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Protein

Protection of telomeres protein 1

Gene

POT1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the telomerase ribonucleoprotein (RNP) complex that is essential for the replication of chromosome termini. Is a component of the double-stranded telomeric DNA-binding TRF1 complex which is involved in the regulation of telomere length by cis-inhibition of telomerase. Also acts as a single-stranded telomeric DNA-binding protein and thus may act as a downstream effector of the TRF1 complex and may transduce information about telomere maintenance and/or length to the telomere terminus. 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. Binds to two or more telomeric single-stranded 5'-TTAGGG-3' repeats (G-strand) and with high specificity to a minimal telomeric single-stranded 5'-TAGGGTTAG-3' sequence. Binds telomeric single-stranded sequences internally or at proximity of a 3'-end. Its activity is TERT dependent but it does not increase TERT activity by itself. In contrast, the ACD-POT1 heterodimer enhances telomere elongation by increasing telomerase processivity.5 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei243 – 2431DNA binding

GO - Molecular functioni

  • DEAD/H-box RNA helicase binding Source: BHF-UCL
  • G-rich strand telomeric DNA binding Source: BHF-UCL
  • single-stranded telomeric DNA binding Source: UniProtKB
  • telomerase inhibitor activity Source: BHF-UCL
  • telomeric DNA binding Source: BHF-UCL

GO - Biological processi

  • DNA duplex unwinding Source: BHF-UCL
  • establishment of protein localization to telomere Source: BHF-UCL
  • negative regulation of telomerase activity Source: BHF-UCL
  • positive regulation of DNA strand elongation Source: BHF-UCL
  • positive regulation of helicase activity Source: BHF-UCL
  • positive regulation of telomerase activity Source: BHF-UCL
  • positive regulation of telomere maintenance via telomerase Source: BHF-UCL
  • telomere assembly Source: BHF-UCL
  • telomere capping Source: BHF-UCL
  • telomere maintenance via telomerase Source: UniProtKB
Complete GO annotation...

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.
SIGNORiQ9NUX5.

Names & Taxonomyi

Protein namesi
Recommended name:
Protection of telomeres protein 1
Short name:
hPot1
Alternative name(s):
POT1-like telomere end-binding protein
Gene namesi
Name:POT1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:17284. POT1.

Subcellular locationi

  • Nucleus 1 Publication
  • Chromosometelomere 1 Publication

  • Note: Colocalizes with telomeric DNA.

GO - Cellular componenti

  • chromosome, telomeric region Source: UniProtKB
  • nuclear chromosome, telomeric region Source: BHF-UCL
  • nuclear telomere cap complex Source: BHF-UCL
  • nucleoplasm Source: Reactome
  • nucleus Source: HPA
  • telosome Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus, Telomere

Pathology & Biotechi

Involvement in diseasei

Melanoma, cutaneous malignant 10 (CMM10)2 Publications
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA malignant neoplasm of melanocytes, arising de novo or from a pre-existing benign nevus, which occurs most often in the skin but also may involve other sites.
See also OMIM:615848
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti89 – 891Y → C in CMM10; complete abolition of POT1-DNA complex formation, thus disrupting the interaction with telomeres and leading to elongated telomeres. 1 Publication
Corresponds to variant rs587777472 [ dbSNP | Ensembl ].
VAR_071390
Natural varianti94 – 941Q → E in CMM10; complete abolition of POT1-DNA complex formation, thus disrupting the interaction with telomeres and leading to elongated telomeres. 1 Publication
Corresponds to variant rs587777474 [ dbSNP | Ensembl ].
VAR_071391
Natural varianti137 – 1371R → H in CMM10; increased telomere intensity signals and telomere fragility. 1 Publication
Corresponds to variant rs587777475 [ dbSNP | Ensembl ].
VAR_071392
Natural varianti224 – 2241D → N in CMM10. 1 Publication
Corresponds to variant rs202187871 [ dbSNP | Ensembl ].
VAR_071393
Natural varianti270 – 2701S → N in CMM10; significantly increased telomere length and numbers of fragile telomeres. 1 Publication
Corresponds to variant rs587777477 [ dbSNP | Ensembl ].
VAR_071394
Natural varianti273 – 2731R → L in CMM10; complete abolition of POT1-DNA complex formation, thus disrupting the interaction with telomeres and leading to elongated telomeres. 1 Publication
Corresponds to variant rs587777476 [ dbSNP | Ensembl ].
VAR_071395
Natural varianti532 – 5321A → P in CMM10. 1 Publication
VAR_071396
Natural varianti623 – 6231Q → H in CMM10; increased telomere intensity signals and telomere fragility. 1 Publication
Corresponds to variant rs587777478 [ dbSNP | Ensembl ].
VAR_071397
Glioma 9 (GLM9)1 Publication
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionGliomas are benign or malignant central nervous system neoplasms derived from glial cells. They comprise astrocytomas and glioblastoma multiforme that are derived from astrocytes, oligodendrogliomas derived from oligodendrocytes and ependymomas derived from ependymocytes.
See also OMIM:616568
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti95 – 951G → C in GLM9. 1 Publication
VAR_075717

Keywords - Diseasei

Disease mutation

Organism-specific databases

MalaCardsiPOT1.
MIMi615848. phenotype.
616568. phenotype.
Orphaneti67038. B-cell chronic lymphocytic leukemia.
618. Familial melanoma.
PharmGKBiPA134934904.

Chemistry

ChEMBLiCHEMBL5908.

Polymorphism and mutation databases

BioMutaiPOT1.
DMDMi50401179.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 634634Protection of telomeres protein 1PRO_0000121728Add
BLAST

Proteomic databases

EPDiQ9NUX5.
MaxQBiQ9NUX5.
PaxDbiQ9NUX5.
PeptideAtlasiQ9NUX5.
PRIDEiQ9NUX5.

PTM databases

iPTMnetiQ9NUX5.
PhosphoSiteiQ9NUX5.

Expressioni

Tissue specificityi

Ubiquitous.2 Publications

Gene expression databases

BgeeiQ9NUX5.
CleanExiHS_POT1.
ExpressionAtlasiQ9NUX5. baseline and differential.
GenevisibleiQ9NUX5. HS.

Interactioni

Subunit structurei

Homodimer or homooligomer. Component of the shelterin complex (telosome) composed of TERF1, TERF2, TINF2, TERF2IP, ACD and POT1. Binds single-stranded telomeric DNA as a monomer (By similarity). Component of the telomerase holoenzyme complex at least composed of TERT, DKC1, WRAP53/TCAB1, NOP10, NHP2, GAR1, TEP1, EST1A, POT1 and a telomerase RNA template component (TERC). Found in a complex with TERF1, TINF2 and TNKS1. Interacts with TNKS1. Forms heterodimers with ACD. Identified in a complex with ACD and single-stranded telomeric DNA.By similarity7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ACDQ96AP07EBI-752420,EBI-717666
ALDH3A1P308382EBI-752420,EBI-3905126
ANXA2P073552EBI-752420,EBI-352622
C15orf57Q9BV292EBI-752420,EBI-2874058
CFL2Q549N03EBI-752420,EBI-10201319
CLIC3O958332EBI-752420,EBI-10192241
CNSTQ6PJW82EBI-752420,EBI-750390
DOK2O604962EBI-752420,EBI-1046024
GFPT2O948082EBI-752420,EBI-6916534
GPA33Q997952EBI-752420,EBI-4289554
HAAOP469522EBI-752420,EBI-743215
HLCSP507472EBI-752420,EBI-3915568
HMOX1P096012EBI-752420,EBI-2806151
HSPA1AP0DMV82EBI-752420,EBI-11052499
ISYNA1Q9NPH22EBI-752420,EBI-720563
KIAA1191Q96A732EBI-752420,EBI-725897
MADDQ8WXG62EBI-752420,EBI-310528
MAGEA4P433582EBI-752420,EBI-743122
MAP4K2Q128512EBI-752420,EBI-49783
MVKQ034262EBI-752420,EBI-740630
PACSIN1Q9BY112EBI-752420,EBI-721769
PAGE5Q96GU12EBI-752420,EBI-11305258
PDE1BQ010642EBI-752420,EBI-7413304
PHYHD1Q5SRE72EBI-752420,EBI-2623130
PHYKPLQ8IUZ52EBI-752420,EBI-751947
PIPOXQ9P0Z92EBI-752420,EBI-725582
PROSER2Q86WR72EBI-752420,EBI-2880603
PYM1Q9BRP82EBI-752420,EBI-2352802
RPAP1Q9BWH62EBI-752420,EBI-1048085
SULT1B1O437042EBI-752420,EBI-10179062
SULT4A1Q9BR012EBI-752420,EBI-6690555
SYAP1Q96A492EBI-752420,EBI-10770179
TERF2Q155544EBI-752420,EBI-706637
TINF2Q9BSI43EBI-752420,EBI-717399
TMSB10P633132EBI-752420,EBI-2688673
WIPI2Q9Y4P82EBI-752420,EBI-719396

GO - Molecular functioni

  • DEAD/H-box RNA helicase binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi117417. 213 interactions.
DIPiDIP-29610N.
IntActiQ9NUX5. 176 interactions.
MINTiMINT-1466135.
STRINGi9606.ENSP00000350249.

Chemistry

BindingDBiQ9NUX5.

Structurei

Secondary structure

1
634
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi14 – 163Combined sources
Beta strandi19 – 3719Combined sources
Beta strandi39 – 5012Combined sources
Beta strandi56 – 6510Combined sources
Helixi66 – 683Combined sources
Beta strandi78 – 8912Combined sources
Beta strandi92 – 10615Combined sources
Helixi127 – 14317Combined sources
Helixi153 – 1553Combined sources
Beta strandi161 – 17313Combined sources
Beta strandi175 – 18410Combined sources
Turni200 – 2023Combined sources
Helixi207 – 2137Combined sources
Helixi214 – 2163Combined sources
Beta strandi217 – 2237Combined sources
Helixi226 – 2327Combined sources
Beta strandi238 – 25114Combined sources
Beta strandi257 – 2659Combined sources
Helixi270 – 2723Combined sources
Beta strandi274 – 2785Combined sources
Helixi283 – 29715Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XJVX-ray1.73A6-299[»]
3KJOX-ray1.80A1-299[»]
3KJPX-ray1.80A1-299[»]
ProteinModelPortaliQ9NUX5.
SMRiQ9NUX5. Positions 6-299.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NUX5.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni33 – 4816DNA bindingAdd
BLAST
Regioni270 – 2734DNA binding

Sequence similaritiesi

Belongs to the telombin family.Curated

Phylogenomic databases

eggNOGiKOG4757. Eukaryota.
ENOG410Z1J0. LUCA.
GeneTreeiENSGT00390000018285.
HOGENOMiHOG000015271.
HOVERGENiHBG053641.
InParanoidiQ9NUX5.
KOiK11109.
OMAiDKTSWIP.
OrthoDBiEOG7N0C4C.
PhylomeDBiQ9NUX5.
TreeFamiTF328398.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
InterProiIPR012340. NA-bd_OB-fold.
IPR028389. POT1.
IPR032042. POT1PC.
IPR011564. Telomer_end-bd_POT1/Cdc13.
[Graphical view]
PANTHERiPTHR14513. PTHR14513. 1 hit.
PfamiPF02765. POT1. 1 hit.
PF16686. POT1PC. 1 hit.
[Graphical view]
SMARTiSM00976. Telo_bind. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 2 hits.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Note: A number of isoforms are produced.

Isoform 1 (identifier: Q9NUX5-1) [UniParc]FASTAAdd to basket

Also known as: Variant 1

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
MSLVPATNYI YTPLNQLKGG TIVNVYGVVK FFKPPYLSKG TDYCSVVTIV
60 70 80 90 100
DQTNVKLTCL LFSGNYEALP IIYKNGDIVR FHRLKIQVYK KETQGITSSG
110 120 130 140 150
FASLTFEGTL GAPIIPRTSS KYFNFTTEDH KMVEALRVWA STHMSPSWTL
160 170 180 190 200
LKLCDVQPMQ YFDLTCQLLG KAEVDGASFL LKVWDGTRTP FPSWRVLIQD
210 220 230 240 250
LVLEGDLSHI HRLQNLTIDI LVYDNHVHVA RSLKVGSFLR IYSLHTKLQS
260 270 280 290 300
MNSENQTMLS LEFHLHGGTS YGRGIRVLPE SNSDVDQLKK DLESANLTAN
310 320 330 340 350
QHSDVICQSE PDDSFPSSGS VSLYEVERCQ QLSATILTDH QYLERTPLCA
360 370 380 390 400
ILKQKAPQQY RIRAKLRSYK PRRLFQSVKL HCPKCHLLQE VPHEGDLDII
410 420 430 440 450
FQDGATKTPD VKLQNTSLYD SKIWTTKNQK GRKVAVHFVK NNGILPLSNE
460 470 480 490 500
CLLLIEGGTL SEICKLSNKF NSVIPVRSGH EDLELLDLSA PFLIQGTIHH
510 520 530 540 550
YGCKQCSSLR SIQNLNSLVD KTSWIPSSVA EALGIVPLQY VFVMTFTLDD
560 570 580 590 600
GTGVLEAYLM DSDKFFQIPA SEVLMDDDLQ KSVDMIMDMF CPPGIKIDAY
610 620 630
PWLECFIKSY NVTNGTDNQI CYQIFDTTVA EDVI
Length:634
Mass (Da):71,442
Last modified:October 1, 2000 - v1
Checksum:i123A12CABE708C91
GO
Isoform 2 (identifier: Q9NUX5-2) [UniParc]FASTAAdd to basket

Also known as: Variant 3

The sequence of this isoform differs from the canonical sequence as follows:
     532-538: ALGIVPL → DVNSVLV
     539-634: Missing.

Show »
Length:538
Mass (Da):60,534
Checksum:i7D04F3ECC01D448D
GO

Sequence cautioni

The sequence BAB15404.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti410 – 4101D → V in BAA91568 (PubMed:14702039).Curated
Sequence conflicti412 – 4121K → Q in BAB15404 (PubMed:14702039).Curated
Sequence conflicti499 – 4991H → D in CAB43281 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti89 – 891Y → C in CMM10; complete abolition of POT1-DNA complex formation, thus disrupting the interaction with telomeres and leading to elongated telomeres. 1 Publication
Corresponds to variant rs587777472 [ dbSNP | Ensembl ].
VAR_071390
Natural varianti94 – 941Q → E in CMM10; complete abolition of POT1-DNA complex formation, thus disrupting the interaction with telomeres and leading to elongated telomeres. 1 Publication
Corresponds to variant rs587777474 [ dbSNP | Ensembl ].
VAR_071391
Natural varianti95 – 951G → C in GLM9. 1 Publication
VAR_075717
Natural varianti137 – 1371R → H in CMM10; increased telomere intensity signals and telomere fragility. 1 Publication
Corresponds to variant rs587777475 [ dbSNP | Ensembl ].
VAR_071392
Natural varianti224 – 2241D → N in CMM10. 1 Publication
Corresponds to variant rs202187871 [ dbSNP | Ensembl ].
VAR_071393
Natural varianti270 – 2701S → N in CMM10; significantly increased telomere length and numbers of fragile telomeres. 1 Publication
Corresponds to variant rs587777477 [ dbSNP | Ensembl ].
VAR_071394
Natural varianti273 – 2731R → L in CMM10; complete abolition of POT1-DNA complex formation, thus disrupting the interaction with telomeres and leading to elongated telomeres. 1 Publication
Corresponds to variant rs587777476 [ dbSNP | Ensembl ].
VAR_071395
Natural varianti529 – 5291V → M.
Corresponds to variant rs34973253 [ dbSNP | Ensembl ].
VAR_034393
Natural varianti532 – 5321A → P in CMM10. 1 Publication
VAR_071396
Natural varianti623 – 6231Q → H in CMM10; increased telomere intensity signals and telomere fragility. 1 Publication
Corresponds to variant rs587777478 [ dbSNP | Ensembl ].
VAR_071397

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei532 – 5387ALGIVPL → DVNSVLV in isoform 2. CuratedVSP_010846
Alternative sequencei539 – 63496Missing in isoform 2. CuratedVSP_010847Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY823520 mRNA. Translation: AAW22613.1.
AK001230 mRNA. Translation: BAA91568.1.
AK001935 mRNA. Translation: BAA91988.1.
AK022580 mRNA. Translation: BAB14110.1.
AK026234 mRNA. Translation: BAB15404.1. Different initiation.
AC004925 Genomic DNA. Translation: AAD08852.1.
AC096665 Genomic DNA. No translation available.
AC110791 Genomic DNA. No translation available.
CH471070 Genomic DNA. Translation: EAW83616.1.
BC002923 mRNA. Translation: AAH02923.1.
AL050120 mRNA. Translation: CAB43281.1.
CCDSiCCDS5793.1. [Q9NUX5-1]
PIRiT08766.
RefSeqiNP_001036059.1. NM_001042594.1.
NP_056265.2. NM_015450.2. [Q9NUX5-1]
XP_006715980.1. XM_006715917.2. [Q9NUX5-1]
UniGeneiHs.31968.

Genome annotation databases

EnsembliENST00000357628; ENSP00000350249; ENSG00000128513. [Q9NUX5-1]
GeneIDi25913.
KEGGihsa:25913.
UCSCiuc003vlm.4. human. [Q9NUX5-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY823520 mRNA. Translation: AAW22613.1.
AK001230 mRNA. Translation: BAA91568.1.
AK001935 mRNA. Translation: BAA91988.1.
AK022580 mRNA. Translation: BAB14110.1.
AK026234 mRNA. Translation: BAB15404.1. Different initiation.
AC004925 Genomic DNA. Translation: AAD08852.1.
AC096665 Genomic DNA. No translation available.
AC110791 Genomic DNA. No translation available.
CH471070 Genomic DNA. Translation: EAW83616.1.
BC002923 mRNA. Translation: AAH02923.1.
AL050120 mRNA. Translation: CAB43281.1.
CCDSiCCDS5793.1. [Q9NUX5-1]
PIRiT08766.
RefSeqiNP_001036059.1. NM_001042594.1.
NP_056265.2. NM_015450.2. [Q9NUX5-1]
XP_006715980.1. XM_006715917.2. [Q9NUX5-1]
UniGeneiHs.31968.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XJVX-ray1.73A6-299[»]
3KJOX-ray1.80A1-299[»]
3KJPX-ray1.80A1-299[»]
ProteinModelPortaliQ9NUX5.
SMRiQ9NUX5. Positions 6-299.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117417. 213 interactions.
DIPiDIP-29610N.
IntActiQ9NUX5. 176 interactions.
MINTiMINT-1466135.
STRINGi9606.ENSP00000350249.

Chemistry

BindingDBiQ9NUX5.
ChEMBLiCHEMBL5908.

PTM databases

iPTMnetiQ9NUX5.
PhosphoSiteiQ9NUX5.

Polymorphism and mutation databases

BioMutaiPOT1.
DMDMi50401179.

Proteomic databases

EPDiQ9NUX5.
MaxQBiQ9NUX5.
PaxDbiQ9NUX5.
PeptideAtlasiQ9NUX5.
PRIDEiQ9NUX5.

Protocols and materials databases

DNASUi25913.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000357628; ENSP00000350249; ENSG00000128513. [Q9NUX5-1]
GeneIDi25913.
KEGGihsa:25913.
UCSCiuc003vlm.4. human. [Q9NUX5-1]

Organism-specific databases

CTDi25913.
GeneCardsiPOT1.
HGNCiHGNC:17284. POT1.
MalaCardsiPOT1.
MIMi606478. gene.
615848. phenotype.
616568. phenotype.
neXtProtiNX_Q9NUX5.
Orphaneti67038. B-cell chronic lymphocytic leukemia.
618. Familial melanoma.
PharmGKBiPA134934904.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4757. Eukaryota.
ENOG410Z1J0. LUCA.
GeneTreeiENSGT00390000018285.
HOGENOMiHOG000015271.
HOVERGENiHBG053641.
InParanoidiQ9NUX5.
KOiK11109.
OMAiDKTSWIP.
OrthoDBiEOG7N0C4C.
PhylomeDBiQ9NUX5.
TreeFamiTF328398.

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.
SIGNORiQ9NUX5.

Miscellaneous databases

EvolutionaryTraceiQ9NUX5.
GeneWikiiPOT1.
GenomeRNAii25913.
PROiQ9NUX5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NUX5.
CleanExiHS_POT1.
ExpressionAtlasiQ9NUX5. baseline and differential.
GenevisibleiQ9NUX5. HS.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
InterProiIPR012340. NA-bd_OB-fold.
IPR028389. POT1.
IPR032042. POT1PC.
IPR011564. Telomer_end-bd_POT1/Cdc13.
[Graphical view]
PANTHERiPTHR14513. PTHR14513. 1 hit.
PfamiPF02765. POT1. 1 hit.
PF16686. POT1PC. 1 hit.
[Graphical view]
SMARTiSM00976. Telo_bind. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Pot1, the putative telomere end-binding protein in fission yeast and humans."
    Baumann P., Cech T.R.
    Science 292:1171-1175(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SINGLE-STRANDED TELOMERE DNA-BINDING.
    Tissue: Ovary.
  2. "Human Pot1 (protection of telomeres) protein: cytolocalization, gene structure, and alternative splicing."
    Baumann P., Podell E., Cech T.R.
    Mol. Cell. Biol. 22:8079-8087(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, SINGLE-STRANDED TELOMERE DNA-BINDING.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Placenta, Small intestine and Teratocarcinoma.
  4. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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 1).
    Tissue: Skin.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 499-634 (ISOFORM 1).
    Tissue: Uterus.
  8. "Human POT1 facilitates telomere elongation by telomerase."
    Colgin L.M., Baran K., Baumann P., Cech T.R., Reddel R.R.
    Curr. Biol. 13:942-946(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TELOMERE REGULATION, ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), SINGLE-STRANDED TELOMERE DNA-BINDING.
  9. "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: FUNCTION IN TELOMERE REGULATION, IDENTIFICATION IN A COMPLEX WITH TERF1; TINF2 AND TNKS1, INTERACTION WITH TNKS1.
  10. "DNA binding features of human POT1: a nonamer 5'-TAGGGTTAG-3' minimal binding site, sequence specificity, and internal binding to multimeric sites."
    Loayza D., Parsons H., Donigian J., Hoke K., de Lange T.
    J. Biol. Chem. 279:13241-13248(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SINGLE-STRANDED TELOMERE DNA-BINDING.
  11. "POT1-interacting protein PIP1: a telomere length regulator that recruits POT1 to the TIN2/TRF1 complex."
    Ye J.Z.-S., Hockemeyer D., Krutchinsky A.N., Loayza D., Hooper S.M., Chait B.T., de Lange T.
    Genes Dev. 18:1649-1654(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ACD.
  12. "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.
  13. "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.
  14. "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.
  15. "The POT1-TPP1 telomere complex is a telomerase processivity factor."
    Wang F., Podell E.R., Zaug A.J., Yang Y., Baciu P., Cech T.R., Lei M.
    Nature 445:506-510(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, IDENTIFICATION IN A COMPLEX WITH ACD AND SINGLE-STRANDED TELOMERIC DNA.
  16. "A human telomerase holoenzyme protein required for Cajal body localization and telomere synthesis."
    Venteicher A.S., Abreu E.B., Meng Z., McCann K.E., Terns R.M., Veenstra T.D., Terns M.P., Artandi S.E.
    Science 323:644-648(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE TELOMERASE HOLOENZYME COMPLEX.
  17. "Functional interaction between telomere protein TPP1 and telomerase."
    Zaug A.J., Podell E.R., Nandakumar J., Cech T.R.
    Genes Dev. 24:613-622(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  18. Cited for: INVOLVEMENT IN GLM9, VARIANT GLM9 CYS-95.
  19. "Structure of human POT1 bound to telomeric single-stranded DNA provides a model for chromosome end-protection."
    Lei M., Podell E.R., Cech T.R.
    Nat. Struct. Mol. Biol. 11:1223-1229(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 6-299 IN COMPLEX WITH SINGLE-STRANDED TELOMERIC DNA.
  20. Cited for: INVOLVEMENT IN CMM10, VARIANTS CMM10 CYS-89; GLU-94 AND LEU-273, CHARACTERIZATION OF VARIANTS CMM10 CYS-89; GLU-94 AND LEU-273.
  21. Cited for: VARIANTS CMM10 HIS-137; ASN-224; ASN-270; PRO-532 AND HIS-623, CHARACTERIZATION OF VARIANTS CMM10 HIS-137; ASN-270 AND HIS-623.

Entry informationi

Entry nameiPOTE1_HUMAN
AccessioniPrimary (citable) accession number: Q9NUX5
Secondary accession number(s): O95018
, Q5MJ36, Q9H662, Q9NW19, Q9UG95
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: October 1, 2000
Last modified: July 6, 2016
This is version 154 of the entry and version 1 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, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.