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Protein

CST complex subunit TEN1

Gene

TEN1

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

Functioni

Component of the CST complex proposed to act as a specialized replication factor promoting DNA replication under conditions of replication stress or natural replication barriers such as the telomere duplex. The CST complex binds single-stranded DNA with high affinity in a sequence-independent manner, while isolated subunits bind DNA with low affinity by themselves. Initially the CST complex has been proposed to protect telomeres from DNA degradation (PubMed:19854130). However, the CST complex has been shown to be involved in several aspects of telomere replication. The CST complex inhibits telomerase and is involved in telomere length homeostasis; it is proposed to bind to newly telomerase-synthesized 3' overhangs and to terminate telomerase action implicating the association with the ACD:POT1 complex thus interfering with its telomerase stimulation activity. The CST complex is also proposed to be involved in fill-in synthesis of the telomeric C-strand probably implicating recruitment and activation of DNA polymerase alpha (PubMed:22763445). The CST complex facilitates recovery from many forms of exogenous DNA damage; seems to be involved in the re-initiation of DNA replication at repaired forks and/or dormant origins (PubMed:25483097).3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi2 – 123122OBAdd
BLAST

GO - Molecular functioni

  • single-stranded DNA binding Source: InterPro
  • telomeric DNA binding Source: BHF-UCL

GO - Biological processi

  • negative regulation of telomerase activity Source: BHF-UCL
  • regulation of telomere maintenance via telomere lengthening Source: BHF-UCL
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
CST complex subunit TEN1
Alternative name(s):
Protein telomeric pathways with STN1 homolog
Telomere length regulation protein TEN1 homolog
Gene namesi
Name:TEN1
Synonyms:C17orf106
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:37242. TEN1.

Subcellular locationi

GO - Cellular componenti

  • CST complex Source: UniProtKB
  • nuclear chromosome, telomeric region Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus, Telomere

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi115 – 1151Y → A: 2.5-fold reduction in binding affinity for OBFC1. 1 Publication
Mutagenesisi119 – 1191R → Q: 2-fold reduction in binding affinity for OBFC1. 1 Publication

Organism-specific databases

PharmGKBiPA165431550.

Polymorphism and mutation databases

BioMutaiTEN1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 123123CST complex subunit TEN1PRO_0000334683Add
BLAST

Proteomic databases

MaxQBiQ86WV5.
PaxDbiQ86WV5.
PRIDEiQ86WV5.

Expressioni

Gene expression databases

BgeeiQ86WV5.
ExpressionAtlasiQ86WV5. baseline and differential.
GenevisibleiQ86WV5. HS.

Organism-specific databases

HPAiHPA043486.

Interactioni

Subunit structurei

Component of the CST complex, composed of TEN1/C17orf106, CTC1/C17orf68 and STN1/OBFC1; in the complex interacts directly with STN1/OBFC1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
OBFC1Q9H6683EBI-2562799,EBI-746930

Protein-protein interaction databases

BioGridi756076. 3 interactions.
DIPiDIP-56901N.
IntActiQ86WV5. 3 interactions.
STRINGi9606.ENSP00000380762.

Structurei

Secondary structure

1
123
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi12 – 165Combined sources
Beta strandi25 – 3612Combined sources
Turni37 – 404Combined sources
Beta strandi41 – 488Combined sources
Beta strandi51 – 588Combined sources
Helixi60 – 623Combined sources
Beta strandi71 – 8010Combined sources
Beta strandi83 – 853Combined sources
Beta strandi88 – 969Combined sources
Helixi102 – 11817Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4JOIX-ray2.05C/D2-123[»]
ProteinModelPortaliQ86WV5.
SMRiQ86WV5. Positions 2-119.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TEN1 family.Curated
Contains 1 OB DNA-binding domain.Curated

Phylogenomic databases

eggNOGiENOG410J0UU. Eukaryota.
ENOG4111Y0A. LUCA.
GeneTreeiENSGT00390000017589.
HOGENOMiHOG000152364.
HOVERGENiHBG067571.
InParanoidiQ86WV5.
OMAiYYFPWEI.
OrthoDBiEOG71CFP2.
PhylomeDBiQ86WV5.
TreeFamiTF333010.

Family and domain databases

InterProiIPR029146. Ten1_animal_plant.
[Graphical view]
PfamiPF15490. Ten1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q86WV5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMLPKPGTYY LPWEVSAGQV PDGSTLRTFG RLCLYDMIQS RVTLMAQHGS
60 70 80 90 100
DQHQVLVCTK LVEPFHAQVG SLYIVLGELQ HQQDRGSVVK ARVLTCVEGM
110 120
NLPLLEQAIR EQRLYKQERG GSQ
Length:123
Mass (Da):13,856
Last modified:May 29, 2013 - v2
Checksum:iC713E9B40C2A5E34
GO

Sequence cautioni

The sequence AAH47782.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti46 – 461A → S in BM558420 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK097104 mRNA. No translation available.
BX647274 mRNA. No translation available.
AC040980 Genomic DNA. No translation available.
BC047782 mRNA. Translation: AAH47782.1. Different initiation.
BM558420 mRNA. No translation available.
CCDSiCCDS45780.2.
RefSeqiNP_001106795.2. NM_001113324.2.
UniGeneiHs.593566.

Genome annotation databases

EnsembliENST00000397640; ENSP00000380762; ENSG00000257949.
GeneIDi100134934.
KEGGihsa:100134934.
UCSCiuc060kgd.1. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK097104 mRNA. No translation available.
BX647274 mRNA. No translation available.
AC040980 Genomic DNA. No translation available.
BC047782 mRNA. Translation: AAH47782.1. Different initiation.
BM558420 mRNA. No translation available.
CCDSiCCDS45780.2.
RefSeqiNP_001106795.2. NM_001113324.2.
UniGeneiHs.593566.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4JOIX-ray2.05C/D2-123[»]
ProteinModelPortaliQ86WV5.
SMRiQ86WV5. Positions 2-119.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi756076. 3 interactions.
DIPiDIP-56901N.
IntActiQ86WV5. 3 interactions.
STRINGi9606.ENSP00000380762.

Polymorphism and mutation databases

BioMutaiTEN1.

Proteomic databases

MaxQBiQ86WV5.
PaxDbiQ86WV5.
PRIDEiQ86WV5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000397640; ENSP00000380762; ENSG00000257949.
GeneIDi100134934.
KEGGihsa:100134934.
UCSCiuc060kgd.1. human.

Organism-specific databases

CTDi100134934.
GeneCardsiTEN1.
HGNCiHGNC:37242. TEN1.
HPAiHPA043486.
MIMi613130. gene.
neXtProtiNX_Q86WV5.
PharmGKBiPA165431550.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410J0UU. Eukaryota.
ENOG4111Y0A. LUCA.
GeneTreeiENSGT00390000017589.
HOGENOMiHOG000152364.
HOVERGENiHBG067571.
InParanoidiQ86WV5.
OMAiYYFPWEI.
OrthoDBiEOG71CFP2.
PhylomeDBiQ86WV5.
TreeFamiTF333010.

Miscellaneous databases

GenomeRNAii100134934.
NextBioi20774766.
PROiQ86WV5.
SOURCEiSearch...

Gene expression databases

BgeeiQ86WV5.
ExpressionAtlasiQ86WV5. baseline and differential.
GenevisibleiQ86WV5. HS.

Family and domain databases

InterProiIPR029146. Ten1_animal_plant.
[Graphical view]
PfamiPF15490. Ten1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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].
    Tissue: Spleen.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Retina.
  3. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].
    Tissue: Melanoma and Uterus.
  5. "RPA-like mammalian Ctc1-Stn1-Ten1 complex binds to single-stranded DNA and protects telomeres independently of the Pot1 pathway."
    Miyake Y., Nakamura M., Nabetani A., Shimamura S., Tamura M., Yonehara S., Saito M., Ishikawa F.
    Mol. Cell 36:193-206(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE CST COMPLEX, SUBCELLULAR LOCATION, INTERACTION WITH OBFC1.
  6. "Human CST promotes telomere duplex replication and general replication restart after fork stalling."
    Stewart J.A., Wang F., Chaiken M.F., Kasbek C., Chastain P.D. II, Wright W.E., Price C.M.
    EMBO J. 31:3537-3549(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE CST COMPLEX.
  7. "The human CST complex is a terminator of telomerase activity."
    Chen L.Y., Redon S., Lingner J.
    Nature 488:540-544(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE CST COMPLEX.
  8. "Human CST abundance determines recovery from diverse forms of DNA damage and replication stress."
    Wang F., Stewart J., Price C.M.
    Cell Cycle 13:3488-3498(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE CST COMPLEX.
  9. "Structure of the human telomeric Stn1-Ten1 capping complex."
    Bryan C., Rice C., Harkisheimer M., Schultz D.C., Skordalakes E.
    PLoS ONE 8:E66756-E66756(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 2-123 IN COMPLEX WITH OBFC1, OB FOLD DNA-BINDING, MUTAGENESIS OF TYR-115 AND ARG-119.

Entry informationi

Entry nameiTEN1L_HUMAN
AccessioniPrimary (citable) accession number: Q86WV5
Secondary accession number(s): I3L0C7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 29, 2013
Last modified: March 16, 2016
This is version 85 of the entry and version 2 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

Caution

It is uncertain whether Met-1 or Met-2 is the initiator. Some orthologous sequences cannot be extended.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: 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.