PIGA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PIGA_HUMAN
• UniProt AC: P37287
• Protein Name: Phosphatidylinositol N-acetylglucosaminyltransferase subunit A
• Gene Name: PIGA
• Organism: Homo sapiens (Human).
• Sequence Length: 484
• Subcellular Localization: Endoplasmic reticulum membrane; Single-pass membrane protein.
• Protein Description: Necessary for the synthesis of N-acetylglucosaminyl-phosphatidylinositol, the very early intermediate in GPI-anchor biosynthesis..
• Protein Sequence: MACRGGAGNGHRASATLSRVSPGSLYTCRTRTHNICMVSDFFYPNMGGVESHIYQLSQCLIERGHKVIIVTHAYGNRKGIRYLTSGLKVYYLPLKVMYNQSTATTLFHSLPLLRYIFVRERVTIIHSHSSFSAMAHDALFHAKTMGLQTVFTDHSLFGFADVSSVLTNKLLTVSLCDTNHIICVSYTSKENTVLRAALNPEIVSVIPNAVDPTDFTPDPFRRHDSITIVVVSRLVYRKGIDLLSGIIPELCQKYPDLNFIIGGEGPKRIILEEVRERYQLHDRVRLLGALEHKDVRNVLVQGHIFLNTSLTEAFCMAIVEAASCGLQVVSTRVGGIPEVLPENLIILCEPSVKSLCEGLEKAIFQLKSGTLPAPENIHNIVKTFYTWRNVAERTEKVYDRVSVEAVLPMDKRLDRLISHCGPVTGYIFALLAVFNFLFLIFLRWMTPDSIIDVAIDATGPRGAWTNNYSHSKRGGENNEISETR

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
4	Methylation	----MACRGGAGNGH ----CCCCCCCCCCC	36.72	115487533
21	Phosphorylation	SATLSRVSPGSLYTC CEEECCCCCCCEEEE	23.56	21712546
24	Phosphorylation	LSRVSPGSLYTCRTR ECCCCCCCEEEEECC	22.91	26993267
26	Phosphorylation	RVSPGSLYTCRTRTH CCCCCCEEEEECCCC	12.90	26552605
27	Phosphorylation	VSPGSLYTCRTRTHN CCCCCEEEEECCCCE	10.78	26552605
32	Phosphorylation	LYTCRTRTHNICMVS EEEEECCCCEEEEEE	20.75	-
85	Phosphorylation	KGIRYLTSGLKVYYL CCHHHHCCCCEEEEE	39.26	26503514
90	Phosphorylation	LTSGLKVYYLPLKVM HCCCCEEEEEECEEE	9.56	-
91	Phosphorylation	TSGLKVYYLPLKVMY CCCCEEEEEECEEEC	12.58	-
98	Phosphorylation	YLPLKVMYNQSTATT EEECEEECCCCHHHH	17.03	-
105	Phosphorylation	YNQSTATTLFHSLPL CCCCHHHHHHHHHHH	25.59	22210691
109	Phosphorylation	TATTLFHSLPLLRYI HHHHHHHHHHHHHHH	25.09	22210691
254	Phosphorylation	IPELCQKYPDLNFII HHHHHHHCCCCCEEE	3.98	26074081
293	Ubiquitination	LLGALEHKDVRNVLV HHHHHCCCCHHHHEE	48.85	-
354	Phosphorylation	LCEPSVKSLCEGLEK EECHHHHHHHHHHHH	35.78	27251275
361	Ubiquitination	SLCEGLEKAIFQLKS HHHHHHHHHHHHHHC	52.40	-
367	Ubiquitination	EKAIFQLKSGTLPAP HHHHHHHHCCCCCCC	35.74	-
385	Phosphorylation	HNIVKTFYTWRNVAE HHHHHHHHHHHHHHH	15.60	-
396	Acetylation	NVAERTEKVYDRVSV HHHHHHCHHHHCCCE	45.54	88435
402	Phosphorylation	EKVYDRVSVEAVLPM CHHHHCCCEEEECCC	18.35	26471730
467	N-linked_Glycosylation	PRGAWTNNYSHSKRG CCCCCCCCCCCCCCC	32.10	-

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PIGA_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 PIGA_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TRAF1_HUMAN	TRAF1	physical	28514442
TRFL_HUMAN	LTF	physical	28514442

Drug and Disease Associations

• Kegg Disease
• H01053: Paroxysmal nocturnal hemoglobinuria (PNH)
• OMIM Disease
• 300818: Paroxysmal nocturnal hemoglobinuria 1 (PNH1)
• 300868: Multiple congenital anomalies-hypotonia-seizures syndrome 2 (MCAHS2)
• 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

"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND MASSSPECTROMETRY.
PubMed: 18691976