ACES_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ACES_HUMAN
• UniProt AC: P22303
• Protein Name: Acetylcholinesterase
• Gene Name: ACHE
• Organism: Homo sapiens (Human).
• Sequence Length: 614
• Subcellular Localization: Cell junction, synapse . Secreted. Cell membrane; Peripheral membrane protein.; Isoform T: Nucleus. Only observed in apoptotic nuclei.; Isoform H: Cell membrane; Lipid-anchor, GPI-anchor; Extracellular side.
• Protein Description: Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. Role in neuronal apoptosis..
• Protein Sequence: MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL

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
164	Phosphorylation	GASSLDVYDGRFLVQ CCCCCCEECCEEEEE	16.61	7836436
296	N-linked_Glycosylation	PPGGTGGNDTELVAC CCCCCCCCCHHHHEE	55.14	23035744
296	N-linked_Glycosylation	PPGGTGGNDTELVAC CCCCCCCCCHHHHEE	55.14	23035744
381	N-linked_Glycosylation	APGFSKDNESLISRA CCCCCCCCHHHHHHH	44.48	20408548
381	N-linked_Glycosylation	APGFSKDNESLISRA CCCCCCCCHHHHHHH	44.48	20408548
383	Phosphorylation	GFSKDNESLISRAEF CCCCCCHHHHHHHHH	36.94	24719451
386	Phosphorylation	KDNESLISRAEFLAG CCCHHHHHHHHHHHC	30.63	24719451
402	Phosphorylation	RVGVPQVSDLAAEAV CCCCCCHHHHHHHHH	22.97	28176443
413	Phosphorylation	AEAVVLHYTDWLHPE HHHHHHHHHCCCCCC	11.39	28176443
414	Phosphorylation	EAVVLHYTDWLHPED HHHHHHHHCCCCCCC	15.22	28176443
495	N-linked_Glycosylation	IPLDPSRNYTAEEKI CCCCCCCCCCHHHHH	42.73	23035744
495	N-linked_Glycosylation	IPLDPSRNYTAEEKI CCCCCCCCCCHHHHH	42.73	23035744
517	Phosphorylation	YWANFARTGDPNEPR HHHHHHCCCCCCCCC	42.37	68852579
572 (in isoform 4)	Phosphorylation	-	39.29	25954137
574 (in isoform 4)	Phosphorylation	-	26.58	25954137
582 (in isoform 4)	Phosphorylation	-	55.49	25954137
588 (in isoform 2)	GPI-anchor	-	5.91	15489334

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ACES_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 ACES_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CO4A1_HUMAN	COL4A1	physical	12524166

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
• D00043: Isoflurophate (USP); Fluostigmine; Floropryl (TN)
• D00196: Physostigmine (USP); Eserine (TN)
• D00469: Pralidoxime chloride (USP); Pralidoxime (INN); Protopam (TN)
• D00487: Pyridostigmine bromide (JP16/USP/INN); Mestinon (TN)
• D00667: Demecarium bromide (USP/INN); Humorsol (TN)
• D00670: Donepezil hydrochloride (JP16/USAN); Aricept (TN)
• D00994: Edrophonium chloride (JP16/USP/INN); Enlon (TN); Tensilon (TN)
• D00995: Neostigmine bromide (JAN/USP/INN); Vagostigmin (TN)
• D00998: Neostigmine methylsulfate (JP16/USP); Bloxiverz (TN); Prostigmin (TN)
• D00999: Acetylcholine chloride (JP16/USP/INN); Miochol (TN)
• D01001: Ambenonium chloride (JP16/INN); Mytelase (TN)
• D01228: Distigmine bromide (JP16/INN); Ubretid (TN)
• D01572: Pralidoxime iodide (JAN/USAN); Pam (TN)
• D02068: Tacrine hydrochloride (USP); Cognex (TN)
• D02173: Galantamine hydrobromide (JAN/USAN); Razadyne (TN); Reminyl (TN)
• D02193: Ecothiopate iodide (JP16/INN); Echothiophate iodide (USP); Phospholine iodide (TN)
• D02418: Physostigmine salicylate (JAN/USP); Antilirium (TN)
• D02558: Rivastigmine tartrate; Exelon (TN)
• D02565: Dimetacrine (INN)
• D02729: Itopride hydrochloride (JAN); Ganaton (TN)
• D03099: Besipirdine hydrochloride (USAN)
• D03239: Ladostigil tartrate (USAN)
• D03378: Caracemide (USAN)
• D03751: Icopezil maleate (USAN)
• D03822: Rivastigmine (JAN/USAN/INN); Exelon (TN)
• D03826: Physostigmine sulfate (USP); Eserine sulfate (TN)
• D04292: Galantamine (USAN/INN); Reminyl (TN)
• D05215: Obidoxime chloride (USAN)
• D05590: Pralidoxime mesylate (USAN)
• D06288: Velnacrine maleate (USAN); Mentane (TN)
• D07869: Donepezil (INN); Donaz (TN)
• D08094: Itopride (INN)
• D08261: Neostigmine (BAN); Prostigmin (TN)
• D08555: Tacrine (INN); Tacrinal (TN)
• D08838: Acotiamide hydrochloride hydrate (JAN); Acotiamide hydrochloride (USAN)
• D09750: Ipidacrine hydrochloride hydrate (JAN)
• D09835: Zanapezil fumarate (JAN)
• D09917: Latrepirdine (USAN/INN)
• D09918: Latrepirdine dihydrochloride (USAN); Dimebolin; Dimebon
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"Structures of recombinant native and E202Q mutant humanacetylcholinesterase complexed with the snake-venom toxin fasciculin-II.";
Kryger G., Harel M., Giles K., Toker L., Velan B., Lazar A.,Kronman C., Barak D., Ariel N., Shafferman A., Silman I.,Sussman J.L.;
Acta Crystallogr. D 56:1385-1394(2000).
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 32-614 IN COMPLEX WITHFASCICULIN-2, AND GLYCOSYLATION AT ASN-381 AND ASN-495.
PubMed: 11053835