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Protein Page:
DERL1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
DERL1 Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins. May act by forming a channel that allows the retrotranslocation of misfolded proteins into the cytosol where they are ubiquitinated and degraded by the proteasome. May mediate the interaction between VCP and the degradation substrate. In case of infection by cytomegaloviruses, it plays a central role in the export from the ER and subsequent degradation of MHC class I heavy chains via its interaction with US11 viral protein, which recognizes and associates with MHC class I heavy chains. Also participates in the degradation process of misfolded cytomegalovirus US2 protein. Forms homo- and heterooligomers with DERL2 and DERL3; binding to DERL3 is poorer than that between DERL2 and DERL3. Interacts with AMFR, VIMP/SELS, SEL1L, SYVN1 and VCP, as well as with SEL1L-SYVN1 and VCP-VIMP protein complexes; this interaction is weaker than that observed between DERL2 and these complexes. Interacts with the cytomegalovirus US11 protein. Interacts with NGLY1 and YOD1. Does not bind to EDEM1. Interacts with RNF103. Up-regulated in response to endoplasmic reticulum stress via the ERN1-XBP1 pathway of the unfolded protein response (UPR). Ubiquitous. Belongs to the derlin family. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Chaperone; Endoplasmic reticulum; Membrane protein, integral; Membrane protein, multi-pass
Chromosomal Location of Human Ortholog: 8q24.13
Cellular Component: endoplasmic reticulum; integral to endoplasmic reticulum membrane; integral to membrane; membrane
Molecular Function: ATPase binding; MHC class I protein binding; protease binding; protein binding; ubiquitin protein ligase binding
Biological Process: ER-associated protein catabolic process; establishment of protein localization; intracellular transport of viral proteins in host cell; positive regulation of protein binding; positive regulation of protein ubiquitination; protein destabilization; protein homooligomerization; response to unfolded protein; retrograde protein transport, ER to cytosol; unfolded protein response
Reference #:  Q9BUN8 (UniProtKB)
Alt. Names/Synonyms: Degradation in endoplasmic reticulum protein 1; DER-1; DER1; Der1-like domain family, member 1; Der1-like protein 1; DERL1; Derlin-1; DERtrin-1; FLJ13784; FLJ42092; MGC3067; PRO2577
Gene Symbols: DERL1
Molecular weight: 28,801 Da
Basal Isoelectric point: 9.54  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

DERL1

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment



 LTP 

LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
0 1 S10 DIGDWFRSIPAITRY
0 1 S35 VGKLGLISPAYLFLW
0 1 Y38 LGLISPAYLFLWPEA
0 1 Y190‑p YFFLMFRyPMDLGGR
0 13 S201‑p LGGRNFLstPQFLYR
0 8 T202‑p GGRNFLstPQFLYRW
0 1 R214‑m1 YRWLPSRrGGVsGFG
0 2 S218‑p PSRrGGVsGFGVPPA
0 12 S226‑p GFGVPPAsMRRAADQ
  DERL1 iso2  
S10 DIGDWFRSIPAITRY
S35 VGKLGLISPAYLFLW
Y38 LGLISPAYLFLWPEA
Y170 NYIIGGSYPMDLGGR
S181 LGGRNFLSTPQFLYR
T182 GGRNFLSTPQFLYRW
R194 YRWLPSRRGGVSGFG
S198 PSRRGGVSGFGVPPA
S206 GFGVPPASMRRAADQ
  mouse

 
S10‑p DIGDWFRsIPAITRY
S35‑p IGKLGIIsPAyFFLW
Y38‑p LGIIsPAyFFLWPEA
Y190 YFFLMFRYPMDLGGR
S201‑p LGGRNFLsTPQFLYR
T202 GGRNFLsTPQFLYRW
R214 YRWLPSRRGGVSGFG
S218 PSRRGGVSGFGVPPA
S226‑p GFGVPPAsMRRAADQ
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