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Q08199

- SIL1_YEAST

UniProt

Q08199 - SIL1_YEAST

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Protein

Nucleotide exchange factor SIL1

Gene

SIL1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Required for protein translocation and folding in the endoplasmic reticulum (ER). Functions as a nucleotide exchange factor for the ER lumenal chaperone KAR2.3 Publications

GO - Molecular functioni

  1. adenyl-nucleotide exchange factor activity Source: SGD

GO - Biological processi

  1. regulation of catalytic activity Source: GOC
  2. SRP-dependent cotranslational protein targeting to membrane, translocation Source: SGD
Complete GO annotation...

Keywords - Biological processi

Protein transport, Translocation, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-33447-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleotide exchange factor SIL1
Alternative name(s):
Protein SLS1
Gene namesi
Name:SIL1
Synonyms:PER100, SLS1
Ordered Locus Names:YOL031C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XV

Organism-specific databases

CYGDiYOL031c.
SGDiS000005391. SIL1.

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi365 – 3695Missing: Abrogates interaction with KAR2. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence AnalysisAdd
BLAST
Chaini20 – 421402Nucleotide exchange factor SIL1PRO_0000223364Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi105 – 1051N-linked (GlcNAc...)Sequence Analysis
Glycosylationi181 – 1811N-linked (GlcNAc...)Sequence Analysis
Glycosylationi215 – 2151N-linked (GlcNAc...)Sequence Analysis
Glycosylationi233 – 2331N-linked (GlcNAc...)Sequence Analysis
Glycosylationi315 – 3151N-linked (GlcNAc...)Sequence Analysis
Glycosylationi333 – 3331N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ08199.
PaxDbiQ08199.
PeptideAtlasiQ08199.

Expressioni

Inductioni

By the unfolded protein response (UPR).1 Publication

Gene expression databases

GenevestigatoriQ08199.

Interactioni

Subunit structurei

Interacts with KAR2.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
KAR2P164741EBI-38850,EBI-7876

Protein-protein interaction databases

BioGridi34369. 61 interactions.
DIPiDIP-2622N.
IntActiQ08199. 6 interactions.
MINTiMINT-558162.
STRINGi4932.YOL031C.

Structurei

Secondary structure

1
421
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi127 – 13913
Helixi145 – 15814
Helixi159 – 1613
Helixi165 – 18420
Helixi190 – 20415
Helixi208 – 21710
Helixi221 – 23313
Helixi241 – 25313
Helixi266 – 27510
Turni276 – 2783
Helixi280 – 29718
Helixi321 – 33111
Helixi338 – 35518
Helixi356 – 3583
Helixi363 – 38018
Helixi389 – 40214
Turni403 – 4053

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3QMLX-ray2.31C/D113-421[»]
ProteinModelPortaliQ08199.
SMRiQ08199. Positions 125-406.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi418 – 4214Prevents secretion from ERPROSITE-ProRule annotation

Sequence similaritiesi

Belongs to the SIL1 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG244873.
HOGENOMiHOG000154325.
InParanoidiQ08199.
KOiK14001.
OMAiSHDIEFG.
OrthoDBiEOG7V1G2Q.

Family and domain databases

PROSITEiPS00014. ER_TARGET. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q08199-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVRILPIILS ALSSKLVAST ILHSSIHSVP SGGEIISAED LKELEISGNS
60 70 80 90 100
ICVDNRCYPK IFEPRHDWQP ILPGQELPGG LDIRINMDTG LKEAKLNDEK
110 120 130 140 150
NVGDNGSHEL IVSSEDMKAS PGDYEFSSDF KEMRNIIDSN PTLSSQDIAR
160 170 180 190 200
LEDSFDRIME FAHDYKHGYK IITHEFALLA NLSLNENLPL TLRELSTRVI
210 220 230 240 250
TSCLRNNPPV VEFINESFPN FKSKIMAALS NLNDSNHRSS NILIKRYLSI
260 270 280 290 300
LNELPVTSED LPIYSTVVLQ NVYERNNKDK QLQIKVLELI SKILKADMYE
310 320 330 340 350
NDDTNLILFK RNAENWSSNL QEWANEFQEM VQNKSIDELH TRTFFDTLYN
360 370 380 390 400
LKKIFKSDIT INKGFLNWLA QQCKARQSNL DNGLQERDTE QDSFDKKLID
410 420
SRHLIFGNPM AHRIKNFRDE L
Length:421
Mass (Da):48,275
Last modified:November 1, 1996 - v1
Checksum:i4F6677F5029B6209
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti51 – 511I → T in AAT93120. (PubMed:17322287)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z74773 Genomic DNA. Translation: CAA99031.1.
AY693101 Genomic DNA. Translation: AAT93120.1.
BK006948 Genomic DNA. Translation: DAA10750.1.
PIRiS66714.
RefSeqiNP_014611.1. NM_001183285.1.

Genome annotation databases

EnsemblFungiiYOL031C; YOL031C; YOL031C.
GeneIDi854126.
KEGGisce:YOL031C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z74773 Genomic DNA. Translation: CAA99031.1 .
AY693101 Genomic DNA. Translation: AAT93120.1 .
BK006948 Genomic DNA. Translation: DAA10750.1 .
PIRi S66714.
RefSeqi NP_014611.1. NM_001183285.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3QML X-ray 2.31 C/D 113-421 [» ]
ProteinModelPortali Q08199.
SMRi Q08199. Positions 125-406.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 34369. 61 interactions.
DIPi DIP-2622N.
IntActi Q08199. 6 interactions.
MINTi MINT-558162.
STRINGi 4932.YOL031C.

Proteomic databases

MaxQBi Q08199.
PaxDbi Q08199.
PeptideAtlasi Q08199.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YOL031C ; YOL031C ; YOL031C .
GeneIDi 854126.
KEGGi sce:YOL031C.

Organism-specific databases

CYGDi YOL031c.
SGDi S000005391. SIL1.

Phylogenomic databases

eggNOGi NOG244873.
HOGENOMi HOG000154325.
InParanoidi Q08199.
KOi K14001.
OMAi SHDIEFG.
OrthoDBi EOG7V1G2Q.

Enzyme and pathway databases

BioCyci YEAST:G3O-33447-MONOMER.

Miscellaneous databases

NextBioi 975837.

Gene expression databases

Genevestigatori Q08199.

Family and domain databases

PROSITEi PS00014. ER_TARGET. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation."
    Travers K.J., Patil C.K., Wodicka L., Lockhart D.J., Weissman J.S., Walter P.
    Cell 101:249-258(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  5. "LHS1 and SIL1 provide a lumenal function that is essential for protein translocation into the endoplasmic reticulum."
    Tyson J.R., Stirling C.J.
    EMBO J. 19:6440-6452(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH KAR2.
  6. "Sls1p stimulates Sec63p-mediated activation of Kar2p in a conformation-dependent manner in the yeast endoplasmic reticulum."
    Kabani M., Beckerich J.-M., Gaillardin C.
    Mol. Cell. Biol. 20:6923-6934(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH KAR2, MUTAGENESIS OF 365-PHE--LEU-369.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. Cited for: FUNCTION, INTERACTION WITH KAR2.
  9. "Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals new roles for protein glycosylation in eukaryotes."
    Kung L.A., Tao S.-C., Qian J., Smith M.G., Snyder M., Zhu H.
    Mol. Syst. Biol. 5:308-308(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSIL1_YEAST
AccessioniPrimary (citable) accession number: Q08199
Secondary accession number(s): D6W234, Q6B1H9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2006
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2420 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

External Data

Dasty 3