DDAH1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: DDAH1_HUMAN
• UniProt AC: O94760
• Protein Name: N(G),N(G)-dimethylarginine dimethylaminohydrolase 1
• Gene Name: DDAH1
• Organism: Homo sapiens (Human).
• Sequence Length: 285
• Protein Description: Hydrolyzes N(G),N(G)-dimethyl-L-arginine (ADMA) and N(G)-monomethyl-L-arginine (MMA) which act as inhibitors of NOS. Has therefore a role in the regulation of nitric oxide generation..
• Protein Sequence: MAGLGHPAAFGRATHAVVRALPESLGQHALRSAKGEEVDVARAERQHQLYVGVLGSKLGLQVVELPADESLPDCVFVEDVAVVCEETALITRPGAPSRRKEVDMMKEALEKLQLNIVEMKDENATLDGGDVLFTGREFFVGLSKRTNQRGAEILADTFKDYAVSTVPVADGLHLKSFCSMAGPNLIAIGSSESAQKALKIMQQMSDHRYDKLTVPDDIAANCIYLNIPNKGHVLLHRTPEEYPESAKVYEKLKDHMLIPVSMSELEKVDGLLTCCSVLINKKVDS

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	------MAGLGHPAA ------CCCCCCCCH	23.17	19413330
32	Phosphorylation	LGQHALRSAKGEEVD HHHHHHHHCCCCCCC	34.87	23403867
34	Acetylation	QHALRSAKGEEVDVA HHHHHHCCCCCCCHH	69.01	26051181
34	Ubiquitination	QHALRSAKGEEVDVA HHHHHHCCCCCCCHH	69.01	-
50	Phosphorylation	AERQHQLYVGVLGSK HHHHHHEEEEECCCC	6.65	-
56	Phosphorylation	LYVGVLGSKLGLQVV EEEEECCCCCCEEEE	22.13	28857561
97	Phosphorylation	ITRPGAPSRRKEVDM ECCCCCCCHHHHHHH	44.15	-
106	Ubiquitination	RKEVDMMKEALEKLQ HHHHHHHHHHHHHHC	32.95	-
144	2-Hydroxyisobutyrylation	EFFVGLSKRTNQRGA EEEEECCHHCCCCCC	69.18	-
157	Phosphorylation	GAEILADTFKDYAVS CCHHHHHHHHHCCCE	27.29	-
161	Phosphorylation	LADTFKDYAVSTVPV HHHHHHHCCCEEECC	14.97	-
222	S-nitrosocysteine	PDDIAANCIYLNIPN CCHHHCCEEEEECCC	1.53	-
222	S-nitrosylation	PDDIAANCIYLNIPN CCHHHCCEEEEECCC	1.53	22178444
247	Ubiquitination	EEYPESAKVYEKLKD HHCCCHHHHHHHHCC	55.41	-
247	Acetylation	EEYPESAKVYEKLKD HHCCCHHHHHHHHCC	55.41	27452117
253	2-Hydroxyisobutyrylation	AKVYEKLKDHMLIPV HHHHHHHCCCCEEEC	57.57	-
261	Phosphorylation	DHMLIPVSMSELEKV CCCEEECCHHHHHHH	15.96	20068231
263	Phosphorylation	MLIPVSMSELEKVDG CEEECCHHHHHHHCH	31.36	20068231
274	S-nitrosocysteine	KVDGLLTCCSVLINK HHCHHHHHHHHHHCC	1.32	-
274	S-nitrosylation	KVDGLLTCCSVLINK HHCHHHHHHHHHHCC	1.32	22178444

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

Oops, there are no upstream regulatory protein records of DDAH1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of DDAH1_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 DDAH1_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of DDAH1_HUMAN !!

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
• DB00155: L-Citrulline

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

"Purification, cDNA cloning and expression of human NG,NG-dimethylarginine dimethylaminohydrolase.";
Kimoto M., Miyatake S., Sasagawa T., Yamashita H., Okita M., Oka T.,Ogawa T., Tsuji H.;
Eur. J. Biochem. 258:863-868(1998).
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 2-12 AND35-50, ABSENCE OF BOUND ZINC, AND ACETYLATION AT ALA-2.
PubMed: 9874257