DOPO_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: DOPO_HUMAN
• UniProt AC: P09172
• Protein Name: Dopamine beta-hydroxylase
• Gene Name: DBH
• Organism: Homo sapiens (Human).
• Sequence Length: 617
• Subcellular Localization: Soluble dopamine beta-hydroxylase: Cytoplasmic vesicle, secretory vesicle lumen . Cytoplasmic vesicle, secretory vesicle, chromaffin granule lumen . Secreted .; Cytoplasmic vesicle, secretory vesicle membrane ; Single-pass type II membrane protein . Cytop
• Protein Description: Conversion of dopamine to noradrenaline..
• Protein Sequence: MPALSRWASLPGPSMREAAFMYSTAVAIFLVILVAALQGSAPRESPLPYHIPLDPEGSLELSWNVSYTQEAIHFQLLVRRLKAGVLFGMSDRGELENADLVVLWTDGDTAYFADAWSDQKGQIHLDPQQDYQLLQVQRTPEGLTLLFKRPFGTCDPKDYLIEDGTVHLVYGILEEPFRSLEAINGSGLQMGLQRVQLLKPNIPEPELPSDACTMEVQAPNIQIPSQETTYWCYIKELPKGFSRHHIIKYEPIVTKGNEALVHHMEVFQCAPEMDSVPHFSGPCDSKMKPDRLNYCRHVLAAWALGAKAFYYPEEAGLAFGGPGSSRYLRLEVHYHNPLVIEGRNDSSGIRLYYTAKLRRFNAGIMELGLVYTPVMAIPPRETAFILTGYCTDKCTQLALPPSGIHIFASQLHTHLTGRKVVTVLVRDGREWEIVNQDNHYSPHFQEIRMLKKVVSVHPGDVLITSCTYNTEDRELATVGGFGILEEMCVNYVHYYPQTQLELCKSAVDAGFLQKYFHLINRFNNEDVCTCPQASVSQQFTSVPWNSFNRDVLKALYSFAPISMHCNKSSAVRFQGEWNLQPLPKVISTLEEPTPQCPTSQGRSPAGPTVVSIGGGKG

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
14	Phosphorylation	WASLPGPSMREAAFM HCCCCCCCHHHHHHH	36.07	25262027
64	N-linked_Glycosylation	GSLELSWNVSYTQEA CCEEEEEEEECCHHH	14.96	27152332
82	Ubiquitination	QLLVRRLKAGVLFGM HHHHHHHHHHCEEEC	41.08	23503661
159	Phosphorylation	GTCDPKDYLIEDGTV CCCCCCCEEEECCCE	18.72	22210691
170	Phosphorylation	DGTVHLVYGILEEPF CCCEEEEEEEHHCCH	12.57	22210691
184	N-linked_Glycosylation	FRSLEAINGSGLQMG HHCHHHHCCCCCHHH	45.70	27152332
248	Ubiquitination	FSRHHIIKYEPIVTK CCCCEEEEEEEEEEC	42.85	23503661
310	Phosphorylation	ALGAKAFYYPEEAGL HHCCEEEECCHHHCC	23.99	-
327	Phosphorylation	GGPGSSRYLRLEVHY CCCCCCCEEEEEEEE	9.72	-
334	Phosphorylation	YLRLEVHYHNPLVIE EEEEEEEECCCEEEE	14.41	-
353	Phosphorylation	SSGIRLYYTAKLRRF CCCEEEEEEEECHHC	12.57	-
422	Phosphorylation	LTGRKVVTVLVRDGR HCCCEEEEEEEECCC	15.88	18785766
566	N-linked_Glycosylation	APISMHCNKSSAVRF CCEEECCCCCCCEEE	32.34	27152332
587	Phosphorylation	QPLPKVISTLEEPTP EECCCEEECCCCCCC	29.90	22817900
588	Phosphorylation	PLPKVISTLEEPTPQ ECCCEEECCCCCCCC	27.37	22817900
603	Phosphorylation	CPTSQGRSPAGPTVV CCCCCCCCCCCCEEE	26.40	22817900
616	Ubiquitination	VVSIGGGKG------ EEEECCCCC------	65.80	-

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of DOPO_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 DOPO_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of DOPO_HUMAN !!

Drug and Disease Associations

• Kegg Disease
• H01005: Dopamine beta-hydroxylase deficiency; Norepinephrine deficiency; Noradrenaline deficiency
• OMIM Disease
• 223360: Dopamine beta-hydroxylase deficiency (DBH deficiency)
• Kegg Drug
• D03787: Nepicastat hydrochloride (USAN); Nepicastat hydrochloride monohydrate
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-184, AND MASSSPECTROMETRY.
PubMed: 16335952