dbPTM

EAA2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EAA2_MOUSE
UniProt AC	P43006
Protein Name	Excitatory amino acid transporter 2
Gene Name	Slc1a2
Organism	Mus musculus (Mouse).
Sequence Length	572
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: 7698742]
Protein Sequence	MASTEGANNMPKQVEVRMHDSHLSSDEPKHRNLGMRMCDKLGKNLLLSLTVFGVILGAVCGGLLRLASPIHPDVVMLIAFPGDILMRMLKMLILPLIISSLITGLSGLDAKASGRLGTRAMVYYMSTTIIAAVLGVILVLAIHPGNPKLKKQLGPGKKNDEVSSLDAFLDLIRNLFPENLVQACFQQIQTVTKKVLVAPPSEEANTTKAVISMLNETMNEAPEETKIVIKKGLEFKDGMNVLGLIGFFIAFGIAMGKMGEQAKLMVEFFNILNEIVMKLVIMIMWYSPLGIACLICGKIIAIKDLEVVARQLGMYMITVIVGLIIHGGIFLPLIYFVVTRKNPFSFFAGIFQAWITALGTASSAGTLPVTFRCLEDNLGIDKRVTRFVLPVGATINMDGTALYEAVAAIFIAQMNGVILDGGQIVTVSLTATLASIGAASIPSAGLVTMLLILTAVGLPTEDISLLVAVDWLLDRMRTSVNVVGDSFGAGIVYHLSKSELDTIDSQHRMQEDIEMTKTQSIYDDKNHRESNSNQCVYAAHNSVVIDECKVTLAANGKSADCSVEEEPWKREK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MASTEGANNM -----CCCCCCCCCC	26.20	20415495
4	Phosphorylation	----MASTEGANNMP ----CCCCCCCCCCC	28.97	23527152
9 (in isoform 2)	Ubiquitination	-	47.82	-
12	Ubiquitination	EGANNMPKQVEVRMH CCCCCCCCEEEEEEC	57.09	22790023
21	Phosphorylation	VEVRMHDSHLSSDEP EEEEECCCCCCCCCH	16.20	25521595
24	Phosphorylation	RMHDSHLSSDEPKHR EECCCCCCCCCHHHC	30.25	25521595
25	Phosphorylation	MHDSHLSSDEPKHRN ECCCCCCCCCHHHCC	52.97	25521595
29	Ubiquitination	HLSSDEPKHRNLGMR CCCCCCHHHCCHHHH	53.82	-
38	S-palmitoylation	RNLGMRMCDKLGKNL CCHHHHHHHHHHHHH	2.70	20685337
158	Ubiquitination	KQLGPGKKNDEVSSL HHHCCCCCCCHHHHH	75.45	-
205	N-linked_Glycosylation	APPSEEANTTKAVIS CCCCHHHCHHHHHHH	52.11	-
215	N-linked_Glycosylation	KAVISMLNETMNEAP HHHHHHHHHHHHCCC	33.77	-
370	Phosphorylation	SAGTLPVTFRCLEDN CCCCCCEEEEHHHCC	11.92	-
373	S-nitrosylation	TLPVTFRCLEDNLGI CCCEEEEHHHCCCCC	4.22	22588120
382	Ubiquitination	EDNLGIDKRVTRFVL HCCCCCCCCEEEEEE	47.01	-
478	Phosphorylation	WLLDRMRTSVNVVGD HHHHHHCCCCEECCC	27.90	20415495
486	Phosphorylation	SVNVVGDSFGAGIVY CCEECCCCCCCCHHE	21.46	26239621
493	Phosphorylation	SFGAGIVYHLSKSEL CCCCCHHEEECHHHH	8.63	20415495
496	Phosphorylation	AGIVYHLSKSELDTI CCHHEEECHHHHCCC	22.33	26239621
497	Ubiquitination	GIVYHLSKSELDTID CHHEEECHHHHCCCH	55.07	-
502	Phosphorylation	LSKSELDTIDSQHRM ECHHHHCCCHHHHHH	39.03	29899451
505	Phosphorylation	SELDTIDSQHRMQED HHHCCCHHHHHHHHH	24.84	25521595
516	Phosphorylation	MQEDIEMTKTQSIYD HHHHHHHHCCHHCCC	20.39	29899451
517	Ubiquitination	QEDIEMTKTQSIYDD HHHHHHHCCHHCCCC	43.17	-
518	Phosphorylation	EDIEMTKTQSIYDDK HHHHHHCCHHCCCCC	20.55	20047950
520	Phosphorylation	IEMTKTQSIYDDKNH HHHHCCHHCCCCCCC	28.48	25521595
522	Phosphorylation	MTKTQSIYDDKNHRE HHCCHHCCCCCCCCC	24.28	20047950
525	Ubiquitination	TQSIYDDKNHRESNS CHHCCCCCCCCCCCC	52.32	-
530	Phosphorylation	DDKNHRESNSNQCVY CCCCCCCCCCCCCEE	45.58	25521595
532	Phosphorylation	KNHRESNSNQCVYAA CCCCCCCCCCCEEEE	37.24	25521595
537	Phosphorylation	SNSNQCVYAAHNSVV CCCCCCEEEECCEEE	13.00	24925903
542	Phosphorylation	CVYAAHNSVVIDECK CEEEECCEEEEEECE	14.11	25521595
551	Phosphorylation	VIDECKVTLAANGKS EEEECEEEEEECCCC	9.00	29899451
557	Ubiquitination	VTLAANGKSADCSVE EEEEECCCCCCCCCC	42.13	-
558	Phosphorylation	TLAANGKSADCSVEE EEEECCCCCCCCCCC	30.64	25521595
561	S-nitrosylation	ANGKSADCSVEEEPW ECCCCCCCCCCCCCC	4.99	22588120
562	Phosphorylation	NGKSADCSVEEEPWK CCCCCCCCCCCCCCC	32.86	25521595
569	Ubiquitination	SVEEEPWKREK---- CCCCCCCCCCC----	62.49	-

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
Oops, there are no upstream regulatory protein records of EAA2_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
38	C	Palmitoylation		20685337
Palmitoylation at Cys-38 is not required for correct subcellular localization, but is important for glutamate uptake activity.

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 EAA2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
SUMO1_HUMAN	SUMO1	physical	17823119
UBC9_HUMAN	UBE2I	physical	17823119

Drug and Disease Associations

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

Regulatory Network of EAA2_MOUSE

Related Literatures of Post-Translational Modification

Palmitoylation
Reference	PubMed
"Palmitoylation and function of glial glutamate transporter-1 isreduced in the YAC128 mouse model of Huntington disease."; Huang K., Kang M.H., Askew C., Kang R., Sanders S.S., Wan J.,Davis N.G., Hayden M.R.; Neurobiol. Dis. 40:207-215(2010). Cited for: PALMITOYLATION AT CYS-38, AND MUTAGENESIS OF CYS-38.	20685337 [Abstract]
Phosphorylation
Reference	PubMed
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations."; Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; Mol. Cell. Proteomics 6:283-293(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-562, AND MASSSPECTROMETRY.	17114649 [Abstract]
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain."; Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; J. Proteome Res. 7:311-318(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-493 AND TYR-537, ANDMASS SPECTROMETRY.	18034455 [Abstract]

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