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Protein Page:
SPFH1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

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 T2-p ______MtQARVLVA
0 1 K113-ub NYTADYDkTLIFNKI
0 2 K154-ub NLKQALQkDLNLMAP
0 1 K190-ub FELMEAEkTKLLIAA
0 1 T191 ELMEAEkTKLLIAAQ
0 1 Y262-p KAKADAEyYAAHkYA
0 1 K267-ac AEyYAAHkYATSNKH
0 1 T277-p TSNKHKLtPEYLELK
0 1 R321 YSDIRTGRESsLPSk
0 3 S324-p IRTGRESsLPSkEAL
0 1 K328-ub RESsLPSkEALEPsG
0 1 S334-p SkEALEPsGENVIQN
0 1 K342-ub GENVIQNkESTG___
  mouse

 
T2 ______MTQARLLVA
K113 NYTADYDKTLIFNKI
K154 NLKQALQKDLNTMAP
K190 FELMEAEKtKLLIAA
T191-p ELMEAEKtKLLIAAQ
Y262 KAKADAEYYAAHKYA
K267 AEYYAAHKYATSNKH
T277 TSNKHKLTPEYLELK
R321-m1 YSDGRTGrEDSLPPE
S324 GRTGrEDSLPPEEAR
E328 rEDSLPPEEAREPSG
S334 PEEAREPSGESPIQN
K342 GESPIQNKENAG___
  rat

 
T4 ____MNMTQARLLVA
K115 NYTADYDKTLIFNKI
K156 NLKQALQKDLNTMAP
K192 FELMEAEKTKLLIAA
T193 ELMEAEKTKLLIAAQ
Y264 KAKADAEYYAAHkYA
K269-ac AEYYAAHkYATSNKH
T279 TSNKHKLTPEYLELK
R323 YSDVRTEREGSLSPE
S326 VRTEREGSLSPEETH
E330 REGSLSPEETHEPSG
S336 PEETHEPSGESPIQN
K344 GESPIQNKENAG___
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