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Protein Page:
SPFH1 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
SPFH1 Component of the ERLIN1/ERLIN2 complex which mediates the endoplasmic reticulum-associated degradation (ERAD) of inositol 1,4,5-trisphosphate receptors (IP3Rs). Belongs to the band 7/mec-2 family. Forms a heteromeric complex with ERLIN2. Note: This description may include information from UniProtKB.
Protein type: Membrane protein, integral
Cellular Component: endoplasmic reticulum membrane; protein complex; endoplasmic reticulum; integral to membrane
Molecular Function: protein binding
Biological Process: ER-associated protein catabolic process
Reference #:  O75477 (UniProtKB)
Alt. Names/Synonyms: Band_7 23-211 Keo4 (Interim) similar to C.elegans protein C42C1.9; C10orf69; Endoplasmic reticulum lipid raft-associated protein 1; ER lipid raft associated 1; Erlin-1; ERLIN1; ERLN1; KE04; KEO4; Protein KE04; SPFH domain family, member 1; SPFH domain-containing protein 1; SPFH1; Stomatin-prohibitin-flotillin-HflC/K domain-containing protein 1
Gene Symbols: ERLIN1
Molecular weight: 38,926 Da
Basal Isoelectric point: 7.67  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

SPFH1

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


 SS 

SS: 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.


 MS 

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


       human

 
0 1 K113-u NYTADYDkTLIFNKI
0 2 K154-u NLKQALQkDLNLMAP
0 1 K190-u FELMEAEkTKLLIAA
0 1 K267-a AEYYAAHkYATSNKH
0 2 S324-p IRTGRESsLPSkEAL
0 1 K328-u RESsLPSkEALEPSG
0 1 K342-u GENVIQNkESTG___
  mouse

 
K113 NYTADYDKTLIFNKI
K154 NLKQALQKDLNTMAP
K190 FELMEAEKTKLLIAA
K267 AEYYAAHKYATSNKH
S324 GRTGREDSLPPEEAR
E328 REDSLPPEEAREPSG
K342 GESPIQNKENAG___
  rat

 
K115 NYTADYDKTLIFNKI
K156 NLKQALQKDLNTMAP
K192 FELMEAEKTKLLIAA
K269 AEYYAAHKYATSNKH
S326 VRTEREGSLSPEETH
E330 REGSLSPEETHEPSG
K344 GESPIQNKENAG___
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