P38960 (STN1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein STN1

Gene names

Name:	STN1
Ordered Locus Names:	YDR082W
ORF Names:	D4456, YD8554.15

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	494 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Has a role in telomere length regulation and telomere end protection. Acts as an inhibitor of telomerase loading through its interaction with CDC13. Ref.1 Ref.6
Subunit structure	Interacts with CDC13 and TEN1. Ref.6 Ref.7
Subcellular location	Chromosome › telomere Probable.

Ontologies

Keywords
Cellular component	Chromosome Telomere
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	negative regulation of telomere maintenance via telomerase Inferred from mutant phenotype. Source: SGD telomere capping Inferred from mutant phenotype Ref.1. Source: SGD
Cellular component	nuclear telomere cap complex Inferred from physical interaction Ref.6Ref.1. Source: SGD
Molecular function	protein binding Inferred from physical interaction Ref.6. Source: IntAct single-stranded telomeric DNA binding Inferred from direct assay. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CDC13	P32797	5	EBI-18427,EBI-4187
POL12	P38121	2	EBI-18427,EBI-6111
TEN1	Q07921	7	EBI-18427,EBI-35131

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 494

494

Protein STN1

PRO_0000072279

Amino acid modifications

Modified residue

283

1

Phosphoserine Ref.8

Secondary structure

1

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494

Helix Strand Turn

Details...

Helix

315 – 323

9

Beta strand

328 – 332

5

Helix

333 – 337

5

Helix

340 – 356

17

Helix

365 – 382

18

Turn

391 – 394

4

Beta strand

395 – 397

3

Helix

399 – 417

19

Helix

427 – 434

8

Helix

445 – 458

14

Turn

460 – 462

3

Beta strand

463 – 469

7

Beta strand

484 – 489

6

Turn

491 – 493

3

Sequences

	Sequence		Length	Mass (Da)
	P38960 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 61B691C8D4A2E650	FASTA	494	57,511
	10 20 30 40 50 60 MDKYGHIAHQ EGDVCYYIPR LFKYNSYYSG TEDVRIFVGD LKYRMRVSLQ ICEKYYDRRL 70 80 90 100 110 120 SMLFWKNHPL QQIHLIGCII GLQFKWIGKQ EYIFFQLDDC TSDSSLVGYT SDMRFLTCKV 130 140 150 160 170 180 KKDSILSWGL NITDLIGLTL HVYGQASLNY QELQVEYLRL CYSLTEEIDH WKITMNMREQ 190 200 210 220 230 240 LDTPWSLSDF VIGELFTQEQ EWTPETSQIE VVNPDFVGIG YKTPESKRNE TTFIEQLQEE 250 260 270 280 290 300 RLKDELEIIS PYNSTDTSNS VHSLSFRFVS SLKDFPETHF LNSGDQIDNG NDEQLKKLEY 310 320 330 340 350 360 QSANLPVMIP NRTSAKSNLM LILLGLQMKE ISNSDLYKLK EVRSVVTSLA SFLFQQQNVG 370 380 390 400 410 420 VMKSFDSLEK EAFRDLVNRL VSQGLIGLKD KTSETFDLLP LKNLFEYAEK RISVLMKLQC 430 440 450 460 470 480 YTGTVQLSHV QEKLHLPYIT TNGIVDVFKE CLKRTKKQYP EVLKNWWIDL DPKNGMEDQN 490 SGILLHLEYA AAYS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Stn1, a new Saccharomyces cerevisiae protein, is implicated in telomere size regulation in association with Cdc13." Grandin N., Reed S.I., Charbonneau M. Genes Dev. 11:512-527(1997) [PubMed: 9042864] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[2]	"Analysis of a 32.8 kb segment of yeast chromosome IV reveals 21 open reading frames, including TPS2, PPH3, RAD55, SED1, PDC2, AFR1, SSS1, SLU7 and a tRNA for arginine." Coster F., Jonniaux J.-L., Goffeau A. Yeast 11:673-679(1995) [PubMed: 7483840] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P. Nature 387:75-78(1997) [PubMed: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[6]	"Ten1 functions in telomere end protection and length regulation in association with Stn1 and Cdc13." Grandin N., Damon C., Charbonneau M. EMBO J. 20:1173-1183(2001) [PubMed: 11230140] [Abstract] Cited for: FUNCTION, INTERACTION WITH TEN1.
[7]	"Cdc13 both positively and negatively regulates telomere replication." Chandra A., Hughes T.R., Nugent C.I., Lundblad V. Genes Dev. 15:404-414(2001) [PubMed: 11230149] [Abstract] Cited for: INTERACTION WITH CDC13.
[8]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF002132 Genomic DNA. Translation: AAB60885.1.
X82086 Genomic DNA. Translation: CAA57609.1.
Z46796 Genomic DNA. Translation: CAA86804.1.
Z74378 Genomic DNA. Translation: CAA98902.1.
AY723774 Genomic DNA. Translation: AAU09691.1.
BK006938 Genomic DNA. Translation: DAA11929.1.

PIR

S48769.

RefSeq

NP_010367.1. NM_001180390.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3K10	X-ray	2.50	A	313-491	[»]
3KEY	X-ray	2.10	A	311-494	[»]

ProteinModelPortal

P38960.

SMR

P38960. Positions 312-494.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1230N.

IntAct

P38960. 5 interactions.

MINT

MINT-402087.

STRING

P38960.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YDR082W; YDR082W; YDR082W.

GeneID

851655.

KEGG

sce:YDR082W.

NMPDR

fig|4932.3.peg.1113.

Organism-specific databases

CYGD

YDR082w.

SGD

S000002489. STN1.

Phylogenomic databases

eggNOG

fuNOG12940.

OMA

YINSRIC.

OrthoDB

EOG4WQ4C8.

Gene expression databases

ArrayExpress

P38960.

Genevestigator

P38960.

GermOnline

YDR082W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR024263. STN1_C.
IPR018856. Telomere_reg-Stn1_N.
[Graphical view]

KO

K11117.

Pfam

PF10451. Stn1. 1 hit.
PF12659. Stn1_C. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

969251.

Entry information

Entry name

STN1_YEAST

Accession

Primary (citable) accession number: P38960
Secondary accession number(s): D6VS69

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	December 14, 2011
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program