MVD1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MVD1_HUMAN
• UniProt AC: P53602
• Protein Name: Diphosphomevalonate decarboxylase
• Gene Name: MVD
• Organism: Homo sapiens (Human).
• Sequence Length: 400
• Protein Description: Performs the first committed step in the biosynthesis of isoprenes..
• Protein Sequence: MASEKPLAAVTCTAPVNIAVIKYWGKRDEELVLPINSSLSVTLHQDQLKTTTTAVISKDFTEDRIWLNGREEDVGQPRLQACLREIRCLARKRRNSRDGDPLPSSLSCKVHVASVNNFPTAAGLASSAAGYACLAYTLARVYGVESDLSEVARRGSGSACRSLYGGFVEWQMGEQADGKDSIARQVAPESHWPELRVLILVVSAEKKLTGSTVGMRASVETSPLLRFRAESVVPARMAEMARCIRERDFPSFAQLTMKDSNQFHATCLDTFPPISYLNAISWRIIHLVHRFNAHHGDTKVAYTFDAGPNAVIFTLDDTVAEFVAAVWHGFPPGSNGDTFLKGLQVRPAPLSAELQAALAMEPTPGGVKYIIVTQVGPGPQILDDPCAHLLGPDGLPKPAA

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	------MASEKPLAA ------CCCCCCCEE	26.79	22223895
5	Acetylation	---MASEKPLAAVTC ---CCCCCCCEEEEE	42.72	23749302
5	Ubiquitination	---MASEKPLAAVTC ---CCCCCCCEEEEE	42.72	22505724
37	Ubiquitination	ELVLPINSSLSVTLH EEEEEECCEEEEEEE	33.12	22817900
40	Phosphorylation	LPINSSLSVTLHQDQ EEECCEEEEEEEHHH	18.27	-
50	Phosphorylation	LHQDQLKTTTTAVIS EEHHHCCCCEEEEEE	37.66	16964243
51	Phosphorylation	HQDQLKTTTTAVISK EHHHCCCCEEEEEEC	22.14	28102081
52	Phosphorylation	QDQLKTTTTAVISKD HHHCCCCEEEEEECC	20.28	28102081
53	Phosphorylation	DQLKTTTTAVISKDF HHCCCCEEEEEECCC	19.48	28102081
57	Phosphorylation	TTTTAVISKDFTEDR CCEEEEEECCCCCCC	21.41	28102081
58	Ubiquitination	TTTAVISKDFTEDRI CEEEEEECCCCCCCE	45.82	21906983
62	Ubiquitination	VISKDFTEDRIWLNG EEECCCCCCCEEECC	45.33	22817900
96	Phosphorylation	LARKRRNSRDGDPLP HHHHHHCCCCCCCCC	29.91	23927012
104	Phosphorylation	RDGDPLPSSLSCKVH CCCCCCCCCCCEEEE	52.15	30266825
105	Phosphorylation	DGDPLPSSLSCKVHV CCCCCCCCCCEEEEE	23.51	23927012
107	Phosphorylation	DPLPSSLSCKVHVAS CCCCCCCCEEEEEEE	17.53	23927012
131	Phosphorylation	LASSAAGYACLAYTL HHHHHHHHHHHHHHH	6.87	-
156	Phosphorylation	SEVARRGSGSACRSL HHHHHHCCCHHHHHH	27.97	-
158	Ubiquitination	VARRGSGSACRSLYG HHHHCCCHHHHHHHH	26.37	22817900
158	Phosphorylation	VARRGSGSACRSLYG HHHHCCCHHHHHHHH	26.37	-
162	Phosphorylation	GSGSACRSLYGGFVE CCCHHHHHHHHCEEE	26.31	-
164	Phosphorylation	GSACRSLYGGFVEWQ CHHHHHHHHCEEEEE	19.22	-
179	Ubiquitination	MGEQADGKDSIARQV CCCCCCCCCCHHHHH	49.18	22817900
192	Ubiquitination	QVAPESHWPELRVLI HHCCHHHCCHHEEEE	9.42	22817900
206	Ubiquitination	ILVVSAEKKLTGSTV EEEEECCCCCCCCCC	53.45	33845483
207	Ubiquitination	LVVSAEKKLTGSTVG EEEECCCCCCCCCCC	42.67	-
207	Malonylation	LVVSAEKKLTGSTVG EEEECCCCCCCCCCC	42.67	26320211
207	Acetylation	LVVSAEKKLTGSTVG EEEECCCCCCCCCCC	42.67	25953088
209	Phosphorylation	VSAEKKLTGSTVGMR EECCCCCCCCCCCCC	37.66	20068231
211	Phosphorylation	AEKKLTGSTVGMRAS CCCCCCCCCCCCCEE	18.06	25072903
212	Phosphorylation	EKKLTGSTVGMRASV CCCCCCCCCCCCEEE	23.56	25072903
213	Ubiquitination	KKLTGSTVGMRASVE CCCCCCCCCCCEEEE	6.41	22817900
218	Phosphorylation	STVGMRASVETSPLL CCCCCCEEEECCCCC	15.32	23186163
221	Phosphorylation	GMRASVETSPLLRFR CCCEEEECCCCCCCE	33.23	27794612
222	Phosphorylation	MRASVETSPLLRFRA CCEEEECCCCCCCEE	10.47	27794612
276	Phosphorylation	DTFPPISYLNAISWR CCCCCHHHHHHHHHH	12.51	-
281	Phosphorylation	ISYLNAISWRIIHLV HHHHHHHHHHHHHHH	14.11	24719451
302	Phosphorylation	HGDTKVAYTFDAGPN CCCCEEEEEECCCCC	15.78	-
303	Phosphorylation	GDTKVAYTFDAGPNA CCCEEEEEECCCCCE	12.80	-
397	Ubiquitination	LGPDGLPKPAA---- CCCCCCCCCCC----	52.94	29967540

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
96	S	Phosphorylation	Kinase	AKT1	P31749	PSP

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of MVD1_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 MVD1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BTAF1_HUMAN	BTAF1	physical	12646231
GRP75_HUMAN	HSPA9	physical	12646231
EF1G_HUMAN	EEF1G	physical	16169070
MVD1_HUMAN	MVD	physical	8626466
ASSY_HUMAN	ASS1	physical	22863883
IF5A1_HUMAN	EIF5A	physical	22863883
PSF2_HUMAN	GINS2	physical	22863883
GLSK_HUMAN	GLS	physical	22863883
KYNU_HUMAN	KYNU	physical	22863883
SIAS_HUMAN	NANS	physical	22863883
NDRG1_HUMAN	NDRG1	physical	22863883
KS6A1_HUMAN	RPS6KA1	physical	22863883
WDR1_HUMAN	WDR1	physical	22863883

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• There are no disease associations of PTM sites.
• 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

Phosphorylation

"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, AND MASSSPECTROMETRY.
PubMed: 18669648

"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, AND MASSSPECTROMETRY.
PubMed: 17287340