S38A1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: S38A1_HUMAN
• UniProt AC: Q9H2H9
• Protein Name: Sodium-coupled neutral amino acid transporter 1
• Gene Name: SLC38A1
• Organism: Homo sapiens (Human).
• Sequence Length: 487
• Subcellular Localization: Cell membrane ; Multi-pass membrane protein . Restricted to the somatodendritic compartment of neurons. Found in the cellular processes of neurons in the developing brain (By similarity)..
• Protein Description: Functions as a sodium-dependent amino acid transporter. Mediates the saturable, pH-sensitive and electrogenic cotransport of glutamine and sodium ions with a stoichiometry of 1:1. May also transport small zwitterionic and aliphatic amino acids with a lower affinity. May supply glutamatergic and GABAergic neurons with glutamine which is required for the synthesis of the neurotransmitters glutamate and GABA..
• Protein Sequence: MMHFKSGLELTELQNMTVPEDDNISNDSNDFTEVENGQINSKFISDRESRRSLTNSHLEKKKCDEYIPGTTSLGMSVFNLSNAIMGSGILGLAFALANTGILLFLVLLTSVTLLSIYSINLLLICSKETGCMVYEKLGEQVFGTTGKFVIFGATSLQNTGAMLSYLFIVKNELPSAIKFLMGKEETFSAWYVDGRVLVVIVTFGIILPLCLLKNLGYLGYTSGFSLSCMVFFLIVVIYKKFQIPCIVPELNSTISANSTNADTCTPKYVTFNSKTVYALPTIAFAFVCHPSVLPIYSELKDRSQKKMQMVSNISFFAMFVMYFLTAIFGYLTFYDNVQSDLLHKYQSKDDILILTVRLAVIVAVILTVPVLFFTVRSSLFELAKKTKFNLCRHTVVTCILLVVINLLVIFIPSMKDIFGVVGVTSANMLIFILPSSLYLKITDQDGDKGTQRIWAALFLGLGVLFSLVSIPLVIYDWACSSSSDEGH

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
6	Phosphorylation	--MMHFKSGLELTEL --CCCCCCCCCCHHH	47.90	23927012
11	Phosphorylation	FKSGLELTELQNMTV CCCCCCCHHHCCCCC	25.85	30108239
17	Phosphorylation	LTELQNMTVPEDDNI CHHHCCCCCCCCCCC	40.22	23927012
25	Phosphorylation	VPEDDNISNDSNDFT CCCCCCCCCCCCCCC	40.62	26503892
28	Phosphorylation	DDNISNDSNDFTEVE CCCCCCCCCCCCEEE	42.42	26503892
32	Phosphorylation	SNDSNDFTEVENGQI CCCCCCCCEEECCEE	41.82	23927012
41	Phosphorylation	VENGQINSKFISDRE EECCEECCEECCCHH	30.49	18691976
45	Phosphorylation	QINSKFISDRESRRS EECCEECCCHHHHHH	33.47	23401153
49	Phosphorylation	KFISDRESRRSLTNS EECCCHHHHHHHCHH	33.61	23927012
52	Phosphorylation	SDRESRRSLTNSHLE CCHHHHHHHCHHHHH	38.13	22167270
54	Phosphorylation	RESRRSLTNSHLEKK HHHHHHHCHHHHHHH	35.60	22167270
56	Phosphorylation	SRRSLTNSHLEKKKC HHHHHCHHHHHHHCC	24.98	22167270
60	Ubiquitination	LTNSHLEKKKCDEYI HCHHHHHHHCCCCCC	64.98	21890473
61	Ubiquitination	TNSHLEKKKCDEYIP CHHHHHHHCCCCCCC	49.62	-
129	Phosphorylation	LLICSKETGCMVYEK HHHHCCCCCCCHHHH	39.14	21406692
134	Phosphorylation	KETGCMVYEKLGEQV CCCCCCHHHHHCCCC	4.77	21406692
136	Ubiquitination	TGCMVYEKLGEQVFG CCCCHHHHHCCCCCC	44.07	-
178	Ubiquitination	NELPSAIKFLMGKEE CCCCHHHHHHHCCCC	31.96	21890473
251	N-linked_Glycosylation	PCIVPELNSTISANS CEEECCCCCCCCCCC	35.13	UniProtKB CARBOHYD
257	N-linked_Glycosylation	LNSTISANSTNADTC CCCCCCCCCCCCCCC	42.44	UniProtKB CARBOHYD
265	Phosphorylation	STNADTCTPKYVTFN CCCCCCCCCEEEEEC	25.55	-
288	S-palmitoylation	TIAFAFVCHPSVLPI HHHHHHHHCHHHHHH	2.93	29575903
377	Phosphorylation	VLFFTVRSSLFELAK HHHHHHCHHHHHHHH	27.36	30576142
384	Ubiquitination	SSLFELAKKTKFNLC HHHHHHHHHHCCCCH	73.86	21890473
387	Ubiquitination	FELAKKTKFNLCRHT HHHHHHHCCCCHHHH	40.93	21890473
391	S-palmitoylation	KKTKFNLCRHTVVTC HHHCCCCHHHHHHHH	2.92	29575903
424	Phosphorylation	IFGVVGVTSANMLIF HCCCCCCCCCCEEEE	19.05	22210691
425	Phosphorylation	FGVVGVTSANMLIFI CCCCCCCCCCEEEEE	18.42	22210691
438	Phosphorylation	FILPSSLYLKITDQD EECCCHHEEEEECCC	14.11	22210691
442	Phosphorylation	SSLYLKITDQDGDKG CHHEEEEECCCCCHH	26.48	22210691
448	Ubiquitination	ITDQDGDKGTQRIWA EECCCCCHHHHHHHH	70.19	21890473
450	Phosphorylation	DQDGDKGTQRIWAAL CCCCCHHHHHHHHHH	22.03	30576142

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

Oops, there are no upstream regulatory protein records of S38A1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of S38A1_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 S38A1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FATE1_HUMAN	FATE1	physical	25416956

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.

Related Literatures of Post-Translational Modification

Phosphorylation

"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, AND MASSSPECTROMETRY.
PubMed: 19369195

"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-25; SER-28; SER-52;THR-54 AND SER-56, AND MASS SPECTROMETRY.
PubMed: 18669648

"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52 AND THR-54, AND MASSSPECTROMETRY.
PubMed: 18691976

"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 SER-49 AND THR-54, AND MASSSPECTROMETRY.
PubMed: 17081983