dbPTM

IMT3_SCHPO - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	IMT3_SCHPO
UniProt AC	Q10323
Protein Name	Inositol phosphoceramide mannosyltransferase 3
Gene Name	SPAC17G8.11c
Organism	Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length	356
Subcellular Localization	Endoplasmic reticulum membrane Multi-pass membrane protein. Golgi apparatus, cis-Golgi network membrane Multi-pass membrane protein. Golgi apparatus, trans-Golgi network membrane Multi-pass membrane protein.
Protein Description	With imt1 and imt2, is required for the synthesis of mannosylinositol phosphoceramide (MIPC). Catalyzes the addition of mannosyl to inositol phosphoceramide (IPC). MIPC is essential for cell morphology, cell-surface distribution of ergosterol, localization for plasma-membrane transporters, and lipid-raft-mediated endocytosis of plasma membrane proteins to the vacuole..
Protein Sequence	MNKILFYFFFFLTLILSATVYLFGGPMMLFFINYKTDLLKVDDVYNHEIYSNQSAAIPKIIHQTWKTNEIPEKWVGAQKSCIDLHPDYEYVLWTDESMREFIATDYPWFLTQYDSYPYNIERADVVRYFILYKYGGIYLDLDVGCNRTLDPLLHYPAWVRRTSPSGISNNVMGFAKGHPFLLQVVRNLPRFAFNYHFPYLTVMYSTGPLFLSIIWSAWRKLPDAEAWHHIWVMVPELYEKSHHAFFEIYEGSSWHDSDAGFVFYMLHHWAIFTFLGFLTFFIVVYFIFGYALKPAARVSRTGRRVFSSPFSKTSPSRWKIFHRFTSSNEKYDQTRSDSLPFMSDYDLESQTQSHSP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
52	N-linked_Glycosylation	YNHEIYSNQSAAIPK CCCCCCCCCCCHHHH	23.89	-
146	N-linked_Glycosylation	LDLDVGCNRTLDPLL EEEECCCCCCCHHHH	33.76	-
307	Phosphorylation	RTGRRVFSSPFSKTS CCCCEEECCCCCCCC	33.96	28889911
308	Phosphorylation	TGRRVFSSPFSKTSP CCCEEECCCCCCCCH	20.64	28889911
311	Phosphorylation	RVFSSPFSKTSPSRW EEECCCCCCCCHHHH	38.11	29996109
326	Phosphorylation	KIFHRFTSSNEKYDQ HEEEECCCCCCCCCC	28.58	25720772
327	Phosphorylation	IFHRFTSSNEKYDQT EEEECCCCCCCCCCC	46.05	25720772
338	Phosphorylation	YDQTRSDSLPFMSDY CCCCCCCCCCCCCCC	38.91	25720772
345	Phosphorylation	SLPFMSDYDLESQTQ CCCCCCCCCHHHHCC	18.34	25720772
349	Phosphorylation	MSDYDLESQTQSHSP CCCCCHHHHCCCCCC	45.91	24763107
353	Phosphorylation	DLESQTQSHSP---- CHHHHCCCCCC----	29.35	28889911
355	Phosphorylation	ESQTQSHSP------ HHHCCCCCC------	37.24	28889911

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 IMT3_SCHPO !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of IMT3_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 IMT3_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of IMT3_SCHPO !!

Drug and Disease Associations

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

Regulatory Network of IMT3_SCHPO

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Phosphoproteome analysis of fission yeast."; Wilson-Grady J.T., Villen J., Gygi S.P.; J. Proteome Res. 7:1088-1097(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307; SER-353 ANDSER-355, AND MASS SPECTROMETRY.	18257517 [Abstract]