PIGW_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PIGW_HUMAN
• UniProt AC: Q7Z7B1
• Protein Name: Phosphatidylinositol-glycan biosynthesis class W protein {ECO:0000305}
• Gene Name: PIGW {ECO:0000312|HGNC:HGNC:23213}
• Organism: Homo sapiens (Human).
• Sequence Length: 504
• Subcellular Localization: Endoplasmic reticulum membrane ; Multi-pass membrane protein .
• Protein Description: Required for the transport of GPI-anchored proteins to the plasma membrane. [PubMed: 24367057 Probable acetyltransferase, which acetylates the inositol ring of phosphatidylinositol during biosynthesis of GPI-anchor. Acetylation during GPI-anchor biosynthesis is not essential for the subsequent mannosylation and is usually removed soon after the attachment of GPIs to proteins (By similarity]
• Protein Sequence: MSEKQMKEAFVSNLNGTTVLEITQGLCFPAFCILCRGFLIIFSQYLCSFSPTWKTRFLTDFVVLIVPMVATLTIWASFILLELLGVIIFGAGLLYQIYRRRTCYARLPFLKILEKFLNISLESEYNPAISCFRVITSAFTAIAILAVDFPLFPRRFAKTELYGTGAMDFGVGGFVFGSAMVCLEVRRRKYMEGSKLHYFTNSLYSVWPLVFLGIGRLAIIKSIGYQEHLTEYGVHWNFFFTIIVVKLITPLLLIIFPLNKSWIIALGITVLYQLALDFTSLKRLILYGTDGSGTRVGLLNANREGIISTLGYVAIHMAGVQTGLYMHKNRSHIKDLIKVACFLLLAAISLFISLYVVQVNVEAVSRRMANLAFCIWIVASSLILLSSLLLGDIILSFAKFLIKGALVPCSWKLIQSPVTNKKHSESLVPEAERMEPSLCLITALNRKQLIFFLLSNITTGLINLMVDTLHSSTLWALFVVNLYMFSNCLIVYVLYLQDKTVQFW

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
15	N-linked_Glycosylation	EAFVSNLNGTTVLEI HHHHHCCCCCEEEHH	50.44	UniProtKB CARBOHYD
59	Phosphorylation	TWKTRFLTDFVVLIV HHHHHHHCCCHHHHH	25.36	-
71	Phosphorylation	LIVPMVATLTIWASF HHHHHHHHHHHHHHH	17.02	-
111	Ubiquitination	YARLPFLKILEKFLN HHHCHHHHHHHHHHC	45.70	21906983
115	Ubiquitination	PFLKILEKFLNISLE HHHHHHHHHHCCCCC	52.27	22817900
287	Phosphorylation	SLKRLILYGTDGSGT CCCEEECEECCCCCC	15.81	17924679
292	Phosphorylation	ILYGTDGSGTRVGLL ECEECCCCCCEEECE	39.54	17924679
294	Phosphorylation	YGTDGSGTRVGLLNA EECCCCCCEEECEEC	24.71	17924679
412	Ubiquitination	ALVPCSWKLIQSPVT CCCCCCHHHCCCCCC	21.30	21906983
416	Phosphorylation	CSWKLIQSPVTNKKH CCHHHCCCCCCCCCC	17.84	30266825
419	Phosphorylation	KLIQSPVTNKKHSES HHCCCCCCCCCCCCC	44.71	30266825
421	Ubiquitination	IQSPVTNKKHSESLV CCCCCCCCCCCCCCC	42.36	22817900
422	Ubiquitination	QSPVTNKKHSESLVP CCCCCCCCCCCCCCC	55.20	22817900
426	Phosphorylation	TNKKHSESLVPEAER CCCCCCCCCCCHHHH	37.37	28555341
442	Phosphorylation	EPSLCLITALNRKQL CHHHHHHHHCCHHHH	16.49	24719451

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of PIGW_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PIGW_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of PIGW_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of PIGW_HUMAN !!

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 616025: Hyperphosphatasia with mental retardation syndrome 5 (HPMRS5)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-287; SER-292 ANDTHR-294, AND MASS SPECTROMETRY.
PubMed: 17924679