UBIA1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: UBIA1_HUMAN
• UniProt AC: Q9Y5Z9
• Protein Name: UbiA prenyltransferase domain-containing protein 1
• Gene Name: UBIAD1
• Organism: Homo sapiens (Human).
• Sequence Length: 338
• Subcellular Localization: Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein. Mitochondrion membrane. Cytoplasm. Nucleus.
• Protein Description: Prenyltransferase that mediates the formation of menaquinone-4 (MK-4) and coenzyme Q10. MK-4 is a vitamin K2 isoform present at high concentrations in the brain, kidney and pancreas, and is required for endothelial cell development. Mediates the conversion of phylloquinone (PK) into MK-4, probably by cleaving the side chain of phylloquinone (PK) to release 2-methyl-1,4-naphthoquinone (menadione; K3) and then prenylating it with geranylgeranyl pyrophosphate (GGPP) to form MK-4. Also plays a role in cardiovascular development independently of MK-4 biosynthesis, by acting as a coenzyme Q10 biosynthetic enzyme: coenzyme Q10, also named ubiquinone, plays a important antioxidant role in the cardiovascular system. Mediates biosynthesis of coenzyme Q10 in the Golgi membrane, leading to protect cardiovascular tissues from NOS3/eNOS-dependent oxidative stress..
• Protein Sequence: MAASQVLGEKINILSGETVKAGDRDPLGNDCPEQDRLPQRSWRQKCASYVLALRPWSFSASLTPVALGSALAYRSHGVLDPRLLVGCAVAVLAVHGAGNLVNTYYDFSKGIDHKKSDDRTLVDRILEPQDVVRFGVFLYTLGCVCAACLYYLSPLKLEHLALIYFGGLSGSFLYTGGIGFKYVALGDLIILITFGPLAVMFAYAIQVGSLAIFPLVYAIPLALSTEAILHSNNTRDMESDREAGIVTLAILIGPTFSYILYNTLLFLPYLVFSILATHCTISLALPLLTIPMAFSLERQFRSQAFNKLPQRTAKLNLLLGLFYVFGIILAPAGSLPKI

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
2	Acetylation	------MAASQVLGE ------CCHHHHHHH	18.80	22223895
4	Phosphorylation	----MAASQVLGEKI ----CCHHHHHHHCE	15.98	25159151
10	Ubiquitination	ASQVLGEKINILSGE HHHHHHHCEEECCCC	38.97	22817900
10 (in isoform 1)	Ubiquitination	-	38.97	21890473
10 (in isoform 2)	Ubiquitination	-	38.97	21890473
15	Phosphorylation	GEKINILSGETVKAG HHCEEECCCCCCCCC	30.68	27050516
20	Ubiquitination	ILSGETVKAGDRDPL ECCCCCCCCCCCCCC	54.81	33845483
114	Ubiquitination	FSKGIDHKKSDDRTL CCCCCCCCCCCCCCH	50.66	-
115	Ubiquitination	SKGIDHKKSDDRTLV CCCCCCCCCCCCCHH	56.55	-
153	Phosphorylation	AACLYYLSPLKLEHL HHHHHHHCCCCCHHH	16.44	24719451
307	Ubiquitination	FRSQAFNKLPQRTAK HHHHHHHHCCHHHHH	55.90	27667366

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

Oops, there are no upstream regulatory protein records of UBIA1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of UBIA1_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 UBIA1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HMDH_HUMAN	HMGCR	physical	23169578
SOAT1_HUMAN	SOAT1	physical	23169578
VEGFA_HUMAN	VEGFA	physical	23169578

Drug and Disease Associations

• Kegg Disease
• H00959: Schnyder corneal dystrophy (SCD); Schnyder crystalline corneal dystrophy (SCCD); Crystalline stromal
• OMIM Disease
• 121800: Corneal dystrophy, Schnyder type (SCCD)
• 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

Acetylation

"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.
PubMed: 19413330