dbPTM

EAA2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EAA2_HUMAN
UniProt AC	P43004
Protein Name	Excitatory amino acid transporter 2
Gene Name	SLC1A2
Organism	Homo sapiens (Human).
Sequence Length	574
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: 7521911]
Protein Sequence	MASTEGANNMPKQVEVRMHDSHLGSEEPKHRHLGLRLCDKLGKNLLLTLTVFGVILGAVCGGLLRLASPIHPDVVMLIAFPGDILMRMLKMLILPLIISSLITGLSGLDAKASGRLGTRAMVYYMSTTIIAAVLGVILVLAIHPGNPKLKKQLGPGKKNDEVSSLDAFLDLIRNLFPENLVQACFQQIQTVTKKVLVAPPPDEEANATSAVVSLLNETVTEVPEETKMVIKKGLEFKDGMNVLGLIGFFIAFGIAMGKMGDQAKLMVDFFNILNEIVMKLVIMIMWYSPLGIACLICGKIIAIKDLEVVARQLGMYMVTVIIGLIIHGGIFLPLIYFVVTRKNPFSFFAGIFQAWITALGTASSAGTLPVTFRCLEENLGIDKRVTRFVLPVGATINMDGTALYEAVAAIFIAQMNGVVLDGGQIVTVSLTATLASVGAASIPSAGLVTMLLILTAVGLPTEDISLLVAVDWLLDRMRTSVNVVGDSFGAGIVYHLSKSELDTIDSQHRVHEDIEMTKTQSIYDDMKNHRESNSNQCVYAAHNSVIVDECKVTLAANGKSADCSVEEEPWKREK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MASTEGANNM -----CCCCCCCCCC	26.20	29083192
4	Phosphorylation	----MASTEGANNMP ----CCCCCCCCCCC	28.97	29083192
21	Phosphorylation	VEVRMHDSHLGSEEP EEEEECCCCCCCCCC	13.11	15822905
25	Phosphorylation	MHDSHLGSEEPKHRH ECCCCCCCCCCCCCC	45.18	25332170
38	S-palmitoylation	RHLGLRLCDKLGKNL CCHHHHHHHHHCCHH	3.33	-
99	Phosphorylation	LILPLIISSLITGLS HHHHHHHHHHHHHCC	16.46	22817900
100	Phosphorylation	ILPLIISSLITGLSG HHHHHHHHHHHHCCC	17.24	22817900
103	Phosphorylation	LIISSLITGLSGLDA HHHHHHHHHCCCCCH	37.05	23879269
123	Phosphorylation	LGTRAMVYYMSTTII CCHHHHHHHHHHHHH	4.75	-
124	Phosphorylation	GTRAMVYYMSTTIIA CHHHHHHHHHHHHHH	3.53	-
206	N-linked_Glycosylation	PPPDEEANATSAVVS CCCCHHCCHHHHHHH	47.21	UniProtKB CARBOHYD
216	N-linked_Glycosylation	SAVVSLLNETVTEVP HHHHHHHHCCCCCCC	48.46	UniProtKB CARBOHYD
494	Phosphorylation	SFGAGIVYHLSKSEL CCCCCHHEEECHHHH	8.63	21082442
506	Phosphorylation	SELDTIDSQHRVHED HHHCCCHHCCCHHHH	24.84	-
521	Phosphorylation	IEMTKTQSIYDDMKN HHHHHHHHHHHHHHH	28.48	24076635
523	Phosphorylation	MTKTQSIYDDMKNHR HHHHHHHHHHHHHHH	15.90	25884760
532	Phosphorylation	DMKNHRESNSNQCVY HHHHHHHCCCCCCEE	45.58	25332170
534	Phosphorylation	KNHRESNSNQCVYAA HHHHHCCCCCCEEEE	37.24	25332170
539	Phosphorylation	SNSNQCVYAAHNSVI CCCCCCEEEECCEEE	13.00	25332170
544	Phosphorylation	CVYAAHNSVIVDECK CEEEECCEEEEEECE	11.89	-
560	Phosphorylation	TLAANGKSADCSVEE EEEECCCCCCCCCCC	30.64	-
564	Phosphorylation	NGKSADCSVEEEPWK CCCCCCCCCCCCCCC	32.86	24076635
571	Sumoylation	SVEEEPWKREK---- CCCCCCCCCCC----	62.49	-
571	Sumoylation	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_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
38	C	Palmitoylation		-
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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
AJUBA_HUMAN	AJUBA	physical	11860269
PML_HUMAN	PML	physical	17823119
TAU_HUMAN	MAPT	physical	19527721
RL17_HUMAN	RPL17	physical	26344197
RL23A_HUMAN	RPL23A	physical	26344197
RL32_HUMAN	RPL32	physical	26344197
RL38_HUMAN	RPL38	physical	26344197
RL5_HUMAN	RPL5	physical	26344197

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.

Regulatory Network of EAA2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Phosphoproteomic analysis of synaptosomes from human cerebralcortex."; DeGiorgis J.A., Jaffe H., Moreira J.E., Carlotti C.G. Jr., Leite J.P.,Pant H.C., Dosemeci A.; J. Proteome Res. 4:306-315(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND MASSSPECTROMETRY.	15822905 [Abstract]

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