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Protein

Telomeric repeat-binding factor 1

Gene

TERF1

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 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 motifPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • DNA binding Source: UniProtKB
  • DNA binding, bending Source: BHF-UCL
  • double-stranded telomeric DNA binding Source: UniProtKB
  • G-rich strand telomeric DNA binding Source: BHF-UCL
  • microtubule binding Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • telomeric DNA binding Source: BHF-UCL
  • ubiquitin binding Source: BHF-UCL

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • G2/M transition of mitotic cell cycle Source: UniProtKB
  • meiotic telomere clustering Source: Ensembl
  • mitotic nuclear division Source: UniProtKB-KW
  • mitotic spindle assembly checkpoint Source: UniProtKB
  • negative regulation of DNA replication Source: BHF-UCL
  • negative regulation of establishment of macromolecular complex localization to telomere Source: BHF-UCL
  • negative regulation of establishment of protein localization to telomere Source: BHF-UCL
  • negative regulation of establishment of RNA localization to telomere Source: BHF-UCL
  • negative regulation of telomerase activity Source: BHF-UCL
  • negative regulation of telomere maintenance via semi-conservative replication Source: BHF-UCL
  • negative regulation of telomere maintenance via telomerase Source: BHF-UCL
  • positive regulation of apoptotic process Source: UniProtKB
  • positive regulation of microtubule polymerization Source: UniProtKB
  • positive regulation of mitotic cell cycle Source: UniProtKB
  • positive regulation of mitotic nuclear division Source: UniProtKB
  • positive regulation of telosome assembly Source: BHF-UCL
  • protein homooligomerization Source: UniProtKB
  • response to drug Source: Ensembl
  • telomere capping Source: Reactome
  • telomere maintenance Source: BHF-UCL
  • telomere maintenance via telomerase Source: UniProtKB
  • telomeric loop formation Source: GO_Central
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-1221632. Meiotic synapsis.
R-HSA-171306. Packaging Of Telomere Ends.
R-HSA-2559586. DNA Damage/Telomere Stress Induced Senescence.
SIGNORiP54274.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:11728. TERF1.

Subcellular locationi

GO - Cellular componenti

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

Polymorphism and mutation databases

BioMutaiTERF1.
DMDMi206729904.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 439438Telomeric repeat-binding factor 1PRO_0000197129Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei11 – 111PhosphoserineCombined sources
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

EPDiP54274.
MaxQBiP54274.
PaxDbiP54274.
PeptideAtlasiP54274.
PRIDEiP54274.

PTM databases

iPTMnetiP54274.
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

BgeeiENSG00000147601.
CleanExiHS_TERF1.
ExpressionAtlasiP54274. baseline and differential.
GenevisibleiP54274. HS.

Organism-specific databases

HPAiHPA048379.
HPA056046.

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).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
ACAT2Q9BWD12EBI-710997,EBI-1047273
ACY1Q031542EBI-710997,EBI-742064
AMPD2Q014332EBI-710997,EBI-8796759
AMPHP494182EBI-710997,EBI-7121510
ATMQ133155EBI-711018,EBI-495465
BLMP541323EBI-710997,EBI-621372
C12orf43Q96C572EBI-710997,EBI-11305571
CEP85Q6P2H32EBI-710997,EBI-2808308
CORO1BQ9BR762EBI-710997,EBI-351152
CRYBB1P536742EBI-710997,EBI-7519424
CRYMQ148942EBI-710997,EBI-7107048
DDX19BQ9UMR22EBI-710997,EBI-719232
DDX23Q9BUQ82EBI-710997,EBI-540096
DDX39AO001482EBI-710997,EBI-348253
DNAJB1P256852EBI-710997,EBI-357034
DNPH1O435982EBI-710997,EBI-748674
EPB41L1Q9H4G02EBI-710997,EBI-465536
FBXO4Q9UKT5-13EBI-711018,EBI-960421
FESP073322EBI-710997,EBI-1055635
GSSP486372EBI-710997,EBI-2969145
HCLS1P143172EBI-710997,EBI-750369
HEXIM2Q96MH22EBI-710997,EBI-5460660
HGDQ930992EBI-710997,EBI-3907760
HSPA6P170662EBI-710997,EBI-355106
KEAP1Q141452EBI-710997,EBI-751001
KLHDC4Q8TBB52EBI-710997,EBI-8472352
LDHBP071952EBI-710997,EBI-358748
LRSAM1Q6UWE02EBI-710997,EBI-720984
MAPRE1Q156912EBI-710997,EBI-1004115
MDH1P409252EBI-710997,EBI-709625
MMTAG2Q9BU762EBI-710997,EBI-742459
MSNP260382EBI-710997,EBI-528768
NAP1L1P552092EBI-710997,EBI-356392
NEFLP071962EBI-710997,EBI-475646
NOL12Q9UGY12EBI-710997,EBI-716098
PACSIN2Q9UNF02EBI-710997,EBI-742503
PAK4O960132EBI-710997,EBI-713738
PEPDP129552EBI-710997,EBI-948765
PINX1Q96BK52EBI-710997,EBI-721782
PPM1GO153552EBI-710997,EBI-725702
PRDX1Q068302EBI-710997,EBI-353193
PRDX6P300412EBI-710997,EBI-2255129
PTPN5P548292EBI-710997,EBI-1220572
RBMY1A1P0DJD32EBI-710997,EBI-8638511
RECQL4O947612EBI-710997,EBI-722861
RNF10Q8N5U62EBI-710997,EBI-714023
RPAP3Q9H6T32EBI-710997,EBI-356928
RPL19P840982EBI-710997,EBI-916524
RTN3O951972EBI-710997,EBI-740467
RYDENQ9NUL52EBI-710997,EBI-10313866
SH3BP1Q9Y3L32EBI-710997,EBI-346869
SNCGO760702EBI-710997,EBI-1053810
SOAT1P356102EBI-710997,EBI-6621955
SRMP196232EBI-710997,EBI-1056183
STAG1Q8WVM74EBI-710997,EBI-1175097
SUPT5HO002672EBI-710997,EBI-710464
SYKP434052EBI-710997,EBI-78302
THG1LQ9NWX62EBI-710997,EBI-746510
TINF2Q9BSI48EBI-710997,EBI-717399
TKTP294012EBI-710997,EBI-1050560
TNKSO952714EBI-710997,EBI-1105254
TNKS2Q9H2K22EBI-710997,EBI-4398527
TNPO2O147872EBI-710997,EBI-431907
TPI1P601742EBI-710997,EBI-717475
TRMT1Q9NXH92EBI-710997,EBI-748900
TUBB3Q135092EBI-710997,EBI-350989
WARSP233812EBI-710997,EBI-721244
WFS1O760242EBI-710997,EBI-720609

GO - Molecular functioni

  • microtubule binding Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • ubiquitin binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi112872. 309 interactions.
DIPiDIP-29412N.
IntActiP54274. 206 interactions.
MINTiMINT-221323.
STRINGi9606.ENSP00000276603.

Structurei

Secondary structure

1
439
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi63 – 9230Combined sources
Helixi95 – 11016Combined sources
Beta strandi113 – 1153Combined sources
Helixi117 – 13317Combined sources
Turni134 – 1363Combined sources
Beta strandi143 – 1453Combined sources
Helixi150 – 1589Combined sources
Helixi167 – 18620Combined sources
Helixi190 – 20011Combined sources
Beta strandi203 – 2053Combined sources
Helixi211 – 2199Combined sources
Helixi226 – 2305Combined sources
Helixi233 – 25119Combined sources
Beta strandi252 – 2543Combined sources
Helixi255 – 26511Combined sources
Beta strandi377 – 3793Combined sources
Helixi385 – 39814Combined sources
Helixi403 – 4097Combined sources
Helixi417 – 42812Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
5HKPX-ray2.20C/D1-55[»]
ProteinModelPortaliP54274.
SMRiP54274. Positions 64-266, 373-439.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP54274.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini375 – 43258HTH myb-typePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni58 – 268211TRFH dimerizationAdd
BLAST
Regioni265 – 378114Interaction with RLIMAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi337 – 35620Nuclear localization signalSequence analysisAdd
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

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

Phylogenomic databases

eggNOGiENOG410IIKA. Eukaryota.
ENOG4111QH9. LUCA.
GeneTreeiENSGT00530000063796.
HOGENOMiHOG000132847.
HOVERGENiHBG054097.
InParanoidiP54274.
KOiK11110.
OMAiQKAWLWE.
OrthoDBiEOG091G04CC.
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.
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]

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. AlignAdd to basket

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

        10         20         30         40         50
MAEDVSSAAP SPRGCADGRD ADPTEEQMAE TERNDEEQFE CQELLECQVQ
60 70 80 90 100
VGAPEEEEEE EEDAGLVAEA EAVAAGWMLD FLCLSLCRAF RDGRSEDFRR
110 120 130 140 150
TRNSAEAIIH GLSSLTACQL RTIYICQFLT RIAAGKTLDA QFENDERITP
160 170 180 190 200
LESALMIWGS IEKEHDKLHE EIQNLIKIQA IAVCMENGNF KEAEEVFERI
210 220 230 240 250
FGDPNSHMPF KSKLLMIISQ KDTFHSFFQH FSYNHMMEKI KSYVNYVLSE
260 270 280 290 300
KSSTFLMKAA AKVVESKRTR TITSQDKPSG NDVEMETEAN LDTRKSVSDK
310 320 330 340 350
QSAVTESSEG TVSLLRSHKN LFLSKLQHGT QQQDLNKKER RVGTPQSTKK
360 370 380 390 400
KKESRRATES RIPVSKSQPV TPEKHRARKR QAWLWEEDKN LRSGVRKYGE
410 420 430
GNWSKILLHY KFNNRTSVML KDRWRTMKKL KLISSDSED
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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 141G → R in AAB54036 (PubMed:7502076).Curated
Sequence conflicti14 – 141G → R in AAB17975 (PubMed:9326950).Curated
Sequence conflicti14 – 141G → R in AAB81137 (PubMed:9326950).Curated
Sequence conflicti14 – 141G → R in AAB53363 (PubMed:9391075).Curated
Sequence conflicti338 – 3381K → E in CAA63768 (PubMed:8614633).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei296 – 31520Missing in isoform 2. 3 PublicationsVSP_003303Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.3. human. [P54274-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

NIEHS SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
5HKPX-ray2.20C/D1-55[»]
ProteinModelPortaliP54274.
SMRiP54274. Positions 64-266, 373-439.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112872. 309 interactions.
DIPiDIP-29412N.
IntActiP54274. 206 interactions.
MINTiMINT-221323.
STRINGi9606.ENSP00000276603.

PTM databases

iPTMnetiP54274.
PhosphoSiteiP54274.

Polymorphism and mutation databases

BioMutaiTERF1.
DMDMi206729904.

Proteomic databases

EPDiP54274.
MaxQBiP54274.
PaxDbiP54274.
PeptideAtlasiP54274.
PRIDEiP54274.

Protocols and materials databases

DNASUi7013.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000276602; ENSP00000276602; ENSG00000147601. [P54274-2]
ENST00000276603; ENSP00000276603; ENSG00000147601. [P54274-1]
GeneIDi7013.
KEGGihsa:7013.
UCSCiuc003xzd.3. human. [P54274-1]

Organism-specific databases

CTDi7013.
GeneCardsiTERF1.
H-InvDBHIX0007582.
HGNCiHGNC:11728. TERF1.
HPAiHPA048379.
HPA056046.
MIMi600951. gene.
neXtProtiNX_P54274.
PharmGKBiPA36445.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IIKA. Eukaryota.
ENOG4111QH9. LUCA.
GeneTreeiENSGT00530000063796.
HOGENOMiHOG000132847.
HOVERGENiHBG054097.
InParanoidiP54274.
KOiK11110.
OMAiQKAWLWE.
OrthoDBiEOG091G04CC.
PhylomeDBiP54274.
TreeFamiTF333209.

Enzyme and pathway databases

ReactomeiR-HSA-1221632. Meiotic synapsis.
R-HSA-171306. Packaging Of Telomere Ends.
R-HSA-2559586. DNA Damage/Telomere Stress Induced Senescence.
SIGNORiP54274.

Miscellaneous databases

ChiTaRSiTERF1. human.
EvolutionaryTraceiP54274.
GeneWikiiTERF1.
GenomeRNAii7013.
PROiP54274.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000147601.
CleanExiHS_TERF1.
ExpressionAtlasiP54274. baseline and differential.
GenevisibleiP54274. 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.
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...

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 7, 2016
This is version 188 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

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.