ENPP4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ENPP4_HUMAN
• UniProt AC: Q9Y6X5
• Protein Name: Bis(5'-adenosyl)-triphosphatase ENPP4
• Gene Name: ENPP4
• Organism: Homo sapiens (Human).
• Sequence Length: 453
• Subcellular Localization: Cell membrane ; Single-pass type I membrane protein .
• Protein Description: Hydrolyzes extracellular Ap3A into AMP and ADP, and Ap4A into AMP and ATP. Ap3A and Ap4A are diadenosine polyphosphates thought to induce proliferation of vascular smooth muscle cells. Acts as a procoagulant, mediating platelet aggregation at the site of nascent thrombus via release of ADP from Ap3A and activation of ADP receptors..
• Protein Sequence: MKLLVILLFSGLITGFRSDSSSSLPPKLLLVSFDGFRADYLKNYEFPHLQNFIKEGVLVEHVKNVFITKTFPNHYSIVTGLYEESHGIVANSMYDAVTKKHFSDSNDKDPFWWNEAVPIWVTNQLQENRSSAAAMWPGTDVPIHDTISSYFMNYNSSVSFEERLNNITMWLNNSNPPVTFATLYWEEPDASGHKYGPEDKENMSRVLKKIDDLIGDLVQRLKMLGLWENLNVIITSDHGMTQCSQDRLINLDSCIDHSYYTLIDLSPVAAILPKINRTEVYNKLKNCSPHMNVYLKEDIPNRFYYQHNDRIQPIILVADEGWTIVLNESSQKLGDHGYDNSLPSMHPFLAAHGPAFHKGYKHSTINIVDIYPMMCHILGLKPHPNNGTFGHTKCLLVDQWCINLPEAIAIVIGSLLVLTMLTCLIIIMQNRLSVPRPFSRLQLQEDDDDPLIG

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
10	Phosphorylation	LLVILLFSGLITGFR HHHHHHHCCHHHCCC	32.43	-
14	Phosphorylation	LLFSGLITGFRSDSS HHHCCHHHCCCCCCC	35.00	23403867
20	Phosphorylation	ITGFRSDSSSSLPPK HHCCCCCCCCCCCCE	33.11	23532336
21	Phosphorylation	TGFRSDSSSSLPPKL HCCCCCCCCCCCCEE	29.01	23532336
23	Phosphorylation	FRSDSSSSLPPKLLL CCCCCCCCCCCEEEE	47.01	24505115
68	Phosphorylation	HVKNVFITKTFPNHY EEEEEEEECCCCCCH	16.74	26074081
70	Phosphorylation	KNVFITKTFPNHYSI EEEEEECCCCCCHHH	35.36	25849741
75	Phosphorylation	TKTFPNHYSIVTGLY ECCCCCCHHHHHCCC	13.51	27080861
76	Phosphorylation	KTFPNHYSIVTGLYE CCCCCCHHHHHCCCH	11.75	26074081
79	Phosphorylation	PNHYSIVTGLYEESH CCCHHHHHCCCHHHC	21.57	26074081
82	Phosphorylation	YSIVTGLYEESHGIV HHHHHCCCHHHCCEE	20.99	27080861
155	N-linked_Glycosylation	SSYFMNYNSSVSFEE HHHHCCCCCCCCHHH	23.86	24338010
159	Phosphorylation	MNYNSSVSFEERLNN CCCCCCCCHHHHHHH	28.96	24719451
166	N-linked_Glycosylation	SFEERLNNITMWLNN CHHHHHHHHEHHHHC	35.38	24338010
168	Phosphorylation	EERLNNITMWLNNSN HHHHHHHEHHHHCCC	12.38	22210691
174	Phosphorylation	ITMWLNNSNPPVTFA HEHHHHCCCCCCEEE	50.03	22210691
179	Phosphorylation	NNSNPPVTFATLYWE HCCCCCCEEEEEEEE	17.21	22210691
276	N-linked_Glycosylation	AAILPKINRTEVYNK HHHHCCCCHHHHHHH	51.45	UniProtKB CARBOHYD
386	N-linked_Glycosylation	GLKPHPNNGTFGHTK CCCCCCCCCCCCCCE	56.16	24338010
433	Phosphorylation	IIMQNRLSVPRPFSR HHHHCCCCCCCCCCC	27.17	23312004
439	Phosphorylation	LSVPRPFSRLQLQED CCCCCCCCCCCCCCC	34.46	30266825

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

Oops, there are no upstream regulatory protein records of ENPP4_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ENPP4_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 ENPP4_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of ENPP4_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
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433, AND MASSSPECTROMETRY.
PubMed: 17081983