dbPTM

PA24A_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PA24A_MOUSE
UniProt AC	P47713
Protein Name	Cytosolic phospholipase A2
Gene Name	Pla2g4a
Organism	Mus musculus (Mouse).
Sequence Length	748
Subcellular Localization	Cytoplasm. Cytoplasmic vesicle. Translocates to membrane vesicles in a calcium-dependent fashion.
Protein Description	Selectively hydrolyzes arachidonyl phospholipids in the sn-2 position releasing arachidonic acid. Together with its lysophospholipid activity, it is implicated in the initiation of the inflammatory response..
Protein Sequence	MSFIDPYQHIIVEHQYSHKFTVVVLRATKVTKGTFGDMLDTPDPYVELFISTTPDSRKRTRHFNNDINPVWNETFEFILDPNQENVLEITLMDANYVMDETLGTATFPVSSMKVGEKKEVPFIFNQVTEMILEMSLEVCSCPDLRFSMALCDQEKTFRQQRKENIKENMKKLLGPKKSEGLYSTRDVPVVAILGSGGGFRAMVGFSGVMKALYESGILDCATYIAGLSGSTWYMSTLYSHPDFPEKGPEEINEELMKNVSHNPLLLLTPQKVKRYVESLWKKKSSGQPVTFTDIFGMLIGETLIQNRMSMTLSSLKEKVNAARCPLPLFTCLHVKPDVSELMFADWVEFSPYEIGMAKYGTFMAPDLFGSKFFMGTVVKKYEENPLHFLMGVWGSAFSILFNRVLGVSGSQNKGSTMEEELENITAKHIVSNDSSDSDDEAQGPKGTENEEAEKEYQSDNQASWVHRMLMALVSDSALFNTREGRAGKVHNFMLGLNLNTSYPLSPLRDFSSQDSFDDELDAAVADPDEFERIYEPLDVKSKKIHVVDSGLTFNLPYPLILRPQRGVDLIISFDFSARPSDTSPPFKELLLAEKWAKMNKLPFPKIDPYVFDREGLKECYVFKPKNPDVEKDCPTIIHFVLANINFRKYKAPGVLRETKEEKEIADFDIFDDPESPFSTFNFQYPNQAFKRLHDLMYFNTLNNIDVIKDAIVESIEYRRQNPSRCSVSLSNVEARKFFNKEFLSKPTV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSFIDPYQH ------CCCCCCCCE	30.80	26824392
96	Phosphorylation	ITLMDANYVMDETLG EEEEECCCCCCCCCC	10.00	-
101	Phosphorylation	ANYVMDETLGTATFP CCCCCCCCCCEEEEE	26.65	-
104	Phosphorylation	VMDETLGTATFPVSS CCCCCCCEEEEECHH	26.15	-
156	Phosphorylation	ALCDQEKTFRQQRKE HHHHHHHHHHHHHHH	24.25	24719451
171	Acetylation	NIKENMKKLLGPKKS HHHHHHHHHHCCCCC	37.87	7666959
268	Phosphorylation	HNPLLLLTPQKVKRY CCCEEECCHHHHHHH	24.52	26824392
302	Phosphorylation	FGMLIGETLIQNRMS HHHHHHHHHHHHCHH	24.77	28576409
309	Phosphorylation	TLIQNRMSMTLSSLK HHHHHCHHCCHHHHH	12.84	22418434
313	Phosphorylation	NRMSMTLSSLKEKVN HCHHCCHHHHHHHHH	25.18	27149854
371	Ubiquitination	APDLFGSKFFMGTVV CCHHHCCCCCCEEEE	42.89	-
410	Phosphorylation	RVLGVSGSQNKGSTM HHHCCCCCCCCCCCH	24.07	29514104
431	Phosphorylation	ITAKHIVSNDSSDSD CCHHHCCCCCCCCCC	34.02	23684622
434	Phosphorylation	KHIVSNDSSDSDDEA HHCCCCCCCCCCCCC	40.05	27087446
435	Phosphorylation	HIVSNDSSDSDDEAQ HCCCCCCCCCCCCCC	43.95	27087446
437	Phosphorylation	VSNDSSDSDDEAQGP CCCCCCCCCCCCCCC	49.24	27087446
447	Phosphorylation	EAQGPKGTENEEAEK CCCCCCCCCCHHHHH	41.59	25159016
456	Phosphorylation	NEEAEKEYQSDNQAS CHHHHHHHCCCCHHH	25.12	25159016
458	Phosphorylation	EAEKEYQSDNQASWV HHHHHHCCCCHHHHH	37.31	25777480
463	Phosphorylation	YQSDNQASWVHRMLM HCCCCHHHHHHHHHH	21.62	25777480
500	Phosphorylation	MLGLNLNTSYPLSPL EEEEECCCCCCCCCC	32.57	25619855
501	Phosphorylation	LGLNLNTSYPLSPLR EEEECCCCCCCCCCC	24.55	25619855
502	Phosphorylation	GLNLNTSYPLSPLRD EEECCCCCCCCCCCC	13.22	25619855
505	Phosphorylation	LNTSYPLSPLRDFSS CCCCCCCCCCCCCCC	19.86	10978317
511	Phosphorylation	LSPLRDFSSQDSFDD CCCCCCCCCCCCCCH	31.23	25619855
512	Phosphorylation	SPLRDFSSQDSFDDE CCCCCCCCCCCCCHH	37.69	22942356
515	Phosphorylation	RDFSSQDSFDDELDA CCCCCCCCCCHHHHH	23.96	27087446
534	Phosphorylation	PDEFERIYEPLDVKS HHHHHHHHCCCCCCC	20.09	25159016
572	Phosphorylation	RGVDLIISFDFSARP CCCCEEEEEECCCCC	16.27	24759943
580	Phosphorylation	FDFSARPSDTSPPFK EECCCCCCCCCCCHH	48.22	21183079
619	Glutathionylation	DREGLKECYVFKPKN CCCCCEEEEEECCCC	3.16	24333276
690	Acetylation	QYPNQAFKRLHDLMY CCCCHHHHHHHHHCC	58.00	15613257
723	Phosphorylation	EYRRQNPSRCSVSLS HHHHHCCCCCEEECC	54.17	25168779
725	Glutathionylation	RRQNPSRCSVSLSNV HHHCCCCCEEECCHH	5.74	24333276
726	Phosphorylation	RQNPSRCSVSLSNVE HHCCCCCEEECCHHH	17.40	25521595
728	Phosphorylation	NPSRCSVSLSNVEAR CCCCCEEECCHHHHH	15.13	27087446
730	Phosphorylation	SRCSVSLSNVEARKF CCCEEECCHHHHHHH	31.18	25619855

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
505	S	Phosphorylation	Kinase	MAPK1	P63085	GPS
505	S	Phosphorylation	Kinase	MAPK3	Q63844	GPS
505	S	Phosphorylation	Kinase	MAPK-FAMILY	-	GPS
505	S	Phosphorylation	Kinase	MAPK	-	Uniprot
726	S	Phosphorylation	Kinase	RPS6KA5	Q8C050	GPS
726	S	Phosphorylation	Kinase	MAPKAPK5	O54992	PSP
726	S	Phosphorylation	Kinase	MKNK1	O08605	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
505	S	Phosphorylation	10978317
Phosphorylated at both Ser-505 and Ser-726 in response to mitogenic stimuli.
726	S	Phosphorylation	10978317
Phosphorylated at both Ser-505 and Ser-726 in response to mitogenic stimuli.

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 PA24A_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
VIME_MOUSE	Vim	physical	10625659
VIME_RAT	Vim	physical	10625659
SIR2_MOUSE	Sirt2	physical	26303530
CDK2_MOUSE	Cdk2	physical	26303530

Drug and Disease Associations

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

Regulatory Network of PA24A_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"The phagosomal proteome in interferon-gamma-activated macrophages."; Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.; Immunity 30:143-154(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437, AND MASSSPECTROMETRY.	19144319 [Abstract]
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437, AND MASSSPECTROMETRY.	19367708 [Abstract]
"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 SER-726, AND MASSSPECTROMETRY.	17242355 [Abstract]
"Serine 727 phosphorylation and activation of cytosolic phospholipaseA2 by MNK1-related protein kinases."; Hefner Y., Boersch-Haubold A.G., Murakami M., Wilde J.I., Pasquet S.,Schieltz D., Ghomashchi F., Yates J.R. III, Armstrong C.G.,Paterson A., Cohen P., Fukunaga R., Hunter T., Kudo I., Watson S.P.,Gelb M.H.; J. Biol. Chem. 275:37542-37551(2000). Cited for: PHOSPHORYLATION AT SER-505 AND SER-726, AND ACTIVATION.	10978317 [Abstract]

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