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There was also overexpression of PIG-U and GPI8 in lymphoma. Paper-12942924.
Alterations of GPI transamidase subunits in head and neck squamous carcinoma. Paper-13443366.
GPI transamidase is a key enzyme of this posttranslational modification. Paper-8477459.
When RM from K562 mutant K cells which lack Gpi8p were used, anti- PLAP antibody coprecipitated Gaa1p. Paper-9905279.
To definitively characterize this product, RM from K cells transfected with FLAG-tagged GPI8 were employed. Paper-9905279.
This reaction depends on GAA1 and GPI8, the latter belonging to a novel cysteine protease family. Paper-2186134.
These data, taken together, lead us to conclude that mutant K cells are defective in part of the GPI transamidase machinery. Paper-552622.
GPI8 encodes for an essential 47 kDa type I membrane glycoprotein residing on the luminal side of the ER membrane. Paper-828375.
Active site determination of Gpi8p, a caspase-related enzyme required for glycosylphosphatidylinositol anchor addition to proteins. Paper-2186134.
Reconstitution of class K cells with hGPI8 abolishes their accumulation of GPI precursors and restores C-terminal processing of GPI-anchored proteins. Paper-1238728.
A conserved proline in the last transmembrane segment of Gaa1 is required for glycosylphosphatidylinositol (GPI) recognition by GPI transamidase. Paper-10210093.
Forced overexpression of two GPIT subunits; PIG-S and GPI8 alone or in combination induced increased proliferation and invasion of breast cancer cells. Paper-12942924.
Assignment of phosphatidylinositol glycan, class K ( PIGK) gene to porcine chromosome 6q32 by somatic cell and radiation hybrid panel mapping. Paper-11034187.
Glycosylphosphatidylinositol (GPI) anchoring of proteins is catalyzed by GPI transamidase (GPIT), a multisubunit, endoplasmic reticulum (ER)-localized enzyme. Paper-12350268.
Glycosylphosphatidylinositol (GPI)-anchored proteins are synthesized as precursor proteins that are processed in the endoplasmic reticulum by GPI transamidase (GPIT). Paper-10210093.
The GPI transamidase mediates GPI anchoring in the endoplasmic reticulum, by replacing a protein's C-terminal GPI attachment signal peptide with a pre-assembled GPI. Paper-9036538.
We have identified the active site histidine and cysteine residues of leishmanial GPI8 and generated Deltagpi8 lines expressing modified GPI8 proteins. Paper-9167145.
Here we report that two subunits of mammalian GPI transamidase, GPI8 and PIG-T, form a functionally important disulfide bond between conserved cysteine residues. Paper-9668728.
With this system, rough microsomal membranes (RM) containing either [(35)S]-labeled Gaa1p or epitope-tagged Gpi8p, alternative components of the enzymatic complex, were first prepared. Paper-9905279.
GPI transamidase is localized in the endoplasmic reticulum and mediates post-translational transfer of preformed GPI to proteins bearing a carboxyl-terminal GPI attachment signal. Paper-9668728.
We also show that cysteine and histidine residues of Gpi8p, which are conserved in members of a cysteine protease family, are essential for generation of a carbonyl intermediate. Paper-8477459.
Ethanolamine phosphate linked to the first mannose residue of glycosylphosphatidylinositol (GPI) lipids is a major feature of the GPI structure that is recognized by human GPI transamidase. Paper-12350268.
Also, hGPI8 restores the ability of microsomes from the mutant cells to yield an active carbonyl in the presence of a proprotein which is considered to be an intermediate in catalysis by a transamidase. Paper-1238728.
With transamidase competent HeLa cell RM, anti- PLAP or anti-epitope antibody coprecipitated both Gaa1p and Gpi8p consistent with the assembly of the proprotein into a Gaa1p:Gpi8p-containing complex. Paper-9905279.
GPI8 and PIG-T mutants in which relevant cysteines were replaced with serines were unable to fully restore the surface expression of GPI-anchored proteins upon transfection into their respective mutant cells. Paper-9668728.
Furthermore trypanosome GPI8 forms a similar intermolecular disulfide bond via its conserved cysteine residue, suggesting that the trypanosome GPI transamidase is also a multimeric complex likely containing the orthologue of PIG-T. Paper-9668728.
We report that GPI transamidase of Trypanosoma brucei (Tb), a causative agent of African sleeping sickness, shares only three components (TbGAA1, TbGPI8, and TbGPI16) with humans and S. cerevisiae but has two other specific components, trypanosomatid transamidase 1 (TTA1) and TTA2. Paper-10029444.
The lumenal part of PIG-T/GPI16 apparently consists of a beta-propeller with a central hole that regulates the access of substrate protein C termini to the active site of the cysteine protease PIG-K/ GPI8 (gating mechanism) as well as of a polypeptide hook that embraces PIG-K/ GPI8. Paper-9725852.
These synonyms are used for gene PIGK (phosphatidylinositol glycan anchor biosynthesis, class K): PIG-K, Phosphatidylinositol-glycan biosynthesis class K protein, MGC22559, hGPI8, GPI transamidase, GPI-anchor transamidase, GPI8.
These accession numbers are used for gene PIGK: CAA68871 (NCBI_GENBANK__AC), B2R7K3 (UNIPROT__AC), AAB81597 (NCBI_GENBANK__AC), A6NEM5 (UNIPROT__AC).
PIGK is a homologue of T05E11.6 (hypothetical protein) from Caenorhabditis elegans.
PIGK is a homologue of PIGK (phosphatidylinositol glycan anchor biosynthesis, class K) from Bos taurus.
PIGK is a homologue of PIGK (phosphatidylinositol glycan anchor biosynthesis, class K) from Pan troglodytes.
PIGK is a homologue of PIGK (phosphatidylinositol glycan anchor biosynthesis, class K) from Gallus gallus.
PIGK is a homologue of PIGK (phosphatidylinositol glycan anchor biosynthesis, class K) from Canis lupus familiaris.
PIGK is a homologue of Pigk (phosphatidylinositol glycan anchor biosynthesis, class K) from Mus musculus.
PIGK is a homologue of Pigk (phosphatidylinositol glycan, class K) from Rattus norvegicus.
PIGK is a homologue of pigk (phosphatidylinositol glycan, class K) from Danio rerio.
PIGK is a homologue of Os02g0219400 (Os02g0219400) from Oryza sativa Japonica Group.
PIGK is a homologue of NCU07259 (GPI-anchor transamidase precursor) from Neurospora crassa OR74A.
PIGK is a homologue of MGG_10490 (hypothetical protein) from Magnaporthe grisea 70-15.
PIGK is a homologue of KLLA0E17105g (hypothetical protein) from Kluyveromyces lactis NRRL Y-1140.
PIGK is a homologue of GPI8 (ER membrane glycoprotein subunit of the glycosylphosphatidylinositol...) from Saccharomyces cerevisiae.
PIGK is a homologue of gpi8 (pig-K) from Schizosaccharomyces pombe.
PIGK is a homologue of CG4406 (CG4406 gene product from transcript CG4406-RA) from Drosophila melanogaster.
PIGK is a homologue of AT1G08750 (GPI-anchor transamidase, putative) from Arabidopsis thaliana.
PIGK is a homologue of AGOS_ADR299W (ADR299Wp) from Ashbya gossypii ATCC 10895.
PIGK is a homologue of AgaP_AGAP004301 (AGAP004301-PA) from Anopheles gambiae str. PEST.
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