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Q9NUX5 (POTE1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protection of telomeres protein 1

Short name=hPot1
Alternative name(s):
POT1-like telomere end-binding protein
Gene names
Name:POT1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length634 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8 Ref.9 Ref.14 Ref.15 Ref.17

Subunit structure

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. Ref.9 Ref.11 Ref.12 Ref.13 Ref.15 Ref.16

Subcellular location

Nucleus. Chromosometelomere. Note: Colocalizes with telomeric DNA. Ref.2

Tissue specificity

Ubiquitous. Ref.1 Ref.2

Sequence similarities

Belongs to the telombin family.

Sequence caution

The sequence BAB15404.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentChromosome
Nucleus
Telomere
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandDNA-binding
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA duplex unwinding

Inferred from direct assay PubMed 16030011. Source: BHF-UCL

negative regulation of telomerase activity

Inferred from direct assay PubMed 15632080. Source: BHF-UCL

negative regulation of telomere maintenance via telomerase

Inferred from mutant phenotype PubMed 15181449. Source: BHF-UCL

positive regulation of DNA strand elongation

Inferred from direct assay PubMed 16043710. Source: BHF-UCL

positive regulation of helicase activity

Inferred from direct assay PubMed 16030011. Source: BHF-UCL

positive regulation of telomerase activity

Inferred from direct assay PubMed 16043710Ref.15. Source: BHF-UCL

positive regulation of telomere maintenance via telomerase

Inferred from mutant phenotype Ref.9Ref.8. Source: BHF-UCL

telomere capping

Inferred from mutant phenotype PubMed 15657433. Source: BHF-UCL

telomere formation via telomerase

Inferred from direct assay PubMed 16043710. Source: BHF-UCL

telomere maintenance

Traceable author statement. Source: Reactome

telomere maintenance via telomerase

Inferred from direct assay Ref.9. Source: UniProtKB

   Cellular_componentchromosome, telomeric region

Inferred from direct assay Ref.9. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

nuclear telomere cap complex

Inferred from direct assay PubMed 16880378. Source: BHF-UCL

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionDEAD/H-box RNA helicase binding

Inferred from physical interaction PubMed 16030011. Source: BHF-UCL

protein binding

Inferred from physical interaction Ref.11. Source: IntAct

single-stranded telomeric DNA binding

Inferred from mutant phenotype Ref.9. Source: UniProtKB

telomerase inhibitor activity

Inferred from direct assay PubMed 15632080. Source: BHF-UCL

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Note: A number of isoforms are produced.
Isoform 1 (identifier: Q9NUX5-1)

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.
Isoform 2 (identifier: Q9NUX5-2)

Also known as: Variant 3;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 634634Protection of telomeres protein 1
PRO_0000121728

Regions

Region33 – 4816DNA binding
Region270 – 2734DNA binding

Sites

Site2431DNA binding

Natural variations

Alternative sequence532 – 5387ALGIVPL → DVNSVLV in isoform 2.
VSP_010846
Alternative sequence539 – 63496Missing in isoform 2.
VSP_010847
Natural variant5291V → M.
Corresponds to variant rs34973253 [ dbSNP | Ensembl ].
VAR_034393

Experimental info

Sequence conflict4101D → V in BAA91568. Ref.3
Sequence conflict4121K → Q in BAB15404. Ref.3
Sequence conflict4991H → D in CAB43281. Ref.7

Secondary structure

........................................ 634
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Variant 1) [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 123A12CABE708C91

FASTA63471,442
        10         20         30         40         50         60 
MSLVPATNYI YTPLNQLKGG TIVNVYGVVK FFKPPYLSKG TDYCSVVTIV DQTNVKLTCL 

        70         80         90        100        110        120 
LFSGNYEALP IIYKNGDIVR FHRLKIQVYK KETQGITSSG FASLTFEGTL GAPIIPRTSS 

       130        140        150        160        170        180 
KYFNFTTEDH KMVEALRVWA STHMSPSWTL LKLCDVQPMQ YFDLTCQLLG KAEVDGASFL 

       190        200        210        220        230        240 
LKVWDGTRTP FPSWRVLIQD LVLEGDLSHI HRLQNLTIDI LVYDNHVHVA RSLKVGSFLR 

       250        260        270        280        290        300 
IYSLHTKLQS MNSENQTMLS LEFHLHGGTS YGRGIRVLPE SNSDVDQLKK DLESANLTAN 

       310        320        330        340        350        360 
QHSDVICQSE PDDSFPSSGS VSLYEVERCQ QLSATILTDH QYLERTPLCA ILKQKAPQQY 

       370        380        390        400        410        420 
RIRAKLRSYK PRRLFQSVKL HCPKCHLLQE VPHEGDLDII FQDGATKTPD VKLQNTSLYD 

       430        440        450        460        470        480 
SKIWTTKNQK GRKVAVHFVK NNGILPLSNE CLLLIEGGTL SEICKLSNKF NSVIPVRSGH 

       490        500        510        520        530        540 
EDLELLDLSA PFLIQGTIHH YGCKQCSSLR SIQNLNSLVD KTSWIPSSVA EALGIVPLQY 

       550        560        570        580        590        600 
VFVMTFTLDD GTGVLEAYLM DSDKFFQIPA SEVLMDDDLQ KSVDMIMDMF CPPGIKIDAY 

       610        620        630 
PWLECFIKSY NVTNGTDNQI CYQIFDTTVA EDVI 

« Hide

Isoform 2 (Variant 3) [UniParc].

Checksum: 7D04F3ECC01D448D
Show »

FASTA53860,534

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS5793.1. [Q9NUX5-1]
PIRT08766.
RefSeqNP_001036059.1. NM_001042594.1.
NP_056265.2. NM_015450.2. [Q9NUX5-1]
XP_006715980.1. XM_006715917.1. [Q9NUX5-1]
UniGeneHs.31968.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1XJVX-ray1.73A6-299[»]
3KJOX-ray1.80A1-299[»]
3KJPX-ray1.80A1-299[»]
ProteinModelPortalQ9NUX5.
SMRQ9NUX5. Positions 6-299.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117417. 204 interactions.
DIPDIP-29610N.
IntActQ9NUX5. 28 interactions.
MINTMINT-1466135.
STRING9606.ENSP00000350249.

Chemistry

BindingDBQ9NUX5.
ChEMBLCHEMBL5908.

PTM databases

PhosphoSiteQ9NUX5.

Polymorphism databases

DMDM50401179.

Proteomic databases

MaxQBQ9NUX5.
PaxDbQ9NUX5.
PRIDEQ9NUX5.

Protocols and materials databases

DNASU25913.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000357628; ENSP00000350249; ENSG00000128513. [Q9NUX5-1]
GeneID25913.
KEGGhsa:25913.
UCSCuc003vlm.3. human. [Q9NUX5-1]

Organism-specific databases

CTD25913.
GeneCardsGC07M124462.
HGNCHGNC:17284. POT1.
HPAHPA051625.
MIM606478. gene.
neXtProtNX_Q9NUX5.
Orphanet67038. B-cell chronic lymphocytic leukemia.
PharmGKBPA134934904.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG284004.
HOGENOMHOG000015271.
HOVERGENHBG053641.
InParanoidQ9NUX5.
KOK11109.
OMADKTSWIP.
OrthoDBEOG7N0C4C.
PhylomeDBQ9NUX5.
TreeFamTF328398.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_120956. Cellular responses to stress.

Gene expression databases

ArrayExpressQ9NUX5.
BgeeQ9NUX5.
CleanExHS_POT1.
GenevestigatorQ9NUX5.

Family and domain databases

Gene3D2.40.50.140. 1 hit.
InterProIPR012340. NA-bd_OB-fold.
IPR028389. POT1.
IPR011564. Telomer_end-bd_POT1/Cdc13.
[Graphical view]
PANTHERPTHR14513. PTHR14513. 1 hit.
PfamPF02765. POT1. 1 hit.
[Graphical view]
SMARTSM00976. Telo_bind. 1 hit.
[Graphical view]
SUPFAMSSF50249. SSF50249. 2 hits.
ProtoNetSearch...

Other

EvolutionaryTraceQ9NUX5.
GeneWikiPOT1.
GenomeRNAi25913.
NextBio47408.
PROQ9NUX5.
SOURCESearch...

Entry information

Entry namePOTE1_HUMAN
AccessionPrimary (citable) accession number: Q9NUX5
Secondary accession number(s): O95018 expand/collapse secondary AC list , Q5MJ36, Q9H662, Q9NW19, Q9UG95
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM