ARC_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ARC_RAT
• UniProt AC: Q63053
• Protein Name: Activity-regulated cytoskeleton-associated protein {ECO:0000303|PubMed:7857651}
• Gene Name: Arc {ECO:0000303|PubMed:7857651, ECO:0000312|RGD:62037}
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 396
• Subcellular Localization: Extracellular vesicle membrane ; Lipid-anchor . Cell junction, synapse, postsynaptic cell membrane ; Lipid-anchor . Cell junction, synapse . Cell junction, synapse, postsynaptic cell membrane, postsynaptic density . Early endosome membrane . Cell projecti
• Protein Description: Master regulator of synaptic plasticity that self-assembles into virion-like capsids that encapsulate RNAs and mediate intercellular RNA transfer in the nervous system. [PubMed: 29328916 ARC protein is released from neurons in extracellular vesicles that mediate the transfer of ARC mRNA into new target cells, where ARC mRNA can undergo activity-dependent translation]
• Protein Sequence: MELDHMTTGGLHAYPAPRGGPAAKPNVILQIGKCRAEMLEHVRRTHRHLLTEVSKQVERELKGLHRSVGKLENNLDGYVPTGDSQRWKKSIKACLCRCQETIANLERWVKREMHVWREVFYRLERWADRLESMGGKYPVGSEPARHTVSVGVGGPEPYCQEADGYDYTVSPYAITPPPAAGELPEQESVGAQQYQSWVPGEDGQPSPGVDTQIFEDPREFLSHLEEYLRQVGGSEEYWLSQIQNHMNGPAKKWWEFKQGSVKNWVEFKKEFLQYSEGTLSREAIQRELDLPQKQGEPLDQFLWRKRDLYQTLYVDAEEEEIIQYVVGTLQPKFKRFLRHPLPKTLEQLIQRGMEVQDGLEQAAEPSVTPLPTEDETEALTPALTSESVASDRTQPE

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
24	Ubiquitination	PRGGPAAKPNVILQI CCCCCCCCCCEEEEE	38.95	-
84	Phosphorylation	GYVPTGDSQRWKKSI CCCCCCCHHHHHHHH	24.00	-
170	Phosphorylation	DGYDYTVSPYAITPP CCCCEEECCCEECCC	12.37	-
175	Phosphorylation	TVSPYAITPPPAAGE EECCCEECCCCCCCC	22.90	-
206	Phosphorylation	PGEDGQPSPGVDTQI CCCCCCCCCCCCCCH	26.80	-
252	Ubiquitination	HMNGPAKKWWEFKQG HCCCCCHHCHHHHCC	60.69	-
260	Phosphorylation	WWEFKQGSVKNWVEF CHHHHCCCCCCHHHH	27.68	-
269	Ubiquitination	KNWVEFKKEFLQYSE CCHHHHHHHHHHHCC	60.05	-
274	Phosphorylation	FKKEFLQYSEGTLSR HHHHHHHHCCCCCCH	15.73	-
278	Phosphorylation	FLQYSEGTLSREAIQ HHHHCCCCCCHHHHH	19.94	-
293	Ubiquitination	RELDLPQKQGEPLDQ HHCCCCHHCCCCHHH	59.33	-
309	Phosphorylation	LWRKRDLYQTLYVDA HHHHHCHHHHHCCCC	12.07	-
343	Ubiquitination	FLRHPLPKTLEQLIQ HHCCCCCHHHHHHHH	73.71	-
368	Phosphorylation	QAAEPSVTPLPTEDE HHCCCCCCCCCCCCH	24.36	-
380	Phosphorylation	EDETEALTPALTSES CCHHHCCCHHHCCHH	17.35	-
393	Phosphorylation	ESVASDRTQPE---- HHHHCCCCCCC----	54.16	-

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
206	S	Phosphorylation	Kinase	MAPK1	P63086	GPS
368	T	Phosphorylation	Kinase	MAPK1	P63086	GPS
380	T	Phosphorylation	Kinase	MAPK1	P63086	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
260	S	Phosphorylation	Phosphorylation at Ser-260 by CaMK2 prevents homooligomerization into virion-like capsids by disrupting an interaction surface essential for high-order oligomerization.	-

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of ARC_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TFPT_RAT	Tfpt	physical	10644725

Drug and Disease Associations

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