dbPTM

S38A2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	S38A2_HUMAN
UniProt AC	Q96QD8
Protein Name	Sodium-coupled neutral amino acid transporter 2
Gene Name	SLC38A2
Organism	Homo sapiens (Human).
Sequence Length	506
Subcellular Localization	Cell membrane Multi-pass membrane protein . Insulin promotes recruitment to the plasma membrane from a pool localized in the trans-Golgi network or endosomes (By similarity). Enriched in the somatodendritic compartment of neurons, it is also detect
Protein Description	Functions as a sodium-dependent amino acid transporter. Mediates the saturable, pH-sensitive and electrogenic cotransport of neutral amino acids and sodium ions with a stoichiometry of 1:1. May function in the transport of amino acids at the blood-brain barrier and in the supply of maternal nutrients to the fetus through the placenta..
Protein Sequence	MKKAEMGRFSISPDEDSSSYSSNSDFNYSYPTKQAALKSHYADVDPENQNFLLESNLGKKKYETEFHPGTTSFGMSVFNLSNAIVGSGILGLSYAMANTGIALFIILLTFVSIFSLYSVHLLLKTANEGGSLLYEQLGYKAFGLVGKLAASGSITMQNIGAMSSYLFIVKYELPLVIQALTNIEDKTGLWYLNGNYLVLLVSLVVILPLSLFRNLGYLGYTSGLSLLCMVFFLIVVICKKFQVPCPVEAALIINETINTTLTQPTALVPALSHNVTENDSCRPHYFIFNSQTVYAVPILIFSFVCHPAVLPIYEELKDRSRRRMMNVSKISFFAMFLMYLLAALFGYLTFYEHVESELLHTYSSILGTDILLLIVRLAVLMAVTLTVPVVIFPIRSSVTHLLCASKDFSWWRHSLITVSILAFTNLLVIFVPTIRDIFGFIGASAASMLIFILPSAFYIKLVKKEPMKSVQKIGALFFLLSGVLVMTGSMALIVLDWVHNAPGGGH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Ubiquitination	------MKKAEMGRF ------CCCCCCCCC	61.77	-
3	Ubiquitination	-----MKKAEMGRFS -----CCCCCCCCCC	48.56	-
3 (in isoform 1)	Ubiquitination	-	48.56	21890473
10	Phosphorylation	KAEMGRFSISPDEDS CCCCCCCCCCCCCCC	22.31	21945579
12	Phosphorylation	EMGRFSISPDEDSSS CCCCCCCCCCCCCCC	25.71	23401153
17	Phosphorylation	SISPDEDSSSYSSNS CCCCCCCCCCCCCCC	21.09	25463755
18	Phosphorylation	ISPDEDSSSYSSNSD CCCCCCCCCCCCCCC	45.69	21945579
19	Phosphorylation	SPDEDSSSYSSNSDF CCCCCCCCCCCCCCC	32.74	21945579
20	Phosphorylation	PDEDSSSYSSNSDFN CCCCCCCCCCCCCCC	20.33	21945579
21	Phosphorylation	DEDSSSYSSNSDFNY CCCCCCCCCCCCCCC	25.62	21945579
22	Phosphorylation	EDSSSYSSNSDFNYS CCCCCCCCCCCCCCC	31.92	21945579
24	Phosphorylation	SSSYSSNSDFNYSYP CCCCCCCCCCCCCCC	45.59	21945579
28	Phosphorylation	SSNSDFNYSYPTKQA CCCCCCCCCCCCHHH	15.02	21945579
29	Phosphorylation	SNSDFNYSYPTKQAA CCCCCCCCCCCHHHH	26.24	21945579
30	Phosphorylation	NSDFNYSYPTKQAAL CCCCCCCCCCHHHHH	12.45	21945579
32	Phosphorylation	DFNYSYPTKQAALKS CCCCCCCCHHHHHHH	27.79	21945579
33 (in isoform 1)	Ubiquitination	-	33.17	21890473
33	Ubiquitination	FNYSYPTKQAALKSH CCCCCCCHHHHHHHC	33.17	21890473
38	Ubiquitination	PTKQAALKSHYADVD CCHHHHHHHCCCCCC	30.38	21890473
38	Methylation	PTKQAALKSHYADVD CCHHHHHHHCCCCCC	30.38	24575611
38 (in isoform 1)	Ubiquitination	-	30.38	21890473
39	Phosphorylation	TKQAALKSHYADVDP CHHHHHHHCCCCCCH	23.68	21945579
40 (in isoform 2)	Ubiquitination	-	21.88	21906983
41	Phosphorylation	QAALKSHYADVDPEN HHHHHHCCCCCCHHH	16.16	23927012
55	Phosphorylation	NQNFLLESNLGKKKY HCCCHHHHCCCCCCE	37.01	21945579
59	Ubiquitination	LLESNLGKKKYETEF HHHHCCCCCCEECCC	49.62	20972266
59 (in isoform 1)	Ubiquitination	-	49.62	21890473
60	Ubiquitination	LESNLGKKKYETEFH HHHCCCCCCEECCCC	59.81	-
60 (in isoform 1)	Ubiquitination	-	59.81	21890473
134	Phosphorylation	NEGGSLLYEQLGYKA CCCCCHHHHCCCCCH	13.61	-
140 (in isoform 1)	Ubiquitination	-	35.13	21890473
140	Ubiquitination	LYEQLGYKAFGLVGK HHHCCCCCHHHHHHH	35.13	-
210	Phosphorylation	LVVILPLSLFRNLGY HHHHHHHHHHCCCCC	24.42	24719451
217	Phosphorylation	SLFRNLGYLGYTSGL HHHCCCCCCCHHCHH	10.50	-
220	Phosphorylation	RNLGYLGYTSGLSLL CCCCCCCHHCHHHHH	8.64	-
221	Phosphorylation	NLGYLGYTSGLSLLC CCCCCCHHCHHHHHH	17.96	-
258	N-linked_Glycosylation	LIINETINTTLTQPT EEEECCCCCCCCCCC	34.14	UniProtKB CARBOHYD
274	N-linked_Glycosylation	LVPALSHNVTENDSC HHCHHCCCCCCCCCC	38.74	UniProtKB CARBOHYD
320	Phosphorylation	YEELKDRSRRRMMNV HHHHHHHHHHHHCCH	40.03	24719451
324	Sulfoxidation	KDRSRRRMMNVSKIS HHHHHHHHCCHHHHH	1.86	30846556
325	Sulfoxidation	DRSRRRMMNVSKISF HHHHHHHCCHHHHHH	4.20	30846556
328	Phosphorylation	RRRMMNVSKISFFAM HHHHCCHHHHHHHHH	21.19	24719451
403	S-palmitoylation	SSVTHLLCASKDFSW HHHHHHHHHCCCCCH	5.17	29575903
469	Phosphorylation	VKKEPMKSVQKIGAL HCCCCCCHHHHHHHH	24.43	18669648

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
-	K	Ubiquitination	E3 ubiquitin ligase	NEDD4L	Q96PU5	PMID:17003038

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of S38A2_HUMAN !!

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 S38A2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
A4_HUMAN	APP	physical	21832049

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 S38A2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10 AND SER-12, AND MASSSPECTROMETRY.	19413330 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-12 AND SER-469,AND MASS SPECTROMETRY.	18669648 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-41, AND MASSSPECTROMETRY.	19534553 [Abstract]
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks."; Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.; Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-20 AND TYR-41, AND MASSSPECTROMETRY.	17389395 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-41, AND MASSSPECTROMETRY.	18083107 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-41, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Time-resolved mass spectrometry of tyrosine phosphorylation sites inthe epidermal growth factor receptor signaling network reveals dynamicmodules."; Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J.,Lauffenburger D.A., White F.M.; Mol. Cell. Proteomics 4:1240-1250(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-20, AND MASSSPECTROMETRY.	15951569 [Abstract]