EAA4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: EAA4_HUMAN
• UniProt AC: P48664
• Protein Name: Excitatory amino acid transporter 4
• Gene Name: SLC1A6
• Organism: Homo sapiens (Human).
• Sequence Length: 564
• Subcellular Localization: Cell membrane ; Multi-pass membrane protein .
• Protein Description: Sodium-dependent, high-affinity amino acid transporter that mediates the uptake of L-glutamate and also L-aspartate and D-aspartate. [PubMed: 7791878 Functions as a symporter that transports one amino acid molecule together with two or three Na(+) ions and one proton, in parallel with the counter-transport of one K(+) ion. Mediates Cl(-) flux that is not coupled to amino acid transport; this avoids the accumulation of negative charges due to aspartate and Na(+) symport (By similarity Plays a redundant role in the rapid removal of released glutamate from the synaptic cleft, which is essential for terminating the postsynaptic action of glutamate (Probable]
• Protein Sequence: MSSHGNSLFLRESGQRLGRVGWLQRLQESLQQRALRTRLRLQTMTLEHVLRFLRRNAFILLTVSAVVIGVSLAFALRPYQLTYRQIKYFSFPGELLMRMLQMLVLPLIVSSLVTGMASLDNKATGRMGMRAAVYYMVTTIIAVFIGILMVTIIHPGKGSKEGLHREGRIETIPTADAFMDLIRNMFPPNLVEACFKQFKTQYSTRVVTRTMVRTENGSEPGASMPPPFSVENGTSFLENVTRALGTLQEMLSFEETVPVPGSANGINALGLVVFSVAFGLVIGGMKHKGRVLRDFFDSLNEAIMRLVGIIIWYAPVGILFLIAGKILEMEDMAVLGGQLGMYTLTVIVGLFLHAGIVLPLIYFLVTHRNPFPFIGGMLQALITAMGTSSSSATLPITFRCLEEGLGVDRRITRFVLPVGATVNMDGTALYEALAAIFIAQVNNYELNLGQITTISITATAASVGAAGIPQAGLVTMVIVLTSVGLPTEDITLIIAVDWFLDRLRTMTNVLGDSIGAAVIEHLSQRELELQEAELTLPSLGKPYKSLMAQEKGASRGRGGNESAM

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
2	Phosphorylation	------MSSHGNSLF ------CCCCCCCEE	30.92	22617229
3	Phosphorylation	-----MSSHGNSLFL -----CCCCCCCEEE	33.83	28122231
7	Phosphorylation	-MSSHGNSLFLRESG -CCCCCCCEEECCHH	25.70	22617229
13	Phosphorylation	NSLFLRESGQRLGRV CCEEECCHHHCCCHH	33.52	29507054
29	Phosphorylation	WLQRLQESLQQRALR HHHHHHHHHHHHHHH	20.65	-
37	Phosphorylation	LQQRALRTRLRLQTM HHHHHHHHHHHHHHC	34.60	-
171	Phosphorylation	HREGRIETIPTADAF CCCCCCEECCCHHHH	29.86	24260401
174	Phosphorylation	GRIETIPTADAFMDL CCCEECCCHHHHHHH	33.06	24260401
202	Phosphorylation	FKQFKTQYSTRVVTR HHHHHHHHCCEEEEE	19.76	29759185
216	N-linked_Glycosylation	RTMVRTENGSEPGAS EEEEECCCCCCCCCC	59.69	UniProtKB CARBOHYD
232	N-linked_Glycosylation	PPPFSVENGTSFLEN CCCCCCCCCCHHHHH	57.81	UniProtKB CARBOHYD
239	N-linked_Glycosylation	NGTSFLENVTRALGT CCCHHHHHHHHHHHH	42.48	UniProtKB CARBOHYD
551	Ubiquitination	KSLMAQEKGASRGRG HHHHHHHHCCCCCCC	47.93	-

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

Oops, there are no upstream regulatory protein records of EAA4_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of EAA4_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 EAA4_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of EAA4_HUMAN !!

Drug and Disease Associations

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