Human Gene SEL1L (uc010tvv.2) Description and Page Index
Description: Homo sapiens sel-1 suppressor of lin-12-like (C. elegans) (SEL1L), transcript variant 1, mRNA. RefSeq Summary (NM_005065): The protein encoded by this gene is part of a protein complex required for the retrotranslocation or dislocation of misfolded proteins from the endoplasmic reticulum lumen to the cytosol, where they are degraded by the proteasome in a ubiquitin-dependent manner. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Oct 2011]. Transcript (Including UTRs) Position: hg19 chr14:81,937,891-82,000,205 Size: 62,315 Total Exon Count: 21 Strand: - Coding Region Position: hg19 chr14:81,943,316-82,000,088 Size: 56,773 Coding Exon Count: 21
ID:SE1L1_HUMAN DESCRIPTION: RecName: Full=Protein sel-1 homolog 1; AltName: Full=Suppressor of lin-12-like protein 1; Short=Sel-1L; Flags: Precursor; FUNCTION: May play a role in Notch signaling (By similarity). May be involved in the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. SUBUNIT: Part of a complex containing SEL1L, SYVN1 and DERL2. May form a complex with ERLEC1, HSPA5, OS9, and SYVN1. Interacts with FOXRED2 and EDEM1. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein. TISSUE SPECIFICITY: Highly expressed in pancreas. PTM: N-glycosylated. SIMILARITY: Belongs to the sel-1 family. SIMILARITY: Contains 1 fibronectin type-II domain. SIMILARITY: Contains 11 Sel1-like repeats. WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/SEL1LID42246ch14q24.html";
Genetic Association Studies of Complex Diseases and Disorders
Genetic Association Database (archive): SEL1L CDC HuGE Published Literature: SEL1L Positive Disease Associations: Platelet Aggregation Related Studies:
Platelet Aggregation Qiong Yang et al. BMC medical genetics 2007, Genome-wide association and linkage analyses of hemostatic factors and hematological phenotypes in the Framingham Heart Study., BMC medical genetics.
Using genome-wide association methodology, we have successfully identified a SNP in complete LD with a sequence variant previously shown to be strongly associated with factor VII, providing proof of principle for this approach. Further study of additional strongly associated SNPs and linked regions may identify novel variants that influence the inter-individual variability in hemostatic factors and hematological phenotypes.
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on Q9UBV2
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
R-HSA-5362441 C-terminal Hh fragments are recruited to SEL1:SYVN1 at the ER membrane R-HSA-5387386 Hh processing variants are recruited to SEL1:SYVN at the ER membrane R-HSA-5362459 VCP-catalyzed ATP hydrolysis promotes the translocation of Hh-C into the cytosol R-HSA-5387389 Hh processing variants are translocated to the cytosol in a VCP-dependent manner R-HSA-8866551 CFTR binds components of the ERAD machinery for ubiquitination and degradation R-HSA-8866857 CFTR F508del binds components of the ERAD machinery for ubiquitination and degradation R-HSA-8866542 VCP-catalyzed ATP hydrolysis promotes the translocation of misfolded CFTR into the cytosol R-HSA-8866854 VCP-catalyzed ATP hydrolysis promotes the translocation of CFTR F508del into the cytosol R-HSA-5362412 SYVN1 ubiquitinates Hh C-terminal fragments R-HSA-5483238 Hh processing variants are ubiquitinated R-HSA-8866546 RNF5 and RNF185 ubiquitinate misfolded CFTR R-HSA-8866856 RNF5 and RNF185 ubiquitinate CFTR F508del R-HSA-8867288 OS9:SEL1:ERAD E3 ligase:DERL2 ubiquitinates unfolded protein:(GlcNAc)2 (Man)9-5 R-HSA-1022127 OS9:SEL1:ERAD E3 ligase:DERL2 transports Ub-unfolded protein:(GlcNAc)2 (Man)9-5 from ERQC to cytosol R-HSA-5358346 Hedgehog ligand biogenesis R-HSA-5362768 Hh mutants that don't undergo autocatalytic processing are degraded by ERAD R-HSA-382556 ABC-family proteins mediated transport R-HSA-5678895 Defective CFTR causes cystic fibrosis R-HSA-5358351 Signaling by Hedgehog R-HSA-5387390 Hh mutants abrogate ligand secretion R-HSA-382551 Transport of small molecules R-HSA-5619084 ABC transporter disorders R-HSA-901032 ER Quality Control Compartment (ERQC) R-HSA-162582 Signal Transduction R-HSA-5663202 Diseases of signal transduction R-HSA-5619115 Disorders of transmembrane transporters R-HSA-901042 Calnexin/calreticulin cycle R-HSA-1643685 Disease R-HSA-532668 N-glycan trimming in the ER and Calnexin/Calreticulin cycle R-HSA-446203 Asparagine N-linked glycosylation R-HSA-597592 Post-translational protein modification R-HSA-392499 Metabolism of proteins