dbPTM

NOS3_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NOS3_MOUSE
UniProt AC	P70313
Protein Name	Nitric oxide synthase, endothelial
Gene Name	Nos3
Organism	Mus musculus (Mouse).
Sequence Length	1202
Subcellular Localization	Membrane, caveola. Cytoplasm, cytoskeleton. Golgi apparatus. Cell membrane. Specifically associates with actin cytoskeleton in the G2 phase of the cell cycle, which is favored by interaction with NOSIP and results in a reduced enzymatic activity..
Protein Description	Produces nitric oxide (NO) which is implicated in vascular smooth muscle relaxation through a cGMP-mediated signal transduction pathway. NO mediates vascular endothelial growth factor (VEGF)-induced angiogenesis in coronary vessels and promotes blood clotting through the activation of platelets. May play a significant role in normal and abnormal limb development..
Protein Sequence	MGNLKSVGQEPGPPCGLGLGLGLGLCGKQGPASPAPEPSQAPAPPSPTRPAPDHSPPLTRPPDGPRFPRVKNWEVGSITYDTLSAQAQQDGPCTSRRCLGSLVFPRKLQSRPTQGPSPTEQLLGQARDFINQYYNSIKRSGSQAHEQRLQEVEAEVAATGTYQLRESELVFGAKQAWRNAPRCVGRIQWGKLQVFDARDCRTAQEMFTYICNHIKYATNRGNLRSAITVFPQRCPGRGDFRIWNSQLIRYAGYRQQDGSVRGDPANVEITELCIQHGWTPGNGRFDVLPLLLQAPDEPPELFTLPPEMVLEVPLEHPTLEWFAALGLRWYALPAVSNMLLEIGGLEFPAAPFSGWYMSSEIGMRDLCDPHRYNILEDVAVCMDLDTRTTSSLWKDKAAVEINVAVLHSYQLAKVTIVDHHAATASFMKHLENEQKARGGCPADWAWIVPPISGSLTPVFHQEMVNYFLSPAFRYQPDPWKGSAAKGAGITRKKTFKEVANAVKISASLMGTVMAKRVKATILYGSETGRAQSYAQQLGRLFRKAFDPRVLCMDEYDVVSLEHEALVLVVTSTFGNGDPPENGESFAAALMEMSGPYNSSPRPEQHKSYKIRFNSVSCSDPLVSSWRRKRKESSNTDSAGALGTLRFCVFGLGSRAYPHFCAFARAVDTRLEELGGERLLQLGQGDELCGQEEAFRGWAQAAFQAACETFCVGEDAKAAARDIFSPKRSWKRQRYRLSTQAESLQLLPGLTHVHRRKMFQATILSVENLQSSKSTRATILVRLDTGGQEGLQYQPGDHIGVCPPNRPGLVEALLSRVEDPPPSTEPVAVEQLEKGSPGGPPPGWVRDPRLPPCTLRQALTYFLDITSPPSPRLLRLLSTLAEESSEQQELEALSQDPRRYEEWKWFSCPTLLEVLEQFPSVALPAPLILTQLPLLQPRYYSVSSAPSAHPGEIHLTIAVLAYRTQDGLGPLHYGVCSTWMSQLKAGDPVPCFIRGAPSFRLPPDPNLPCILVGPGTGIAPFRGFWQDRLHDIEIKGLQPAPMTLVFGCRCSQLDHLYRDEVLDAQQRGVFGQVLTAFSRDPGSPKTYVQDLLRTELAAEVHRVLCLEQGHMFVCGDVTMATSVLQTVQRILATEGGMELDEAGDVIGVLRDQQRYHEDIFGLTLRTQEVTSRIRTQSFSLQERQLRGAVPWSFDPPGPEIPGS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Myristoylation	------MGNLKSVGQ ------CCCCCCCCC	60.53	-
15	S-palmitoylation	GQEPGPPCGLGLGLG CCCCCCCCCCCCCCC	8.71	28680068
26	S-palmitoylation	LGLGLGLCGKQGPAS CCCCCCCCCCCCCCC	6.41	-
39	Phosphorylation	ASPAPEPSQAPAPPS CCCCCCCCCCCCCCC	36.99	23140645
46	Phosphorylation	SQAPAPPSPTRPAPD CCCCCCCCCCCCCCC	37.53	22817900
48	Phosphorylation	APAPPSPTRPAPDHS CCCCCCCCCCCCCCC	54.33	22817900
55	Phosphorylation	TRPAPDHSPPLTRPP CCCCCCCCCCCCCCC	35.28	19060867
59	Phosphorylation	PDHSPPLTRPPDGPR CCCCCCCCCCCCCCC	47.07	22817900
211	S-nitrosocysteine	QEMFTYICNHIKYAT HHHHHHHHHHHHHHH	1.82	-
482	Phosphorylation	QPDPWKGSAAKGAGI CCCCCCCCCCCCCCC	22.71	23684622
494	Phosphorylation	AGITRKKTFKEVANA CCCCCCHHHHHHHHH	42.87	17635857
614	Phosphorylation	SYKIRFNSVSCSDPL CCEEEECCCCCCCCH	16.82	22817900
616	Phosphorylation	KIRFNSVSCSDPLVS EEEECCCCCCCCHHH	14.02	19060867
617	Glutathionylation	IRFNSVSCSDPLVSS EEECCCCCCCCHHHH	5.12	24333276
617	S-palmitoylation	IRFNSVSCSDPLVSS EEECCCCCCCCHHHH	5.12	28680068
618	Phosphorylation	RFNSVSCSDPLVSSW EECCCCCCCCHHHHH	34.45	23984901
623	Phosphorylation	SCSDPLVSSWRRKRK CCCCCHHHHHHHHHC	31.69	19060867
624	Phosphorylation	CSDPLVSSWRRKRKE CCCCHHHHHHHHHCC	19.68	29472430
632	Phosphorylation	WRRKRKESSNTDSAG HHHHHCCCCCCCCHH	31.74	17000928
633	Phosphorylation	RRKRKESSNTDSAGA HHHHCCCCCCCCHHH	44.86	27742792
635	Phosphorylation	KRKESSNTDSAGALG HHCCCCCCCCHHHHH	33.02	27742792
637	Phosphorylation	KESSNTDSAGALGTL CCCCCCCCHHHHHHH	26.94	27742792
643	Phosphorylation	DSAGALGTLRFCVFG CCHHHHHHHHHHHHC	18.66	24759943
656	Phosphorylation	FGLGSRAYPHFCAFA HCCCCCCCHHHHHHH	8.98	22817900
688	Glutathionylation	LGQGDELCGQEEAFR CCCCCCCCCCHHHHH	5.07	24333276
835	Phosphorylation	VEQLEKGSPGGPPPG HHHHCCCCCCCCCCC	31.29	-
1008	Glutathionylation	PPDPNLPCILVGPGT CCCCCCCEEEECCCC	4.18	24333276
1174	Phosphorylation	EVTSRIRTQSFSLQE HHHHHHHHCCCCCHH	26.62	27742792
1176	Phosphorylation	TSRIRTQSFSLQERQ HHHHHHCCCCCHHHH	19.05	17635857
1178	Phosphorylation	RIRTQSFSLQERQLR HHHHCCCCCHHHHHH	34.10	27742792

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
494	T	Phosphorylation	Kinase	AMPK	-	Uniprot
656	Y	Phosphorylation	Kinase	PTK2B	Q14289	GPS
1176	S	Phosphorylation	Kinase	AKT1	P31750	GPS
1176	S	Phosphorylation	Kinase	PKACA	P17612	PSP
1176	S	Phosphorylation	Kinase	CAMK2A	Q9UQM7	PSP
1176	S	Phosphorylation	Kinase	AMPK	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
494	T	Phosphorylation	-
In absence of Ca(2+)-calmodulin, AMPK also phosphorylates Thr-494, resulting in inhibition of activity (By similarity).
1176	S	Phosphorylation	21183079
Phosphorylation by AMPK at Ser-1176 in the presence of Ca(2+)-calmodulin (CaM) activates 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 NOS3_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of NOS3_MOUSE !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of NOS3_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1174 AND SER-1176, ANDMASS SPECTROMETRY.	17242355 [Abstract]

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