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UniProtKB/Swiss-Prot entry Q9H173


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name SIL1_HUMAN
Primary accession number Q9H173
Secondary accession number Q8N2L3
Integrated into Swiss-Prot on February 21, 2006
Sequence was last modified on March 1, 2001 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 56)
Name and origin of the protein
Protein name Nucleotide exchange factor SIL1 [Precursor]
Synonyms BiP-associated protein
BAP
Gene name
Name: SIL1
ORFNames: UNQ545/PRO836
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1093/emboj/19.23.6440; PubMed=11101517 [NCBI, ExPASy, EBI, Israel, Japan]
Tyson J.R., Stirling C.J.;
"LHS1 and SIL1 provide a lumenal function that is essential for protein translocation into the endoplasmic reticulum.";
EMBO J. 19:6440-6452(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH HSPA5, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION.
DOI=10.1074/jbc.M208377200; PubMed=12356756 [NCBI, ExPASy, EBI, Israel, Japan]
Chung K.T., Shen Y., Hendershot L.M.;
"BAP, a mammalian BiP-associated protein, is a nucleotide exchange factor that regulates the ATPase activity of BiP.";
J. Biol. Chem. 277:47557-47563(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
DOI=10.1101/gr.1293003; PubMed=12975309 [NCBI, ExPASy, EBI, Israel, Japan]
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Embryo, and Placenta;
DOI=10.1093/dnares/12.2.117; PubMed=16303743 [NCBI, ExPASy, EBI, Israel, Japan]
Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y., Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.;
"Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries.";
DNA Res. 12:117-126(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INVOLVEMENT IN MSS.
DOI=10.1038/ng1677; PubMed=16282978 [NCBI, ExPASy, EBI, Israel, Japan]
Anttonen A.-K., Mahjneh I., Haemaelaeinen R.H., Lagier-Tourenne C., Kopra O., Waris L., Anttonen M., Joensuu T., Kalimo H., Paetau A., Tranebjaerg L., Chaigne D., Koenig M., Eeg-Olofsson O., Udd B., Somer M., Somer H., Lehesjoki A.-E.;
"The gene disrupted in Marinesco-Sjoegren syndrome encodes SIL1, an HSPA5 cochaperone.";
Nat. Genet. 37:1309-1311(2005).
[7]
INVOLVEMENT IN MSS.
DOI=10.1038/ng1678; PubMed=16282977 [NCBI, ExPASy, EBI, Israel, Japan]
Senderek J., Krieger M., Stendel C., Bergmann C., Moser M., Breitbach-Faller N., Rudnik-Schoeneborn S., Blaschek A., Wolf N.I., Harting I., North K., Smith J., Muntoni F., Brockington M., Quijano-Roy S., Renault F., Herrmann R., Hendershot L.M., Schroeder J.M., Lochmueller H., Topaloglu H., Voit T., Weis J., Ebinger F., Zerres K.;
"Mutations in SIL1 cause Marinesco-Sjoegren syndrome, a cerebellar ataxia with cataract and myopathy.";
Nat. Genet. 37:1312-1314(2005).
[8]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-193, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1021/pr8008012; PubMed=19159218 [NCBI, ExPASy, EBI, Israel, Japan]
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
Comments
  • FUNCTION: Required for protein translocation and folding in the endoplasmic reticulum (ER). Functions as a nucleotide exchange factor for the ER lumenal chaperone HSPA5.
  • SUBUNIT: Interacts with HSPA5.
  • SUBCELLULAR LOCATION: Endoplasmic reticulum lumen.
  • TISSUE SPECIFICITY: Highly expressed in tissues which produce large amounts of secreted proteins such as kidney, liver and placenta. Also expressed in colon, heart, lung, ovary, pancreas, peripheral leukocyte, prostate, spleen and thymus. Expressed at low levels throughout the brain.
  • DEVELOPMENTAL STAGE: Expressed in fetal kidney, fetal lung, fetal liver and at low levels in fetal brain.
  • PTM: N-glycosylated.
  • DISEASE: Defects in SIL1 are a cause of Marinesco-Sjoegren syndrome (MSS) [MIM:248800]. MSS is an autosomal recessive multisystem disorder which is characterized by cerebellar ataxia due to cerebellar atrophy, with Purkinje and granule cell loss and myopathy featuring marked muscle replacement with fat and connective tissue. Other cardinal features include bilateral cataracts, hypergonadotrophic hypogonadism and mild to severe mental retardation. Skeletal abnormalities, short stature, dysarthria, strabismus and nystagmus are also frequent findings. Mutational inactivation of this protein may result in ER stress-induced cell death signaling or malfunctioning chaperone machineries that mishandle client proteins which are critical for the organs targeted in MSS.
  • SIMILARITY: Belongs to the SIL1 family.
  • WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=SIL1";.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AJ299442; CAC17773.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF547994; AAN84477.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY358950; AAQ89309.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK074624; BAC11096.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK075177; BAC11452.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC011568; AAH11568.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00296197; -.
RefSeq NP_001032722.1; -.
NP_071909.1; -.
UniGene Hs.483521
3D structure databases
ModBase Q9H173.
PTM databases
PhosphoSite Q9H173; -.
Organism-specific databases
GeneCards GC05M138310; -.
H-InvDB HIX0005218; -.
HGNC HGNC:24624; SIL1.
GenAtlas SIL1.
HPA HPA011949; -.
MIM 248800; phenotype. [NCBI / EBI]
608005; gene. [NCBI / EBI]
Orphanet 559; Marinesco-Sjogren syndrome.
PharmGKB PA142670916; -.
Gene expression databases
ArrayExpress Q9H173; -.
Bgee Q9H173; -.
CleanEx HS_SIL1; -.
GermOnline ENSG00000120725; Homo sapiens.
Ontologies
GO
GO:0005783; Cellular component: endoplasmic reticulum (non-traceable author statement from UniProtKB).
GO:0005788; Cellular component: endoplasmic reticulum lumen (inferred from electronic annotation from UniProtKB-SubCell).
GO:0051082; Molecular function: unfolded protein binding (non-traceable author statement from UniProtKB).
GO:0065002; Biological process: intracellular protein transmembrane transport (inferred from electronic annotation from UniProtKB-KW).
GO:0006457; Biological process: protein folding (non-traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR011989; ARM-like.
Graphical view of domain structure.
Gene3D G3DSA:1.25.10.10; ARM-like; 1.
Proteomic databases
PRIDE Q9H173; -.
Genome annotation databases
Ensembl ENSG00000120725; Homo sapiens. [Contig view]
GeneID 64374; -.
KEGG hsa:64374; -.
Phylogenomic databases
HOGENOM Q9H173; -.
HOVERGEN Q9H173; -.
OMA Q9H173; LREQGWC.
Other
NextBio 66295; -.
SOURCE SIL1; Homo sapiens.
ProtoNet Q9H173.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Disease mutation; Endoplasmic reticulum; Glycoprotein; Polymorphism; Protein transport; Signal; Translocation; Transport.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    31  31     Potential. 
CHAIN   32   461  430     Nucleotide exchange factor SIL1. PRO_0000223354
REGION   1   256  256     Interaction with HSPA5 and localization to the endoplasmic reticulum (By similarity). 
CARBOHYD   193   193        N-linked (GlcNAc...). 
CARBOHYD   236   236        N-linked (GlcNAc...) (Potential). 
VARIANT   80    80  1     Q -> R (in dbSNP:rs35581768 [NCBI]). VAR_034495 
CONFLICT   57    57        K -> E (in Ref. 4; BAC11096). 
Sequence information
Length: 461 AA [This is the length of the unprocessed precursor] Molecular weight: 52085 Da [This is the MW of the unprocessed precursor] CRC64: C4DD7E880A610880 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAPQSLPSSR MAPLGMLLGL LMAACFTFCL SHQNLKEFAL TNPEKSSTKE TERKETKAEE 

        70         80         90        100        110        120 
ELDAEVLEVF HPTHEWQALQ PGQAVPAGSH VRLNLQTGER EAKLQYEDKF RNNLKGKRLD 

       130        140        150        160        170        180 
INTNTYTSQD LKSALAKFKE GAEMESSKED KARQAEVKRL FRPIEELKKD FDELNVVIET 

       190        200        210        220        230        240 
DMQIMVRLIN KFNSSSSSLE EKIAALFDLE YYVHQMDNAQ DLLSFGGLQV VINGLNSTEP 

       250        260        270        280        290        300 
LVKEYAAFVL GAAFSSNPKV QVEAIEGGAL QKLLVILATE QPLTAKKKVL FALCSLLRHF 

       310        320        330        340        350        360 
PYAQRQFLKL GGLQVLRTLV QEKGTEVLAV RVVTLLYDLV TEKMFAEEEA ELTQEMSPEK 

       370        380        390        400        410        420 
LQQYRQVHLL PGLWEQGWCE ITAHLLALPE HDAREKVLQT LGVLLTTCRD RYRQDPQLGR 

       430        440        450        460 
TLASLQAEYQ VLASLELQDG EDEGYFQELL GSVNSLLKEL R 

Q9H173 in FASTA format

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