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Q9NUX5

- POTE1_HUMAN

UniProt

Q9NUX5 - POTE1_HUMAN

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Protein

Protection of telomeres protein 1

Gene
POT1
Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. DEAD/H-box RNA helicase binding Source: BHF-UCL
  2. protein binding Source: IntAct
  3. single-stranded telomeric DNA binding Source: UniProtKB
  4. telomerase inhibitor activity Source: BHF-UCL

GO - Biological processi

  1. DNA duplex unwinding Source: BHF-UCL
  2. negative regulation of telomerase activity Source: BHF-UCL
  3. negative regulation of telomere maintenance via telomerase Source: BHF-UCL
  4. positive regulation of DNA strand elongation Source: BHF-UCL
  5. positive regulation of helicase activity Source: BHF-UCL
  6. positive regulation of telomerase activity Source: BHF-UCL
  7. positive regulation of telomere maintenance via telomerase Source: BHF-UCL
  8. telomere capping Source: BHF-UCL
  9. telomere formation via telomerase Source: BHF-UCL
  10. telomere maintenance Source: Reactome
  11. telomere maintenance via telomerase Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_169185. DNA Damage/Telomere Stress Induced Senescence.
REACT_75792. Meiotic synapsis.
REACT_7963. Packaging Of Telomere Ends.

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
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:17284. POT1.

Subcellular locationi

Nucleus. Chromosometelomere
Note: Colocalizes with telomeric DNA.1 Publication

GO - Cellular componenti

  1. chromosome, telomeric region Source: UniProtKB
  2. cytoplasm Source: HPA
  3. nuclear telomere cap complex Source: BHF-UCL
  4. nucleoplasm Source: Reactome
  5. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus, Telomere

Pathology & Biotechi

Organism-specific databases

Orphaneti67038. B-cell chronic lymphocytic leukemia.
PharmGKBiPA134934904.

PTM / Processingi

Molecule processing

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

Proteomic databases

MaxQBiQ9NUX5.
PaxDbiQ9NUX5.
PRIDEiQ9NUX5.

PTM databases

PhosphoSiteiQ9NUX5.

Expressioni

Tissue specificityi

Ubiquitous.2 Publications

Gene expression databases

ArrayExpressiQ9NUX5.
BgeeiQ9NUX5.
CleanExiHS_POT1.
GenevestigatoriQ9NUX5.

Organism-specific databases

HPAiHPA051625.

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.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ACDQ96AP03EBI-752435,EBI-717666
TERF2Q155543EBI-752420,EBI-706637

Protein-protein interaction databases

BioGridi117417. 204 interactions.
DIPiDIP-29610N.
IntActiQ9NUX5. 28 interactions.
MINTiMINT-1466135.
STRINGi9606.ENSP00000350249.

Structurei

Secondary structure

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

3D structure databases

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

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.

Phylogenomic databases

eggNOGiNOG284004.
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.
IPR011564. Telomer_end-bd_POT1/Cdc13.
[Graphical view]
PANTHERiPTHR14513. PTHR14513. 1 hit.
PfamiPF02765. POT1. 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. Align

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

MSLVPATNYI YTPLNQLKGG TIVNVYGVVK FFKPPYLSKG TDYCSVVTIV    50
DQTNVKLTCL LFSGNYEALP IIYKNGDIVR FHRLKIQVYK KETQGITSSG 100
FASLTFEGTL GAPIIPRTSS KYFNFTTEDH KMVEALRVWA STHMSPSWTL 150
LKLCDVQPMQ YFDLTCQLLG KAEVDGASFL LKVWDGTRTP FPSWRVLIQD 200
LVLEGDLSHI HRLQNLTIDI LVYDNHVHVA RSLKVGSFLR IYSLHTKLQS 250
MNSENQTMLS LEFHLHGGTS YGRGIRVLPE SNSDVDQLKK DLESANLTAN 300
QHSDVICQSE PDDSFPSSGS VSLYEVERCQ QLSATILTDH QYLERTPLCA 350
ILKQKAPQQY RIRAKLRSYK PRRLFQSVKL HCPKCHLLQE VPHEGDLDII 400
FQDGATKTPD VKLQNTSLYD SKIWTTKNQK GRKVAVHFVK NNGILPLSNE 450
CLLLIEGGTL SEICKLSNKF NSVIPVRSGH EDLELLDLSA PFLIQGTIHH 500
YGCKQCSSLR SIQNLNSLVD KTSWIPSSVA EALGIVPLQY VFVMTFTLDD 550
GTGVLEAYLM DSDKFFQIPA SEVLMDDDLQ KSVDMIMDMF CPPGIKIDAY 600
PWLECFIKSY NVTNGTDNQI CYQIFDTTVA EDVI 634
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.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti529 – 5291V → M.
Corresponds to variant rs34973253 [ dbSNP | Ensembl ].
VAR_034393

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei532 – 5387ALGIVPL → DVNSVLV in isoform 2. VSP_010846
Alternative sequencei539 – 63496Missing in isoform 2. VSP_010847Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti410 – 4101D → V in BAA91568. 1 Publication
Sequence conflicti412 – 4121K → Q in BAB15404. 1 Publication
Sequence conflicti499 – 4991H → D in CAB43281. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_006715917.1. [Q9NUX5-1]
UniGeneiHs.31968.

Genome annotation databases

EnsembliENST00000357628; ENSP00000350249; ENSG00000128513. [Q9NUX5-1]
GeneIDi25913.
KEGGihsa:25913.
UCSCiuc003vlm.3. human. [Q9NUX5-1]

Polymorphism databases

DMDMi50401179.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS5793.1. [Q9NUX5-1 ]
PIRi T08766.
RefSeqi NP_001036059.1. NM_001042594.1.
NP_056265.2. NM_015450.2. [Q9NUX5-1 ]
XP_006715980.1. XM_006715917.1. [Q9NUX5-1 ]
UniGenei Hs.31968.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1XJV X-ray 1.73 A 6-299 [» ]
3KJO X-ray 1.80 A 1-299 [» ]
3KJP X-ray 1.80 A 1-299 [» ]
ProteinModelPortali Q9NUX5.
SMRi Q9NUX5. Positions 6-299.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117417. 204 interactions.
DIPi DIP-29610N.
IntActi Q9NUX5. 28 interactions.
MINTi MINT-1466135.
STRINGi 9606.ENSP00000350249.

Chemistry

BindingDBi Q9NUX5.
ChEMBLi CHEMBL5908.

PTM databases

PhosphoSitei Q9NUX5.

Polymorphism databases

DMDMi 50401179.

Proteomic databases

MaxQBi Q9NUX5.
PaxDbi Q9NUX5.
PRIDEi Q9NUX5.

Protocols and materials databases

DNASUi 25913.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000357628 ; ENSP00000350249 ; ENSG00000128513 . [Q9NUX5-1 ]
GeneIDi 25913.
KEGGi hsa:25913.
UCSCi uc003vlm.3. human. [Q9NUX5-1 ]

Organism-specific databases

CTDi 25913.
GeneCardsi GC07M124462.
HGNCi HGNC:17284. POT1.
HPAi HPA051625.
MIMi 606478. gene.
neXtProti NX_Q9NUX5.
Orphaneti 67038. B-cell chronic lymphocytic leukemia.
PharmGKBi PA134934904.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG284004.
HOGENOMi HOG000015271.
HOVERGENi HBG053641.
InParanoidi Q9NUX5.
KOi K11109.
OMAi DKTSWIP.
OrthoDBi EOG7N0C4C.
PhylomeDBi Q9NUX5.
TreeFami TF328398.

Enzyme and pathway databases

Reactomei REACT_169185. DNA Damage/Telomere Stress Induced Senescence.
REACT_75792. Meiotic synapsis.
REACT_7963. Packaging Of Telomere Ends.

Miscellaneous databases

EvolutionaryTracei Q9NUX5.
GeneWikii POT1.
GenomeRNAii 25913.
NextBioi 47408.
PROi Q9NUX5.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9NUX5.
Bgeei Q9NUX5.
CleanExi HS_POT1.
Genevestigatori Q9NUX5.

Family and domain databases

Gene3Di 2.40.50.140. 1 hit.
InterProi IPR012340. NA-bd_OB-fold.
IPR028389. POT1.
IPR011564. Telomer_end-bd_POT1/Cdc13.
[Graphical view ]
PANTHERi PTHR14513. PTHR14513. 1 hit.
Pfami PF02765. POT1. 1 hit.
[Graphical view ]
SMARTi SM00976. Telo_bind. 1 hit.
[Graphical view ]
SUPFAMi SSF50249. SSF50249. 2 hits.
ProtoNeti Search...

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. "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.

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: September 3, 2014
This is version 134 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

External Data

Dasty 3

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