dbPTM

MPU1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MPU1_HUMAN
UniProt AC	O75352
Protein Name	Mannose-P-dolichol utilization defect 1 protein
Gene Name	MPDU1
Organism	Homo sapiens (Human).
Sequence Length	247
Subcellular Localization	Membrane Multi-pass membrane protein .
Protein Description	Required for normal utilization of mannose-dolichol phosphate (Dol-P-Man) in the synthesis of N-linked and O-linked oligosaccharides and GPI anchors..
Protein Sequence	MAAEADGPLKRLLVPILLPEKCYDQLFVQWDLLHVPCLKILLSKGLGLGIVAGSLLVKLPQVFKILGAKSAEGLSLQSVMLELVALTGTMVYSITNNFPFSSWGEALFLMLQTITICFLVMHYRGQTVKGVAFLACYGLVLLVLLSPLTPLTVVTLLQASNVPAVVVGRLLQAATNYHNGHTGQLSAITVFLLFGGSLARIFTSIQETGDPLMAGTFVVSSLCNGLIAAQLLFYWNAKPPHKQKKAQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAAEADGPL ------CCCCCCCCH	17.63	25944712
10	Ubiquitination	AEADGPLKRLLVPIL CCCCCCHHHHHHHHH	44.10	-
10	Ubiquitination	AEADGPLKRLLVPIL CCCCCCHHHHHHHHH	44.10	-
10	2-Hydroxyisobutyrylation	AEADGPLKRLLVPIL CCCCCCHHHHHHHHH	44.10	-
43	Phosphorylation	PCLKILLSKGLGLGI HHHHHHHHCCCCCCH	22.64	-
44	Ubiquitination	CLKILLSKGLGLGIV HHHHHHHCCCCCCHH	59.11	-
54	Phosphorylation	GLGIVAGSLLVKLPQ CCCHHHHHHHHHHHH	14.59	-
64	Ubiquitination	VKLPQVFKILGAKSA HHHHHHHHHHCCCCC	37.86	-

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 MPU1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of MPU1_HUMAN !!

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 MPU1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MO4L2_HUMAN	MORF4L2	physical	17353931
PMVK_HUMAN	PMVK	physical	17353931
AAAT_HUMAN	SLC1A5	physical	17353931
QRIC2_HUMAN	QRICH2	physical	17353931
RS3A_HUMAN	RPS3A	physical	17353931
HERC2_HUMAN	HERC2	physical	17353931

Drug and Disease Associations

Kegg Disease
H00118	Congenital disorders of glycosylation (CDG) type I
OMIM Disease
609180	Congenital disorder of glycosylation 1F (CDG1F)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of MPU1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.	19413330 [Abstract]