dbPTM

BST1_SCHPO - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	BST1_SCHPO
UniProt AC	Q9UT41
Protein Name	GPI inositol-deacylase
Gene Name	bst1
Organism	Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length	1142
Subcellular Localization	Endoplasmic reticulum membrane Multi-pass membrane protein.
Protein Description	Involved in inositol deacylation of GPI-anchored proteins which plays important roles in the quality control and ER-associated degradation of GPI-anchored proteins..
Protein Sequence	MKDDKGRSDTVNGYYISNSKLSSGFYKRNNANTASNDEKPNLEQNDIPSVTSSGSSTPSSISIEKEIKISKGNVIVKAIRSWSLYVAIIAILLLLVILHSFQGRPQDNGCGKSYVWPSYVRFVDFDERYTRFANKYSLYLYREKSVEESDEPSGIPILFIPGNAGSYKQVRAFAAQAAHVYANAYAEDADGTLNAGKLVPDFFVVDFNEDFSAFHGQTLLDQAEYVNDAIPYILSLYRQNRKISSEYDNEAFPPPTSVILLGHSMGGIVAQATFTMKNYVDGSVNTLITLATPHAMAPLPFDRHLVEFYESIKNFWSQSFLLSPEENSLDDVLLVSIAGGGLDTHVVPEYSSISTFVPPSNGLMVFTSGIPSVWAEIDHQAMAWCENFRRVLIRGIFAIMDARTSKCTVSLNLRKELLSRAYIQGSSFQNDITQISKPIAQYKALDLDLTYVYSEMPGQLLFLNQLGVSYIRHHIFPIPKPTSSIDRFELLTDQPIDLSSSNIKVLACRLDPKIDNTISALLENGNNKVINANCHLLRELVTLLPASTAYTSSPYGGDSFYNYVLPKEKMDDYHFILVSDDSKAPASGFVVGGFSNVSLDPKTIKGSQIELFKSGRKFQFDTKGSISKRFRFPGIQSSIMAYTISVTYELYPGAVPQKEFTPMLKQSIESPFETKYHVNMSNTELSVHGISPFMEFFGKESEKSLTLEFFLNPAIYKSVYVSIQPSYYRSAGRLLMRYRTLLASFPVVVISLAAYNQFRYFHYGSAYLSMSAALEVMIRKGLIKLLFLVSILSIAFSYLISRVELIVADGADPVASWKIFAMMVPKSFWKQNHLLFGLQTAQFWFLAPLLTLMFVGLVITASVIILCVMHLLAFIYGIYLRYKGLTFTGVCQAVKFSFQCLRTRNTRKLDHGEFKKLSSFLSQRNMYYANPSLCYVYGKKHMQARIIGIMLLLLMAMTVVPFQLVYGVALCTQTVTTAKALHLARFCTKSSHYRKKLWDFYNFSCTITILMLLLAPLDFPVLIVWARNLSMHWSIPFPTHHNFFSIIPFILLTEILRTGKMLPRLNDVEYYINNVFLFLLSFYSLIYGAEKPYLIHNVVGLYFFWLLFLYAKNGFFVQNISKWPIIPRMKYFIKHKFLRSIS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
596	N-linked_Glycosylation	FVVGGFSNVSLDPKT EEEECEECEECCCCC	25.74	-
679	N-linked_Glycosylation	FETKYHVNMSNTELS CEEEEEECCCCCEEE	18.17	-
1002	N-linked_Glycosylation	KKLWDFYNFSCTITI HHHHHHHCHHHHHHH	23.50	-
1028	N-linked_Glycosylation	VLIVWARNLSMHWSI EEEEEECCCCCCCCC	28.81	-
1119	N-linked_Glycosylation	KNGFFVQNISKWPII HHCCCCCCHHCCCCH	34.89	-

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

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
Oops, there are no upstream regulatory protein records of BST1_SCHPO !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of BST1_SCHPO !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of BST1_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of BST1_SCHPO !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of BST1_SCHPO

Related Literatures of Post-Translational Modification