dbPTM

PTPS_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PTPS_HUMAN
UniProt AC	Q03393
Protein Name	6-pyruvoyl tetrahydrobiopterin synthase
Gene Name	PTS
Organism	Homo sapiens (Human).
Sequence Length	145
Subcellular Localization
Protein Description	Involved in the biosynthesis of tetrahydrobiopterin, an essential cofactor of aromatic amino acid hydroxylases. Catalyzes the transformation of 7,8-dihydroneopterin triphosphate into 6-pyruvoyl tetrahydropterin..
Protein Sequence	MSTEGGGRRCQAQVSRRISFSASHRLYSKFLSDEENLKLFGKCNNPNGHGHNYKVVVTVHGEIDPATGMVMNLADLKKYMEEAIMQPLDHKNLDMDVPYFADVVSTTENVAVYIWDNLQKVLPVGVLYKVKVYETDNNIVVYKGE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSTEGGGRR ------CCCCCCCCC	34.86	22210691
3	Phosphorylation	-----MSTEGGGRRC -----CCCCCCCCCC	37.03	22210691
19	Phosphorylation	AQVSRRISFSASHRL HCHHHCCEEEHHHHH	16.02	30266825
21	Phosphorylation	VSRRISFSASHRLYS HHHCCEEEHHHHHHH	23.28	29255136
23	Phosphorylation	RRISFSASHRLYSKF HCCEEEHHHHHHHHH	14.14	23927012
28	Phosphorylation	SASHRLYSKFLSDEE EHHHHHHHHHCCCHH	22.86	-
29	Ubiquitination	ASHRLYSKFLSDEEN HHHHHHHHHCCCHHH	36.45	22817900
32	Phosphorylation	RLYSKFLSDEENLKL HHHHHHCCCHHHHEE	46.22	-
38	Ubiquitination	LSDEENLKLFGKCNN CCCHHHHEEEEECCC	54.04	23000965
42	Ubiquitination	ENLKLFGKCNNPNGH HHHEEEEECCCCCCC	26.84	23000965
58	Phosphorylation	HNYKVVVTVHGEIDP CCCEEEEEECCEECC	8.65	-
77	Ubiquitination	VMNLADLKKYMEEAI EEEHHHHHHHHHHHH	42.26	29967540
128	Phosphorylation	VLPVGVLYKVKVYET EECEEEEEEEEEEEC	16.01	10874306
129	Ubiquitination	LPVGVLYKVKVYETD ECEEEEEEEEEEECC	31.27	33845483
131	Ubiquitination	VGVLYKVKVYETDNN EEEEEEEEEEECCCC	34.64	29967540
133	Phosphorylation	VLYKVKVYETDNNIV EEEEEEEEECCCCEE	13.85	29496907
143	Ubiquitination	DNNIVVYKGE----- CCCEEEEECC-----	44.98	21906983

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
19	S	Phosphorylation	Kinase	PRKG1	Q13976	GPS
19	S	Phosphorylation	Kinase	PRKG2	Q13237	GPS
19	S	Phosphorylation	Kinase	PKG-FAMILY	-	GPS
19	S	Phosphorylation	Kinase	PKG	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
19	S	Phosphorylation		18669648
Phosphorylation of Ser-19 is required for maximal enzyme activity.

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 PTPS_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PTPS_HUMAN	PTS	physical	16189514
PTPS_HUMAN	PTS	physical	16169070
PTPS_HUMAN	PTS	physical	25416956
SDCB1_HUMAN	SDCBP	physical	25416956
COIL_HUMAN	COIL	physical	25416956
THA10_HUMAN	THAP10	physical	25416956
LNX1_HUMAN	LNX1	physical	25416956
SAHH2_HUMAN	AHCYL1	physical	26344197
NIT1_HUMAN	NIT1	physical	26344197
PTPS_HUMAN	PTS	physical	21516116

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
261640	Hyperphenylalaninemia, BH4-deficient, A (HPABH4A)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of PTPS_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Serine 19 of human 6-pyruvoyltetrahydropterin synthase isphosphorylated by cGMP protein kinase II."; Scherer-Oppliger T., Leimbacher W., Blau N., Thoeny B.; J. Biol. Chem. 274:31341-31348(1999). Cited for: CHARACTERIZATION OF VARIANTS HPABH4A CYS-16 AND GLN-25, KINETICPARAMETERS, PHOSPHORYLATION AT SER-19, AND MUTAGENESIS OF SER-19.	10531334 [Abstract]
"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-19, AND MASSSPECTROMETRY.	18669648 [Abstract]