Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9H173 (SIL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nucleotide exchange factor SIL1
Alternative name(s):
BiP-associated protein
Short name=BAP
Gene names
Name:SIL1
ORF Names:UNQ545/PRO836
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length461 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (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. Ref.2

Subunit structure

Interacts with HSPA5. Ref.2

Subcellular location

Endoplasmic reticulum lumen Ref.2 Ref.7.

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. Ref.2 Ref.7

Developmental stage

Expressed in fetal kidney, fetal lung, fetal liver and at low levels in fetal brain. Ref.7

Post-translational modification

N-glycosylated. Ref.2

Involvement in disease

Marinesco-Sjoegren syndrome (MSS) [MIM:248800]: 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7 Ref.8

Sequence similarities

Belongs to the SIL1 family.

Ontologies

Keywords
   Biological processProtein transport
Translocation
Transport
   Cellular componentEndoplasmic reticulum
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   DomainSignal
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processintracellular protein transport

Non-traceable author statement Ref.1. Source: UniProtKB

protein folding

Non-traceable author statement Ref.1. Source: UniProtKB

   Cellular_componentendoplasmic reticulum

Non-traceable author statement Ref.1. Source: UniProtKB

endoplasmic reticulum lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionunfolded protein binding

Non-traceable author statement Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Potential
Chain32 – 461430Nucleotide exchange factor SIL1
PRO_0000223354

Regions

Region1 – 256256Interaction with HSPA5 and localization to the endoplasmic reticulum By similarity

Amino acid modifications

Glycosylation1931N-linked (GlcNAc...) Ref.9
Glycosylation2361N-linked (GlcNAc...) Potential

Natural variations

Natural variant801Q → R.
Corresponds to variant rs35581768 [ dbSNP | Ensembl ].
VAR_034495

Experimental info

Sequence conflict571K → E in BAC11096. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q9H173 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: C4DD7E880A610880

FASTA46152,085
        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 

« Hide

References

« Hide 'large scale' references
[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]"BAP, a mammalian BiP-associated protein, is a nucleotide exchange factor that regulates the ATPase activity of BiP."
Chung K.T., Shen Y., Hendershot L.M.
J. Biol. Chem. 277:47557-47563(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH HSPA5, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION.
[3]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
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. expand/collapse author list , 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.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
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. expand/collapse author list , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Embryo and Placenta.
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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].
Tissue: Skin.
[7]"The gene disrupted in Marinesco-Sjoegren syndrome encodes SIL1, an HSPA5 cochaperone."
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.
Nat. Genet. 37:1309-1311(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INVOLVEMENT IN MSS.
[8]"Mutations in SIL1 cause Marinesco-Sjoegren syndrome, a cerebellar ataxia with cataract and myopathy."
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. expand/collapse author list , Schroeder J.M., Lochmueller H., Topaloglu H., Voit T., Weis J., Ebinger F., Zerres K.
Nat. Genet. 37:1312-1314(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN MSS.
[9]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-193.
Tissue: Liver.
[10]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ299442 mRNA. Translation: CAC17773.1.
AF547994 mRNA. Translation: AAN84477.1.
AY358950 mRNA. Translation: AAQ89309.1.
AK074624 mRNA. Translation: BAC11096.1.
AK075177 mRNA. Translation: BAC11452.1.
CH471062 Genomic DNA. Translation: EAW62120.1.
CH471062 Genomic DNA. Translation: EAW62121.1.
BC011568 mRNA. Translation: AAH11568.1.
CCDSCCDS4209.1.
RefSeqNP_001032722.1. NM_001037633.1.
NP_071909.1. NM_022464.4.
UniGeneHs.483521.

3D structure databases

ProteinModelPortalQ9H173.
SMRQ9H173. Positions 195-459.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122145. 6 interactions.
IntActQ9H173. 3 interactions.
MINTMINT-1199811.
STRING9606.ENSP00000265195.

PTM databases

PhosphoSiteQ9H173.

Polymorphism databases

DMDM74733533.

Proteomic databases

MaxQBQ9H173.
PaxDbQ9H173.
PRIDEQ9H173.

Protocols and materials databases

DNASU64374.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265195; ENSP00000265195; ENSG00000120725.
ENST00000394817; ENSP00000378294; ENSG00000120725.
GeneID64374.
KEGGhsa:64374.
UCSCuc003ldo.3. human.

Organism-specific databases

CTD64374.
GeneCardsGC05M138282.
GeneReviewsSIL1.
HGNCHGNC:24624. SIL1.
HPAHPA011949.
MIM248800. phenotype.
608005. gene.
neXtProtNX_Q9H173.
Orphanet559. Marinesco-Sjogren syndrome.
PharmGKBPA142670916.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG310365.
HOGENOMHOG000154326.
HOVERGENHBG093955.
InParanoidQ9H173.
KOK14001.
PhylomeDBQ9H173.
TreeFamTF324307.

Gene expression databases

ArrayExpressQ9H173.
BgeeQ9H173.
CleanExHS_SIL1.
GenevestigatorQ9H173.

Family and domain databases

Gene3D1.25.10.10. 1 hit.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
[Graphical view]
SUPFAMSSF48371. SSF48371. 1 hit.
ProtoNetSearch...

Other

GeneWikiSIL1.
GenomeRNAi64374.
NextBio66295.
PROQ9H173.
SOURCESearch...

Entry information

Entry nameSIL1_HUMAN
AccessionPrimary (citable) accession number: Q9H173
Secondary accession number(s): D3DQC2, Q8N2L3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2006
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM