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Q9EPK6

- SIL1_MOUSE

UniProt

Q9EPK6 - SIL1_MOUSE

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Protein

Nucleotide exchange factor SIL1

Gene

Sil1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 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 HSPA5 (By similarity).By similarity

GO - Biological processi

  1. protein transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Protein transport, Translocation, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleotide exchange factor SIL1
Gene namesi
Name:Sil1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 18

Organism-specific databases

MGIiMGI:1932040. Sil1.

Subcellular locationi

Endoplasmic reticulum lumen 1 Publication

GO - Cellular componenti

  1. endoplasmic reticulum Source: MGI
  2. extracellular space Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Disruption phenotypei

Mice develop adult-onset ataxia with cerebellar Purkinje cell loss. Affected cells have intracellular protein accumulations in the endoplasmic reticulum and the nucleus.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3131Sequence AnalysisAdd
BLAST
Chaini32 – 465434Nucleotide exchange factor SIL1PRO_0000223355Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi197 – 1971N-linked (GlcNAc...)Sequence Analysis
Glycosylationi240 – 2401N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ9EPK6.
PaxDbiQ9EPK6.
PRIDEiQ9EPK6.

PTM databases

PhosphoSiteiQ9EPK6.

Expressioni

Tissue specificityi

Expressed in several areas of the brain including the cerebellum, cerebral cortex, cortical neurons, glial cells of white matter, hippocampus, olfactory bulb, Purkinje cells, inferior olive and the choroids plexus. Also expressed in the eye and skeletal muscle.3 Publications

Developmental stagei

Expressed in the developing retina and epithelial cells of the lens at E12.5. Expressed in the developing cerebral cortex at E15.5.1 Publication

Gene expression databases

BgeeiQ9EPK6.
GenevestigatoriQ9EPK6.

Interactioni

Subunit structurei

Interacts with HSPA5.1 Publication

Protein-protein interaction databases

BioGridi219881. 2 interactions.
IntActiQ9EPK6. 1 interaction.
MINTiMINT-4128883.

Structurei

3D structure databases

ProteinModelPortaliQ9EPK6.
SMRiQ9EPK6. Positions 239-324.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 260260Interaction with HSPA5 and localization to the endoplasmic reticulumAdd
BLAST

Sequence similaritiesi

Belongs to the SIL1 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG310365.
GeneTreeiENSGT00510000048102.
HOGENOMiHOG000154326.
HOVERGENiHBG093955.
InParanoidiQ9EPK6.
KOiK14001.
OMAiQGWCEIT.
OrthoDBiEOG72G176.
PhylomeDBiQ9EPK6.
TreeFamiTF324307.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q9EPK6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAPQHLPSTR MASPGMLLGL LLTSCLTLCL SCQNSNNFAL TNPEKSIHQE
60 70 80 90 100
SDTKETREEE ELDTEILEVF HPTQEWQTLQ PGQAVPAGSH VRMNLQTGVN
110 120 130 140 150
EVKLQQEDKF QNNLKGFKRG RRLDINANTY TSQDLKSALA KFKEGTEMEN
160 170 180 190 200
SKDELARQAT VKQLFRPIEE LKKEFDELNV VLETDMQIMV RLINKFNSSS
210 220 230 240 250
SSLEEKVAAL FDLEYYVHQM DNAQDLLSFG GLQVVINGLN STEPLVKEYA
260 270 280 290 300
AFVLGAAFSS NPKVQVEAIE GGALQKLLVI LATNQPLPAK KKVLFALCSL
310 320 330 340 350
LRHFPYAQQQ FLKLGGLQVL RSLVQEKSAK VLAVRVVTLL YDLVTEKMFA
360 370 380 390 400
EEEAELTQDS SPEKLQQYRQ VQLLPGLQEQ GWCEITAQLL ALPEHDAREK
410 420 430 440 450
VLQTLGALLT TCRDRYRQDL QLSRTLGRLQ AEYQALASLE LQEGEDDGYF
460
RELLASINSL MKELR
Length:465
Mass (Da):52,430
Last modified:February 21, 2006 - v2
Checksum:iC3E2DB44394F1161
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti143 – 1431K → T in CAC17789. (PubMed:11101517)Curated
Sequence conflicti152 – 1521K → Q in CAC17789. (PubMed:11101517)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ297884 mRNA. Translation: CAC17789.1.
AK170415 mRNA. Translation: BAE41781.1.
BC016119 mRNA. Translation: AAH16119.1.
BC016466 mRNA. Translation: AAH16466.1.
CCDSiCCDS29140.1.
RefSeqiNP_109674.2. NM_030749.2.
XP_006526428.1. XM_006526365.1.
XP_006526429.1. XM_006526366.1.
UniGeneiMm.291482.

Genome annotation databases

EnsembliENSMUST00000025215; ENSMUSP00000025215; ENSMUSG00000024357.
GeneIDi81500.
KEGGimmu:81500.
UCSCiuc008emc.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ297884 mRNA. Translation: CAC17789.1 .
AK170415 mRNA. Translation: BAE41781.1 .
BC016119 mRNA. Translation: AAH16119.1 .
BC016466 mRNA. Translation: AAH16466.1 .
CCDSi CCDS29140.1.
RefSeqi NP_109674.2. NM_030749.2.
XP_006526428.1. XM_006526365.1.
XP_006526429.1. XM_006526366.1.
UniGenei Mm.291482.

3D structure databases

ProteinModelPortali Q9EPK6.
SMRi Q9EPK6. Positions 239-324.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 219881. 2 interactions.
IntActi Q9EPK6. 1 interaction.
MINTi MINT-4128883.

PTM databases

PhosphoSitei Q9EPK6.

Proteomic databases

MaxQBi Q9EPK6.
PaxDbi Q9EPK6.
PRIDEi Q9EPK6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000025215 ; ENSMUSP00000025215 ; ENSMUSG00000024357 .
GeneIDi 81500.
KEGGi mmu:81500.
UCSCi uc008emc.2. mouse.

Organism-specific databases

CTDi 64374.
MGIi MGI:1932040. Sil1.

Phylogenomic databases

eggNOGi NOG310365.
GeneTreei ENSGT00510000048102.
HOGENOMi HOG000154326.
HOVERGENi HBG093955.
InParanoidi Q9EPK6.
KOi K14001.
OMAi QGWCEIT.
OrthoDBi EOG72G176.
PhylomeDBi Q9EPK6.
TreeFami TF324307.

Miscellaneous databases

ChiTaRSi SIL1. mouse.
NextBioi 350402.
PROi Q9EPK6.
SOURCEi Search...

Gene expression databases

Bgeei Q9EPK6.
Genevestigatori Q9EPK6.

Family and domain databases

Gene3Di 1.25.10.10. 1 hit.
InterProi IPR011989. ARM-like.
IPR016024. ARM-type_fold.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "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].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  4. "Protein accumulation and neurodegeneration in the woozy mutant mouse is caused by disruption of SIL1, a cochaperone of BiP."
    Zhao L., Longo-Guess C., Harris B.S., Lee J.-W., Ackerman S.L.
    Nat. Genet. 37:974-979(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HSPA5, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  5. Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
  6. Cited for: TISSUE SPECIFICITY.

Entry informationi

Entry nameiSIL1_MOUSE
AccessioniPrimary (citable) accession number: Q9EPK6
Secondary accession number(s): Q91V34
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2006
Last sequence update: February 21, 2006
Last modified: October 29, 2014
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3