhosphoSite

P54274.

Polymorphism databases

DMDM

206729904.

Proteomic databases

PaxDb

P54274.

PRIDE

P54274.

Protocols and materials databases

DNASU

7013.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000276602; ENSP00000276602; ENSG00000147601.
ENST00000276603; ENSP00000276603; ENSG00000147601.

GeneID

7013.

KEGG

hsa:7013.

UCSC

uc003xzd.2. human.
uc003xze.2. human.

Organism-specific databases

CTD

7013.

GeneCards

GC08P073921.

H-InvDB

HIX0007582.

HGNC

HGNC:11728. TERF1.

MIM

600951. gene.

neXtProt

NX_P54274.

PharmGKB

PA36445.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG72230.

HOGENOM

HOG000132847.

HOVERGEN

HBG054097.

InParanoid

P54274.

KO

K11110.

OMA

AYQLRTV.

Enzyme and pathway databases

Pathway_Interaction_DB

telomerasepathway. Regulation of Telomerase.

Reactome

REACT_111183. Meiosis.
REACT_115566. Cell Cycle.

Gene expression databases

ArrayExpress

P54274.

Bgee

P54274.

CleanEx

HS_TERF1.

Genevestigator

P54274.

GermOnline

ENSG00000147601. Homo sapiens.

Family and domain databases

Gene3D

1.10.10.60. 1 hit.
1.25.40.210. 1 hit.

InterPro

IPR009057. Homeodomain-like.
IPR017930. Myb_dom.
IPR001005. SANT/Myb.
IPR017357. Telomere_repeat-bd-1/2.
IPR013867. Telomere_rpt-bd_fac_dimer_dom.
[Graphical view]

Pfam

PF00249. Myb_DNA-binding. 1 hit.
PF08558. TRF. 1 hit.
[Graphical view]

PIRSF

PIRSF038016. Telomere_bd-1_Pin2. 1 hit.

ProDom

PD014243. Telomere_repeat-bd_fac_dimer. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00717. SANT. 1 hit.
[Graphical view]

SUPFAM

SSF46689. Homeodomain_like. 1 hit.
SSF63600. Telo_rept_bnd_D. 1 hit.

PROSITE

PS51294. HTH_MYB. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

TERF1. human.

EvolutionaryTrace

P54274.

GenomeRNAi

7013.

NextBio

27395.

SOURCE

Search...

Entry information

Entry name

TERF1_HUMAN

Accession

Primary (citable) accession number: P54274
Secondary accession number(s): A7XP29 , Q15553, Q8NHT6, Q93029

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	September 23, 2008
Last modified:	May 1, 2013
This is version 153 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.