PA24E_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PA24E_HUMAN
• UniProt AC: Q3MJ16
• Protein Name: Cytosolic phospholipase A2 epsilon {ECO:0000305}
• Gene Name: PLA2G4E {ECO:0000312|HGNC:HGNC:24791}
• Organism: Homo sapiens (Human).
• Sequence Length: 868
• Subcellular Localization: Cytoplasm, cytosol. Lysosome membrane; Peripheral membrane protein; Cytoplasmic side. Translocates to lysosomal membranes in a calcium-dependent fashion..
• Protein Description: Calcium-dependent phospholipase A2 that selectively hydrolyzes glycerophospholipids in the sn-2 position..
• Protein Sequence: MSLQASEGCPGLGTNVFVPQSPQTDEEGSRSGRSFSEFEDTQDLDTPGLPPFCPMAPWGSEEGLSPCHLLTVRVIRMKNVRQADMLSQTDCFVSLWLPTASQKKLRTRTISNCPNPEWNESFNFQIQSRVKNVLELSVCDEDTVTPDDHLLTVLYDLTKLCFRKKTHVKFPLNPQGMEELEVEFLLEESPSPPETLVTNGVLVSRQVSCLEVHAQSRRRRKREKMKDLLVMVNESFENTQRVRPCLEPCCPTSACFQTAACFHYPKYFQSQVHVEVPKSHWSCGLCCRSRKKGPISQPLDCLSDGQVMTLPVGESYELHMKSTPCPETLDVRLGFSLCPAELEFLQKRKVVVAKALKQVLQLEEDLQEDEVPLIAIMATGGGTRSMTSMYGHLLGLQKLNLLDCASYITGLSGATWTMATLYRDPDWSSKNLEPAIFEARRHVVKDKLPSLFPDQLRKFQEELRQRSQEGYRVTFTDFWGLLIETCLGDERNECKLSDQRAALSCGQNPLPIYLTINVKDDVSNQDFREWFEFSPYEVGLQKYGAFIPSELFGSEFFMGRLVKRIPESRICYMLGLWSSIFSLNLLDAWNLSHTSEEFFHRWTREKVQDIEDEPILPEIPKCDANILETTVVIPGSWLSNSFREILTHRSFVSEFHNFLSGLQLHTNYLQNGQFSRWKDTVLDGFPNQLTESANHLCLLDTAFFVNSSYPPLLRPERKADLIIHLNYCAGSQTKPLKQTCEYCTVQNIPFPKYELPDENENLKECYLMENPQEPDAPIVTFFPLINDTFRKYKAPGVERSPEELEQGQVDIYGPKTPYATKELTYTEATFDKLVKLSEYNILNNKDTLLQALRLAVEKKKRLKGQCPS

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
47	Phosphorylation	DTQDLDTPGLPPFCP CCCCCCCCCCCCCCC	36.02	22210691
228	Phosphorylation	KREKMKDLLVMVNES HHHHHHHHHHHHCCC	32.43	29978859
232	Phosphorylation	MKDLLVMVNESFENT HHHHHHHHCCCCCCC	15.56	29978859
367	Phosphorylation	LQLEEDLQEDEVPLI HCHHHHHCCCCCCEE	20.98	22210691
378	Phosphorylation	VPLIAIMATGGGTRS CCEEEEEECCCCHHH	10.93	22210691
537	Phosphorylation	WFEFSPYEVGLQKYG HHHCCHHHHHHHHHC	41.96	-
715	Phosphorylation	SYPPLLRPERKADLI CCCCCCCHHHHCCEE	7.05	-
741	Phosphorylation	KPLKQTCEYCTVQNI CCHHHHCCEEEECCC	23.96	17693683
753	Phosphorylation	QNIPFPKYELPDENE CCCCCCCCCCCCCCC	2.78	17693683
788	Phosphorylation	FFPLINDTFRKYKAP EEHHHCHHHHHCCCC	24.13	-
800	Phosphorylation	KAPGVERSPEELEQG CCCCCCCCHHHHHCC	23.94	-
825	Phosphorylation	YATKELTYTEATFDK CCCCEEEECEEHHHH	32.11	25907765
827	Phosphorylation	TKELTYTEATFDKLV CCEEEECEEHHHHHH	12.25	25907765
835	Phosphorylation	ATFDKLVKLSEYNIL EHHHHHHHHHHHCCC	30.86	24670416

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

Oops, there are no upstream regulatory protein records of PA24E_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PA24E_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 PA24E_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of PA24E_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

"Quantitative phosphoproteome profiling of Wnt3a-mediated signalingnetwork: indicating the involvement of ribonucleoside-diphosphatereductase M2 subunit phosphorylation at residue serine 20 in canonicalWnt signal transduction.";
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
Mol. Cell. Proteomics 6:1952-1967(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-741, AND MASSSPECTROMETRY.
PubMed: 17693683