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Protein Page:
PIGK (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
PIGK Mediates GPI anchoring in the endoplasmic reticulum, by replacing a protein's C-terminal GPI attachment signal peptide with a pre-assembled GPI. During this transamidation reaction, the GPI transamidase forms a carbonyl intermediate with the substrate protein. Belongs to the peptidase C13 family. Note: This description may include information from UniProtKB.
Protein type: Glycan Metabolism - glycosylphosphatidylinositol (GPI)-anchor biosynthesis; Endoplasmic reticulum; EC 3.-.-.-; Membrane protein, integral; Protease
Cellular Component: endoplasmic reticulum membrane; integral to endoplasmic reticulum membrane; GPI-anchor transamidase complex
Molecular Function: protein binding; cysteine-type endopeptidase activity; protein disulfide isomerase activity; GPI-anchor transamidase activity
Biological Process: cellular protein metabolic process; protein folding; attachment of GPI anchor to protein; C-terminal protein lipidation; post-translational protein modification; proteolysis
Reference #:  Q92643 (UniProtKB)
Alt. Names/Synonyms: GPI transamidase; GPI transamidase subunit; GPI-anchor transamidase; GPI8; GPI8 homolog; hGPI8; MGC22559; phosphatidylinositol glycan anchor biosynthesis, class K; phosphatidylinositol glycan, class K; Phosphatidylinositol-glycan biosynthesis class K protein; PIG-K; PIGK
Gene Symbols: PIGK
Molecular weight: 45,252 Da
Basal Isoelectric point: 5.76  Predict pI for various phosphorylation states
Select Structure to View Below

PIGK

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 K193-u AFEQMWQkRRYNELL
0 1 K296-u DLFQRDPkNVLITDF
0 1 K331-u EIMESSYkEDQMDEK
0 1 K358-u VAQIIHQkPKLKDWH
  mouse

 
K193 AFEQMWQKRRYNELL
K296 DLFQRDPKNVLITDF
K331 QVVDSSSKEDGTAEE
K358 VAQIIHQKPKPRDWH
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