Skip Header

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

Protection of telomeres protein 1

Gene

Pot1

Organism
Mus musculus (Mouse)
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 similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-1221633. Meiotic Synapsis.
R-MMU-171306. Packaging Of Telomere Ends.
R-MMU-2559586. DNA Damage/Telomere Stress Induced Senescence.

Names & Taxonomyi

Protein namesi
Recommended name:
Protection of telomeres protein 1
Short name:
mPot1
Alternative name(s):
POT1-like telomere end-binding protein
Gene namesi
Name:Pot1
Synonyms:Pot1a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:2141503. Pot1a.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Chromosome, Nucleus, Telomere

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 640640Protection of telomeres protein 1PRO_0000121730Add
BLAST

Proteomic databases

EPDiQ91WC1.
MaxQBiQ91WC1.
PaxDbiQ91WC1.
PRIDEiQ91WC1.

PTM databases

PhosphoSiteiQ91WC1.

Expressioni

Gene expression databases

BgeeiQ91WC1.
CleanExiMM_POT1A.
ExpressionAtlasiQ91WC1. baseline and differential.
GenevisibleiQ91WC1. MM.

Interactioni

Subunit structurei

Homodimer or homooligomer. 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). Component of the shelterin complex (telosome) composed of TERF1, TERF2, TINF2, TERF2IP, ACD and POT1. Binds single-stranded telomeric DNA as a monomer. Found in a complex with TERF1, TINF2 and TNKS1. Interacts with TNKS1. Forms heterodimers with ACD (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Tpp1O890232EBI-7051001,EBI-7051084

GO - Molecular functioni

Protein-protein interaction databases

BioGridi221602. 1 interaction.
DIPiDIP-29608N.
IntActiQ91WC1. 3 interactions.
MINTiMINT-3379580.
STRINGi10090.ENSMUSP00000110986.

Structurei

3D structure databases

ProteinModelPortaliQ91WC1.
SMRiQ91WC1. Positions 9-299.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the telombin family.Curated

Phylogenomic databases

eggNOGiKOG4757. Eukaryota.
ENOG410Z1J0. LUCA.
GeneTreeiENSGT00390000018285.
HOGENOMiHOG000015271.
HOVERGENiHBG053641.
InParanoidiQ91WC1.
KOiK11109.
OMAiDKTSWIP.
OrthoDBiEOG7N0C4C.
PhylomeDBiQ91WC1.
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

Isoform 1 (identifier: Q91WC1-1) [UniParc]FASTAAdd to basket

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
MSLVSTAPYT YTPLNLLKEG TIANVYGVVK FFKPPYVSKG TDYCSVVTIV
60 70 80 90 100
DQTNVKLTCM LFSGNYEALP IIYKVGDIVR FHRLKIQVYK NELQGINCSG
110 120 130 140 150
FASLTFEGTV GMPVTARTSS KVFSFTPQDQ KMVEALRVWA SKHISASSTL
160 170 180 190 200
VQLCDAQPMQ YYDLTCQLLG KAQVDSTAFL LKVWDGTQTV LPSWRVSTQD
210 220 230 240 250
LTFEGDLSHI ERLQSLVVDI LVYDNHVQVA RSIEVGCFLR LYSLHTKLQP
260 270 280 290 300
GNSETSSSES LRLEFHLHGG TSYGRGIRVL PDTSPCVDQL KKALEGANLP
310 320 330 340 350
VTETSTGICQ SENGDSSALS NSGSGAVSPY EEERCQQVSA TILTNHQHLE
360 370 380 390 400
KTPLCAILTQ KAPQQYRVRA KLRSYLPRRL SQSVKLLCPK CHSVQEVPHG
410 420 430 440 450
DSLDKILQDA ATEAPDIKLK ATSLYYSKVW TTEDQGGRQV AVHFVKNNGI
460 470 480 490 500
LPASSECLIL IEGGRLCEVS KLSSKFHSVM PVRSGPESLE LLTLSAPFLI
510 520 530 540 550
QGKVHHYGCK QCSSLKPIQN LNSRFHKGPW TPSSVAEALG VVPLQYVFVM
560 570 580 590 600
VFTLDDGTGV LEAYLKDSEH FFKIPASEVL TDDDLQRSLE TIMDMICPPG
610 620 630 640
IKVDAYPWLE CLLKSYNVTI GTERRICYQI FDTTVAENVV
Length:640
Mass (Da):70,863
Last modified:December 1, 2001 - v1
Checksum:i64393BA48F14965E
GO
Isoform 2 (identifier: Q91WC1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     538-538: A → G
     539-640: Missing.

Note: No experimental confirmation available.
Show »
Length:538
Mass (Da):59,299
Checksum:i408F0D9F7CF4AD83
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei538 – 5381A → G in isoform 2. 1 PublicationVSP_010848
Alternative sequencei539 – 640102Missing in isoform 2. 1 PublicationVSP_010849Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK036052 mRNA. Translation: BAC29288.1.
AK040864 mRNA. Translation: BAC30723.1.
AK085041 mRNA. Translation: BAC39349.1.
BC016121 mRNA. Translation: AAH16121.1.
CCDSiCCDS39442.1. [Q91WC1-1]
RefSeqiNP_598692.1. NM_133931.4. [Q91WC1-1]
UniGeneiMm.274589.
Mm.397208.

Genome annotation databases

EnsembliENSMUST00000115330; ENSMUSP00000110986; ENSMUSG00000029676. [Q91WC1-1]
ENSMUST00000166445; ENSMUSP00000131928; ENSMUSG00000029676. [Q91WC1-1]
GeneIDi101185.
KEGGimmu:101185.
UCSCiuc009bce.1. mouse. [Q91WC1-1]
uc009bcf.1. mouse. [Q91WC1-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK036052 mRNA. Translation: BAC29288.1.
AK040864 mRNA. Translation: BAC30723.1.
AK085041 mRNA. Translation: BAC39349.1.
BC016121 mRNA. Translation: AAH16121.1.
CCDSiCCDS39442.1. [Q91WC1-1]
RefSeqiNP_598692.1. NM_133931.4. [Q91WC1-1]
UniGeneiMm.274589.
Mm.397208.

3D structure databases

ProteinModelPortaliQ91WC1.
SMRiQ91WC1. Positions 9-299.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi221602. 1 interaction.
DIPiDIP-29608N.
IntActiQ91WC1. 3 interactions.
MINTiMINT-3379580.
STRINGi10090.ENSMUSP00000110986.

PTM databases

PhosphoSiteiQ91WC1.

Proteomic databases

EPDiQ91WC1.
MaxQBiQ91WC1.
PaxDbiQ91WC1.
PRIDEiQ91WC1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000115330; ENSMUSP00000110986; ENSMUSG00000029676. [Q91WC1-1]
ENSMUST00000166445; ENSMUSP00000131928; ENSMUSG00000029676. [Q91WC1-1]
GeneIDi101185.
KEGGimmu:101185.
UCSCiuc009bce.1. mouse. [Q91WC1-1]
uc009bcf.1. mouse. [Q91WC1-2]

Organism-specific databases

CTDi101185.
MGIiMGI:2141503. Pot1a.

Phylogenomic databases

eggNOGiKOG4757. Eukaryota.
ENOG410Z1J0. LUCA.
GeneTreeiENSGT00390000018285.
HOGENOMiHOG000015271.
HOVERGENiHBG053641.
InParanoidiQ91WC1.
KOiK11109.
OMAiDKTSWIP.
OrthoDBiEOG7N0C4C.
PhylomeDBiQ91WC1.
TreeFamiTF328398.

Enzyme and pathway databases

ReactomeiR-MMU-1221633. Meiotic Synapsis.
R-MMU-171306. Packaging Of Telomere Ends.
R-MMU-2559586. DNA Damage/Telomere Stress Induced Senescence.

Miscellaneous databases

NextBioi354800.
PROiQ91WC1.
SOURCEiSearch...

Gene expression databases

BgeeiQ91WC1.
CleanExiMM_POT1A.
ExpressionAtlasiQ91WC1. baseline and differential.
GenevisibleiQ91WC1. MM.

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

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Aorta, Cerebellum, Lung and Vein.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Retina.

Entry informationi

Entry nameiPOTE1_MOUSE
AccessioniPrimary (citable) accession number: Q91WC1
Secondary accession number(s): Q8BUH9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: December 1, 2001
Last modified: May 11, 2016
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.