S22A1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: S22A1_HUMAN
• UniProt AC: O15245
• Protein Name: Solute carrier family 22 member 1
• Gene Name: SLC22A1
• Organism: Homo sapiens (Human).
• Sequence Length: 554
• Subcellular Localization: Basolateral cell membrane ; Multi-pass membrane protein .
• Protein Description: Translocates a broad array of organic cations with various structures and molecular weights including the model compounds 1-methyl-4-phenylpyridinium (MPP), tetraethylammonium (TEA), N-1-methylnicotinamide (NMN), 4-(4-(dimethylamino)styryl)-N-methylpyridinium (ASP), the endogenous compounds choline, guanidine, histamine, epinephrine, adrenaline, noradrenaline and dopamine, and the drugs quinine, and metformin. The transport of organic cations is inhibited by a broad array of compounds like tetramethylammonium (TMA), cocaine, lidocaine, NMDA receptor antagonists, atropine, prazosin, cimetidine, TEA and NMN, guanidine, cimetidine, choline, procainamide, quinine, tetrabutylammonium, and tetrapentylammonium. Translocates organic cations in an electrogenic and pH-independent manner. Translocates organic cations across the plasma membrane in both directions. Transports the polyamines spermine and spermidine. Transports pramipexole across the basolateral membrane of the proximal tubular epithelial cells. The choline transport is activated by MMTS. Regulated by various intracellular signaling pathways including inhibition by protein kinase A activation, and endogenously activation by the calmodulin complex, the calmodulin-dependent kinase II and LCK tyrosine kinase..
• Protein Sequence: MPTVDDILEQVGESGWFQKQAFLILCLLSAAFAPICVGIVFLGFTPDHHCQSPGVAELSQRCGWSPAEELNYTVPGLGPAGEAFLGQCRRYEVDWNQSALSCVDPLASLATNRSHLPLGPCQDGWVYDTPGSSIVTEFNLVCADSWKLDLFQSCLNAGFLFGSLGVGYFADRFGRKLCLLGTVLVNAVSGVLMAFSPNYMSMLLFRLLQGLVSKGNWMAGYTLITEFVGSGSRRTVAIMYQMAFTVGLVALTGLAYALPHWRWLQLAVSLPTFLFLLYYWCVPESPRWLLSQKRNTEAIKIMDHIAQKNGKLPPADLKMLSLEEDVTEKLSPSFADLFRTPRLRKRTFILMYLWFTDSVLYQGLILHMGATSGNLYLDFLYSALVEIPGAFIALITIDRVGRIYPMAMSNLLAGAACLVMIFISPDLHWLNIIIMCVGRMGITIAIQMICLVNAELYPTFVRNLGVMVCSSLCDIGGIITPFIVFRLREVWQALPLILFAVLGLLAAGVTLLLPETKGVALPETMKDAENLGRKAKPKENTIYLKVQTSEPSGT

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
71	N-linked_Glycosylation	WSPAEELNYTVPGLG CCCHHHCCCCCCCCC	33.44	UniProtKB CARBOHYD
196	Phosphorylation	SGVLMAFSPNYMSML HHHHHHCCCCHHHHH	11.60	-
213	Phosphorylation	RLLQGLVSKGNWMAG HHHHHHHHCCCCHHH	39.63	29978859
221	Phosphorylation	KGNWMAGYTLITEFV CCCCHHHHEEEEEEC	6.71	23663014
222	Phosphorylation	GNWMAGYTLITEFVG CCCHHHHEEEEEECC	15.69	23663014
225	Phosphorylation	MAGYTLITEFVGSGS HHHHEEEEEECCCCC	26.87	23663014
230	Phosphorylation	LITEFVGSGSRRTVA EEEEECCCCCHHHHH	28.44	23663014
232	Phosphorylation	TEFVGSGSRRTVAIM EEECCCCCHHHHHHH	21.93	23663014
331	Phosphorylation	EDVTEKLSPSFADLF HHHHHHCCHHHHHHH	29.57	28450419
333	Phosphorylation	VTEKLSPSFADLFRT HHHHCCHHHHHHHCC	29.68	28450419
361	Phosphorylation	WFTDSVLYQGLILHM HCCHHHHHHHHHHHC	9.81	-
510	Phosphorylation	GLLAAGVTLLLPETK HHHHHCHHHHCCCCC	15.69	22210691
541	Phosphorylation	KAKPKENTIYLKVQT CCCCCCCEEEEEEEE	16.46	15499200
543	Phosphorylation	KPKENTIYLKVQTSE CCCCCEEEEEEEECC	9.83	26503514
549	Phosphorylation	IYLKVQTSEPSGT-- EEEEEEECCCCCC--	30.34	26503514
552	Phosphorylation	KVQTSEPSGT----- EEEECCCCCC-----	51.52	26503514

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

Oops, there are no upstream regulatory protein records of S22A1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of S22A1_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 S22A1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CERS2_HUMAN	CERS2	physical	11543633

Drug and Disease Associations

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