dbPTM

PA24A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PA24A_HUMAN
UniProt AC	P47712
Protein Name	Cytosolic phospholipase A2
Gene Name	PLA2G4A
Organism	Homo sapiens (Human).
Sequence Length	749
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	MSFIDPYQHIIVEHQYSHKFTVVVLRATKVTKGAFGDMLDTPDPYVELFISTTPDSRKRTRHFNNDINPVWNETFEFILDPNQENVLEITLMDANYVMDETLGTATFTVSSMKVGEKKEVPFIFNQVTEMVLEMSLEVCSCPDLRFSMALCDQEKTFRQQRKEHIRESMKKLLGPKNSEGLHSARDVPVVAILGSGGGFRAMVGFSGVMKALYESGILDCATYVAGLSGSTWYMSTLYSHPDFPEKGPEEINEELMKNVSHNPLLLLTPQKVKRYVESLWKKKSSGQPVTFTDIFGMLIGETLIHNRMNTTLSSLKEKVNTAQCPLPLFTCLHVKPDVSELMFADWVEFSPYEIGMAKYGTFMAPDLFGSKFFMGTVVKKYEENPLHFLMGVWGSAFSILFNRVLGVSGSQSRGSTMEEELENITTKHIVSNDSSDSDDESHEPKGTENEDAGSDYQSDNQASWIHRMIMALVSDSALFNTREGRAGKVHNFMLGLNLNTSYPLSPLSDFATQDSFDDDELDAAVADPDEFERIYEPLDVKSKKIHVVDSGLTFNLPYPLILRPQRGVDLIISFDFSARPSDSSPPFKELLLAEKWAKMNKLPFPKIDPYVFDREGLKECYVFKPKNPDMEKDCPTIIHFVLANINFRKYRAPGVPRETEEEKEIADFDIFDDPESPFSTFNFQYPNQAFKRLHDLMHFNTLNNIDVIKEAMVESIEYRRQNPSRCSVSLSNVEARRFFNKEFLSKPKA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSFIDPYQH ------CCCCCCCCE	30.80	20873877
7	Phosphorylation	-MSFIDPYQHIIVEH -CCCCCCCCEEEEEE	14.69	25159151
16	Phosphorylation	HIIVEHQYSHKFTVV EEEEEECCCCCEEEE	18.04	23186163
17	Phosphorylation	IIVEHQYSHKFTVVV EEEEECCCCCEEEEE	17.40	23186163
21	Phosphorylation	HQYSHKFTVVVLRAT ECCCCCEEEEEEECE	19.73	20068231
31	Phosphorylation	VLRATKVTKGAFGDM EEECEECCCCCCCCC	25.89	-
32	Ubiquitination	LRATKVTKGAFGDML EECEECCCCCCCCCC	51.75	-
41	Phosphorylation	AFGDMLDTPDPYVEL CCCCCCCCCCCCEEE	26.15	29978859
45	Phosphorylation	MLDTPDPYVELFIST CCCCCCCCEEEEEEC	17.59	29978859
51	Phosphorylation	PYVELFISTTPDSRK CCEEEEEECCCCHHH	20.92	29978859
52	Phosphorylation	YVELFISTTPDSRKR CEEEEEECCCCHHHH	37.22	29978859
53	Phosphorylation	VELFISTTPDSRKRT EEEEEECCCCHHHHH	20.50	25627689
56	Phosphorylation	FISTTPDSRKRTRHF EEECCCCHHHHHCCC	40.69	29978859
151	S-nitrosocysteine	LRFSMALCDQEKTFR HHHHHHHHHHHHHHH	3.54	-
151	S-nitrosylation	LRFSMALCDQEKTFR HHHHHHHHHHHHHHH	3.54	22178444
155	Ubiquitination	MALCDQEKTFRQQRK HHHHHHHHHHHHHHH	47.53	-
155	2-Hydroxyisobutyrylation	MALCDQEKTFRQQRK HHHHHHHHHHHHHHH	47.53	-
155	Acetylation	MALCDQEKTFRQQRK HHHHHHHHHHHHHHH	47.53	26051181
156	Phosphorylation	ALCDQEKTFRQQRKE HHHHHHHHHHHHHHH	24.25	24719451
171	Acetylation	HIRESMKKLLGPKNS HHHHHHHHHHCCCCC	40.06	7666953
176	Acetylation	MKKLLGPKNSEGLHS HHHHHCCCCCCCCCC	71.90	7666965
176	Ubiquitination	MKKLLGPKNSEGLHS HHHHHCCCCCCCCCC	71.90	-
178	Phosphorylation	KLLGPKNSEGLHSAR HHHCCCCCCCCCCCC	38.89	20068231
183	Phosphorylation	KNSEGLHSARDVPVV CCCCCCCCCCCCCEE	30.00	20068231
228	Phosphorylation	ATYVAGLSGSTWYMS HHHHHCCCCCCEEEE	29.76	22817900
257	Ubiquitination	EINEELMKNVSHNPL HHCHHHHHCCCCCCE	67.81	-
260	Phosphorylation	EELMKNVSHNPLLLL HHHHHCCCCCCEEEC	27.26	24732914
268	Phosphorylation	HNPLLLLTPQKVKRY CCCEEECCHHHHHHH	24.52	22167270
271	Ubiquitination	LLLLTPQKVKRYVES EEECCHHHHHHHHHH	51.42	-
273	Ubiquitination	LLTPQKVKRYVESLW ECCHHHHHHHHHHHH	45.08	-
281	Ubiquitination	RYVESLWKKKSSGQP HHHHHHHHCCCCCCC	56.46	-
283	Ubiquitination	VESLWKKKSSGQPVT HHHHHHCCCCCCCCC	46.24	-
310	Phosphorylation	LIHNRMNTTLSSLKE HHHHCHHCHHHHHHH	21.55	20873877
311	Phosphorylation	IHNRMNTTLSSLKEK HHHCHHCHHHHHHHH	21.46	23403867
313	Phosphorylation	NRMNTTLSSLKEKVN HCHHCHHHHHHHHCC	31.37	23403867
314	Phosphorylation	RMNTTLSSLKEKVNT CHHCHHHHHHHHCCC	46.72	26699800
316	Ubiquitination	NTTLSSLKEKVNTAQ HCHHHHHHHHCCCCC	58.39	21906983
359	Phosphorylation	YEIGMAKYGTFMAPD HHCHHCCCCCCCCCH	16.32	-
370	Phosphorylation	MAPDLFGSKFFMGTV CCCHHHCCCCCCEEE	20.96	21712546
371	Ubiquitination	APDLFGSKFFMGTVV CCHHHCCCCCCEEEE	42.89	21906983
376	Phosphorylation	GSKFFMGTVVKKYEE CCCCCCEEEEHHHCC	15.44	-
408	Phosphorylation	FNRVLGVSGSQSRGS HHHHHCCCCCCCCCC	30.81	20873877
410	Phosphorylation	RVLGVSGSQSRGSTM HHHCCCCCCCCCCCH	19.92	20873877
412	Phosphorylation	LGVSGSQSRGSTMEE HCCCCCCCCCCCHHH	40.06	20873877
415	Phosphorylation	SGSQSRGSTMEEELE CCCCCCCCCHHHHHH	24.38	20873877
416	Phosphorylation	GSQSRGSTMEEELEN CCCCCCCCHHHHHHH	31.27	20873877
417	Sulfoxidation	SQSRGSTMEEELENI CCCCCCCHHHHHHHC	6.99	21406390
431	Phosphorylation	ITTKHIVSNDSSDSD CCCCCCCCCCCCCCC	34.02	25463755
434	Phosphorylation	KHIVSNDSSDSDDES CCCCCCCCCCCCCCC	40.05	22167270
435	Phosphorylation	HIVSNDSSDSDDESH CCCCCCCCCCCCCCC	43.95	22167270
437	Phosphorylation	VSNDSSDSDDESHEP CCCCCCCCCCCCCCC	49.24	29255136
441	Phosphorylation	SSDSDDESHEPKGTE CCCCCCCCCCCCCCC	39.90	22167270
447	Phosphorylation	ESHEPKGTENEDAGS CCCCCCCCCCCCCCC	41.59	30576142
454	Phosphorylation	TENEDAGSDYQSDNQ CCCCCCCCCCCCHHH	34.56	23401153
456	Phosphorylation	NEDAGSDYQSDNQAS CCCCCCCCCCHHHHH	16.18	21082442
458	Phosphorylation	DAGSDYQSDNQASWI CCCCCCCCHHHHHHH	32.09	28450419
463	Phosphorylation	YQSDNQASWIHRMIM CCCHHHHHHHHHHHH	19.46	20068231
500	Phosphorylation	MLGLNLNTSYPLSPL EEEEECCCCCCCCCH	32.57	20068231
501	Phosphorylation	LGLNLNTSYPLSPLS EEEECCCCCCCCCHH	24.55	20068231
502	Phosphorylation	GLNLNTSYPLSPLSD EEECCCCCCCCCHHH	13.22	20068231
505	Phosphorylation	LNTSYPLSPLSDFAT CCCCCCCCCHHHCCC	21.20	18632668
508	Phosphorylation	SYPLSPLSDFATQDS CCCCCCHHHCCCCCC	33.78	20068231
512	Phosphorylation	SPLSDFATQDSFDDD CCHHHCCCCCCCCHH	32.66	20068231
515	Phosphorylation	SDFATQDSFDDDELD HHCCCCCCCCHHHHH	22.28	11479288
535	Phosphorylation	PDEFERIYEPLDVKS HHHHHHHHCCCCCCC	20.09	21945579
541	Ubiquitination	IYEPLDVKSKKIHVV HHCCCCCCCCEEEEE	57.11	-
541	Sumoylation	IYEPLDVKSKKIHVV HHCCCCCCCCEEEEE	57.11	-
541	Sumoylation	IYEPLDVKSKKIHVV HHCCCCCCCCEEEEE	57.11	28112733
595	Ubiquitination	KELLLAEKWAKMNKL HHHHHHHHHHHHCCC	47.01	-
595	2-Hydroxyisobutyrylation	KELLLAEKWAKMNKL HHHHHHHHHHHHCCC	47.01	-
595	Acetylation	KELLLAEKWAKMNKL HHHHHHHHHHHHCCC	47.01	27452117
598	Acetylation	LLAEKWAKMNKLPFP HHHHHHHHHCCCCCC	41.72	26051181
606	Sumoylation	MNKLPFPKIDPYVFD HCCCCCCCCCCCEEC	61.18	28112733
606	Ubiquitination	MNKLPFPKIDPYVFD HCCCCCCCCCCCEEC	61.18	-
618	Ubiquitination	VFDREGLKECYVFKP EECCCCCEEEEEECC	57.50	-
691	Ubiquitination	QYPNQAFKRLHDLMH CCCCHHHHHHHHHCC	58.00	-
701	Phosphorylation	HDLMHFNTLNNIDVI HHHCCHHHCCCHHHH	29.89	20873877
709	Ubiquitination	LNNIDVIKEAMVESI CCCHHHHHHHHHHHH	38.99	-
724	Phosphorylation	EYRRQNPSRCSVSLS HHHHHCCCCCEEECC	54.17	23401153
727	Phosphorylation	RQNPSRCSVSLSNVE HHCCCCCEEECCHHH	17.40	19664994
729	Phosphorylation	NPSRCSVSLSNVEAR CCCCCEEECCHHHHH	15.13	29255136
731	Phosphorylation	SRCSVSLSNVEARRF CCCEEECCHHHHHHH	31.18	29255136
741	Ubiquitination	EARRFFNKEFLSKPK HHHHHHCHHHHCCCC	44.69	-
745	Phosphorylation	FFNKEFLSKPKA--- HHCHHHHCCCCC---	52.84	24719451

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
376	T	Phosphorylation	Kinase	PKCZ	Q05513	PSP
505	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
505	S	Phosphorylation	Kinase	MAPK-FAMILY	-	GPS
505	S	Phosphorylation	Kinase	MAPK	-	Uniprot
505	S	Phosphorylation	Kinase	MAPK_GROUP	-	PhosphoELM
515	S	Phosphorylation	Kinase	KCC2A	Q9UQM7	PhosphoELM
515	S	Phosphorylation	Kinase	CAMK2A	P11275	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
505	S	Phosphorylation	8381049
Phosphorylated at both Ser-505 and Ser-727 in response to mitogenic stimuli.
727	S	Phosphorylation	9468497
Phosphorylated at both Ser-505 and Ser-727 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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KAT5_HUMAN	KAT5	physical	11416127
RUVB2_HUMAN	RUVBL2	physical	22863883
JAK1_HUMAN	JAK1	physical	8612580
BORC6_HUMAN	C17orf59	physical	18330356
CAP1_HUMAN	CAP1	physical	18330356
UBXN1_HUMAN	UBXN1	physical	18330356
TF65_HUMAN	RELA	physical	18330356
XAGE1_HUMAN	XAGE1E	physical	18330356
S10AA_HUMAN	S100A10	physical	14599294
ANXA2_HUMAN	ANXA2	physical	14599294
EHD1_HUMAN	EHD1	physical	22456504
MK03_HUMAN	MAPK3	physical	21185392
MK01_HUMAN	MAPK1	physical	21185392
KPCA_HUMAN	PRKCA	physical	16963226
LOX12_HUMAN	ALOX12	physical	15474031
MYBB_HUMAN	MYBL2	physical	14769798
ITB3_HUMAN	ITGB3	physical	18840708
VIME_HUMAN	VIM	physical	18840708
NCF1_HUMAN	NCF1	physical	18765662
NCF2_HUMAN	NCF2	physical	18765662
ANXA1_HUMAN	ANXA1	physical	17873281
NCF2_HUMAN	NCF2	physical	16844764
NCF1_HUMAN	NCF1	physical	16844764
S10AA_HUMAN	S100A10	physical	12163506
KAT5_HUMAN	KAT5	physical	26303530
SIR2_HUMAN	SIRT2	physical	26303530
CDK2_HUMAN	CDK2	physical	26303530
CCNA2_HUMAN	CCNA2	physical	26303530

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
DB00041	Aldesleukin
DB00411	Carbachol
DB00578	Carbenicillin
DB00445	Epirubicin
DB00591	Fluocinolone Acetonide
DB00588	Fluticasone Propionate
DB04552	Niflumic Acid
DB01083	Orlistat
DB01103	Quinacrine
DB00086	Streptokinase
DB04786	Suramin

Regulatory Network of PA24A_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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 THR-268; SER-437; SER-727AND SER-729, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-434; SER-435 ANDSER-437, AND MASS SPECTROMETRY.	18088087 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-729, AND MASSSPECTROMETRY.	18187866 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-727 AND SER-729, ANDMASS SPECTROMETRY.	16964243 [Abstract]
"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-437, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-729, AND MASSSPECTROMETRY.	15302935 [Abstract]
"Identification of the phosphorylation sites of cytosolicphospholipase A2 in agonist-stimulated human platelets and HeLacells."; Boersch-Haubold A.G., Bartoli F., Asselin J., Dudler T., Kramer R.M.,Apitz-Castro R., Watson S.P., Gelb M.H.; J. Biol. Chem. 273:4449-4458(1998). Cited for: PHOSPHORYLATION AT SER-505 AND SER-727.	9468497 [Abstract]
"cPLA2 is phosphorylated and activated by MAP kinase."; Lin L.-L., Wartmann M., Lin A.Y., Knopf J.L., Seth A., Davis R.J.; Cell 72:269-278(1993). Cited for: MUTAGENESIS OF SER-505, AND PHOSPHORYLATION AT SER-505.	8381049 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-535, AND MASSSPECTROMETRY.	18083107 [Abstract]

show

show