Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Telomeric repeat-binding factor 1

Gene

Terf1

Organism
Mus musculus (Mouse)
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 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 bindingi390 – 41526H-T-H motifPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-1221632. Meiotic synapsis.
R-MMU-1221633. Meiotic Synapsis.
R-MMU-2559586. DNA Damage/Telomere Stress Induced Senescence.

Names & Taxonomyi

Protein namesi
Recommended name:
Telomeric repeat-binding factor 1
Alternative name(s):
TTAGGG repeat-binding factor 1
Gene namesi
Name:Terf1
Synonyms:Trf1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:109634. Terf1.

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation
  • Chromosometelomere By similarity
  • Cytoplasmcytoskeletonspindle By similarity

  • Note: Colocalizes with telomeric DNA in interphase and prophase cells. Telomeric localization decreases in metaphase, anaphase and telophase. Associates with the mitotic spindle (By similarity).By similarity

GO - Cellular componenti

  • chromosome, telomeric region Source: MGI
  • cytoplasm Source: UniProtKB-KW
  • nuclear chromosome, telomeric region Source: BHF-UCL
  • nuclear telomere cap complex Source: BHF-UCL
  • nucleolus Source: MGI
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • spindle Source: UniProtKB-SubCell
  • telosome Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Cytoskeleton, Nucleus, Telomere

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 421420Telomeric repeat-binding factor 1PRO_0000197130Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei206 – 2061Phosphoserine; by ATMBy similarity

Post-translational modificationi

Phosphorylated preferentially on Ser-219 in an ATM-dependent manner in response to ionizing DNA damage.By similarity
ADP-ribosylation by TNKS1 or TNKS2 diminishes its ability to bind to telomeric DNA.By similarity
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 (By similarity).By similarity

Keywords - PTMi

Acetylation, ADP-ribosylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP70371.
MaxQBiP70371.
PaxDbiP70371.
PRIDEiP70371.

PTM databases

iPTMnetiP70371.
PhosphoSiteiP70371.

Expressioni

Gene expression databases

BgeeiP70371.
CleanExiMM_TERF1.
ExpressionAtlasiP70371. baseline and differential.
GenevisibleiP70371. MM.

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 (By similarity). Interacts with GNL3L; this interaction promotes homodimerization. Interacts with TIN2. Interactions with GNL3L and TIN2 are mutually exclusive. Interacts with RTEL1 (By similarity). Interacts with CCDC79/TERB1.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Dna2Q6ZQJ54EBI-6919183,EBI-6919222

GO - Molecular functioni

Protein-protein interaction databases

BioGridi204116. 11 interactions.
DIPiDIP-44231N.
IntActiP70371. 14 interactions.
MINTiMINT-3379583.
STRINGi10090.ENSMUSP00000027057.

Structurei

3D structure databases

ProteinModelPortaliP70371.
SMRiP70371. Positions 63-253, 365-421.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini362 – 41958HTH myb-typePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 255207TRFH dimerizationBy similarityAdd
BLAST
Regioni252 – 365114Interaction with RLIMBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi313 – 36755Nuclear localization signalSequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2 – 6766Asp/Glu-rich (acidic)Add
BLAST

Domaini

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

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG410IIKA. Eukaryota.
ENOG4111QH9. LUCA.
GeneTreeiENSGT00530000063796.
HOGENOMiHOG000132847.
HOVERGENiHBG054097.
InParanoidiP70371.
KOiK11110.
OMAiQKAWLWE.
OrthoDBiEOG7DFXCF.
PhylomeDBiP70371.
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.
IPR017357. TERF1.
[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]

Sequencei

Sequence statusi: Complete.

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

P70371-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAETVSSAAR DAPSREGWTD SDSPEQEEVG DDAELLQCQL QLGTPREMEN
60 70 80 90 100
AELVAEVEAV AAGWMLDFLC LSLCRAFRDG RSEDFRRTRD SAEAIIHGLH
110 120 130 140 150
RLTAYQLKTV YICQFLTRVA SGKALDAQFE VDERITPLES ALMIWNSIEK
160 170 180 190 200
EHDKLHDEIK NLIKIQAVAV CMEIGSFKEA EEVFERIFGD PEFYTPLERK
210 220 230 240 250
LLKIISQKDV FHSLFQHFSY SCMMEKIQSY VGDVLSEKSS TFLMKAATKV
260 270 280 290 300
VENEKARTQA SKDRPDATNT GMDTEVGLNK EKSVNGQQST ETEPLVDTVS
310 320 330 340 350
SIRSHKNALS QLKHRRAPSD FSRNEARTGT LQCETTMERN RRTSGRNRLC
360 370 380 390 400
VSENQPDTDD KSGRRKRQTW LWEEDRILKC GVKKYGEGNW AKILSHYKFN
410 420
NRTSVMLKDR WRTMKRLKLI S
Length:421
Mass (Da):48,224
Last modified:February 1, 1997 - v1
Checksum:i3F648F18C3ECF20A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti283 – 31230SVNGQ…ALSQL → RSFAPSLPYGSTSCDYHIRK QTGIYGIIIQ (PubMed:16141072).CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U65586 mRNA. Translation: AAB53970.1.
BC034866 mRNA. Translation: AAH34866.1.
U70994 Genomic DNA. Translation: AAB17974.1.
AK021235 mRNA. Translation: BAB32340.1.
CCDSiCCDS14827.1.
RefSeqiNP_033378.1. NM_009352.3.
UniGeneiMm.4306.

Genome annotation databases

EnsembliENSMUST00000188371; ENSMUSP00000140744; ENSMUSG00000025925.
GeneIDi21749.
KEGGimmu:21749.
UCSCiuc007ajf.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U65586 mRNA. Translation: AAB53970.1.
BC034866 mRNA. Translation: AAH34866.1.
U70994 Genomic DNA. Translation: AAB17974.1.
AK021235 mRNA. Translation: BAB32340.1.
CCDSiCCDS14827.1.
RefSeqiNP_033378.1. NM_009352.3.
UniGeneiMm.4306.

3D structure databases

ProteinModelPortaliP70371.
SMRiP70371. Positions 63-253, 365-421.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204116. 11 interactions.
DIPiDIP-44231N.
IntActiP70371. 14 interactions.
MINTiMINT-3379583.
STRINGi10090.ENSMUSP00000027057.

PTM databases

iPTMnetiP70371.
PhosphoSiteiP70371.

Proteomic databases

EPDiP70371.
MaxQBiP70371.
PaxDbiP70371.
PRIDEiP70371.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000188371; ENSMUSP00000140744; ENSMUSG00000025925.
GeneIDi21749.
KEGGimmu:21749.
UCSCiuc007ajf.2. mouse.

Organism-specific databases

CTDi7013.
MGIiMGI:109634. Terf1.

Phylogenomic databases

eggNOGiENOG410IIKA. Eukaryota.
ENOG4111QH9. LUCA.
GeneTreeiENSGT00530000063796.
HOGENOMiHOG000132847.
HOVERGENiHBG054097.
InParanoidiP70371.
KOiK11110.
OMAiQKAWLWE.
OrthoDBiEOG7DFXCF.
PhylomeDBiP70371.
TreeFamiTF333209.

Enzyme and pathway databases

ReactomeiR-MMU-1221632. Meiotic synapsis.
R-MMU-1221633. Meiotic Synapsis.
R-MMU-2559586. DNA Damage/Telomere Stress Induced Senescence.

Miscellaneous databases

ChiTaRSiTerf1. mouse.
PROiP70371.
SOURCEiSearch...

Gene expression databases

BgeeiP70371.
CleanExiMM_TERF1.
ExpressionAtlasiP70371. baseline and differential.
GenevisibleiP70371. MM.

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.
IPR017357. TERF1.
[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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Comparison of the human and mouse genes encoding the telomeric protein, TRF1: chromosomal localization, expression and conserved protein domains."
    Broccoli D., Chong L., Oelmann S., Fernald A.A., Marziliano N., van Steensel B., Kipling D., le Beau M.M., de Lange T.
    Hum. Mol. Genet. 6:69-76(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Strain: 129/Sv and BALB/c.
    Tissue: Brain.
  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].
    Strain: C57BL/6J.
    Tissue: Thymus.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-312.
    Strain: C57BL/6J.
    Tissue: Embryo.
  4. "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: INTERACTION WITH GNL3L AND TIN2.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Testis.
  6. "The TRF1-binding protein TERB1 promotes chromosome movement and telomere rigidity in meiosis."
    Shibuya H., Ishiguro K.I., Watanabe Y.
    Nat. Cell Biol. 16:145-156(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CCDC79.

Entry informationi

Entry nameiTERF1_MOUSE
AccessioniPrimary (citable) accession number: P70371
Secondary accession number(s): Q9CY71
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: June 8, 2016
This is version 148 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.