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Protein

CST complex subunit STN1

Gene

STN1

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:22964711, 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). Required for efficicient replication of the duplex region of the telomere. Promotes efficient replication of lagging-strand telomeres (PubMed:22863775, PubMed:22964711). Promotes general replication start following replication-fork stalling implicating new origin firing (PubMed:22863775). May be in involved in C-strand fill-in during late S/G2 phase independent of its role in telomere duplex replication (PubMed:23142664).1 Publication7 Publications
Component of the CST complex, a complex that binds to single-stranded DNA and is required to protect telomeres from DNA degradation. 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. In addition to telomere protection, the CST complex has probably a more general role in DNA metabolism at non-telomeric sites.2 Publications

Miscellaneous

Cells expressing STN1 mutants defective for dimerization with TEN1 display elongated telomeres and telomere defects associated with telomere uncapping.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi57 – 155OBAdd BLAST99

GO - Molecular functioni

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

GO - Biological processi

  • negative regulation of telomere maintenance via telomerase Source: BHF-UCL
  • positive regulation of DNA replication Source: UniProtKB
  • telomere capping Source: BHF-UCL
  • telomere maintenance Source: UniProtKB
  • telomere maintenance via telomere lengthening Source: UniProtKB

Keywordsi

Molecular functionDNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
CST complex subunit STN1
Alternative name(s):
Oligonucleotide/oligosaccharide-binding fold-containing protein 1
Suppressor of cdc thirteen homolog
Gene namesi
Name:STN1Imported
Synonyms:OBFC1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

EuPathDBiHostDB:ENSG00000107960.10.
HGNCiHGNC:26200. STN1.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Chromosome, Nucleus, Telomere

Pathology & Biotechi

Involvement in diseasei

Cerebroretinal microangiopathy with calcifications and cysts 2 (CRMCC2)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive, multisystemic disorder characterized by intrauterine growth retardation and, later in life, premature aging symptoms, including poor growth, graying hair, liver fibrosis, portal hypertension, esophageal varices, osteopenia, pancytopenia, hypocellular bone marrow, and vascular telangiectasia resulting in gastrointestinal bleeding. Brain calcifications and white matter changes are responsible for signs including spasticity, ataxia, or dystonia observed in some patients.
See also OMIM:617341
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_078499135R → T in CRMCC2. 1 Publication1
Natural variantiVAR_078500157D → Y in CRMCC2. 1 PublicationCorresponds to variant dbSNP:rs765462548Ensembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi78D → A: Defective of TEN1 binding; when associated with ALA-164 or ALA-167. 1 Publication1
Mutagenesisi164I → A: Defective of TEN1 binding; when associated with ALA-78. 1 Publication1
Mutagenesisi167M → A: Defective of TEN1 binding; when associated with ALA-78. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi79991.
MalaCardsiSTN1.
MIMi617341. phenotype.
OpenTargetsiENSG00000107960.
Orphaneti2032. Idiopathic pulmonary fibrosis.
PharmGKBiPA134987118.

Polymorphism and mutation databases

BioMutaiOBFC1.
DMDMi62900737.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000580201 – 368CST complex subunit STN1Add BLAST368

Proteomic databases

EPDiQ9H668.
MaxQBiQ9H668.
PaxDbiQ9H668.
PeptideAtlasiQ9H668.
PRIDEiQ9H668.

PTM databases

iPTMnetiQ9H668.
PhosphoSitePlusiQ9H668.

Expressioni

Gene expression databases

BgeeiENSG00000107960.
CleanExiHS_OBFC1.
GenevisibleiQ9H668. HS.

Organism-specific databases

HPAiHPA037924.
HPA037925.

Interactioni

Subunit structurei

Component of the CST complex, composed of TEN1/C17orf106, CTC1/C17orf68 and STN1; in the complex interacts directly with TEN1 and CTC1. Interacts with ACD/TPP1, POT1 and POLA1.4 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi123054. 62 interactors.
CORUMiQ9H668.
DIPiDIP-59914N.
IntActiQ9H668. 24 interactors.
MINTiMINT-1482105.
STRINGi9606.ENSP00000224950.

Structurei

Secondary structure

1368
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi31 – 36Combined sources6
Beta strandi41 – 43Combined sources3
Beta strandi47 – 49Combined sources3
Beta strandi52 – 54Combined sources3
Beta strandi56 – 68Combined sources13
Beta strandi70 – 78Combined sources9
Beta strandi83 – 89Combined sources7
Helixi113 – 117Combined sources5
Helixi118 – 122Combined sources5
Beta strandi131 – 141Combined sources11
Beta strandi144 – 155Combined sources12
Helixi161 – 176Combined sources16
Turni177 – 179Combined sources3
Helixi191 – 194Combined sources4
Helixi196 – 198Combined sources3
Helixi201 – 218Combined sources18
Beta strandi223 – 225Combined sources3
Helixi226 – 230Combined sources5
Helixi233 – 239Combined sources7
Helixi242 – 245Combined sources4
Helixi259 – 276Combined sources18
Beta strandi279 – 281Combined sources3
Beta strandi284 – 286Combined sources3
Beta strandi290 – 293Combined sources4
Helixi294 – 296Combined sources3
Helixi298 – 309Combined sources12
Helixi311 – 313Combined sources3
Beta strandi320 – 323Combined sources4
Helixi324 – 334Combined sources11
Helixi341 – 353Combined sources13
Beta strandi356 – 361Combined sources6
Beta strandi364 – 367Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4JOIX-ray2.05A/B19-184[»]
4JQFX-ray1.60A191-368[»]
ProteinModelPortaliQ9H668.
SMRiQ9H668.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 185Interaction with CTC11 PublicationAdd BLAST185
Regioni191 – 295Winged helix-turn-helix (wHTH) 1Add BLAST105
Regioni296 – 368Winged helix-turn-helix (wHTH) 2Add BLAST73

Sequence similaritiesi

Belongs to the STN1 family.Curated

Phylogenomic databases

eggNOGiKOG3108. Eukaryota.
COG5235. LUCA.
GeneTreeiENSGT00390000000909.
HOGENOMiHOG000088638.
HOVERGENiHBG053364.
InParanoidiQ9H668.
OMAiFFYNGHP.
OrthoDBiEOG091G0A0K.
PhylomeDBiQ9H668.
TreeFamiTF328623.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiView protein in InterPro
IPR015253. CST_STN1_C.
IPR012340. NA-bd_OB-fold.
IPR004365. NA-bd_OB_tRNA.
IPR014647. Stn1.
IPR036388. WH-like_DNA-bd_sf.
IPR036390. WH_DNA-bd_sf.
PfamiView protein in Pfam
PF09170. STN1_2. 1 hit.
PF01336. tRNA_anti-codon. 1 hit.
PIRSFiPIRSF036950. UCP036950. 1 hit.
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF50249. SSF50249. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9H668-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQPGSSRCEE ETPSLLWGLD PVFLAFAKLY IRDILDMKES RQVPGVFLYN
60 70 80 90 100
GHPIKQVDVL GTVIGVRERD AFYSYGVDDS TGVINCICWK KLNTESVSAA
110 120 130 140 150
PSAARELSLT SQLKKLQETI EQKTKIEIGD TIRVRGSIRT YREEREIHAT
160 170 180 190 200
TYYKVDDPVW NIQIARMLEL PTIYRKVYDQ PFHSSALEKE EALSNPGALD
210 220 230 240 250
LPSLTSLLSE KAKEFLMENR VQSFYQQELE MVESLLSLAN QPVIHSASSD
260 270 280 290 300
QVNFKKDTTS KAIHSIFKNA IQLLQEKGLV FQKDDGFDNL YYVTREDKDL
310 320 330 340 350
HRKIHRIIQQ DCQKPNHMEK GCHFLHILAC ARLSIRPGLS EAVLQQVLEL
360
LEDQSDIVST MEHYYTAF
Length:368
Mass (Da):42,119
Last modified:April 26, 2005 - v2
Checksum:i087E7EF75544A1F0
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_078499135R → T in CRMCC2. 1 Publication1
Natural variantiVAR_022364151T → A2 PublicationsCorresponds to variant dbSNP:rs2487999Ensembl.1
Natural variantiVAR_078500157D → Y in CRMCC2. 1 PublicationCorresponds to variant dbSNP:rs765462548Ensembl.1
Natural variantiVAR_022365248S → C2 PublicationsCorresponds to variant dbSNP:rs10786775Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK026212 mRNA. Translation: BAB15396.1.
AL133355 Genomic DNA. No translation available.
CH471066 Genomic DNA. Translation: EAW49619.1.
CH471066 Genomic DNA. Translation: EAW49620.1.
BC017400 mRNA. Translation: AAH17400.1.
CCDSiCCDS7552.1.
RefSeqiNP_079204.2. NM_024928.4.
XP_006718039.1. XM_006717976.3.
XP_016872158.1. XM_017016669.1.
XP_016872159.1. XM_017016670.1.
UniGeneiHs.62314.

Genome annotation databases

EnsembliENST00000224950; ENSP00000224950; ENSG00000107960.
ENST00000369764; ENSP00000358779; ENSG00000107960.
GeneIDi79991.
KEGGihsa:79991.
UCSCiuc001kxl.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiSTN1_HUMAN
AccessioniPrimary (citable) accession number: Q9H668
Secondary accession number(s): D3DR99, Q5TCZ0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: April 26, 2005
Last modified: November 22, 2017
This is version 140 of the entry and version 2 of the sequence. See 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 10
    Human chromosome 10: 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