STN1_HUMAN
ID STN1_HUMAN Reviewed; 368 AA.
AC Q9H668; D3DR99; Q5TCZ0;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=CST complex subunit STN1;
DE AltName: Full=Oligonucleotide/oligosaccharide-binding fold-containing protein 1;
DE AltName: Full=Suppressor of cdc thirteen homolog;
GN Name=STN1 {ECO:0000312|HGNC:HGNC:26200}; Synonyms=OBFC1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ALA-151 AND CYS-248.
RC TISSUE=Small intestine;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ALA-151 AND CYS-248.
RC TISSUE=Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, IDENTIFICATION IN THE CST COMPLEX, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH CTC1 AND TEN1.
RX PubMed=19854130; DOI=10.1016/j.molcel.2009.08.009;
RA Miyake Y., Nakamura M., Nabetani A., Shimamura S., Tamura M., Yonehara S.,
RA Saito M., Ishikawa F.;
RT "RPA-like mammalian Ctc1-Stn1-Ten1 complex binds to single-stranded DNA and
RT protects telomeres independently of the Pot1 pathway.";
RL Mol. Cell 36:193-206(2009).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, DNA-BINDING, AND INTERACTION WITH ACD.
RX PubMed=19648609; DOI=10.1074/jbc.m109.021105;
RA Wan M., Qin J., Songyang Z., Liu D.;
RT "OB fold-containing protein 1 (OBFC1), a human homolog of yeast Stn1,
RT associates with TPP1 and is implicated in telomere length regulation.";
RL J. Biol. Chem. 284:26725-26731(2009).
RN [7]
RP FUNCTION.
RX PubMed=23142664; DOI=10.1016/j.celrep.2012.10.007;
RA Wang F., Stewart J.A., Kasbek C., Zhao Y., Wright W.E., Price C.M.;
RT "Human CST has independent functions during telomere duplex replication and
RT C-strand fill-in.";
RL Cell Rep. 2:1096-1103(2012).
RN [8]
RP FUNCTION.
RX PubMed=22964711; DOI=10.1038/cr.2012.132;
RA Huang C., Dai X., Chai W.;
RT "Human Stn1 protects telomere integrity by promoting efficient lagging-
RT strand synthesis at telomeres and mediating C-strand fill-in.";
RL Cell Res. 22:1681-1695(2012).
RN [9]
RP FUNCTION, AND FUNCTION OF THE CST COMPLEX.
RX PubMed=22863775; DOI=10.1038/emboj.2012.215;
RA Stewart J.A., Wang F., Chaiken M.F., Kasbek C., Chastain P.D. II,
RA Wright W.E., Price C.M.;
RT "Human CST promotes telomere duplex replication and general replication
RT restart after fork stalling.";
RL EMBO J. 31:3537-3549(2012).
RN [10]
RP FUNCTION OF THE CST COMPLEX, INTERACTION WITH CTC1; ACD AND POT1, AND
RP SUBCELLULAR LOCATION.
RX PubMed=22763445; DOI=10.1038/nature11269;
RA Chen L.Y., Redon S., Lingner J.;
RT "The human CST complex is a terminator of telomerase activity.";
RL Nature 488:540-544(2012).
RN [11]
RP INTERACTION WITH CTC1, AND FUNCTION.
RX PubMed=23851344; DOI=10.4161/nucl.25701;
RA Chen L.Y., Lingner J.;
RT "CST for the grand finale of telomere replication.";
RL Nucleus 4:277-282(2013).
RN [12]
RP FUNCTION OF THE CST COMPLEX.
RX PubMed=25483097; DOI=10.4161/15384101.2014.964100;
RA Wang F., Stewart J., Price C.M.;
RT "Human CST abundance determines recovery from diverse forms of DNA damage
RT and replication stress.";
RL Cell Cycle 13:3488-3498(2014).
RN [13]
RP INTERACTION WITH POLA1; ACD AND POT1.
RX PubMed=25519149; DOI=10.1158/1541-7786.mcr-14-0381;
RA Diotti R., Kalan S., Matveyenko A., Loayza D.;
RT "DNA-directed polymerase subunits play a vital role in human telomeric
RT overhang processing.";
RL Mol. Cancer Res. 13:402-410(2015).
RN [14]
RP INVOLVEMENT IN CRMCC2, AND VARIANTS CRMCC2 THR-135 AND TYR-157.
RX PubMed=27432940; DOI=10.1084/jem.20151618;
RA Simon A.J., Lev A., Zhang Y., Weiss B., Rylova A., Eyal E., Kol N.,
RA Barel O., Cesarkas K., Soudack M., Greenberg-Kushnir N., Rhodes M.,
RA Wiest D.L., Schiby G., Barshack I., Katz S., Pras E., Poran H.,
RA Reznik-Wolf H., Ribakovsky E., Simon C., Hazou W., Sidi Y., Lahad A.,
RA Katzir H., Sagie S., Aqeilan H.A., Glousker G., Amariglio N., Tzfati Y.,
RA Selig S., Rechavi G., Somech R.;
RT "Mutations in STN1 cause Coats plus syndrome and are associated with
RT genomic and telomere defects.";
RL J. Exp. Med. 213:1429-1440(2016).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 19-184 IN COMPLEX WITH TEN1,
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 191-368, DNA-BINDING, WHTH
RP REGIONS, AND MUTAGENESIS OF ASP-78; ILE-164 AND MET-167.
RX PubMed=23826127; DOI=10.1371/journal.pone.0066756;
RA Bryan C., Rice C., Harkisheimer M., Schultz D.C., Skordalakes E.;
RT "Structure of the human telomeric Stn1-Ten1 capping complex.";
RL PLoS ONE 8:E66756-E66756(2013).
CC -!- FUNCTION: Component of the CST complex proposed to act as a specialized
CC replication factor promoting DNA replication under conditions of
CC replication stress or natural replication barriers such as the telomere
CC duplex. The CST complex binds single-stranded DNA with high affinity in
CC a sequence-independent manner, while isolated subunits bind DNA with
CC low affinity by themselves. Initially the CST complex has been proposed
CC to protect telomeres from DNA degradation (PubMed:19854130). However,
CC the CST complex has been shown to be involved in several aspects of
CC telomere replication. The CST complex inhibits telomerase and is
CC involved in telomere length homeostasis; it is proposed to bind to
CC newly telomerase-synthesized 3' overhangs and to terminate telomerase
CC action implicating the association with the ACD:POT1 complex thus
CC interfering with its telomerase stimulation activity. The CST complex
CC is also proposed to be involved in fill-in synthesis of the telomeric
CC C-strand probably implicating recruitment and activation of DNA
CC polymerase alpha (PubMed:22964711, PubMed:22763445). The CST complex
CC facilitates recovery from many forms of exogenous DNA damage; seems to
CC be involved in the re-initiation of DNA replication at repaired forks
CC and/or dormant origins (PubMed:25483097). Required for efficicient
CC replication of the duplex region of the telomere. Promotes efficient
CC replication of lagging-strand telomeres (PubMed:22863775,
CC PubMed:22964711). Promotes general replication start following
CC replication-fork stalling implicating new origin firing
CC (PubMed:22863775). May be in involved in C-strand fill-in during late
CC S/G2 phase independent of its role in telomere duplex replication
CC (PubMed:23142664). {ECO:0000269|PubMed:19648609,
CC ECO:0000269|PubMed:19854130, ECO:0000269|PubMed:22763445,
CC ECO:0000269|PubMed:22863775, ECO:0000269|PubMed:22964711,
CC ECO:0000269|PubMed:23142664, ECO:0000269|PubMed:25483097,
CC ECO:0000305|PubMed:23851344}.
CC -!- FUNCTION: Component of the CST complex, a complex that binds to single-
CC stranded DNA and is required to protect telomeres from DNA degradation.
CC The CST complex binds single-stranded DNA with high affinity in a
CC sequence-independent manner, while isolated subunits bind DNA with low
CC affinity by themselves. In addition to telomere protection, the CST
CC complex has probably a more general role in DNA metabolism at non-
CC telomeric sites. {ECO:0000269|PubMed:19648609,
CC ECO:0000269|PubMed:19854130}.
CC -!- SUBUNIT: Component of the CST complex, composed of TEN1/C17orf106,
CC CTC1/C17orf68 and STN1; in the complex interacts directly with TEN1 and
CC CTC1. Interacts with ACD/TPP1, POT1 and POLA1.
CC {ECO:0000269|PubMed:19648609, ECO:0000269|PubMed:19854130,
CC ECO:0000269|PubMed:23826127, ECO:0000269|PubMed:25519149}.
CC -!- INTERACTION:
CC Q9H668; Q96AP0: ACD; NbExp=4; IntAct=EBI-746930, EBI-717666;
CC Q9H668; Q9NWQ9: C14orf119; NbExp=4; IntAct=EBI-746930, EBI-725606;
CC Q9H668; Q9NX04: C1orf109; NbExp=5; IntAct=EBI-746930, EBI-8643161;
CC Q9H668; Q2NKJ3: CTC1; NbExp=7; IntAct=EBI-746930, EBI-2562802;
CC Q9H668; Q2NKJ3-1: CTC1; NbExp=5; IntAct=EBI-746930, EBI-15994382;
CC Q9H668; P42858: HTT; NbExp=3; IntAct=EBI-746930, EBI-466029;
CC Q9H668; Q5SW96: LDLRAP1; NbExp=12; IntAct=EBI-746930, EBI-747813;
CC Q9H668; Q8TCE9: LGALS14; NbExp=3; IntAct=EBI-746930, EBI-10274069;
CC Q9H668; Q13064: MKRN3; NbExp=3; IntAct=EBI-746930, EBI-2340269;
CC Q9H668; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-746930, EBI-741158;
CC Q9H668; Q9P2K3-2: RCOR3; NbExp=3; IntAct=EBI-746930, EBI-1504830;
CC Q9H668; P51687: SUOX; NbExp=3; IntAct=EBI-746930, EBI-3921347;
CC Q9H668; Q9BT92: TCHP; NbExp=3; IntAct=EBI-746930, EBI-740781;
CC Q9H668; Q86WV5: TEN1; NbExp=11; IntAct=EBI-746930, EBI-2562799;
CC Q9H668; Q9H0E2: TOLLIP; NbExp=3; IntAct=EBI-746930, EBI-74615;
CC Q9H668; O14773-1: TPP1; NbExp=2; IntAct=EBI-746930, EBI-15619703;
CC Q9H668; Q8N7C3: TRIML2; NbExp=3; IntAct=EBI-746930, EBI-11059915;
CC Q9H668; Q99757: TXN2; NbExp=3; IntAct=EBI-746930, EBI-2932492;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19854130}.
CC Chromosome, telomere {ECO:0000269|PubMed:19648609,
CC ECO:0000269|PubMed:19854130, ECO:0000269|PubMed:22763445}.
CC -!- DISEASE: Cerebroretinal microangiopathy with calcifications and cysts 2
CC (CRMCC2) [MIM:617341]: An autosomal recessive, multisystemic disorder
CC characterized by intrauterine growth retardation and, later in life,
CC premature aging symptoms, including poor growth, graying hair, liver
CC fibrosis, portal hypertension, esophageal varices, osteopenia,
CC pancytopenia, hypocellular bone marrow, and vascular telangiectasia
CC resulting in gastrointestinal bleeding. Brain calcifications and white
CC matter changes are responsible for signs including spasticity, ataxia,
CC or dystonia observed in some patients. {ECO:0000269|PubMed:27432940}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- MISCELLANEOUS: Cells expressing STN1 mutants defective for dimerization
CC with TEN1 display elongated telomeres and telomere defects associated
CC with telomere uncapping.
CC -!- SIMILARITY: Belongs to the STN1 family. {ECO:0000305}.
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DR EMBL; AK026212; BAB15396.1; -; mRNA.
DR EMBL; AL133355; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW49619.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49620.1; -; Genomic_DNA.
DR EMBL; BC017400; AAH17400.1; -; mRNA.
DR CCDS; CCDS7552.1; -.
DR RefSeq; NP_079204.2; NM_024928.4.
DR RefSeq; XP_006718039.1; XM_006717976.3.
DR RefSeq; XP_016872158.1; XM_017016669.1.
DR RefSeq; XP_016872159.1; XM_017016670.1.
DR PDB; 4JOI; X-ray; 2.05 A; A/B=19-184.
DR PDB; 4JQF; X-ray; 1.60 A; A=191-368.
DR PDB; 6W6W; EM; 3.00 A; C=2-368.
DR PDBsum; 4JOI; -.
DR PDBsum; 4JQF; -.
DR PDBsum; 6W6W; -.
DR AlphaFoldDB; Q9H668; -.
DR SMR; Q9H668; -.
DR BioGRID; 123054; 98.
DR ComplexPortal; CPX-2129; CST complex.
DR CORUM; Q9H668; -.
DR DIP; DIP-59914N; -.
DR IntAct; Q9H668; 60.
DR MINT; Q9H668; -.
DR STRING; 9606.ENSP00000224950; -.
DR iPTMnet; Q9H668; -.
DR PhosphoSitePlus; Q9H668; -.
DR BioMuta; STN1; -.
DR DMDM; 62900737; -.
DR EPD; Q9H668; -.
DR jPOST; Q9H668; -.
DR MassIVE; Q9H668; -.
DR MaxQB; Q9H668; -.
DR PaxDb; Q9H668; -.
DR PeptideAtlas; Q9H668; -.
DR PRIDE; Q9H668; -.
DR ProteomicsDB; 80961; -.
DR Antibodypedia; 31566; 187 antibodies from 21 providers.
DR DNASU; 79991; -.
DR Ensembl; ENST00000224950.8; ENSP00000224950.3; ENSG00000107960.11.
DR Ensembl; ENST00000369764.1; ENSP00000358779.1; ENSG00000107960.11.
DR GeneID; 79991; -.
DR KEGG; hsa:79991; -.
DR MANE-Select; ENST00000224950.8; ENSP00000224950.3; NM_024928.5; NP_079204.2.
DR UCSC; uc001kxl.4; human.
DR CTD; 79991; -.
DR DisGeNET; 79991; -.
DR GeneCards; STN1; -.
DR GeneReviews; STN1; -.
DR HGNC; HGNC:26200; STN1.
DR HPA; ENSG00000107960; Low tissue specificity.
DR MalaCards; STN1; -.
DR MIM; 613128; gene.
DR MIM; 617341; phenotype.
DR neXtProt; NX_Q9H668; -.
DR OpenTargets; ENSG00000107960; -.
DR Orphanet; 313838; Coats plus syndrome.
DR Orphanet; 2032; Idiopathic pulmonary fibrosis.
DR PharmGKB; PA134987118; -.
DR VEuPathDB; HostDB:ENSG00000107960; -.
DR eggNOG; KOG3108; Eukaryota.
DR GeneTree; ENSGT00390000000909; -.
DR HOGENOM; CLU_063889_0_0_1; -.
DR InParanoid; Q9H668; -.
DR OMA; LCWKDEK; -.
DR OrthoDB; 1451022at2759; -.
DR PhylomeDB; Q9H668; -.
DR TreeFam; TF328623; -.
DR PathwayCommons; Q9H668; -.
DR Reactome; R-HSA-174411; Polymerase switching on the C-strand of the telomere.
DR Reactome; R-HSA-174430; Telomere C-strand synthesis initiation.
DR SignaLink; Q9H668; -.
DR BioGRID-ORCS; 79991; 319 hits in 1078 CRISPR screens.
DR ChiTaRS; STN1; human.
DR GenomeRNAi; 79991; -.
DR Pharos; Q9H668; Tbio.
DR PRO; PR:Q9H668; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9H668; protein.
DR Bgee; ENSG00000107960; Expressed in lower esophagus mucosa and 201 other tissues.
DR Genevisible; Q9H668; HS.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:UniProtKB.
DR GO; GO:1990879; C:CST complex; IDA:BHF-UCL.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0043047; F:single-stranded telomeric DNA binding; IDA:UniProtKB.
DR GO; GO:0042162; F:telomeric DNA binding; IDA:BHF-UCL.
DR GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; IDA:BHF-UCL.
DR GO; GO:0045740; P:positive regulation of DNA replication; ISS:UniProtKB.
DR GO; GO:0016233; P:telomere capping; TAS:BHF-UCL.
DR GO; GO:0000723; P:telomere maintenance; IMP:UniProtKB.
DR GO; GO:0010833; P:telomere maintenance via telomere lengthening; IMP:UniProtKB.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.10.10.980; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR015253; CST_STN1_C.
DR InterPro; IPR042082; CST_Stn1_wHTH1_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR InterPro; IPR040260; RFA2-like.
DR InterPro; IPR014647; Stn1.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR13989; PTHR13989; 1.
DR Pfam; PF09170; STN1_2; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR PIRSF; PIRSF036950; UCP036950; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome; Disease variant; DNA-binding; Nucleus;
KW Reference proteome; Telomere.
FT CHAIN 1..368
FT /note="CST complex subunit STN1"
FT /id="PRO_0000058020"
FT DNA_BIND 57..155
FT /note="OB"
FT REGION 1..185
FT /note="Interaction with CTC1"
FT /evidence="ECO:0000269|PubMed:23851344"
FT REGION 191..295
FT /note="Winged helix-turn-helix (wHTH) 1"
FT REGION 296..368
FT /note="Winged helix-turn-helix (wHTH) 2"
FT VARIANT 135
FT /note="R -> T (in CRMCC2; dbSNP:rs1057519583)"
FT /evidence="ECO:0000269|PubMed:27432940"
FT /id="VAR_078499"
FT VARIANT 151
FT /note="T -> A (in dbSNP:rs2487999)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_022364"
FT VARIANT 157
FT /note="D -> Y (in CRMCC2; dbSNP:rs765462548)"
FT /evidence="ECO:0000269|PubMed:27432940"
FT /id="VAR_078500"
FT VARIANT 248
FT /note="S -> C (in dbSNP:rs10786775)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_022365"
FT MUTAGEN 78
FT /note="D->A: Defective of TEN1 binding; when associated
FT with ALA-164 or ALA-167."
FT /evidence="ECO:0000269|PubMed:23826127"
FT MUTAGEN 164
FT /note="I->A: Defective of TEN1 binding; when associated
FT with ALA-78."
FT /evidence="ECO:0000269|PubMed:23826127"
FT MUTAGEN 167
FT /note="M->A: Defective of TEN1 binding; when associated
FT with ALA-78."
FT /evidence="ECO:0000269|PubMed:23826127"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:6W6W"
FT HELIX 21..24
FT /evidence="ECO:0007829|PDB:6W6W"
FT HELIX 31..36
FT /evidence="ECO:0007829|PDB:4JOI"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:4JOI"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:4JOI"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:4JOI"
FT STRAND 56..68
FT /evidence="ECO:0007829|PDB:4JOI"
FT STRAND 70..78
FT /evidence="ECO:0007829|PDB:4JOI"
FT STRAND 83..89
FT /evidence="ECO:0007829|PDB:4JOI"
FT HELIX 113..117
FT /evidence="ECO:0007829|PDB:4JOI"
FT HELIX 118..122
FT /evidence="ECO:0007829|PDB:4JOI"
FT STRAND 131..141
FT /evidence="ECO:0007829|PDB:4JOI"
FT STRAND 144..155
FT /evidence="ECO:0007829|PDB:4JOI"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:6W6W"
FT HELIX 161..176
FT /evidence="ECO:0007829|PDB:4JOI"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:4JOI"
FT HELIX 191..194
FT /evidence="ECO:0007829|PDB:4JQF"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:4JQF"
FT HELIX 201..218
FT /evidence="ECO:0007829|PDB:4JQF"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:4JQF"
FT HELIX 226..230
FT /evidence="ECO:0007829|PDB:4JQF"
FT HELIX 233..239
FT /evidence="ECO:0007829|PDB:4JQF"
FT HELIX 242..245
FT /evidence="ECO:0007829|PDB:4JQF"
FT HELIX 259..276
FT /evidence="ECO:0007829|PDB:4JQF"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:4JQF"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:4JQF"
FT STRAND 290..293
FT /evidence="ECO:0007829|PDB:4JQF"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:4JQF"
FT HELIX 298..309
FT /evidence="ECO:0007829|PDB:4JQF"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:4JQF"
FT STRAND 320..323
FT /evidence="ECO:0007829|PDB:4JQF"
FT HELIX 324..334
FT /evidence="ECO:0007829|PDB:4JQF"
FT HELIX 341..353
FT /evidence="ECO:0007829|PDB:4JQF"
FT STRAND 356..361
FT /evidence="ECO:0007829|PDB:4JQF"
FT STRAND 364..367
FT /evidence="ECO:0007829|PDB:4JQF"
SQ SEQUENCE 368 AA; 42119 MW; 087E7EF75544A1F0 CRC64;
MQPGSSRCEE ETPSLLWGLD PVFLAFAKLY IRDILDMKES RQVPGVFLYN GHPIKQVDVL
GTVIGVRERD AFYSYGVDDS TGVINCICWK KLNTESVSAA PSAARELSLT SQLKKLQETI
EQKTKIEIGD TIRVRGSIRT YREEREIHAT TYYKVDDPVW NIQIARMLEL PTIYRKVYDQ
PFHSSALEKE EALSNPGALD LPSLTSLLSE KAKEFLMENR VQSFYQQELE MVESLLSLAN
QPVIHSASSD QVNFKKDTTS KAIHSIFKNA IQLLQEKGLV FQKDDGFDNL YYVTREDKDL
HRKIHRIIQQ DCQKPNHMEK GCHFLHILAC ARLSIRPGLS EAVLQQVLEL LEDQSDIVST
MEHYYTAF
